HNRNPC (heterogeneous nuclear ribonucleoprotein C1/C2) is an abundant nuclear RNA-binding protein with a single RRM that assembles as a (C1)3C2 heterotetramer. The tetramer binds uridine-rich stretches of nascent RNA polymerase II transcripts cooperatively (about 230-240 nucleotides per tetramer) and nucleates the packaging of pre-mRNA into 40S hnRNP particles. By binding long unstructured RNA it acts as a molecular ruler that sorts transcripts longer than about 200-300 nucleotides to the mRNA export route rather than the snRNA route. HNRNPC regulates pre-mRNA splicing, notably by competing with U2AF65 at poly(U) tracts to suppress the inclusion of cryptic Alu-derived exons genome-wide, and its binding is enhanced at sites where N6-methyladenosine opens local RNA structure (m6A-switch). It also binds poly(U) elements in 3'-UTRs to influence mRNA stability. Beyond RNA, hnRNP C1/C2 can bind specific DNA elements: it provides sequence-specific DNA recognition to a beta-globin LCR remodelling complex and occupies vitamin D response elements in a cyclical, competitive manner with the VDR-RXR heterodimer; constitutive overexpression of this VDRE-binding activity causes a VDR-normal form of hereditary vitamin D-resistant rickets.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000398 mRNA splicing, via spliceosome | IC PMID:11991638 Purification and characterization of native spliceosomes sui... | MODIFY | Summary: Loss of m6A-dependent HNRNPC binding alters alternative splicing of target mRNAs. Reason: HNRNPC regulates splice-site choice (suppression of cryptic Alu exons by competition with U2AF65; m6A-switch-dependent alternative splicing) rather than performing the splicing reaction; regulation of alternative splicing is more precise. Proposed replacements: regulation of alternative mRNA splicing, via spliceosome Supporting Evidence: PMID:25719671 these m(6)A-switch-regulated HNRNPC-binding activities affect the abundance as well as alternative splicing of target mRNAs, demonstrating the regulatory role of m(6)A-switches on gene expression and RNA maturation. PMID:23374342 Quantitative iCLIP data show that the RNA-binding protein hnRNP C competes with the splicing factor U2AF65 at many genuine and cryptic splice sites. PMID:23374342 Loss of hnRNP C leads to formation of previously suppressed Alu exons, which severely disrupt transcript function. |
| GO:0000398 mRNA splicing, via spliceosome | IC PMID:9731529 Mass spectrometry and EST-database searching allows characte... | MODIFY | Summary: Loss of m6A-dependent HNRNPC binding alters alternative splicing of target mRNAs. Reason: HNRNPC regulates splice-site choice (suppression of cryptic Alu exons by competition with U2AF65; m6A-switch-dependent alternative splicing) rather than performing the splicing reaction; regulation of alternative splicing is more precise. Proposed replacements: regulation of alternative mRNA splicing, via spliceosome Supporting Evidence: PMID:25719671 these m(6)A-switch-regulated HNRNPC-binding activities affect the abundance as well as alternative splicing of target mRNAs, demonstrating the regulatory role of m(6)A-switches on gene expression and RNA maturation. PMID:23374342 Quantitative iCLIP data show that the RNA-binding protein hnRNP C competes with the splicing factor U2AF65 at many genuine and cryptic splice sites. PMID:23374342 Loss of hnRNP C leads to formation of previously suppressed Alu exons, which severely disrupt transcript function. |
| GO:0000398 mRNA splicing, via spliceosome | IMP PMID:25719671 N(6)-methyladenosine-dependent RNA structural switches regul... | MODIFY | Summary: Loss of m6A-dependent HNRNPC binding alters alternative splicing of target mRNAs. Reason: HNRNPC regulates splice-site choice (suppression of cryptic Alu exons by competition with U2AF65; m6A-switch-dependent alternative splicing) rather than performing the splicing reaction; regulation of alternative splicing is more precise. Proposed replacements: regulation of alternative mRNA splicing, via spliceosome Supporting Evidence: PMID:25719671 these m(6)A-switch-regulated HNRNPC-binding activities affect the abundance as well as alternative splicing of target mRNAs, demonstrating the regulatory role of m(6)A-switches on gene expression and RNA maturation. PMID:23374342 Quantitative iCLIP data show that the RNA-binding protein hnRNP C competes with the splicing factor U2AF65 at many genuine and cryptic splice sites. PMID:23374342 Loss of hnRNP C leads to formation of previously suppressed Alu exons, which severely disrupt transcript function. |
| GO:0000785 chromatin | HDA PMID:16217013 Heterogeneous nuclear ribonucleoprotein C1/C2, MeCP1, and SW... | KEEP AS NON CORE | Summary: hnRNP C1/C2 is the sequence-specific DNA-recognition subunit of the LARC remodelling complex at the beta-globin LCR. Reason: Biochemically supported (PMID:16217013); a specialised DNA-associated role distinct from its main RNA-packaging function. Supporting Evidence: PMID:16217013 Heterogeneous nuclear ribonucleoprotein C1/C2, previously known as a general RNA binding protein, provides a sequence-specific DNA recognition element for LARC, and the LARC DNA-recognition sequence is essential for the enhancement of transcription by HS2. PMID:16217013 LARC binds to the hypersensitive 2 (HS2)-Maf recognition element (MARE) DNA in a sequence-specific manner and remodels nucleosomes. |
| GO:0001649 osteoblast differentiation | HDA PMID:16210410 Differential expression profiling of membrane proteins by qu... | MARK AS OVER ANNOTATED | Summary: HNRNPC identified in a proteomic screen of osteoblast differentiation. Reason: High-throughput expression profiling does not show that HNRNPC is required for osteoblast differentiation. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). |
| GO:0003676 nucleic acid binding | IEA GO_REF:0000002 | MODIFY | Summary: Generic nucleic acid binding from InterPro (RRM). Reason: Correct but the principal activity is RNA binding (poly(U)-rich pre-mRNA); DNA binding is a secondary, context-specific activity. Proposed replacements: RNA binding Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). |
| GO:0003723 RNA binding | HDA PMID:22658674 Insights into RNA biology from an atlas of mammalian mRNA-bi... | ACCEPT | Summary: HNRNPC is a major nuclear RNA-binding protein that binds uridine-rich pre-mRNA regions. Reason: Extensively documented (pre-mRNA packaging, iCLIP/PAR-CLIP, 3'-UTR binding); core activity (PMID:8264621, PMID:23374342, PMID:25719671). Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:8264621 a single C-protein tetramer has an RNA site size of 230 to 240 nucleotides (nt) PMID:23374342 Quantitative iCLIP data show that the RNA-binding protein hnRNP C competes with the splicing factor U2AF65 at many genuine and cryptic splice sites. |
| GO:0003723 RNA binding | HDA PMID:22681889 The mRNA-bound proteome and its global occupancy profile on ... | ACCEPT | Summary: HNRNPC is a major nuclear RNA-binding protein that binds uridine-rich pre-mRNA regions. Reason: Extensively documented (pre-mRNA packaging, iCLIP/PAR-CLIP, 3'-UTR binding); core activity (PMID:8264621, PMID:23374342, PMID:25719671). Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:8264621 a single C-protein tetramer has an RNA site size of 230 to 240 nucleotides (nt) PMID:23374342 Quantitative iCLIP data show that the RNA-binding protein hnRNP C competes with the splicing factor U2AF65 at many genuine and cryptic splice sites. |
| GO:0003723 RNA binding | IBA GO_REF:0000033 | ACCEPT | Summary: HNRNPC is a major nuclear RNA-binding protein that binds uridine-rich pre-mRNA regions. Reason: Extensively documented (pre-mRNA packaging, iCLIP/PAR-CLIP, 3'-UTR binding); core activity (PMID:8264621, PMID:23374342, PMID:25719671). Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:8264621 a single C-protein tetramer has an RNA site size of 230 to 240 nucleotides (nt) PMID:23374342 Quantitative iCLIP data show that the RNA-binding protein hnRNP C competes with the splicing factor U2AF65 at many genuine and cryptic splice sites. |
| GO:0003723 RNA binding | IEA GO_REF:0000002 | ACCEPT | Summary: HNRNPC is a major nuclear RNA-binding protein that binds uridine-rich pre-mRNA regions. Reason: Extensively documented (pre-mRNA packaging, iCLIP/PAR-CLIP, 3'-UTR binding); core activity (PMID:8264621, PMID:23374342, PMID:25719671). Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:8264621 a single C-protein tetramer has an RNA site size of 230 to 240 nucleotides (nt) PMID:23374342 Quantitative iCLIP data show that the RNA-binding protein hnRNP C competes with the splicing factor U2AF65 at many genuine and cryptic splice sites. |
| GO:0003723 RNA binding | IPI PMID:18082603 Purification of human telomerase complexes identifies factor... | ACCEPT | Summary: HNRNPC is a major nuclear RNA-binding protein that binds uridine-rich pre-mRNA regions. Reason: Extensively documented (pre-mRNA packaging, iCLIP/PAR-CLIP, 3'-UTR binding); core activity (PMID:8264621, PMID:23374342, PMID:25719671). Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:8264621 a single C-protein tetramer has an RNA site size of 230 to 240 nucleotides (nt) PMID:23374342 Quantitative iCLIP data show that the RNA-binding protein hnRNP C competes with the splicing factor U2AF65 at many genuine and cryptic splice sites. |
| GO:0003723 RNA binding | NAS PMID:9731529 Mass spectrometry and EST-database searching allows characte... | ACCEPT | Summary: HNRNPC is a major nuclear RNA-binding protein that binds uridine-rich pre-mRNA regions. Reason: Extensively documented (pre-mRNA packaging, iCLIP/PAR-CLIP, 3'-UTR binding); core activity (PMID:8264621, PMID:23374342, PMID:25719671). Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:8264621 a single C-protein tetramer has an RNA site size of 230 to 240 nucleotides (nt) PMID:23374342 Quantitative iCLIP data show that the RNA-binding protein hnRNP C competes with the splicing factor U2AF65 at many genuine and cryptic splice sites. |
| GO:0003730 mRNA 3'-UTR binding | IDA PMID:16010978 Regulation of urokinase receptor mRNA stability by hnRNP C i... | ACCEPT | Summary: HNRNPC binds a U-rich element in the uPAR mRNA 3'-UTR. Reason: Direct binding demonstrated by EMSA, UV cross-linking and RNA immunoprecipitation (PMID:16010978). Supporting Evidence: PMID:16010978 The 40 kDa uPAR 3'UTR Bp was purified using poly (U) sepharose and identified as heterogeneous nuclear ribonucleoprotein C (hnRNPC). PMID:16010978 Direct in vivo interaction of hnRNPC with the uPAR mRNA 3'UTR was demonstrated by immunoprecipitation and combined RT PCR-Southern blotting assay. |
| GO:0005515 protein binding | IPI PMID:11546873 Role of the nonsense-mediated decay factor hUpf3 in the spli... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:11687588 Nuclear DNA helicase II/RNA helicase A binds to filamentous ... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:11687588 Nuclear DNA helicase II/RNA helicase A binds to filamentous ... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:15034300 Identification of toposome, a novel multisubunit complex con... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:15161933 Comprehensive proteomic analysis of interphase and mitotic 1... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:17289661 Molecular composition of IMP1 ribonucleoprotein granules. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:17500595 Huntingtin interacting proteins are genetic modifiers of neu... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:19447967 Shifted Transversal Design smart-pooling for high coverage i... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:19447967 Shifted Transversal Design smart-pooling for high coverage i... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:20467437 Direct interaction between hnRNP-M and CDC5L/PLRG1 proteins ... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:20618440 Proteomic and biochemical analysis of 14-3-3-binding protein... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:21516116 Next-generation sequencing to generate interactome datasets. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:21653829 Protein interactome reveals converging molecular pathways am... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:22365833 Dynamic protein-protein interaction wiring of the human spli... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:22365833 Dynamic protein-protein interaction wiring of the human spli... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:22365833 Dynamic protein-protein interaction wiring of the human spli... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:22446626 DBIRD complex integrates alternative mRNA splicing with RNA ... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:22720776 PHF6 interacts with the nucleosome remodeling and deacetylat... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:23602568 The protein interaction landscape of the human CMGC kinase g... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:24965446 Host factors that interact with the pestivirus N-terminal pr... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:24981860 Human-chromatin-related protein interactions identify a deme... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:25678563 Peptidylprolyl isomerase A governs TARDBP function and assem... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:35044719 Proteome-scale mapping of binding sites in the unstructured ... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:39251607 Systematic identification of post-transcriptional regulatory... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:39251607 Systematic identification of post-transcriptional regulatory... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:39251607 Systematic identification of post-transcriptional regulatory... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:39251607 Systematic identification of post-transcriptional regulatory... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:39251607 Systematic identification of post-transcriptional regulatory... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:39251607 Systematic identification of post-transcriptional regulatory... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:39251607 Systematic identification of post-transcriptional regulatory... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:39251607 Systematic identification of post-transcriptional regulatory... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005515 protein binding | IPI PMID:39251607 Systematic identification of post-transcriptional regulatory... | REMOVE | Summary: HNRNPC physically interacts with many proteins (other hnRNPs, DHX9, splicing factors, high-throughput interactors). Reason: Bare protein binding is uninformative; removal does not dispute the interactions. Functionally relevant partnerships (tetramer, hnRNP particle assembly) are captured by other terms. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. |
| GO:0005576 extracellular region | HDA PMID:27068509 Extracellular matrix remodelling in response to venous hyper... | MARK AS OVER ANNOTATED | Summary: HNRNPC detected in membrane, extracellular and exosome proteomes. Reason: High-throughput detection of an extremely abundant nuclear protein in these fractions likely reflects contamination or incidental cargo; no function there is known. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). |
| GO:0005634 nucleus | EXP PMID:37599448 Nucleo-cytoplasmic shuttling of 14-3-3 epsilon carrying hnRN... | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005634 nucleus | HDA PMID:21630459 Proteomic characterization of the human sperm nucleus. | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005634 nucleus | IBA GO_REF:0000033 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005634 nucleus | IDA PMID:11687588 Nuclear DNA helicase II/RNA helicase A binds to filamentous ... | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005634 nucleus | IDA PMID:22720776 PHF6 interacts with the nucleosome remodeling and deacetylat... | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005634 nucleus | IEA GO_REF:0000044 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | IDA GO_REF:0000052 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-4570493 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-72103 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9770119 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9770129 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9770131 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9770132 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9770141 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9770142 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9770145 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9770236 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9770847 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9794542 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9921507 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970141 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970179 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970189 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970190 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970191 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970193 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970282 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970294 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970318 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970320 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970428 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970429 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005654 nucleoplasm | TAS Reactome:R-HSA-9970431 | ACCEPT | Summary: HNRNPC is an abundant nuclear (nucleoplasmic) protein. Reason: Well-established nuclear localisation consistent with its pre-mRNA packaging role. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). PMID:22461616 the tetramer sorts the transcripts into two RNA categories, to be exported as either messenger RNA or uridine-rich small nuclear RNA (U snRNA) |
| GO:0005681 spliceosomal complex | IDA PMID:9731529 Mass spectrometry and EST-database searching allows characte... | KEEP AS NON CORE | Summary: HNRNPC co-purifies with spliceosomes, including C complex. Reason: Mass-spectrometry identification in purified spliceosomes (PMID:9731529, PMID:11991638); hnRNP C is an abundant pre-mRNA-associated protein rather than a core snRNP component. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Identified in the spliceosome C complex. PMID:11991638 These spliceosomes consist largely of C complex containing splicing intermediates. |
| GO:0005697 telomerase holoenzyme complex | IDA PMID:18082603 Purification of human telomerase complexes identifies factor... | KEEP AS NON CORE | Summary: HNRNPC associates with human telomerase RNPs. Reason: Co-purifies with telomerase and its RNA (PMID:18082603), but telomerase lacking hnRNP C remains fully functional. Supporting Evidence: PMID:18082603 telomerase RNPs lacking interaction with Sm proteins or hnRNP C remain fully functional for telomere elongation. |
| GO:0005829 cytosol | IDA PMID:16010978 Regulation of urokinase receptor mRNA stability by hnRNP C i... | KEEP AS NON CORE | Summary: HNRNPC detected in cytosolic fractions of lung epithelial cells. Reason: HNRNPC is predominantly nuclear; cytosolic detection (PMID:16010978) may reflect a minor pool relevant to mRNA stability. Supporting Evidence: PMID:16010978 The 40 kDa uPAR 3'UTR Bp was purified using poly (U) sepharose and identified as heterogeneous nuclear ribonucleoprotein C (hnRNPC). |
| GO:0006338 chromatin remodeling | HDA PMID:16217013 Heterogeneous nuclear ribonucleoprotein C1/C2, MeCP1, and SW... | KEEP AS NON CORE | Summary: hnRNP C1/C2 is the sequence-specific DNA-recognition subunit of the LARC remodelling complex at the beta-globin LCR. Reason: Biochemically supported (PMID:16217013); a specialised DNA-associated role distinct from its main RNA-packaging function. Supporting Evidence: PMID:16217013 Heterogeneous nuclear ribonucleoprotein C1/C2, previously known as a general RNA binding protein, provides a sequence-specific DNA recognition element for LARC, and the LARC DNA-recognition sequence is essential for the enhancement of transcription by HS2. PMID:16217013 LARC binds to the hypersensitive 2 (HS2)-Maf recognition element (MARE) DNA in a sequence-specific manner and remodels nucleosomes. |
| GO:0008266 poly(U) RNA binding | IDA PMID:16010978 Regulation of urokinase receptor mRNA stability by hnRNP C i... | ACCEPT | Summary: HNRNPC binds poly(U) tracts. Reason: HNRNPC was purified on poly(U) sepharose (PMID:16010978) and its binding preference for U-tracts underlies its competition with U2AF65 (PMID:23374342); this is the most informative MF. Supporting Evidence: PMID:16010978 The 40 kDa uPAR 3'UTR Bp was purified using poly (U) sepharose and identified as heterogeneous nuclear ribonucleoprotein C (hnRNPC). PMID:23374342 Quantitative iCLIP data show that the RNA-binding protein hnRNP C competes with the splicing factor U2AF65 at many genuine and cryptic splice sites. file:human/HNRNPC/HNRNPC-uniprot.txt Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules (PubMed:12509468, PubMed:16010978, PubMed:7567451, PubMed:8264621). |
| GO:0008380 RNA splicing | TAS PMID:3110598 Primary structure of human nuclear ribonucleoprotein particl... | KEEP AS NON CORE | Summary: HNRNPC is found in spliceosomal complexes and participates in pre-mRNA processing. Reason: Supported by spliceosome proteomics (PMID:9731529, PMID:11991638); its specific role is regulatory (splice-site choice) rather than core catalytic splicing. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Identified in the spliceosome C complex. PMID:23374342 Quantitative iCLIP data show that the RNA-binding protein hnRNP C competes with the splicing factor U2AF65 at many genuine and cryptic splice sites. |
| GO:0015629 actin cytoskeleton | IDA PMID:11687588 Nuclear DNA helicase II/RNA helicase A binds to filamentous ... | KEEP AS NON CORE | Summary: HNRNPC co-purifies with DHX9 and F-actin and with protein complexes. Reason: Biochemical co-fractionation (PMID:11687588, PMID:16217013) supports association with nuclear actin/protein complexes, but this is not a defining location. Supporting Evidence: PMID:11687588 NDH II and hnRNP C from the HeLa nuclear extract coeluted with F-actin on Sepharose 4B in an RNase-resistant manner, whereas hnRNP A1 was nearly completely removed from F-actin-associated hnRNP complexes following RNA digestion. PMID:16217013 Heterogeneous nuclear ribonucleoprotein C1/C2, previously known as a general RNA binding protein, provides a sequence-specific DNA recognition element for LARC, and the LARC DNA-recognition sequence is essential for the enhancement of transcription by HS2. |
| GO:0016020 membrane | HDA PMID:16210410 Differential expression profiling of membrane proteins by qu... | MARK AS OVER ANNOTATED | Summary: HNRNPC detected in membrane, extracellular and exosome proteomes. Reason: High-throughput detection of an extremely abundant nuclear protein in these fractions likely reflects contamination or incidental cargo; no function there is known. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). |
| GO:0031492 nucleosomal DNA binding | HDA PMID:16217013 Heterogeneous nuclear ribonucleoprotein C1/C2, MeCP1, and SW... | KEEP AS NON CORE | Summary: hnRNP C1/C2 is the sequence-specific DNA-recognition subunit of the LARC remodelling complex at the beta-globin LCR. Reason: Biochemically supported (PMID:16217013); a specialised DNA-associated role distinct from its main RNA-packaging function. Supporting Evidence: PMID:16217013 Heterogeneous nuclear ribonucleoprotein C1/C2, previously known as a general RNA binding protein, provides a sequence-specific DNA recognition element for LARC, and the LARC DNA-recognition sequence is essential for the enhancement of transcription by HS2. PMID:16217013 LARC binds to the hypersensitive 2 (HS2)-Maf recognition element (MARE) DNA in a sequence-specific manner and remodels nucleosomes. |
| GO:0032211 negative regulation of telomere maintenance via telomerase | IMP PMID:18082603 Purification of human telomerase complexes identifies factor... | MARK AS OVER ANNOTATED | Summary: Overexpression of HNRNPC induced telomere shortening. Reason: The effect was seen only on overexpression, while telomerase lacking hnRNP C association was fully functional (PMID:18082603); evidence for a physiological negative regulatory role is weak. Supporting Evidence: PMID:18082603 telomerase RNPs lacking interaction with Sm proteins or hnRNP C remain fully functional for telomere elongation. PMID:18082603 overexpression of either associated hnRNP protein (hnRNP C and hnRNP U) or either NTPase protein (NAT10 and GNL3L) induced telomere shortening. |
| GO:0032991 protein-containing complex | HDA PMID:16217013 Heterogeneous nuclear ribonucleoprotein C1/C2, MeCP1, and SW... | KEEP AS NON CORE | Summary: HNRNPC co-purifies with DHX9 and F-actin and with protein complexes. Reason: Biochemical co-fractionation (PMID:11687588, PMID:16217013) supports association with nuclear actin/protein complexes, but this is not a defining location. Supporting Evidence: PMID:11687588 NDH II and hnRNP C from the HeLa nuclear extract coeluted with F-actin on Sepharose 4B in an RNase-resistant manner, whereas hnRNP A1 was nearly completely removed from F-actin-associated hnRNP complexes following RNA digestion. PMID:16217013 Heterogeneous nuclear ribonucleoprotein C1/C2, previously known as a general RNA binding protein, provides a sequence-specific DNA recognition element for LARC, and the LARC DNA-recognition sequence is essential for the enhancement of transcription by HS2. |
| GO:0032991 protein-containing complex | IDA PMID:11687588 Nuclear DNA helicase II/RNA helicase A binds to filamentous ... | KEEP AS NON CORE | Summary: HNRNPC co-purifies with DHX9 and F-actin and with protein complexes. Reason: Biochemical co-fractionation (PMID:11687588, PMID:16217013) supports association with nuclear actin/protein complexes, but this is not a defining location. Supporting Evidence: PMID:11687588 NDH II and hnRNP C from the HeLa nuclear extract coeluted with F-actin on Sepharose 4B in an RNase-resistant manner, whereas hnRNP A1 was nearly completely removed from F-actin-associated hnRNP complexes following RNA digestion. PMID:16217013 Heterogeneous nuclear ribonucleoprotein C1/C2, previously known as a general RNA binding protein, provides a sequence-specific DNA recognition element for LARC, and the LARC DNA-recognition sequence is essential for the enhancement of transcription by HS2. |
| GO:0042802 identical protein binding | IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in... | KEEP AS NON CORE | Summary: HNRNPC self-associates; C1 and C2 form a (C1)3C2 tetramer. Reason: Tetramer formation is required for its RNA-ruler and packaging function, but identical protein binding itself is not informative. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. PMID:22461616 measures the length of the transcripts like a molecular ruler, by selectively binding to the unstructured RNA regions longer than 200 to 300 nucleotides. |
| GO:0042802 identical protein binding | IPI PMID:21516116 Next-generation sequencing to generate interactome datasets. | KEEP AS NON CORE | Summary: HNRNPC self-associates; C1 and C2 form a (C1)3C2 tetramer. Reason: Tetramer formation is required for its RNA-ruler and packaging function, but identical protein binding itself is not informative. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. PMID:22461616 measures the length of the transcripts like a molecular ruler, by selectively binding to the unstructured RNA regions longer than 200 to 300 nucleotides. |
| GO:0042802 identical protein binding | IPI PMID:22365833 Dynamic protein-protein interaction wiring of the human spli... | KEEP AS NON CORE | Summary: HNRNPC self-associates; C1 and C2 form a (C1)3C2 tetramer. Reason: Tetramer formation is required for its RNA-ruler and packaging function, but identical protein binding itself is not informative. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. PMID:22461616 measures the length of the transcripts like a molecular ruler, by selectively binding to the unstructured RNA regions longer than 200 to 300 nucleotides. |
| GO:0042802 identical protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: HNRNPC self-associates; C1 and C2 form a (C1)3C2 tetramer. Reason: Tetramer formation is required for its RNA-ruler and packaging function, but identical protein binding itself is not informative. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. PMID:22461616 measures the length of the transcripts like a molecular ruler, by selectively binding to the unstructured RNA regions longer than 200 to 300 nucleotides. |
| GO:0042802 identical protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: HNRNPC self-associates; C1 and C2 form a (C1)3C2 tetramer. Reason: Tetramer formation is required for its RNA-ruler and packaging function, but identical protein binding itself is not informative. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Tetramer composed of 3 copies of isoform C1 and 1 copy of isoform C2. PMID:22461616 measures the length of the transcripts like a molecular ruler, by selectively binding to the unstructured RNA regions longer than 200 to 300 nucleotides. |
| GO:0070034 telomerase RNA binding | IPI PMID:18082603 Purification of human telomerase complexes identifies factor... | KEEP AS NON CORE | Summary: HNRNPC associates with human telomerase RNPs. Reason: Co-purifies with telomerase and its RNA (PMID:18082603), but telomerase lacking hnRNP C remains fully functional. Supporting Evidence: PMID:18082603 telomerase RNPs lacking interaction with Sm proteins or hnRNP C remain fully functional for telomere elongation. |
| GO:0070062 extracellular exosome | HDA PMID:20458337 MHC class II-associated proteins in B-cell exosomes and pote... | MARK AS OVER ANNOTATED | Summary: HNRNPC detected in membrane, extracellular and exosome proteomes. Reason: High-throughput detection of an extremely abundant nuclear protein in these fractions likely reflects contamination or incidental cargo; no function there is known. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles (PubMed:8264621). |
| GO:0070935 3'-UTR-mediated mRNA stabilization | IMP PMID:16010978 Regulation of urokinase receptor mRNA stability by hnRNP C i... | KEEP AS NON CORE | Summary: HNRNPC stabilises uPAR mRNA through 3'-UTR binding. Reason: Supported for a specific transcript in lung epithelial cells (PMID:16010978); a transcript-specific consequence of its RNA binding, not the central function. Supporting Evidence: PMID:16010978 The 40 kDa uPAR 3'UTR Bp was purified using poly (U) sepharose and identified as heterogeneous nuclear ribonucleoprotein C (hnRNPC). file:human/HNRNPC/HNRNPC-uniprot.txt Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules (PubMed:12509468, PubMed:16010978, PubMed:7567451, PubMed:8264621). |
| GO:0071013 catalytic step 2 spliceosome | IDA PMID:11991638 Purification and characterization of native spliceosomes sui... | KEEP AS NON CORE | Summary: HNRNPC co-purifies with spliceosomes, including C complex. Reason: Mass-spectrometry identification in purified spliceosomes (PMID:9731529, PMID:11991638); hnRNP C is an abundant pre-mRNA-associated protein rather than a core snRNP component. Supporting Evidence: file:human/HNRNPC/HNRNPC-uniprot.txt Identified in the spliceosome C complex. PMID:11991638 These spliceosomes consist largely of C complex containing splicing intermediates. |
| GO:1990247 N6-methyladenosine-containing RNA reader activity | IDA PMID:25719671 N(6)-methyladenosine-dependent RNA structural switches regul... | KEEP AS NON CORE | Summary: HNRNPC binding is enhanced at m6A sites through an m6A-induced RNA structural switch. Reason: PMID:25719671 shows m6A increases HNRNPC binding indirectly by opening local RNA structure to expose U-tracts, rather than HNRNPC directly recognising the methylated base as YTH-domain readers do; the annotation is curator-supported but describes an indirect reader mechanism. Supporting Evidence: PMID:25719671 m(6)A alters the local structure in mRNA and long non-coding RNA (lncRNA) to facilitate binding of heterogeneous nuclear ribonucleoprotein C (HNRNPC) PMID:25719671 these m(6)A-switch-regulated HNRNPC-binding activities affect the abundance as well as alternative splicing of target mRNAs, demonstrating the regulatory role of m(6)A-switches on gene expression and RNA maturation. |
| GO:0000976 transcription cis-regulatory region binding | IDA PMID:17071612 Functional characterization of heterogeneous nuclear ribonuc... | NEW | Summary: hnRNP C1/C2 binds vitamin D response elements in chromatin, competing reciprocally with VDR-RXR. Reason: EMSA and ChIP show hnRNP C1/C2 occupies the VDRE of the CYP24 promoter in vitamin D-responsive human cells in a cyclical pattern reciprocal to VDR, and knockdown increases VDR transactivation (PMID:17071612, PMID:21123297). Non-core relative to its RNA functions; the VDR-normal HVDRR form results from overexpression of this activity. Supporting Evidence: PMID:17071612 cyclical movement of the VDR on and off the VDRE is legislated by competitive, reciprocal occupancy of the VDRE by hnRNP C1/C2. PMID:17071612 transient expression of an hnRNP C1/C2 small interfering RNA increased VDR transactivation by 39% (p < 0.005). PMID:17071612 Hormone resistance resulted from constitutive overexpression of heterogeneous nuclear ribonucleoprotein (hnRNP) that competed with a normally functioning VDR-retinoid X receptor (RXR) dimer for binding to the vitamin D response element (VDRE). PMID:21123297 This relationship is disrupted by elevated VDRE-BP, causing a form of hereditary vitamin D-resistant rickets (HVDRR). |
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Download this section (compressed HTML)Q: Is the VDRE occupancy by hnRNP C1/C2 a general feature of nuclear-receptor response elements in normal cells, or mainly relevant when HNRNPC is overexpressed?
Q: How does an RNA-binding protein achieve sequence-specific DNA recognition at the VDRE and the beta-globin LCR?
Experiment: Genome-wide ChIP-seq of HNRNPC with and without calcitriol, compared with VDR ChIP-seq, in cells with physiological HNRNPC levels, to test whether competitive VDRE occupancy is widespread and RNA-dependent.
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