PPP1CA encodes PP1-alpha, one of three catalytic subunits (with PP1-beta and PP1-gamma) of protein phosphatase 1, a PPP-family metallo-phosphatase with a binuclear Fe/Zn (Mn in vitro) active site that hydrolyses phosphoserine and phosphothreonine on proteins. The catalytic subunit has little intrinsic substrate selectivity; it acts almost entirely as part of holoenzymes formed with more than 200 regulatory, targeting and inhibitor subunits, most of which dock on the RVxF-binding groove and direct PP1 to particular locations and substrates. PP1-alpha is predominantly nucleoplasmic but shuttles to the cytoplasm. Well-characterised holoenzymes include PNUTS-TOX4-WDR82-PP1, which dephosphorylates CDK9, MEPCE, SPT5, SPT6 and the RNA polymerase II CTD to promote promoter-proximal pause release, set elongation rate and drive poly(A)-coupled termination; the SHOC2-MRAS-PP1C holophosphatase, which removes the inhibitory 14-3-3-site phosphate of RAF kinases to activate RAS-MAPK signalling; GADD34/CReP-PP1, which dephosphorylates eIF2alpha to end the integrated stress response; glycogen-targeted PP1 in glycogen metabolism; and mitotic-exit and kinetochore holoenzymes (Repo-Man, Sds22). Other reported substrates include NBS1 (telomere repair choice), MYC, axin, PER proteins (circadian period), RIG-I/MDA5 and ATG16L1.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000164 protein phosphatase type 1 complex | IDA PMID:35768504 Structural basis for SHOC2 modulation of RAS signalling. | ACCEPT | Summary: PPP1CA as catalytic subunit of a PP1 holoenzyme (SHOC2-MRAS-PP1C or GADD34-PP1). Reason: PP1-alpha functions only as the catalytic subunit of PP1 holoenzymes, each defined by a regulatory/targeting subunit; membership of a protein phosphatase type 1 complex is a core feature. Supporting Evidence: PMID:35768504 SHOC2 is as an essential scaffolding protein that engages both PP1C and RAS to dephosphorylate RAF |
| GO:0000164 protein phosphatase type 1 complex | IDA PMID:35830882 Structure of the MRAS-SHOC2-PP1C phosphatase complex. | ACCEPT | Summary: PPP1CA as catalytic subunit of a PP1 holoenzyme (SHOC2-MRAS-PP1C or GADD34-PP1). Reason: PP1-alpha functions only as the catalytic subunit of PP1 holoenzymes, each defined by a regulatory/targeting subunit; membership of a protein phosphatase type 1 complex is a core feature. Supporting Evidence: PMID:35830882 The MRAS-SHOC2-PP1C holophosphatase dephosphorylates RAF at serine 259 |
| GO:0000164 protein phosphatase type 1 complex | IDA PMID:35831509 Structure-function analysis of the SHOC2-MRAS-PP1C holophosp... | ACCEPT | Summary: PPP1CA as catalytic subunit of a PP1 holoenzyme (SHOC2-MRAS-PP1C or GADD34-PP1). Reason: PP1-alpha functions only as the catalytic subunit of PP1 holoenzymes, each defined by a regulatory/targeting subunit; membership of a protein phosphatase type 1 complex is a core feature. Supporting Evidence: PMID:35831509 Finally, the SMP holophosphatase complex dephosphorylates RAF at the βS259β position |
| GO:0000164 protein phosphatase type 1 complex | IDA PMID:36175670 Structure of the SHOC2-MRAS-PP1C complex provides insights i... | ACCEPT | Summary: PPP1CA as catalytic subunit of a PP1 holoenzyme (SHOC2-MRAS-PP1C or GADD34-PP1). Reason: PP1-alpha functions only as the catalytic subunit of PP1 holoenzymes, each defined by a regulatory/targeting subunit; membership of a protein phosphatase type 1 complex is a core feature. Supporting Evidence: PMID:36175670 The dephosphorylation of CR2-pS is mediated by a heterotrimeric complex comprising SHOC2, MRAS, and PP1C (the SMP complex) |
| GO:0000164 protein phosphatase type 1 complex | IEA GO_REF:0000120 | ACCEPT | Summary: PPP1CA as catalytic subunit of a PP1 holoenzyme (SHOC2-MRAS-PP1C or GADD34-PP1). Reason: PP1-alpha functions only as the catalytic subunit of PP1 holoenzymes, each defined by a regulatory/targeting subunit; membership of a protein phosphatase type 1 complex is a core feature. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0000164 protein phosphatase type 1 complex | IPI PMID:26095357 Structural and Functional Analysis of the GADD34:PP1 eIF2Ξ± P... | ACCEPT | Summary: PPP1CA as catalytic subunit of a PP1 holoenzyme (SHOC2-MRAS-PP1C or GADD34-PP1). Reason: PP1-alpha functions only as the catalytic subunit of PP1 holoenzymes, each defined by a regulatory/targeting subunit; membership of a protein phosphatase type 1 complex is a core feature. Supporting Evidence: PMID:26095357 Here, we report detailed structural and functional analyses of the GADD34:PP1 holoenzyme and its recruitment of eIF2Ξ±. |
| GO:0000164 protein phosphatase type 1 complex | IPI PMID:35831509 Structure-function analysis of the SHOC2-MRAS-PP1C holophosp... | ACCEPT | Summary: PPP1CA as catalytic subunit of a PP1 holoenzyme (SHOC2-MRAS-PP1C or GADD34-PP1). Reason: PP1-alpha functions only as the catalytic subunit of PP1 holoenzymes, each defined by a regulatory/targeting subunit; membership of a protein phosphatase type 1 complex is a core feature. Supporting Evidence: PMID:35831509 Finally, the SMP holophosphatase complex dephosphorylates RAF at the βS259β position |
| GO:0000164 protein phosphatase type 1 complex | IPI PMID:36175670 Structure of the SHOC2-MRAS-PP1C complex provides insights i... | ACCEPT | Summary: PPP1CA as catalytic subunit of a PP1 holoenzyme (SHOC2-MRAS-PP1C or GADD34-PP1). Reason: PP1-alpha functions only as the catalytic subunit of PP1 holoenzymes, each defined by a regulatory/targeting subunit; membership of a protein phosphatase type 1 complex is a core feature. Supporting Evidence: PMID:36175670 The dephosphorylation of CR2-pS is mediated by a heterotrimeric complex comprising SHOC2, MRAS, and PP1C (the SMP complex) |
| GO:0000781 chromosome, telomeric region | IDA PMID:24270157 A quantitative telomeric chromatin isolation protocol identi... | KEEP AS NON CORE | Summary: Detected at telomeric chromatin by QTIP proteomics (abstract-only). Reason: Colocalization with telomeres from a proteomic screen; consistent with PP1-alpha dephosphorylating NBS1 to promote its TRF2 binding at telomeres. Peripheral location. Supporting Evidence: PMID:24270157 identify and validate known, as well as novel telomere-associated polypeptides PMID:28216226 The phosphatase PP1-Ξ± de-phosphorylates mNBS1S433 to promote interaction between NBS1 and TRF2 |
| GO:0001111 RNA polymerase II promoter clearance | IDA PMID:39603239 The PNUTS phosphatase complex controls transcription pause r... | ACCEPT | Summary: PNUTS-PP1 promotes RNAPII pause release / transition into productive elongation. Reason: Within PNUTS-PP1, PPP1CA dephosphorylates CDK9, MEPCE, NCBP1, SUPT6H and other pausing regulators, promoting release of promoter-proximally paused RNAPII. PPP1CA performs the catalytic step, so it participates directly. Two independent 2024 studies agree. GO has no dedicated pause-release term; the curators chose promoter clearance (transition from initiation to elongation) alongside positive regulation of elongation, which is defensible. Supporting Evidence: PMID:39603239 Here, we discover that the mouse PNUTS-PP1 phosphatase complex plays an essential role in controlling transcription pause release |
| GO:0001111 RNA polymerase II promoter clearance | IDA PMID:39603240 The phosphatase PP1 sustains global transcription by promoti... | ACCEPT | Summary: PNUTS-PP1 promotes RNAPII pause release / transition into productive elongation. Reason: Within PNUTS-PP1, PPP1CA dephosphorylates CDK9, MEPCE, NCBP1, SUPT6H and other pausing regulators, promoting release of promoter-proximally paused RNAPII. PPP1CA performs the catalytic step, so it participates directly. Two independent 2024 studies agree. GO has no dedicated pause-release term; the curators chose promoter clearance (transition from initiation to elongation) alongside positive regulation of elongation, which is defensible. Supporting Evidence: PMID:39603240 PNUTS-PP1 promotes pause release by dephosphorylating multiple substrates, including the 7SK small nuclear ribonucleoprotein particle (snRNP) subunit MEPCE |
| GO:0004721 phosphoprotein phosphatase activity | IEA GO_REF:0000120 | MODIFY | Summary: Electronic phosphoprotein phosphatase activity. Reason: The phosphatase activity is real, but the evidence (and every other line) supports the specific child protein serine/threonine phosphatase activity (GO:0004722), already carried by this gene. Proposed replacements: protein serine/threonine phosphatase activity Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0004721 phosphoprotein phosphatase activity | IMP PMID:22311981 Protein phosphatase 1Ξ± mediates ceramide-induced ERM protein... | MODIFY | Summary: PP1-alpha siRNA blocks ceramide-induced ERM dephosphorylation (abstract-only). Reason: The phosphatase activity is real, but the evidence (and every other line) supports the specific child protein serine/threonine phosphatase activity (GO:0004722), already carried by this gene. ERM proteins are dephosphorylated on a C-terminal threonine. Proposed replacements: protein serine/threonine phosphatase activity Supporting Evidence: PMID:22311981 ERM dephosphorylation was blocked by treatment with protein phosphatase 1 (PP1) pharmacological inhibitors and specifically by siRNA to PP1Ξ± |
| GO:0004721 phosphoprotein phosphatase activity | ISS GO_REF:0000024 | MODIFY | Summary: Phosphoprotein phosphatase activity by similarity. Reason: The phosphatase activity is real, but the evidence (and every other line) supports the specific child protein serine/threonine phosphatase activity (GO:0004722), already carried by this gene. Proposed replacements: protein serine/threonine phosphatase activity Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0004722 protein serine/threonine phosphatase activity | EXP PMID:26083323 ATG16L1 phosphorylation is oppositely regulated by CSNK2/cas... | ACCEPT | Summary: PP1 dephosphorylates ATG16L1 Ser139 (abstract-only paper). Reason: PP1-alpha is a PPP-family Ser/Thr protein phosphatase (EC 3.1.3.16) with an Fe/Mn binuclear metal centre; this is its core catalytic activity, exercised on many substrates as directed by its regulatory subunits. Supporting Evidence: PMID:26083323 wild-type PPP1 (protein phosphatase 1), but not the inactive mutant, associated with ATG16L1 and antagonized CSNK2-mediated phosphorylation of ATG16L1 |
| GO:0004722 protein serine/threonine phosphatase activity | EXP PMID:33264625 WDR82/PNUTS-PP1 Prevents Transcription-Replication Conflicts... | ACCEPT | Summary: PNUTS-PP1 dephosphorylates the RNAPII CTD (abstract-only paper). Reason: PP1-alpha is a PPP-family Ser/Thr protein phosphatase (EC 3.1.3.16) with an Fe/Mn binuclear metal centre; this is its core catalytic activity, exercised on many substrates as directed by its regulatory subunits. Supporting Evidence: PMID:33264625 the RNA polymerase II (RNAPII) C-terminal domain (CTD) phosphatase protein phosphatase 1 (PP1) nuclear targeting subunit (PNUTS)-PP1 inhibits replication stress |
| GO:0004722 protein serine/threonine phosphatase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetic inference of Ser/Thr phosphatase activity across the PPP family. Reason: PP1-alpha is a PPP-family Ser/Thr protein phosphatase (EC 3.1.3.16) with an Fe/Mn binuclear metal centre; this is its core catalytic activity, exercised on many substrates as directed by its regulatory subunits. The PAINT node for PPP-family catalytic subunits is well placed; PPP1CA has abundant direct evidence. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Belongs to the PPP phosphatase family. PP-1 subfamily. file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0004722 protein serine/threonine phosphatase activity | IDA PMID:28216226 NBS1 Phosphorylation Status Dictates Repair Choice of Dysfun... | ACCEPT | Summary: PP1-alpha dephosphorylates NBS1 S432/S433. Reason: PP1-alpha is a PPP-family Ser/Thr protein phosphatase (EC 3.1.3.16) with an Fe/Mn binuclear metal centre; this is its core catalytic activity, exercised on many substrates as directed by its regulatory subunits. Supporting Evidence: PMID:28216226 The phosphatase PP1-Ξ± de-phosphorylates mNBS1S433 to promote interaction between NBS1 and TRF2 |
| GO:0004722 protein serine/threonine phosphatase activity | IDA PMID:30158517 MYC dephosphorylation by the PP1/PNUTS phosphatase complex r... | ACCEPT | Summary: PP1 dephosphorylates multiple Ser/Thr residues on MYC. Reason: PP1-alpha is a PPP-family Ser/Thr protein phosphatase (EC 3.1.3.16) with an Fe/Mn binuclear metal centre; this is its core catalytic activity, exercised on many substrates as directed by its regulatory subunits. Supporting Evidence: PMID:30158517 PP1 dephosphorylates multiple serine and threonine residues on MYC. |
| GO:0004722 protein serine/threonine phosphatase activity | IDA PMID:31677974 Control of RNA Pol II Speed by PNUTS-PP1 and Spt5 Dephosphor... | ACCEPT | Summary: PNUTS-PP1 dephosphorylates SPT5 downstream of poly(A) sites. Reason: PP1-alpha is a PPP-family Ser/Thr protein phosphatase (EC 3.1.3.16) with an Fe/Mn binuclear metal centre; this is its core catalytic activity, exercised on many substrates as directed by its regulatory subunits. Supporting Evidence: PMID:31677974 We report that PNUTS-PP1 phosphatase is a negative regulator of RNA polymerase II (Pol II) elongation rate. |
| GO:0004722 protein serine/threonine phosphatase activity | IDA PMID:35768504 Structural basis for SHOC2 modulation of RAS signalling. | ACCEPT | Summary: PP1C dephosphorylates RAF in the SHOC2-MRAS-PP1C complex. Reason: PP1-alpha is a PPP-family Ser/Thr protein phosphatase (EC 3.1.3.16) with an Fe/Mn binuclear metal centre; this is its core catalytic activity, exercised on many substrates as directed by its regulatory subunits. Supporting Evidence: PMID:35768504 SHOC2 is as an essential scaffolding protein that engages both PP1C and RAS to dephosphorylate RAF |
| GO:0004722 protein serine/threonine phosphatase activity | IDA PMID:35830882 Structure of the MRAS-SHOC2-PP1C phosphatase complex. | ACCEPT | Summary: SMP holophosphatase dephosphorylates RAF Ser259. Reason: PP1-alpha is a PPP-family Ser/Thr protein phosphatase (EC 3.1.3.16) with an Fe/Mn binuclear metal centre; this is its core catalytic activity, exercised on many substrates as directed by its regulatory subunits. Supporting Evidence: PMID:35830882 The MRAS-SHOC2-PP1C holophosphatase dephosphorylates RAF at serine 259 |
| GO:0004722 protein serine/threonine phosphatase activity | IDA PMID:35831509 Structure-function analysis of the SHOC2-MRAS-PP1C holophosp... | ACCEPT | Summary: SMP holophosphatase dephosphorylates RAF S259. Reason: PP1-alpha is a PPP-family Ser/Thr protein phosphatase (EC 3.1.3.16) with an Fe/Mn binuclear metal centre; this is its core catalytic activity, exercised on many substrates as directed by its regulatory subunits. Supporting Evidence: PMID:35831509 Finally, the SMP holophosphatase complex dephosphorylates RAF at the βS259β position |
| GO:0004722 protein serine/threonine phosphatase activity | IDA PMID:36175670 Structure of the SHOC2-MRAS-PP1C complex provides insights i... | ACCEPT | Summary: SMP complex dephosphorylates RAF CR2-pS. Reason: PP1-alpha is a PPP-family Ser/Thr protein phosphatase (EC 3.1.3.16) with an Fe/Mn binuclear metal centre; this is its core catalytic activity, exercised on many substrates as directed by its regulatory subunits. Supporting Evidence: PMID:36175670 The dephosphorylation of CR2-pS is mediated by a heterotrimeric complex comprising SHOC2, MRAS, and PP1C (the SMP complex) |
| GO:0004722 protein serine/threonine phosphatase activity | IDA PMID:39603239 The PNUTS phosphatase complex controls transcription pause r... | ACCEPT | Summary: PNUTS-PP1 dephosphorylates NCBP1, CDK9 and SPT6 peptides. Reason: PP1-alpha is a PPP-family Ser/Thr protein phosphatase (EC 3.1.3.16) with an Fe/Mn binuclear metal centre; this is its core catalytic activity, exercised on many substrates as directed by its regulatory subunits. Supporting Evidence: PMID:39603239 Importantly, when we tested the putative substrates identified from our proteomics, we observed dephosphorylation of NCBP1-T21, CDK9-S347, and SPT6H-T1530. |
| GO:0004722 protein serine/threonine phosphatase activity | IDA PMID:39603240 The phosphatase PP1 sustains global transcription by promoti... | ACCEPT | Summary: PNUTS-PP1 dephosphorylates MEPCE and other pause-release regulators (abstract-only). Reason: PP1-alpha is a PPP-family Ser/Thr protein phosphatase (EC 3.1.3.16) with an Fe/Mn binuclear metal centre; this is its core catalytic activity, exercised on many substrates as directed by its regulatory subunits. Supporting Evidence: PMID:39603240 PNUTS-PP1 promotes pause release by dephosphorylating multiple substrates, including the 7SK small nuclear ribonucleoprotein particle (snRNP) subunit MEPCE |
| GO:0004722 protein serine/threonine phosphatase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic mapping of Ser/Thr phosphatase activity. Reason: PP1-alpha is a PPP-family Ser/Thr protein phosphatase (EC 3.1.3.16) with an Fe/Mn binuclear metal centre; this is its core catalytic activity, exercised on many substrates as directed by its regulatory subunits. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0004722 protein serine/threonine phosphatase activity | TAS PMID:10640627 Regulation of phosphorylation of neuronal microtubule-associ... | ACCEPT | Summary: TAS from a rat brain study of MAP1b/MAP2 phosphorylation. Reason: PP1-alpha is a PPP-family Ser/Thr protein phosphatase (EC 3.1.3.16) with an Fe/Mn binuclear metal centre; this is its core catalytic activity, exercised on many substrates as directed by its regulatory subunits. The cited paper actually implicates PP2A and PP2B rather than PP1, so it is a poor source, but the activity itself is certain. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets PMID:10640627 These results suggest that PP2A might be the major PP that participates in regulation of the phosphorylation of MAP1b and MAP2 |
| GO:0004722 protein serine/threonine phosphatase activity | TAS PMID:16262633 Contributions of protein phosphatases PP1, PP2A, PP2B and PP... | ACCEPT | Summary: PP1 dephosphorylates tau (brain phosphatases study). Reason: PP1-alpha is a PPP-family Ser/Thr protein phosphatase (EC 3.1.3.16) with an Fe/Mn binuclear metal centre; this is its core catalytic activity, exercised on many substrates as directed by its regulatory subunits. Supporting Evidence: PMID:16262633 We found that these four phosphatases all dephosphorylated tau at Ser199 |
| GO:0004722 protein serine/threonine phosphatase activity | TAS PMID:8392016 Cloning and characterization of a human protein phosphatase ... | ACCEPT | Summary: Cloning of the human PP1 (alpha) cDNA. Reason: PP1-alpha is a PPP-family Ser/Thr protein phosphatase (EC 3.1.3.16) with an Fe/Mn binuclear metal centre; this is its core catalytic activity, exercised on many substrates as directed by its regulatory subunits. The cloning paper is a weak TAS source, but the activity is well established. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005506 iron ion binding | IDA PMID:30403291 Effects of stably incorporated iron on protein phosphatase-1... | KEEP AS NON CORE | Summary: Native and recombinant PP1 incorporates iron at the binuclear metal site. Reason: PP1 is a metallo-phosphatase whose binuclear centre holds Fe and Zn natively (Mn in recombinant enzyme). Metal binding is a cofactor requirement of the catalytic activity rather than a function in its own right. Supporting Evidence: PMID:30403291 The phosphatase requires divalent metal cations for catalytic activity and contains iron naturally. |
| GO:0005515 protein binding | IPI PMID:10807923 Interaction of inhibitor-2 with the catalytic subunit of typ... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:11739654 Dynamic targeting of protein phosphatase 1 within the nuclei... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:12434308 Protein Phosphatase 1 binds strongly to the retinoblastoma p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:15231748 Functional proteomics mapping of a human signaling pathway. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:15231748 Functional proteomics mapping of a human signaling pathway. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:15231748 Functional proteomics mapping of a human signaling pathway. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:15231748 Functional proteomics mapping of a human signaling pathway. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:15231748 Functional proteomics mapping of a human signaling pathway. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:15231748 Functional proteomics mapping of a human signaling pathway. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:15231748 Functional proteomics mapping of a human signaling pathway. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:15231748 Functional proteomics mapping of a human signaling pathway. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:15231748 Functional proteomics mapping of a human signaling pathway. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:15231748 Functional proteomics mapping of a human signaling pathway. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:15231748 Functional proteomics mapping of a human signaling pathway. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:15231748 Functional proteomics mapping of a human signaling pathway. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:15231748 Functional proteomics mapping of a human signaling pathway. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:15231748 Functional proteomics mapping of a human signaling pathway. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:15231748 Functional proteomics mapping of a human signaling pathway. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:15231748 Functional proteomics mapping of a human signaling pathway. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:15231748 Functional proteomics mapping of a human signaling pathway. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:15231748 Functional proteomics mapping of a human signaling pathway. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:15231748 Functional proteomics mapping of a human signaling pathway. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:16263087 The protein phosphatase-1 targeting subunit TIMAP regulates ... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:16732323 Downregulation of Fer induces PP1 activation and cell-cycle ... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:17274640 A limited screen for protein interactions reveals new roles ... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:17274640 A limited screen for protein interactions reveals new roles ... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:17274640 A limited screen for protein interactions reveals new roles ... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:17274640 A limited screen for protein interactions reveals new roles ... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:17274640 A limited screen for protein interactions reveals new roles ... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:17318175 Protein phosphatase 1 regulates assembly and function of the... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:17511879 The interaction of PP1 with BRCA1 and analysis of their expr... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:17965019 NOM1 targets protein phosphatase I to the nucleolus. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:18068675 A conserved domain of herpes simplex virus ICP34.5 regulates... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:18842582 Nuclear inhibitor of protein phosphatase-1 (NIPP1) directs p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:19389623 Docking motif-guided mapping of the interactome of protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:19389623 Docking motif-guided mapping of the interactome of protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:19389623 Docking motif-guided mapping of the interactome of protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:19389623 Docking motif-guided mapping of the interactome of protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:19389623 Docking motif-guided mapping of the interactome of protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:19389623 Docking motif-guided mapping of the interactome of protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:19389623 Docking motif-guided mapping of the interactome of protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:19389623 Docking motif-guided mapping of the interactome of protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:19389623 Docking motif-guided mapping of the interactome of protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:19389623 Docking motif-guided mapping of the interactome of protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:19389623 Docking motif-guided mapping of the interactome of protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:19389623 Docking motif-guided mapping of the interactome of protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:19389623 Docking motif-guided mapping of the interactome of protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:19389623 Docking motif-guided mapping of the interactome of protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:19389623 Docking motif-guided mapping of the interactome of protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:19389623 Docking motif-guided mapping of the interactome of protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:19389623 Docking motif-guided mapping of the interactome of protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:19389623 Docking motif-guided mapping of the interactome of protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:19389623 Docking motif-guided mapping of the interactome of protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:19389623 Docking motif-guided mapping of the interactome of protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:19389623 Docking motif-guided mapping of the interactome of protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:19389623 Docking motif-guided mapping of the interactome of protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:19389623 Docking motif-guided mapping of the interactome of protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:19389623 Docking motif-guided mapping of the interactome of protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:20186153 Protein phosphatase-1 regulates Akt1 signal transduction pat... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:20305656 Spinophilin directs protein phosphatase 1 specificity by blo... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:20305656 Spinophilin directs protein phosphatase 1 specificity by blo... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:20424263 SUMOylation of the transcriptional co-repressor KAP1 is regu... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:20467437 Direct interaction between hnRNP-M and CDC5L/PLRG1 proteins ... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:20516061 Identification and characterization of a novel human PP1 pho... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:20516061 Identification and characterization of a novel human PP1 pho... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:20516061 Identification and characterization of a novel human PP1 pho... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:20826336 Structural diversity in free and bound states of intrinsical... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:20926688 RRP1B targets PP1 to mammalian cell nucleoli and is associat... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:21094159 Flexibility in the PP1:spinophilin holoenzyme. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:21382349 Identification of the human testis protein phosphatase 1 int... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:21382349 Identification of the human testis protein phosphatase 1 int... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:21518769 Association with endoplasmic reticulum promotes proteasomal ... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:21666598 Shugoshin is a Mad1/Cdc20-like interactor of Mad2. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:21998301 Inhibitory member of the apoptosis-stimulating proteins of t... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:21998301 Inhibitory member of the apoptosis-stimulating proteins of t... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:21998301 Inhibitory member of the apoptosis-stimulating proteins of t... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22321011 Protein phosphatase 1Ξ± interacting proteins in the human bra... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22321011 Protein phosphatase 1Ξ± interacting proteins in the human bra... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22321011 Protein phosphatase 1Ξ± interacting proteins in the human bra... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22321011 Protein phosphatase 1Ξ± interacting proteins in the human bra... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22321011 Protein phosphatase 1Ξ± interacting proteins in the human bra... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22321011 Protein phosphatase 1Ξ± interacting proteins in the human bra... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22321011 Protein phosphatase 1Ξ± interacting proteins in the human bra... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22321011 Protein phosphatase 1Ξ± interacting proteins in the human bra... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22321011 Protein phosphatase 1Ξ± interacting proteins in the human bra... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22321011 Protein phosphatase 1Ξ± interacting proteins in the human bra... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22321011 Protein phosphatase 1Ξ± interacting proteins in the human bra... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22321011 Protein phosphatase 1Ξ± interacting proteins in the human bra... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22321011 Protein phosphatase 1Ξ± interacting proteins in the human bra... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22321011 Protein phosphatase 1Ξ± interacting proteins in the human bra... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22321011 Protein phosphatase 1Ξ± interacting proteins in the human bra... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22321011 Protein phosphatase 1Ξ± interacting proteins in the human bra... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22321011 Protein phosphatase 1Ξ± interacting proteins in the human bra... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22321011 Protein phosphatase 1Ξ± interacting proteins in the human bra... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22321011 Protein phosphatase 1Ξ± interacting proteins in the human bra... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22321011 Protein phosphatase 1Ξ± interacting proteins in the human bra... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22365833 Dynamic protein-protein interaction wiring of the human spli... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22365833 Dynamic protein-protein interaction wiring of the human spli... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22365833 Dynamic protein-protein interaction wiring of the human spli... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22940584 The molecular basis for substrate specificity of the nuclear... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:22940584 The molecular basis for substrate specificity of the nuclear... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:23213405 Taperin (c9orf75), a mutated gene in nonsyndromic deafness, ... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:23396208 Phosphorylation of FOXP3 controls regulatory T cell function... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:23555304 Dynamic circadian protein-protein interaction networks predi... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:23937259 Identification of protein phosphatase 1 as a regulator of th... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:24116158 The nuclear envelope protein, LAP1B, is a novel protein phos... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:24366813 Interaction proteome of human Hippo signaling: modular contr... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:24366813 Interaction proteome of human Hippo signaling: modular contr... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:25544563 Global mapping of herpesvirus-host protein complexes reveals... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:25593058 Alterations in the interactome of serine/threonine protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:25593058 Alterations in the interactome of serine/threonine protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:25593058 Alterations in the interactome of serine/threonine protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:25593058 Alterations in the interactome of serine/threonine protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:25593058 Alterations in the interactome of serine/threonine protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:25593058 Alterations in the interactome of serine/threonine protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:25593058 Alterations in the interactome of serine/threonine protein p... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:25785436 Dissociation of SHP-1 from spinophilin during platelet activ... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:25785436 Dissociation of SHP-1 from spinophilin during platelet activ... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:25852190 Integrative analysis of kinase networks in TRAIL-induced apo... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:25959826 Quantitative interaction proteomics of neurodegenerative dis... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:26095357 Structural and Functional Analysis of the GADD34:PP1 eIF2Ξ± P... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:26095357 Structural and Functional Analysis of the GADD34:PP1 eIF2Ξ± P... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28065597 A Global Analysis of the Receptor Tyrosine Kinase-Protein Ph... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28330616 Systematic Analysis of Human Protein Phosphatase Interaction... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28330616 Systematic Analysis of Human Protein Phosphatase Interaction... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28330616 Systematic Analysis of Human Protein Phosphatase Interaction... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28330616 Systematic Analysis of Human Protein Phosphatase Interaction... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28330616 Systematic Analysis of Human Protein Phosphatase Interaction... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28330616 Systematic Analysis of Human Protein Phosphatase Interaction... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28330616 Systematic Analysis of Human Protein Phosphatase Interaction... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28330616 Systematic Analysis of Human Protein Phosphatase Interaction... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28330616 Systematic Analysis of Human Protein Phosphatase Interaction... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28330616 Systematic Analysis of Human Protein Phosphatase Interaction... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28330616 Systematic Analysis of Human Protein Phosphatase Interaction... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28330616 Systematic Analysis of Human Protein Phosphatase Interaction... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28330616 Systematic Analysis of Human Protein Phosphatase Interaction... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28330616 Systematic Analysis of Human Protein Phosphatase Interaction... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28330616 Systematic Analysis of Human Protein Phosphatase Interaction... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28330616 Systematic Analysis of Human Protein Phosphatase Interaction... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:29109149 Chronic oxidative stress promotes GADD34-mediated phosphoryl... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:30100357 KNL1 Binding to PP1 and Microtubules Is Mutually Exclusive. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:30230954 PPP1R35 ensures centriole homeostasis by promoting centriole... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:34232536 Interactomes of SARS-CoV-2 and human coronaviruses reveal ho... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:34799561 Large scale discovery of coronavirus-host factor protein int... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:35768504 Structural basis for SHOC2 modulation of RAS signalling. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:35830882 Structure of the MRAS-SHOC2-PP1C phosphatase complex. | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:35831509 Structure-function analysis of the SHOC2-MRAS-PP1C holophosp... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:36175670 Structure of the SHOC2-MRAS-PP1C complex provides insights i... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:36175670 Structure of the SHOC2-MRAS-PP1C complex provides insights i... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:37100772 Large-scale phage-based screening reveals extensive pan-vira... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:37776851 Analysis of proteome-wide degradation dynamics in ALS SOD1 i... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:38057879 CircGPRC5A enhances colorectal cancer progress by stabilizin... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Bare protein-binding annotation from an interaction assay (IPI/IDA). PP1-alpha binds more than 200 regulatory, targeting and inhibitor subunits (most via RVxF-type short linear motifs) and many substrates and viral proteins; this row records one such interaction. Reason: Per the protein-binding policy, GO:0005515 carries no functional information. Removal does not dispute the reported interaction. For PP1-alpha the informative content of these interactions is already captured by the catalytic activity (GO:0004722) and by membership of specific holoenzyme complexes (GO:0000164 protein phosphatase type 1 complex, GO:0072357 PTW/PP1 phosphatase complex); the catalytic subunit is the bound partner, so no regulator-side MF (e.g. phosphatase regulator activity) applies to PPP1CA itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0005634 nucleus | EXP PMID:17965019 NOM1 targets protein phosphatase I to the nucleolus. | ACCEPT | Summary: Localization of PP1-alpha in interphase nuclei. Reason: PP1-alpha is predominantly nuclear (nucleoplasm and nuclear speckles, excluded from nucleoli) and acts there on transcription, chromatin and mitotic-exit substrates. Nucleus is not covered by the root-organelle policy, but is an informative location here and is complemented by accepted nucleoplasm rows. Supporting Evidence: PMID:17965019 PP1alpha is primarily nuclear and largely excluded from nucleoli |
| GO:0005634 nucleus | HDA PMID:21630459 Proteomic characterization of the human sperm nucleus. | ACCEPT | Summary: Detected in the human sperm nuclear proteome. Reason: PP1-alpha is predominantly nuclear (nucleoplasm and nuclear speckles, excluded from nucleoli) and acts there on transcription, chromatin and mitotic-exit substrates. Nucleus is not covered by the root-organelle policy, but is an informative location here and is complemented by accepted nucleoplasm rows. Proteomics of purified sperm nuclei cannot resolve sub-compartment. Supporting Evidence: PMID:21630459 With this approach, 403 different proteins have been identified from the isolated sperm nuclei. |
| GO:0005634 nucleus | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetic nuclear localization. Reason: PP1-alpha is predominantly nuclear (nucleoplasm and nuclear speckles, excluded from nucleoli) and acts there on transcription, chromatin and mitotic-exit substrates. Nucleus is not covered by the root-organelle policy, but is an informative location here and is complemented by accepted nucleoplasm rows. Supporting Evidence: PMID:17965019 PP1alpha is primarily nuclear and largely excluded from nucleoli |
| GO:0005634 nucleus | IDA PMID:11739654 Dynamic targeting of protein phosphatase 1 within the nuclei... | ACCEPT | Summary: Live-cell imaging of tagged PP1-alpha. Reason: PP1-alpha is predominantly nuclear (nucleoplasm and nuclear speckles, excluded from nucleoli) and acts there on transcription, chromatin and mitotic-exit substrates. Nucleus is not covered by the root-organelle policy, but is an informative location here and is complemented by accepted nucleoplasm rows. Supporting Evidence: PMID:11739654 tagged PP1alpha is primarily found in the nucleoplasm |
| GO:0005634 nucleus | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic nuclear localization. Reason: PP1-alpha is predominantly nuclear (nucleoplasm and nuclear speckles, excluded from nucleoli) and acts there on transcription, chromatin and mitotic-exit substrates. Nucleus is not covered by the root-organelle policy, but is an informative location here and is complemented by accepted nucleoplasm rows. Supporting Evidence: PMID:17965019 PP1alpha is primarily nuclear and largely excluded from nucleoli |
| GO:0005654 nucleoplasm | IDA GO_REF:0000052 | ACCEPT | Summary: Nucleoplasmic localization (HPA imaging, UniProt, Reactome). Reason: PP1-alpha is primarily nucleoplasmic, where the PNUTS-PP1 complex acts on RNAPII and transcription factors. Reactome nucleoplasm events (TAS) model PNUTS-PP1 and other nuclear PP1 reactions. Supporting Evidence: PMID:11739654 tagged PP1alpha is primarily found in the nucleoplasm |
| GO:0005654 nucleoplasm | IEA GO_REF:0000120 | ACCEPT | Summary: Nucleoplasmic localization (HPA imaging, UniProt, Reactome). Reason: PP1-alpha is primarily nucleoplasmic, where the PNUTS-PP1 complex acts on RNAPII and transcription factors. Reactome nucleoplasm events (TAS) model PNUTS-PP1 and other nuclear PP1 reactions. Supporting Evidence: PMID:11739654 tagged PP1alpha is primarily found in the nucleoplasm |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970179 | ACCEPT | Summary: Nucleoplasmic localization (HPA imaging, UniProt, Reactome). Reason: PP1-alpha is primarily nucleoplasmic, where the PNUTS-PP1 complex acts on RNAPII and transcription factors. Reactome nucleoplasm events (TAS) model PNUTS-PP1 and other nuclear PP1 reactions. Supporting Evidence: PMID:11739654 tagged PP1alpha is primarily found in the nucleoplasm |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970189 | ACCEPT | Summary: Nucleoplasmic localization (HPA imaging, UniProt, Reactome). Reason: PP1-alpha is primarily nucleoplasmic, where the PNUTS-PP1 complex acts on RNAPII and transcription factors. Reactome nucleoplasm events (TAS) model PNUTS-PP1 and other nuclear PP1 reactions. Supporting Evidence: PMID:11739654 tagged PP1alpha is primarily found in the nucleoplasm |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970190 | ACCEPT | Summary: Nucleoplasmic localization (HPA imaging, UniProt, Reactome). Reason: PP1-alpha is primarily nucleoplasmic, where the PNUTS-PP1 complex acts on RNAPII and transcription factors. Reactome nucleoplasm events (TAS) model PNUTS-PP1 and other nuclear PP1 reactions. Supporting Evidence: PMID:11739654 tagged PP1alpha is primarily found in the nucleoplasm |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970191 | ACCEPT | Summary: Nucleoplasmic localization (HPA imaging, UniProt, Reactome). Reason: PP1-alpha is primarily nucleoplasmic, where the PNUTS-PP1 complex acts on RNAPII and transcription factors. Reactome nucleoplasm events (TAS) model PNUTS-PP1 and other nuclear PP1 reactions. Supporting Evidence: PMID:11739654 tagged PP1alpha is primarily found in the nucleoplasm |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970193 | ACCEPT | Summary: Nucleoplasmic localization (HPA imaging, UniProt, Reactome). Reason: PP1-alpha is primarily nucleoplasmic, where the PNUTS-PP1 complex acts on RNAPII and transcription factors. Reactome nucleoplasm events (TAS) model PNUTS-PP1 and other nuclear PP1 reactions. Supporting Evidence: PMID:11739654 tagged PP1alpha is primarily found in the nucleoplasm |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970282 | ACCEPT | Summary: Nucleoplasmic localization (HPA imaging, UniProt, Reactome). Reason: PP1-alpha is primarily nucleoplasmic, where the PNUTS-PP1 complex acts on RNAPII and transcription factors. Reactome nucleoplasm events (TAS) model PNUTS-PP1 and other nuclear PP1 reactions. Supporting Evidence: PMID:11739654 tagged PP1alpha is primarily found in the nucleoplasm |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970294 | ACCEPT | Summary: Nucleoplasmic localization (HPA imaging, UniProt, Reactome). Reason: PP1-alpha is primarily nucleoplasmic, where the PNUTS-PP1 complex acts on RNAPII and transcription factors. Reactome nucleoplasm events (TAS) model PNUTS-PP1 and other nuclear PP1 reactions. Supporting Evidence: PMID:11739654 tagged PP1alpha is primarily found in the nucleoplasm |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970318 | ACCEPT | Summary: Nucleoplasmic localization (HPA imaging, UniProt, Reactome). Reason: PP1-alpha is primarily nucleoplasmic, where the PNUTS-PP1 complex acts on RNAPII and transcription factors. Reactome nucleoplasm events (TAS) model PNUTS-PP1 and other nuclear PP1 reactions. Supporting Evidence: PMID:11739654 tagged PP1alpha is primarily found in the nucleoplasm |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970320 | ACCEPT | Summary: Nucleoplasmic localization (HPA imaging, UniProt, Reactome). Reason: PP1-alpha is primarily nucleoplasmic, where the PNUTS-PP1 complex acts on RNAPII and transcription factors. Reactome nucleoplasm events (TAS) model PNUTS-PP1 and other nuclear PP1 reactions. Supporting Evidence: PMID:11739654 tagged PP1alpha is primarily found in the nucleoplasm |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970428 | ACCEPT | Summary: Nucleoplasmic localization (HPA imaging, UniProt, Reactome). Reason: PP1-alpha is primarily nucleoplasmic, where the PNUTS-PP1 complex acts on RNAPII and transcription factors. Reactome nucleoplasm events (TAS) model PNUTS-PP1 and other nuclear PP1 reactions. Supporting Evidence: PMID:11739654 tagged PP1alpha is primarily found in the nucleoplasm |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970429 | ACCEPT | Summary: Nucleoplasmic localization (HPA imaging, UniProt, Reactome). Reason: PP1-alpha is primarily nucleoplasmic, where the PNUTS-PP1 complex acts on RNAPII and transcription factors. Reactome nucleoplasm events (TAS) model PNUTS-PP1 and other nuclear PP1 reactions. Supporting Evidence: PMID:11739654 tagged PP1alpha is primarily found in the nucleoplasm |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970431 | ACCEPT | Summary: Nucleoplasmic localization (HPA imaging, UniProt, Reactome). Reason: PP1-alpha is primarily nucleoplasmic, where the PNUTS-PP1 complex acts on RNAPII and transcription factors. Reactome nucleoplasm events (TAS) model PNUTS-PP1 and other nuclear PP1 reactions. Supporting Evidence: PMID:11739654 tagged PP1alpha is primarily found in the nucleoplasm |
| GO:0005730 nucleolus | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: UniProt subcellular-location mapping to nucleolus. Reason: PP1-alpha is largely excluded from nucleoli at steady state, but all PP1 isoforms are in the nucleolar proteome and NOM1 can target PP1 to the nucleolus. A minor, conditional location. Supporting Evidence: PMID:17965019 all three PP1 isoforms are included in the nucleolar proteome file:human/PPP1CA/PPP1CA-uniprot.txt NOM1 plays a role in targeting this protein to the nucleolus |
| GO:0005737 cytoplasm | EXP PMID:29769351 Protein Phosphatase 1Ξ± Interacts with Venezuelan Equine Ence... | ACCEPT | Summary: PP1-alpha shuttles to the cytosol during VEEV infection (abstract-only). Reason: PP1-alpha shuttles between nucleus and cytoplasm and is cytoplasmic in many holoenzymes (glycogen-targeted PP1, GADD34-PP1, SHOC2-MRAS-PP1C, the RIG-I/MDA5-dephosphorylating pool). Supporting Evidence: PMID:29769351 Confocal microscopy demonstrated that PP1Ξ± shuttles toward the cytosol during infection with VEEV |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | ACCEPT | Summary: Phylogenetic cytoplasmic localization. Reason: PP1-alpha shuttles between nucleus and cytoplasm and is cytoplasmic in many holoenzymes (glycogen-targeted PP1, GADD34-PP1, SHOC2-MRAS-PP1C, the RIG-I/MDA5-dephosphorylating pool). Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Cytoplasm {ECO:0000269|PubMed:11739654 |
| GO:0005737 cytoplasm | IDA PMID:11739654 Dynamic targeting of protein phosphatase 1 within the nuclei... | ACCEPT | Summary: Live-cell imaging shows cytoplasmic and nuclear PP1. Reason: PP1-alpha shuttles between nucleus and cytoplasm and is cytoplasmic in many holoenzymes (glycogen-targeted PP1, GADD34-PP1, SHOC2-MRAS-PP1C, the RIG-I/MDA5-dephosphorylating pool). Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Cytoplasm {ECO:0000269|PubMed:11739654 |
| GO:0005737 cytoplasm | IDA PMID:23499489 Dephosphorylation of the RNA sensors RIG-I and MDA5 by the p... | ACCEPT | Summary: Cytoplasmic PP1-alpha dephosphorylates RIG-I/MDA5. Reason: PP1-alpha shuttles between nucleus and cytoplasm and is cytoplasmic in many holoenzymes (glycogen-targeted PP1, GADD34-PP1, SHOC2-MRAS-PP1C, the RIG-I/MDA5-dephosphorylating pool). Supporting Evidence: PMID:23499489 we identified PP1Ξ± and PP1Ξ³ as the primary phosphatases that are responsible for MDA5 and RIG-I dephosphorylation and that lead to their activation |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic cytoplasmic localization. Reason: PP1-alpha shuttles between nucleus and cytoplasm and is cytoplasmic in many holoenzymes (glycogen-targeted PP1, GADD34-PP1, SHOC2-MRAS-PP1C, the RIG-I/MDA5-dephosphorylating pool). Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Cytoplasm {ECO:0000269|PubMed:11739654 |
| GO:0005737 cytoplasm | IPI PMID:35831509 Structure-function analysis of the SHOC2-MRAS-PP1C holophosp... | ACCEPT | Summary: SMP complex studies place PP1C in the cytoplasm/at the membrane. Reason: PP1-alpha shuttles between nucleus and cytoplasm and is cytoplasmic in many holoenzymes (glycogen-targeted PP1, GADD34-PP1, SHOC2-MRAS-PP1C, the RIG-I/MDA5-dephosphorylating pool). Supporting Evidence: PMID:35831509 MRAS activation leads to membrane localization of the SHOC2-MRAS-PP1C (SMP) complex |
| GO:0005783 endoplasmic reticulum | IDA PMID:26742780 Targeted redox inhibition of protein phosphatase 1 by Nox4 r... | KEEP AS NON CORE | Summary: GADD34-PP1 acts at the ER, where Nox4 inhibits it. Reason: Root organelle (ER) with direct evidence: the GADD34-targeted PP1 pool that dephosphorylates eIF2alpha acts at the ER. The ER is one of many holoenzyme-specific locations, so non-core. No sub-compartment term added: GADD34 is a cytosol-facing ER-membrane-anchored targeting subunit, but PPP1CA itself has no independent ER-membrane evidence. Supporting Evidence: PMID:26742780 binds to a PP1-targeting subunit GADD34 at the endoplasmic reticulum, and inhibits PP1 activity to increase eIF2Ξ± phosphorylation |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: Cytosolic localization (HPA imaging, Reactome). Reason: PP1-alpha shuttles between nucleus and cytoplasm and is cytoplasmic in many holoenzymes (glycogen-targeted PP1, GADD34-PP1, SHOC2-MRAS-PP1C, the RIG-I/MDA5-dephosphorylating pool). Supporting Evidence: PMID:29769351 Confocal microscopy demonstrated that PP1Ξ± shuttles toward the cytosol during infection with VEEV |
| GO:0005829 cytosol | TAS Reactome:R-HSA-180038 | ACCEPT | Summary: Cytosolic localization (HPA imaging, Reactome). Reason: PP1-alpha shuttles between nucleus and cytoplasm and is cytoplasmic in many holoenzymes (glycogen-targeted PP1, GADD34-PP1, SHOC2-MRAS-PP1C, the RIG-I/MDA5-dephosphorylating pool). Supporting Evidence: PMID:29769351 Confocal microscopy demonstrated that PP1Ξ± shuttles toward the cytosol during infection with VEEV |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9831948 | ACCEPT | Summary: Cytosolic localization (HPA imaging, Reactome). Reason: PP1-alpha shuttles between nucleus and cytoplasm and is cytoplasmic in many holoenzymes (glycogen-targeted PP1, GADD34-PP1, SHOC2-MRAS-PP1C, the RIG-I/MDA5-dephosphorylating pool). Supporting Evidence: PMID:29769351 Confocal microscopy demonstrated that PP1Ξ± shuttles toward the cytosol during infection with VEEV |
| GO:0005829 cytosol | TAS Reactome:R-HSA-9832037 | ACCEPT | Summary: Cytosolic localization (HPA imaging, Reactome). Reason: PP1-alpha shuttles between nucleus and cytoplasm and is cytoplasmic in many holoenzymes (glycogen-targeted PP1, GADD34-PP1, SHOC2-MRAS-PP1C, the RIG-I/MDA5-dephosphorylating pool). Supporting Evidence: PMID:29769351 Confocal microscopy demonstrated that PP1Ξ± shuttles toward the cytosol during infection with VEEV |
| GO:0005912 adherens junction | IDA PMID:25468996 E-cadherin interactome complexity and robustness resolved by... | KEEP AS NON CORE | Summary: Found in E-cadherin proximity proteome. Reason: Proximity biotinylation places PPP1CA near the E-cadherin cytoplasmic tail; plausible peripheral location (PP1 regulates junctional and cytoskeletal proteins) but not a defining one. Supporting Evidence: PMID:25468996 We used proximity biotinylation and quantitative proteomics to identify 561 proteins in the vicinity of the cytoplasmic tail of E-cadherin. |
| GO:0005979 regulation of glycogen biosynthetic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Glycogen metabolism regulation transferred from rodent orthologs. Reason: PP1 catalytic subunits, targeted by PPP1R3 glycogen-binding subunits, dephosphorylate (activate) glycogen synthase and (inactivate) glycogen phosphorylase. Transferred from rodent orthologs. Real but holoenzyme- and tissue-specific. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen file:human/PPP1CA/PPP1CA-uniprot.txt participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis |
| GO:0005981 regulation of glycogen catabolic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Glycogen metabolism regulation transferred from rodent orthologs. Reason: PP1 catalytic subunits, targeted by PPP1R3 glycogen-binding subunits, dephosphorylate (activate) glycogen synthase and (inactivate) glycogen phosphorylase. Transferred from rodent orthologs. Real but holoenzyme- and tissue-specific. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen file:human/PPP1CA/PPP1CA-uniprot.txt participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis |
| GO:0006470 protein dephosphorylation | IMP PMID:22801782 Sds22 and Repo-Man stabilize chromosome segregation by count... | ACCEPT | Summary: PP1-alpha depletion affects Aurora B-opposed Dsn1 phosphorylation at anaphase kinetochores. Reason: Protein dephosphorylation is the process PPP1CA catalyses; the IMP (PP1-alpha RNAi in the Sds22/Repo-Man study) supports it in a mitotic setting. Supporting Evidence: PMID:22801782 By ribonucleic acid interference screening using a phosphorylation biosensor, we identified two PP1-targeting subunits, Sds22 and Repo-Man, which counteracted Aurora B-dependent phosphorylation of the outer kinetochore component Dsn1 during anaphase. |
| GO:0008157 protein phosphatase 1 binding | IEA GO_REF:0000107 | REMOVE | Summary: Electronic transfer of protein phosphatase 1 binding from a rodent ortholog. Reason: GO:0008157 describes binding to PP1, a property of PP1 regulatory, targeting and inhibitor subunits. PPP1CA is itself the PP1 catalytic subunit; no evidence shows it binds another PP1 catalytic subunit as a function. The electronic ortholog transfer therefore asserts a function the catalytic subunit does not have, and is removed rather than kept as an over-annotation. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0010288 response to lead ion | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Response to lead ion transferred from rat. Reason: Response-to-chemical annotation from a rodent observation (expression or activity change on lead exposure). It does not describe a function of PP1-alpha. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0010288 response to lead ion | ISS GO_REF:0000024 | MARK AS OVER ANNOTATED | Summary: Response to lead ion transferred from rat. Reason: Response-to-chemical annotation from a rodent observation (expression or activity change on lead exposure). It does not describe a function of PP1-alpha. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0014069 postsynaptic density | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Neuronal/synaptic location transferred from rodent orthologs. Reason: PP1 catalytic subunits are targeted to synapses (dendritic spines, PSD) by neurabin/spinophilin (PPP1R9A/B) and act in synaptic plasticity; transferred from rodent orthologs. A tissue-specific holoenzyme location, non-core. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Involved in regulation of ionic conductances and long-term synaptic plasticity. file:human/PPP1CA/PPP1CA-uniprot.txt Interacts with PPP1R9A and PPP1R9B. |
| GO:0016787 hydrolase activity | IEA GO_REF:0000002 | TOO GENERAL | Summary: InterPro2GO hydrolase activity. Reason: True but uninformative; entailed by the accepted protein serine/threonine phosphatase activity (GO:0004722). Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Belongs to the PPP phosphatase family. PP-1 subfamily. |
| GO:0016791 phosphatase activity | IDA PMID:23499489 Dephosphorylation of the RNA sensors RIG-I and MDA5 by the p... | MODIFY | Summary: PP1-alpha and PP1-gamma dephosphorylate RIG-I and MDA5 CARDs. Reason: The phosphatase activity is real, but the evidence (and every other line) supports the specific child protein serine/threonine phosphatase activity (GO:0004722), already carried by this gene. Proposed replacements: protein serine/threonine phosphatase activity Supporting Evidence: PMID:23499489 we identified PP1Ξ± and PP1Ξ³ as the primary phosphatases that are responsible for MDA5 and RIG-I dephosphorylation and that lead to their activation |
| GO:0016791 phosphatase activity | IDA PMID:26083323 ATG16L1 phosphorylation is oppositely regulated by CSNK2/cas... | MODIFY | Summary: PP1 dephosphorylates ATG16L1 (abstract-only). Reason: The phosphatase activity is real, but the evidence (and every other line) supports the specific child protein serine/threonine phosphatase activity (GO:0004722), already carried by this gene. Proposed replacements: protein serine/threonine phosphatase activity Supporting Evidence: PMID:26083323 wild-type PPP1 (protein phosphatase 1), but not the inactive mutant, associated with ATG16L1 and antagonized CSNK2-mediated phosphorylation of ATG16L1 |
| GO:0016791 phosphatase activity | IEA GO_REF:0000107 | MODIFY | Summary: Electronic phosphatase activity. Reason: The phosphatase activity is real, but the evidence (and every other line) supports the specific child protein serine/threonine phosphatase activity (GO:0004722), already carried by this gene. Proposed replacements: protein serine/threonine phosphatase activity Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0016791 phosphatase activity | ISS GO_REF:0000024 | MODIFY | Summary: Phosphatase activity by similarity. Reason: The phosphatase activity is real, but the evidence (and every other line) supports the specific child protein serine/threonine phosphatase activity (GO:0004722), already carried by this gene. Proposed replacements: protein serine/threonine phosphatase activity Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0032922 circadian regulation of gene expression | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Circadian regulation of gene expression transferred from mouse. Reason: PP1 dephosphorylates PER proteins (and possibly CK1delta/epsilon), setting circadian period; knockdown of PPP1CA in human U-2 OS cells lengthens the period. A real but peripheral role. Clock-gene expression changes follow from PER phosphorylation control. Supporting Evidence: PMID:21712997 As a result, knock-down of PPP1CA, PPP1CB or PPP1CC provoked lengthening of the circadian period of U-2 OS cells of up to two hours file:human/PPP1CA/PPP1CA-uniprot.txt In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation |
| GO:0032922 circadian regulation of gene expression | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Circadian regulation of gene expression transferred from mouse. Reason: PP1 dephosphorylates PER proteins (and possibly CK1delta/epsilon), setting circadian period; knockdown of PPP1CA in human U-2 OS cells lengthens the period. A real but peripheral role. Clock-gene expression changes follow from PER phosphorylation control. Supporting Evidence: PMID:21712997 As a result, knock-down of PPP1CA, PPP1CB or PPP1CC provoked lengthening of the circadian period of U-2 OS cells of up to two hours file:human/PPP1CA/PPP1CA-uniprot.txt In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation |
| GO:0032968 positive regulation of transcription elongation by RNA polymerase II | IDA PMID:39603239 The PNUTS phosphatase complex controls transcription pause r... | ACCEPT | Summary: PNUTS-PP1 promotes RNAPII pause release. Reason: Within PNUTS-PP1, PPP1CA dephosphorylates CDK9, MEPCE, NCBP1, SUPT6H and other pausing regulators, promoting release of promoter-proximally paused RNAPII. PPP1CA performs the catalytic step, so it participates directly. Two independent 2024 studies agree. Supporting Evidence: PMID:39603239 Here, we discover that the mouse PNUTS-PP1 phosphatase complex plays an essential role in controlling transcription pause release |
| GO:0032968 positive regulation of transcription elongation by RNA polymerase II | IDA PMID:39603240 The phosphatase PP1 sustains global transcription by promoti... | ACCEPT | Summary: PNUTS-PP1 promotes RNAPII pause release. Reason: Within PNUTS-PP1, PPP1CA dephosphorylates CDK9, MEPCE, NCBP1, SUPT6H and other pausing regulators, promoting release of promoter-proximally paused RNAPII. PPP1CA performs the catalytic step, so it participates directly. Two independent 2024 studies agree. Supporting Evidence: PMID:39603240 PNUTS-PP1 promotes pause release by dephosphorylating multiple substrates, including the 7SK small nuclear ribonucleoprotein particle (snRNP) subunit MEPCE |
| GO:0034244 negative regulation of transcription elongation by RNA polymerase II | IDA PMID:31677974 Control of RNA Pol II Speed by PNUTS-PP1 and Spt5 Dephosphor... | ACCEPT | Summary: PNUTS-PP1 slows RNAPII elongation after poly(A) sites. Reason: PNUTS-PP1 dephosphorylates SPT5 downstream of poly(A) sites, slowing RNAPII so the XRN2 torpedo can catch it (the "sitting duck" mechanism). This is the negative-regulation side of the same enzyme; it acts in a different gene region from pause release, so it does not conflict with the positive-regulation rows. Supporting Evidence: PMID:31677974 We report that PNUTS-PP1 phosphatase is a negative regulator of RNA polymerase II (Pol II) elongation rate. PMID:31677974 Immediately downstream of poly(A) sites, Pol II decelerates from >2 kb/min to <1 kb/min, which correlates with Spt5 dephosphorylation. |
| GO:0042587 glycogen granule | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Glycogen granule localization transferred from rodent orthologs. Reason: PP1 catalytic subunits are targeted to glycogen by PPP1R3 subunits, where they dephosphorylate glycogen synthase and phosphorylase. Real but holoenzyme-specific. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen |
| GO:0042752 regulation of circadian rhythm | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PP1 regulates circadian period. Reason: PP1 dephosphorylates PER proteins (and possibly CK1delta/epsilon), setting circadian period; knockdown of PPP1CA in human U-2 OS cells lengthens the period. A real but peripheral role. Supporting Evidence: PMID:21712997 As a result, knock-down of PPP1CA, PPP1CB or PPP1CC provoked lengthening of the circadian period of U-2 OS cells of up to two hours file:human/PPP1CA/PPP1CA-uniprot.txt In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation |
| GO:0042752 regulation of circadian rhythm | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: PP1 regulates circadian period. Reason: PP1 dephosphorylates PER proteins (and possibly CK1delta/epsilon), setting circadian period; knockdown of PPP1CA in human U-2 OS cells lengthens the period. A real but peripheral role. Supporting Evidence: PMID:21712997 As a result, knock-down of PPP1CA, PPP1CB or PPP1CC provoked lengthening of the circadian period of U-2 OS cells of up to two hours file:human/PPP1CA/PPP1CA-uniprot.txt In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation |
| GO:0042752 regulation of circadian rhythm | IMP PMID:21712997 Protein phosphatase 1 (PP1) is a post-translational regulato... | KEEP AS NON CORE | Summary: PP1 regulates circadian period. Reason: PP1 dephosphorylates PER proteins (and possibly CK1delta/epsilon), setting circadian period; knockdown of PPP1CA in human U-2 OS cells lengthens the period. A real but peripheral role. Supporting Evidence: PMID:21712997 As a result, knock-down of PPP1CA, PPP1CB or PPP1CC provoked lengthening of the circadian period of U-2 OS cells of up to two hours file:human/PPP1CA/PPP1CA-uniprot.txt In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation |
| GO:0043021 ribonucleoprotein complex binding | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Electronic transfer of ribonucleoprotein complex binding from a rodent ortholog. Reason: PP1-alpha associates with RNA-processing and RNP complexes through targeting subunits (e.g. the ILF2/ILF3/YLPM1 complex), but binding an RNP complex is not an activity of the catalytic subunit itself. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Forms a complex with ILF2, ILF3, YLPM1, KHDRBS1, RBMX and NCOA5. |
| GO:0043025 neuronal cell body | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Neuronal/synaptic location transferred from rodent orthologs. Reason: PP1 catalytic subunits are targeted to synapses (dendritic spines, PSD) by neurabin/spinophilin (PPP1R9A/B) and act in synaptic plasticity; transferred from rodent orthologs. A tissue-specific holoenzyme location, non-core. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Involved in regulation of ionic conductances and long-term synaptic plasticity. file:human/PPP1CA/PPP1CA-uniprot.txt Interacts with PPP1R9A and PPP1R9B. |
| GO:0043153 entrainment of circadian clock by photoperiod | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Entrainment by photoperiod transferred from the mouse study. Reason: The in vivo evidence is altered light-induced phase shifts in mice expressing a pan-PP1 inhibitor in brain, which does not distinguish PP1-alpha from other isoforms and reflects a modulatory effect rather than a step in light entrainment performed by PP1. Supporting Evidence: PMID:21712997 Moreover, reduction of PP1 activity in the brain altered light-mediated clock resetting behavior in mice, enhancing the phase shifts in either direction. |
| GO:0043153 entrainment of circadian clock by photoperiod | ISS GO_REF:0000024 | MARK AS OVER ANNOTATED | Summary: Entrainment by photoperiod transferred from the mouse study. Reason: The in vivo evidence is altered light-induced phase shifts in mice expressing a pan-PP1 inhibitor in brain, which does not distinguish PP1-alpha from other isoforms and reflects a modulatory effect rather than a step in light entrainment performed by PP1. Supporting Evidence: PMID:21712997 Moreover, reduction of PP1 activity in the brain altered light-mediated clock resetting behavior in mice, enhancing the phase shifts in either direction. |
| GO:0043197 dendritic spine | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Neuronal/synaptic location transferred from rodent orthologs. Reason: PP1 catalytic subunits are targeted to synapses (dendritic spines, PSD) by neurabin/spinophilin (PPP1R9A/B) and act in synaptic plasticity; transferred from rodent orthologs. A tissue-specific holoenzyme location, non-core. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Involved in regulation of ionic conductances and long-term synaptic plasticity. file:human/PPP1CA/PPP1CA-uniprot.txt Interacts with PPP1R9A and PPP1R9B. |
| GO:0043204 perikaryon | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Neuronal/synaptic location transferred from rodent orthologs. Reason: PP1 catalytic subunits are targeted to synapses (dendritic spines, PSD) by neurabin/spinophilin (PPP1R9A/B) and act in synaptic plasticity; transferred from rodent orthologs. A tissue-specific holoenzyme location, non-core. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Involved in regulation of ionic conductances and long-term synaptic plasticity. file:human/PPP1CA/PPP1CA-uniprot.txt Interacts with PPP1R9A and PPP1R9B. |
| GO:0043247 telomere maintenance in response to DNA damage | IDA PMID:28216226 NBS1 Phosphorylation Status Dictates Repair Choice of Dysfun... | KEEP AS NON CORE | Summary: PP1-alpha dephosphorylates NBS1 S432, steering repair of dysfunctional telomeres. Reason: PP1-alpha removes the CDK2 phosphate on NBS1 S432/S433, favouring NBS1-TRF2 binding and alternative-NHEJ at telomeres lacking POT1-TPP1. A genuine but context-specific role; non-core for a phosphatase with hundreds of substrates. Supporting Evidence: PMID:28216226 The phosphatase PP1-Ξ± de-phosphorylates mNBS1S433 to promote interaction between NBS1 and TRF2 |
| GO:0043558 regulation of translational initiation in response to stress | ISS GO_REF:0000024 | MODIFY | Summary: PPP1R15A/B (GADD34/CReP)-PP1 dephosphorylate eIF2alpha (ISS). Reason: Correct, but the specific mechanism is known: PP1 holoenzymes with GADD34 or CReP dephosphorylate eIF2alpha Ser51, terminating the integrated stress response. The descendant GO:0036496 states this precisely. Proposed replacements: regulation of translational initiation by eIF2 alpha dephosphorylation Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Interacts with PPP1R15A and PPP1R15B; the interactions mediate binding to EIF2S1 PMID:26095357 Here, we report detailed structural and functional analyses of the GADD34:PP1 holoenzyme and its recruitment of eIF2Ξ±. |
| GO:0044877 protein-containing complex binding | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Electronic transfer of protein-containing complex binding. Reason: Uninformative; reflects incorporation into PP1 holoenzymes, already captured by the complex (CC) annotations. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets |
| GO:0045725 positive regulation of glycogen biosynthetic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Glycogen metabolism regulation transferred from rodent orthologs. Reason: PP1 catalytic subunits, targeted by PPP1R3 glycogen-binding subunits, dephosphorylate (activate) glycogen synthase and (inactivate) glycogen phosphorylase. Transferred from rodent orthologs. Real but holoenzyme- and tissue-specific. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt PPP1R3A (in skeletal muscle), PPP1R3B (in liver), PPP1R3C, PPP1R3D and PPP1R3F (in brain) mediate binding to glycogen file:human/PPP1CA/PPP1CA-uniprot.txt participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis |
| GO:0046579 positive regulation of Ras protein signal transduction | NAS PMID:35831509 Structure-function analysis of the SHOC2-MRAS-PP1C holophosp... | ACCEPT | Summary: SHOC2-MRAS-PP1C activates RAF by removing the inhibitory 14-3-3 site phosphate (NAS). Reason: In the SMP holophosphatase, PP1C catalyses dephosphorylation of RAF S259/S365/S214, releasing RAF autoinhibition and promoting RAS-MAPK signalling. Gain-of-function SHOC2/PPP1CB mutations cause RASopathies. PPP1CA does the catalytic step. Supporting Evidence: PMID:35831509 Finally, the SMP holophosphatase complex dephosphorylates RAF at the βS259β position, inducing RAF release from its autoinhibited state when bound to 14-3-31. file:human/PPP1CA/PPP1CA-uniprot.txt Core component of the SHOC2-MRAS-PP1c (SMP) holophosphatase complex that regulates the MAPK pathway activation |
| GO:0046914 transition metal ion binding | IDA PMID:30403291 Effects of stably incorporated iron on protein phosphatase-1... | TOO GENERAL | Summary: Transition metal ion binding at the catalytic site. Reason: True, but entailed by iron ion binding (GO:0005506), kept on this gene from the same paper. Supporting Evidence: PMID:30403291 The phosphatase requires divalent metal cations for catalytic activity and contains iron naturally. |
| GO:0050821 protein stabilization | IDA PMID:30158517 MYC dephosphorylation by the PP1/PNUTS phosphatase complex r... | KEEP AS NON CORE | Summary: PP1/PNUTS dephosphorylates MYC and protects it from FBXW7-mediated degradation. Reason: PP1 dephosphorylation of MYC stabilises chromatin-bound MYC. PPP1CA does the catalytic work, but protein stabilization is one downstream consequence among many substrates. Supporting Evidence: PMID:30158517 PP1 dephosphorylates MYC and rescues it from SCFFBXW7-dependent degradation. PMID:30158517 Our work demonstrates that PP1/PNUTS stabilizes chromatin-bound MYC in proliferating cells. |
| GO:0060828 regulation of canonical Wnt signaling pathway | IC PMID:17318175 Protein phosphatase 1 regulates assembly and function of the... | KEEP AS NON CORE | Summary: PP1 dephosphorylates axin and positively regulates Wnt/beta-catenin signalling (abstract-only). Reason: IC from the finding that PP1 dephosphorylates axin, weakening the beta-catenin destruction complex. The study does not single out PP1-alpha among isoforms, but the role is credible for PP1 catalytic subunits. Non-core. Supporting Evidence: PMID:17318175 The data suggest that PP1 controls Wnt signaling through interaction with, and regulated dephosphorylation of, axin. |
| GO:0070062 extracellular exosome | HDA PMID:20458337 MHC class II-associated proteins in B-cell exosomes and pote... | MARK AS OVER ANNOTATED | Summary: Detected in B-cell exosome proteome (abstract-only). Reason: High-abundance cytosolic proteins are routinely captured in exosome proteomes; there is no evidence that PP1-alpha is selectively packaged or functions in exosomes. Supporting Evidence: PMID:20458337 identified 539 proteins, including known and not previously identified constituents |
| GO:0072357 PTW/PP1 phosphatase complex | IDA PMID:20516061 Identification and characterization of a novel human PP1 pho... | ACCEPT | Summary: PPP1CA in the PTW/PP1 (PNUTS-PP1) complex. Reason: PPP1CA is the catalytic subunit of the PNUTS-TOX4-WDR82-PP1 (PTW/PP1) complex, which controls RNAPII pause release, elongation rate and termination. Supporting Evidence: PMID:20516061 a stable multimeric complex composed of regulatory subunits PNUTS, Tox4, and Wdr82 and a PP1 catalytic subunit (denoted as the PTW/PP1 phosphatase complex) file:human/PPP1CA/PPP1CA-uniprot.txt Component of the PNUTS-PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC |
| GO:0072357 PTW/PP1 phosphatase complex | IDA PMID:31677974 Control of RNA Pol II Speed by PNUTS-PP1 and Spt5 Dephosphor... | ACCEPT | Summary: PPP1CA in the PTW/PP1 (PNUTS-PP1) complex. Reason: PPP1CA is the catalytic subunit of the PNUTS-TOX4-WDR82-PP1 (PTW/PP1) complex, which controls RNAPII pause release, elongation rate and termination. Supporting Evidence: PMID:31677974 We report that PNUTS-PP1 phosphatase is a negative regulator of RNA polymerase II (Pol II) elongation rate. file:human/PPP1CA/PPP1CA-uniprot.txt Component of the PNUTS-PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC |
| GO:0072357 PTW/PP1 phosphatase complex | IDA PMID:33264625 WDR82/PNUTS-PP1 Prevents Transcription-Replication Conflicts... | ACCEPT | Summary: PPP1CA in the PTW/PP1 (PNUTS-PP1) complex. Reason: PPP1CA is the catalytic subunit of the PNUTS-TOX4-WDR82-PP1 (PTW/PP1) complex, which controls RNAPII pause release, elongation rate and termination. Supporting Evidence: PMID:33264625 the RNA polymerase II (RNAPII) C-terminal domain (CTD) phosphatase protein phosphatase 1 (PP1) nuclear targeting subunit (PNUTS)-PP1 inhibits replication stress file:human/PPP1CA/PPP1CA-uniprot.txt Component of the PNUTS-PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC |
| GO:0072357 PTW/PP1 phosphatase complex | IDA PMID:39603239 The PNUTS phosphatase complex controls transcription pause r... | ACCEPT | Summary: PPP1CA in the PTW/PP1 (PNUTS-PP1) complex. Reason: PPP1CA is the catalytic subunit of the PNUTS-TOX4-WDR82-PP1 (PTW/PP1) complex, which controls RNAPII pause release, elongation rate and termination. Supporting Evidence: PMID:39603239 Here, we discover that the mouse PNUTS-PP1 phosphatase complex plays an essential role in controlling transcription pause release file:human/PPP1CA/PPP1CA-uniprot.txt Component of the PNUTS-PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC |
| GO:0072357 PTW/PP1 phosphatase complex | IDA PMID:39603240 The phosphatase PP1 sustains global transcription by promoti... | ACCEPT | Summary: PPP1CA in the PTW/PP1 (PNUTS-PP1) complex. Reason: PPP1CA is the catalytic subunit of the PNUTS-TOX4-WDR82-PP1 (PTW/PP1) complex, which controls RNAPII pause release, elongation rate and termination. Supporting Evidence: PMID:39603240 Here, we reveal an unexpected role of PP1, within the phosphatase 1 nuclear targeting subunit (PNUTS)-PP1 complex, in sustaining global transcriptional activation in human cells file:human/PPP1CA/PPP1CA-uniprot.txt Component of the PNUTS-PP1 phosphatase complex, composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC |
| GO:0098609 cell-cell adhesion | IEA GO_REF:0000108 | MARK AS OVER ANNOTATED | Summary: Cell-cell adhesion inferred electronically from cadherin binding involved in cell-cell adhesion. Reason: Derived from the proximity-proteomics cadherin-binding row, itself over-annotated. PP1-alpha does not perform adhesion. Supporting Evidence: PMID:25468996 We used proximity biotinylation and quantitative proteomics to identify 561 proteins in the vicinity of the cytoplasmic tail of E-cadherin. |
| GO:0098641 cadherin binding involved in cell-cell adhesion | IDA PMID:25468996 E-cadherin interactome complexity and robustness resolved by... | MARK AS OVER ANNOTATED | Summary: PPP1CA identified in the E-cadherin proximity interactome (BioID). Reason: Proximity proteomics shows PPP1CA near E-cadherin complexes but does not show that PP1-alpha binds cadherin to mediate adhesion. The term asserts adhesion-mediating activity that the catalytic subunit does not have. Supporting Evidence: PMID:25468996 We used proximity biotinylation and quantitative proteomics to identify 561 proteins in the vicinity of the cytoplasmic tail of E-cadherin. |
| GO:0098793 presynapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Neuronal/synaptic location transferred from rodent orthologs. Reason: PP1 catalytic subunits are targeted to synapses (dendritic spines, PSD) by neurabin/spinophilin (PPP1R9A/B) and act in synaptic plasticity; transferred from rodent orthologs. A tissue-specific holoenzyme location, non-core. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Involved in regulation of ionic conductances and long-term synaptic plasticity. file:human/PPP1CA/PPP1CA-uniprot.txt Interacts with PPP1R9A and PPP1R9B. |
| GO:0098794 postsynapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Neuronal/synaptic location transferred from rodent orthologs. Reason: PP1 catalytic subunits are targeted to synapses (dendritic spines, PSD) by neurabin/spinophilin (PPP1R9A/B) and act in synaptic plasticity; transferred from rodent orthologs. A tissue-specific holoenzyme location, non-core. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Involved in regulation of ionic conductances and long-term synaptic plasticity. file:human/PPP1CA/PPP1CA-uniprot.txt Interacts with PPP1R9A and PPP1R9B. |
| GO:0098978 glutamatergic synapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Neuronal/synaptic location transferred from rodent orthologs. Reason: PP1 catalytic subunits are targeted to synapses (dendritic spines, PSD) by neurabin/spinophilin (PPP1R9A/B) and act in synaptic plasticity; transferred from rodent orthologs. A tissue-specific holoenzyme location, non-core. Supporting Evidence: file:human/PPP1CA/PPP1CA-uniprot.txt Involved in regulation of ionic conductances and long-term synaptic plasticity. file:human/PPP1CA/PPP1CA-uniprot.txt Interacts with PPP1R9A and PPP1R9B. |
| GO:0180007 RNA polymerase II CTD heptapeptide repeat S5 phosphatase activity | IDA PMID:33264625 WDR82/PNUTS-PP1 Prevents Transcription-Replication Conflicts... | ACCEPT | Summary: PNUTS-PP1 dephosphorylates RNAPII CTD Ser5 (abstract-only paper). Reason: UniProt (curated from this paper) records PNUTS-PP1 dephosphorylation of POLR2A CTD Ser5, promoting RNAPII turnover on chromatin during replication stress. A specific substrate-defined child of GO:0004722, exercised in the PNUTS holoenzyme. Supporting Evidence: PMID:33264625 WDR82 also promotes RNAPII-CTD dephosphorylation and suppresses replication stress file:human/PPP1CA/PPP1CA-uniprot.txt PNUTS-PP1 complex is also involved in the response to replication stress by mediating dephosphorylation of POLR2A at 'Ser-5' of the CTD |
| GO:2000806 positive regulation of termination of RNA polymerase II transcription, poly(A)-coupled | IDA PMID:31677974 Control of RNA Pol II Speed by PNUTS-PP1 and Spt5 Dephosphor... | ACCEPT | Summary: PNUTS-PP1 promotes poly(A)-coupled termination. Reason: PNUTS-PP1 dephosphorylates SPT5 downstream of poly(A) sites, slowing RNAPII so the XRN2 torpedo can catch it (the "sitting duck" mechanism). Supporting Evidence: PMID:31677974 We report that PNUTS-PP1 phosphatase is a negative regulator of RNA polymerase II (Pol II) elongation rate. file:human/PPP1CA/PPP1CA-uniprot.txt The PNUTS-PP1 complex also regulates transcription termination by mediating dephosphorylation of SUPT5H in termination zones downstream of poly(A) sites |
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Download this section (compressed HTML)Q: Which PP1 holoenzymes depend specifically on the alpha isoform rather than PP1-beta or PP1-gamma, given >90% identity and largely shared regulatory subunits? Many process annotations (circadian, Wnt, photoperiod entrainment) rest on pan-PP1 inhibitors and may not be isoform-specific.
Q: Should GO provide a term for RNA polymerase II promoter-proximal pause release, so that PNUTS-PP1 annotations need not use promoter clearance?
Experiment: Isoform-selective degron knock-in (PPP1CA vs PPP1CB/PPP1CC) with phosphoproteomics to define alpha-specific substrates and test which holoenzyme functions (PNUTS-PP1, SMP, GADD34-PP1) require PP1-alpha in vivo.
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