COL1A2 encodes the proalpha2(I) collagen chain, a secreted precursor that associates with two proalpha1(I) chains to form the usual type I procollagen heterotrimer. Its C-terminal propeptide contributes to chain recognition and assembly in the endoplasmic reticulum. After secretion and propeptide removal, alpha2-containing collagen molecules assemble into extracellular fibrils that provide tensile support to bone, tendon, skin and other connective tissues. Mutations that disrupt chain folding, processing or assembly can cause osteogenesis imperfecta or Ehlers–Danlos phenotypes.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001501 skeletal system development | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: The skeletal-development inference is consistent with the structural role of type I collagen. Reason: Human COL1A2-mutant mesenchymal stem cells produce abnormal collagen; allele-targeted cells produce improved collagen and can form bone after xenotransplantation. This supports a tissue-level role of the collagen chain, not a separate developmental signaling activity. Current descendant records are retained, while the historical PAINT node placement was not independently reconstructed. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN002770820 UNRESOLVED Original node identifier preserved. Current exact descendant/target records were resolved separately, but the historical PAINT tree, alignment and IBD placement were not reconstructed; target-function confidence is not a claim to have inspected that placement. |
| GO:0001501 skeletal system development | IMP PMID:17955022 Gene targeting of mutant COL1A2 alleles in mesenchymal stem ... | KEEP AS NON CORE | Summary: Human COL1A2 mutation and allele-targeting experiments support a skeletal context. Reason: The original study used human OI-derived MSCs, collagen labeling/thermostability assays and bone formation in implanted matrices in immunodeficient mice. Bone formation occurred in several targeted clones, including some with the wild-type allele targeted; the work is not a demonstration that alpha2 alone instructs osteoblast differentiation. Retain the positive skeletal role outside the molecular core. Supporting Evidence: PMID:17955022 one targeted at the mutant allele and two targeted at the WT allele |
| GO:0001501 skeletal system development | IMP PMID:18375391 Defective C-propeptides of the proalpha2(I) chain of type I ... | KEEP AS NON CORE | Summary: Disease-linked alpha2 C-propeptide defects connect assembly to skeletal disease. Reason: The actual source tests alpha2 C-propeptide-dependent chain association and trimer incorporation and relates patient variants to osteogenesis imperfecta. Intrinsic assembly work is real; skeletal development is a broader tissue context rather than a second autonomous molecular activity. Supporting Evidence: |
| GO:0001501 skeletal system development | IMP PMID:8841196 Reduced bone density and osteoporosis associated with a poly... | KEEP AS NON CORE | Summary: The skeletal role is retained, with the original citation link qualified. Reason: The available PMID:8841196 abstract explicitly studies a COL1A1 Sp1 polymorphism and bone density. Its full text was not independently recovered, so this is not a wrong-gene verdict or a claim that it experimentally tested alpha2. Independent human COL1A2 allele-targeting and assembly studies support the target skeletal context; the original source fields remain exact. |
| GO:0001568 blood vessel development | IMP PMID:17211858 Three arginine to cysteine substitutions in the pro-alpha (I... | UNDECIDED | Summary: The source-specific blood-vessel-development evidence remains unresolved. Reason: The available abstract explicitly reports alpha1(I) substitutions and arterial rupture. It does not resolve all alpha2 measurements in the full paper, which remains unavailable. Arterial disease is not automatically developmental participation, and the source is retained without a misattribution or absence claim. Supporting Evidence: |
| GO:0002020 protease binding | IPI PMID:19932771 MMP-12 catalytic domain recognizes and cleaves at multiple s... | KEEP AS NON CORE | Summary: The reported collagen–MMP12 interaction supports protease binding in a substrate context. Reason: GO:0002020 requires binding to a protease or peptidase, not inhibition or regulation of that enzyme. The genuine abstract describes recognition and cleavage of human skin collagen I, including alpha2 sites, by the MMP12 catalytic domain. Retain this positive IPI annotation as contextual substrate–enzyme binding; it does not make COL1A2 a protease regulator. The full original remains unavailable and exact isolated-chain binding boundaries are not independently resolved. Supporting Evidence: PMID:19932771 catalytic domain of MMP-12 alone binds and degrades collagens I and III. |
| GO:0005201 extracellular matrix structural constituent | IEA GO_REF:0000002 | MODIFY | Summary: Tensile matrix structure is more informative than the broad structural-constituent term. Reason: The preserved InterPro IPR000885 source identifies a fibrillar collagen C-terminal domain; target composition and matrix biology support the refinement. Type I collagen containing alpha2 forms fibrils that resist longitudinal stress. Use the established collagen tensile-strength term, without describing association studies or proteomic detection as a force assay. Proposed replacements: extracellular matrix structural constituent conferring tensile strength Supporting Evidence: file:human/COL1A2/COL1A2-uniprot.txt PMID:1916105 Collagen molecules are structural macro-molecules of the extracellular matrix |
| GO:0005201 extracellular matrix structural constituent | NAS PMID:8982144 Genetic analysis of structural elastic fiber and collagen ge... | MODIFY | Summary: Tensile matrix structure is more informative than the broad structural-constituent term. Reason: The original abstract treats COL1A2 as an ECM structural candidate but excludes linkage in the sampled scoliosis families; this disease-linkage result is not a refutation of matrix function. Type I collagen containing alpha2 forms fibrils that resist longitudinal stress. Use the established collagen tensile-strength term, without describing association studies or proteomic detection as a force assay. Proposed replacements: extracellular matrix structural constituent conferring tensile strength Supporting Evidence: file:human/COL1A2/COL1A2-uniprot.txt Forms the fibrils of tendon, ligaments and bones. |
| GO:0005515 protein binding | IPI PMID:18375391 Defective C-propeptides of the proalpha2(I) chain of type I ... | MODIFY | Summary: Alpha2 associates with alpha1 during type I procollagen assembly. Reason: The actual source tests human alpha2 C-propeptide-dependent association and incorporation with alpha1 chains into procollagen trimers. Collagen binding captures this specific partner class; neither cell-matrix adhesion nor collagen V binding describes the tested pair. This does not assert a free extracellular receptor activity or alpha2 homotrimer formation. Proposed replacements: collagen binding Supporting Evidence: PMID:18375391 Cultured cells synthesized proalpha2(I) chains that were slow to assemble with proalpha1(I) chains to form heterotrimers |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | MODIFY | Summary: The positive full-length SGTA interaction supports protein-folding chaperone binding. Reason: The positive screen pair is preserved at its source-specific assay scope: the literal records match the 313-aa SGTA O43765 and 1366-aa COL1A2 sequences, with no reported truncation. Independently, original PMID28104892 shows SGTA capturing hydrophobic tail-anchored clients and transferring them through targeting or quality-control modules. Current GO:0051087 covers binding to a chaperone that ensures folding or transport, so this evidence supports the partner-class refinement. SGTA does not insert or ubiquitinate the client by itself. The study did not test COL1A2 as a false-positive control, and its triage mechanism does not negate the separately recorded positive pair. Native processing, endogenous colocalization and a collagen-client pathway remain unestablished; none is being added as a process or core function. See the public source index followup2_4928 for exact assay records, sequence hashes, current definition and original assay locators. Proposed replacements: protein-folding chaperone binding Supporting Evidence: PMID:28104892 TA protein released from CaM is captured rapidly (in 2 sec) and completely by SGTA |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: The source-specific ubiquilin interaction is retained. Reason: The positive binary interaction is not removed because it is generic or because the native proteins may occupy different compartments. The recorded full-length partner sequence matches the official product and the positive record ROGID. Ubiquilin participation in proteostasis and ubiquitin-dependent cargo routing does not by itself establish a more specific tested partner class or a collagen regulatory mechanism. No enzymatic activity is transferred to COL1A2. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: The source-specific ubiquilin interaction is retained. Reason: The positive binary interaction is not removed because it is generic or because the native proteins may occupy different compartments. The tested UBQLN1-2 sequence is reconstructed as 561 aa by the official 417–444 deletion, and its ROGID matches the positive records. Ubiquilin participation in proteostasis and ubiquitin-dependent cargo routing does not by itself establish a more specific tested partner class or a collagen regulatory mechanism. No enzymatic activity is transferred to COL1A2. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:26848503 Mapping and Exploring the Collagen-I Proteostasis Network. | MODIFY | Summary: Tagged human alpha1 and alpha2 procollagens associate in the assembly system. Reason: The genuine full variant describes human constructs with a preprotrypsin signal sequence and N-propeptide HA/FLAG tags in HT-1080 cells, with reciprocal recovery of the chains. Refine to collagen binding. The separately selected main cache is limited, and validation of selected proteins in native Saos-2 cells is not assigned automatically to this pair. Proposed replacements: collagen binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:26871637 Widespread Expansion of Protein Interaction Capabilities by ... | MODIFY | Summary: The positive full-length SGTA interaction supports protein-folding chaperone binding. Reason: The positive screen pair is preserved at its source-specific assay scope: the literal records match the 313-aa SGTA O43765 and 1366-aa COL1A2 sequences, with no reported truncation. Independently, original PMID28104892 shows SGTA capturing hydrophobic tail-anchored clients and transferring them through targeting or quality-control modules. Current GO:0051087 covers binding to a chaperone that ensures folding or transport, so this evidence supports the partner-class refinement. SGTA does not insert or ubiquitinate the client by itself. The study did not test COL1A2 as a false-positive control, and its triage mechanism does not negate the separately recorded positive pair. Native processing, endogenous colocalization and a collagen-client pathway remain unestablished; none is being added as a process or core function. See the public source index followup2_4928 for exact assay records, sequence hashes, current definition and original assay locators. Proposed replacements: protein-folding chaperone binding |
| GO:0005515 protein binding | IPI PMID:26871637 Widespread Expansion of Protein Interaction Capabilities by ... | KEEP AS NON CORE | Summary: The positive KCNIP4 interaction is retained with the channel-regulator distinction. Reason: The exact 250-aa Q6PIL6 product is represented in the positive records. KCNIP4 modulates channels but is not itself the pore-forming channel; its class does not justify replacing this row with ion-channel binding. The binary association remains non-core without a native channel mechanism or an absence claim. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:26871637 Widespread Expansion of Protein Interaction Capabilities by ... | KEEP AS NON CORE | Summary: The positive SGTB interaction is retained without an unsupported specific refinement. Reason: The exact 304-aa Q96EQ0 product matches the positive record. Its curated function is regulation of HSC70/HSP70 ATPase activity as a co-chaperone, with similarity-based evidence. That role is not itself the client-binding folding or transport activity specified by GO:0051087. The available evidence does not independently resolve that more specific SGTB capability; this is a biological class-scope limit, not a rule excluding inferred functions. Retain the positive pair without transferring an unestablished client-handling activity from SGTA. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:26871637 Widespread Expansion of Protein Interaction Capabilities by ... | KEEP AS NON CORE | Summary: The source-specific ubiquilin interaction is retained. Reason: The positive binary interaction is not removed because it is generic or because the native proteins may occupy different compartments. The tested UBQLN1-2 sequence is reconstructed as 561 aa by the official 417–444 deletion, and its ROGID matches the positive records. Ubiquilin participation in proteostasis and ubiquitin-dependent cargo routing does not by itself establish a more specific tested partner class or a collagen regulatory mechanism. No enzymatic activity is transferred to COL1A2. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32095531 Broadly conserved roles of TMEM131 family proteins in intrac... | KEEP AS NON CORE | Summary: A collagen C-propeptide fragment binds the TMEM131 PapD-like domain. Reason: The actual screen isolated the last 165 residues of human COL1A2 with downstream untranslated sequence, and recloned C-propeptide binding was tested against worm, fly and human TMEM131-family domains. Human TMEM131 knockdown also affects collagen secretion. Retain the direct association without treating a cargo receptor/assembly-factor label as a demonstrated protease, folding enzyme or adaptor activity of COL1A2. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | MODIFY | Summary: The exact EIF3F interaction supports ubiquitin-specific protease binding. Reason: The positive HuRI pair matches the 357-aa human EIF3F sequence. Independently, original PMID21124883 Results/Figure3A tests GST-tagged full-length human EIF3F and its MPN domain in bacteria coexpressing a ubiquitin-fusion substrate, with GST and active/inactive protease controls. The murine mutant, probe and cellular Notch experiments are separate. Current GO:1990381 defines binding to a ubiquitin-specific protease and gives deubiquitinase binding as an exact synonym; it does not specify active-site contact, a substrate relationship or the mode in which the multifunctional partner is engaged. The positive binary assay and experimentally supported human enzyme class justify this refinement without assigning protease activity, collagen deubiquitination or a Notch mechanism to COL1A2. The normal cache remains abstract-only; the separately accessed original Methods/Results and exact pair/product locators are recorded in the public source index followup2_4928. Proposed replacements: ubiquitin-specific protease binding |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | MODIFY | Summary: The positive full-length SGTA interaction supports protein-folding chaperone binding. Reason: The positive screen pair is preserved at its source-specific assay scope: the literal records match the 313-aa SGTA O43765 and 1366-aa COL1A2 sequences, with no reported truncation. Independently, original PMID28104892 shows SGTA capturing hydrophobic tail-anchored clients and transferring them through targeting or quality-control modules. Current GO:0051087 covers binding to a chaperone that ensures folding or transport, so this evidence supports the partner-class refinement. SGTA does not insert or ubiquitinate the client by itself. The study did not test COL1A2 as a false-positive control, and its triage mechanism does not negate the separately recorded positive pair. Native processing, endogenous colocalization and a collagen-client pathway remain unestablished; none is being added as a process or core function. See the public source index followup2_4928 for exact assay records, sequence hashes, current definition and original assay locators. Proposed replacements: protein-folding chaperone binding |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | MODIFY | Summary: The positive MESD precursor interaction supports protein-folding chaperone binding. Reason: The positive human screen records match the 234-aa MESD Q14696 precursor, including its signal peptide; they do not establish the native processed binding species. Independently, PMID15014448 directly tests fly Boca-dependent receptor-module maturation and mouse Mesd rescue in Boca-depleted S2 cells, while the human LRP1 domain is a substrate rather than human MESD. These experiments and curated human MESD function support the conserved chaperone class. Current GO:0051087 identifies that partner class, so the source-specific positive association supports chaperone binding without claiming that MESD folds COL1A2 or that the 2004 experiment was a direct human MESD folding assay. Exact product/record, species and definition evidence is available in the public source index followup2_4928. Proposed replacements: protein-folding chaperone binding Supporting Evidence: PMID:15014448 mouse Mesd can substitute for Drosophila Boca to allow the maturation of LpR2 in S2 cells. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The positive KCNIP4 interaction is retained with the channel-regulator distinction. Reason: The exact 250-aa Q6PIL6 product is represented in the positive records. KCNIP4 modulates channels but is not itself the pore-forming channel; its class does not justify replacing this row with ion-channel binding. The binary association remains non-core without a native channel mechanism or an absence claim. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | MODIFY | Summary: The exact SMARCD1 interaction supports transcription coactivator binding. Reason: The positive HuRI records match canonical 515-aa SMARCD1 Q96GM5. Its curated experimental FUNCTION describes nuclear-receptor and BRG1-complex interactions supporting transactivation, establishing the coactivator partner class independently of the collagen screen. GO:0001223 inherits GO:0001221 (transcription coregulator binding) and GO:0008134 (transcription factor binding); all three definitions describe binding to the named partner class. The inherited assertion is transcription-factor binding, not transcription-factor or coactivator activity by COL1A2. No nuclear location or transcriptional process is added. The positive heterologous pair and verified partner class therefore support this refinement, while native encounter and a physiological COL1A2 transcriptional role remain unestablished. Exact records, canonical sequences and curated activity provenance are exposed in followup2_4928; full definitions and parent edges are in followup3_4928. The partner activity papers were not newly read in full. Proposed replacements: transcription coactivator binding Supporting Evidence: PMID:32296183 binary protein interactions |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The source-specific ubiquilin interaction is retained. Reason: The positive binary interaction is not removed because it is generic or because the native proteins may occupy different compartments. The recorded full-length partner sequence matches the official product and the positive record ROGID. Ubiquilin participation in proteostasis and ubiquitin-dependent cargo routing does not by itself establish a more specific tested partner class or a collagen regulatory mechanism. No enzymatic activity is transferred to COL1A2. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: The source-specific ubiquilin interaction is retained. Reason: The positive binary interaction is not removed because it is generic or because the native proteins may occupy different compartments. The recorded full-length partner sequence matches the official product and the positive record ROGID. Ubiquilin participation in proteostasis and ubiquitin-dependent cargo routing does not by itself establish a more specific tested partner class or a collagen regulatory mechanism. No enzymatic activity is transferred to COL1A2. Supporting Evidence: |
| GO:0005576 extracellular region | HDA PMID:27068509 Extracellular matrix remodelling in response to venous hyper... | MODIFY | Summary: The extracellular proteomic annotation is refined to the established matrix location. Reason: The original human vein study uses sequential ECM enrichment and proteomics. The exact target table was not independently recovered, so its target-specific detection and condition differences are not newly claimed. Human aortic and colon/liver target rows independently verify COL1A2 in ECM preparations and justify the more specific location while the original HDA source remains intact. Proposed replacements: extracellular matrix |
| GO:0005576 extracellular region | IDA PMID:18375391 Defective C-propeptides of the proalpha2(I) chain of type I ... | ACCEPT | Summary: Secreted procollagen is present outside cells during the assembly assay. Reason: The source measures extracellularly recovered procollagen produced by the tested constructs. This includes soluble precursor forms and is not restricted to already deposited mature matrix, so the broad extracellular-region scope is retained for this source. Supporting Evidence: |
| GO:0005576 extracellular region | IEA GO_REF:0000107 | ACCEPT | Summary: The orthology-based extracellular location is consistent with collagen secretion. Reason: The mouse alpha2 source and current same-term records are retained; human secretion and processed extracellular forms independently support the broad location. This source does not specify that every observed form is already incorporated into a matrix fibril. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-114577 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-114577 (Binding of GPVI:Fc Epsilon R1 gamma receptor complex with collagen) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-114577 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-114600 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-114600 (Fyn/Lyn-mediated phosphorylation of FcR1 gamma) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-114600 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-114670 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-114670 (GPIb-IX-V binds to vWF:Collagen complex) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-114670 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-114671 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-114671 (vWF binds to collagen) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-114671 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-139842 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-139842 (Binding of Syk tyrosine kinase) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-139842 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-1454757 | ACCEPT | Summary: The event retains extracellular precursor, released or cleaved collagen forms. Reason: Reactome:R-HSA-1454757 (Gelatin degradation by MMP1, 2, 3, 7, 8, 9, 12, 13) contains an authenticated nested P08123 entity. The modeled scope includes secretion, processing, degradation or newly expressed protein and is not confined to an intact deposited fibril. Retain extracellular region; no catalyst, signaling-effector or processing activity is assigned to COL1A2 from its occurrence in the event. Supporting Evidence: Reactome:R-HSA-1454757 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-1454822 | ACCEPT | Summary: The event retains extracellular precursor, released or cleaved collagen forms. Reason: Reactome:R-HSA-1454822 (Collagen type I degradation by MMP1,2,8,13, PRSS2) contains an authenticated nested P08123 entity. The modeled scope includes secretion, processing, degradation or newly expressed protein and is not confined to an intact deposited fibril. Retain extracellular region; no catalyst, signaling-effector or processing activity is assigned to COL1A2 from its occurrence in the event. Supporting Evidence: Reactome:R-HSA-1454822 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-1474266 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-1474266 (Formation of collagen fibrils) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-1474266 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2002428 | ACCEPT | Summary: The event retains extracellular precursor, released or cleaved collagen forms. Reason: Reactome:R-HSA-2002428 (Removal of fibrillar collagen N-propeptides) contains an authenticated nested P08123 entity. The modeled scope includes secretion, processing, degradation or newly expressed protein and is not confined to an intact deposited fibril. Retain extracellular region; no catalyst, signaling-effector or processing activity is assigned to COL1A2 from its occurrence in the event. Supporting Evidence: Reactome:R-HSA-2002428 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2002440 | ACCEPT | Summary: The event retains extracellular precursor, released or cleaved collagen forms. Reason: Reactome:R-HSA-2002440 (Removal of fibrillar collagen C-propeptides) contains an authenticated nested P08123 entity. The modeled scope includes secretion, processing, degradation or newly expressed protein and is not confined to an intact deposited fibril. Retain extracellular region; no catalyst, signaling-effector or processing activity is assigned to COL1A2 from its occurrence in the event. Supporting Evidence: Reactome:R-HSA-2002440 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2002466 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-2002466 (Formation of allysine by LOX) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2002466 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2089971 | ACCEPT | Summary: The event retains extracellular precursor, released or cleaved collagen forms. Reason: Reactome:R-HSA-2089971 (Secretion of collagens) contains an authenticated nested P08123 entity. The modeled scope includes secretion, processing, degradation or newly expressed protein and is not confined to an intact deposited fibril. Retain extracellular region; no catalyst, signaling-effector or processing activity is assigned to COL1A2 from its occurrence in the event. Supporting Evidence: Reactome:R-HSA-2089971 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-216045 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-216045 (Collagen type I binds integrin alpha11beta1) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-216045 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2213201 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-2213201 (Formation of collagen fibres) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2213201 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2213205 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-2213205 (Type XII and XIV collagens associate with type I and type II fibrils) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2213205 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2243926 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-2243926 (Formation of histidino-hydroxylysinonorleucine cross-links) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2243926 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2243931 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-2243931 (Formation of dehydro-lysinonorleucine cross-links) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2243931 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2250301 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-2250301 (Formation of lysyl-pyrrole cross-links) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2250301 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2327733 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-2327733 (FN1 binds Collagen types I-V, VII) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2327733 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2327738 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-2327738 (DDR1 binds collagen type I, II, III, IV, V, XI fibrils) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2327738 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2327909 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-2327909 (DCN binds collagen I, II, III, VI fibrils) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2327909 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2395223 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-2395223 (Formation of hydroxylysyl-pyridinoline cross-links) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2395223 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2395257 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-2395257 (Formation of dehydro-hydroxylysino-norleucine cross-links) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2395257 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2395302 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-2395302 (Formation of hydroxylysino-5-ketonorleucine cross-links) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2395302 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2395314 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-2395314 (Formation of lysino-5-ketonorleucine cross-links) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2395314 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2395322 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-2395322 (Formation of lysyl-pyridinoline cross-links) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2395322 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2395324 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-2395324 (Formation of hydroxylysyl-pyrrole cross-links) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2395324 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2395340 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-2395340 (Formation of hydroxyallysine by LOX) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2395340 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2396234 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-2396234 (Collagen type VII binds laminin-322 and collagen IV) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2396234 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2424243 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-2424243 (SPARC binds Collagen type I fibril, hydroxylapatite and Ca2+) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2424243 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2424252 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-2424252 (COMP binds collagen, fibronectin, aggrecan and matrilins) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2424252 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2465890 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-2465890 (DDR2 binds collagen type I, II, III, V, X fibrils) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2465890 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2466106 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-2466106 (BGN binds Collagen types I, VI, (IX)) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2466106 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2473596 | ACCEPT | Summary: The event retains extracellular precursor, released or cleaved collagen forms. Reason: Reactome:R-HSA-2473596 (Collagen type I degradation by MMP15) contains an authenticated nested P08123 entity. The modeled scope includes secretion, processing, degradation or newly expressed protein and is not confined to an intact deposited fibril. Retain extracellular region; no catalyst, signaling-effector or processing activity is assigned to COL1A2 from its occurrence in the event. Supporting Evidence: Reactome:R-HSA-2473596 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-429529 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-429529 (Thrombin binding to GP1b:IX:V) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-429529 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-430073 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-430073 (GPIb-IX-V binding to 14-3-3 zeta is reduced by shear stress) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-430073 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-430076 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-430076 (GP1b-IX-V binds 14-3-3-zeta) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-430076 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-430096 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-430096 (GP1b-IX-V binds filamin) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-430096 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-437118 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-437118 (GPVI stimulates PI3K beta, gamma) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-437118 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-443402 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-443402 (GP1b-IX-V:13-3-3-zeta complexes with p85 PI3K) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-443402 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-443418 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-443418 (GP1b signaling involves c-Src) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-443418 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-453183 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-453183 (p-Y348-SYK dissociates) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-453183 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-453200 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-453200 (SYK autophosphorylates) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-453200 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5696356 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-5696356 (OSCAR binds collagen and SP-D) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-5696356 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5696357 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-5696357 (LAIR2 binds collagen) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-5696357 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-6785895 | ACCEPT | Summary: The event retains extracellular precursor, released or cleaved collagen forms. Reason: Reactome:R-HSA-6785895 (Expression of IL4, IL13-upregulated extracellular proteins) contains an authenticated nested P08123 entity. The modeled scope includes secretion, processing, degradation or newly expressed protein and is not confined to an intact deposited fibril. Retain extracellular region; no catalyst, signaling-effector or processing activity is assigned to COL1A2 from its occurrence in the event. Supporting Evidence: Reactome:R-HSA-6785895 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-9822532 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-9822532 (ADAMTS13 cleaves VWF multimer) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-9822532 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-9822539 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-9822539 (VWF multimer binds to collagen type I) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-9822539 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-9822734 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-9822734 (Caplacizumab binds VWF) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-9822734 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-9823065 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-9823065 (GPIb:IX:V binds to VWF multimer:collagen) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-9823065 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-9823593 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-9823593 (VWF variant does not bind to collagen type I ) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-9823593 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-9823706 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-9823706 (VWF variant does not bind GPIb:IX:V) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-9823706 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-9824402 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-9824402 (ADAMTS13 variant does not cleave VWF multimer) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-9824402 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-9844241 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-9844241 (ADAMTS13 cleaves VWF variant multimer) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-9844241 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-9844251 | MODIFY | Summary: The modeled collagen-I fibril supports the more specific ECM location. Reason: Reactome:R-HSA-9844251 (GP1BA variant binds to VWF multimer:collagen) reaches P08123 through an explicitly extracellular collagen-I fibril/assembly entity. Refine this source-specific location to extracellular matrix. Some enclosing receptor complexes are assigned to plasma membrane, but that does not move the collagen subunit into the membrane or transfer the receptor/enzyme activity to it. The original event and qualifier remain unchanged. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-9844251 |
| GO:0005581 collagen trimer | IEA GO_REF:0000107 | MODIFY | Summary: The generic collagen trimer is specifically a type I collagen trimer. Reason: The official composition is two alpha1(I) chains and one alpha2(I) chain, corroborated by direct assembly experiments. Refine the broad inherited trimer term; no alpha2 homotrimer or all-collagen-subtype equivalence is implied. Proposed replacements: collagen type I trimer |
| GO:0005584 collagen type I trimer | IBA GO_REF:0000033 | ACCEPT | Summary: COL1A2 contributes the alpha2 chain of the type I collagen heterotrimer. Reason: Current mouse/rat/target source premises are preserved; target self-evidence is legitimate grounding, not circularity. Independent assembly and official product evidence support this precise complex membership. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN002770820 UNRESOLVED Original node identifier preserved. Current exact descendant/target records were resolved separately, but the historical PAINT tree, alignment and IBD placement were not reconstructed; target-function confidence is not a claim to have inspected that placement. |
| GO:0005584 collagen type I trimer | IDA PMID:18375391 Defective C-propeptides of the proalpha2(I) chain of type I ... | ACCEPT | Summary: COL1A2 contributes the alpha2 chain of the type I collagen heterotrimer. Reason: The alpha2 C-propeptide incorporation experiments directly address assembly. Independent assembly and official product evidence support this precise complex membership. |
| GO:0005584 collagen type I trimer | IDA PMID:19932771 MMP-12 catalytic domain recognizes and cleaves at multiple s... | ACCEPT | Summary: COL1A2 contributes the alpha2 chain of the type I collagen heterotrimer. Reason: The MMP12 study uses type I collagen substrate; its abstract does not define all isolated-chain preparation boundaries. Independent assembly and official product evidence support this precise complex membership. |
| GO:0005584 collagen type I trimer | IEA GO_REF:0000107 | ACCEPT | Summary: COL1A2 contributes the alpha2 chain of the type I collagen heterotrimer. Reason: The exact mouse orthology source is preserved. Independent assembly and official product evidence support this precise complex membership. |
| GO:0005584 collagen type I trimer | IMP PMID:17955022 Gene targeting of mutant COL1A2 alleles in mesenchymal stem ... | ACCEPT | Summary: COL1A2 contributes the alpha2 chain of the type I collagen heterotrimer. Reason: Human OI MSC labeling and thermostability experiments distinguish alpha2-containing type I collagen. Independent assembly and official product evidence support this precise complex membership. |
| GO:0005584 collagen type I trimer | IPI PMID:26848503 Mapping and Exploring the Collagen-I Proteostasis Network. | ACCEPT | Summary: COL1A2 contributes the alpha2 chain of the type I collagen heterotrimer. Reason: The genuine full tagged-human-chain association study supports complex membership; selected main text remains limited. Independent assembly and official product evidence support this precise complex membership. |
| GO:0005584 collagen type I trimer | TAS PMID:6267597 Cloning a cDNA for the pro-alpha 2 chain of human type I col... | ACCEPT | Summary: COL1A2 contributes the alpha2 chain of the type I collagen heterotrimer. Reason: The original human fibroblast cDNA identifies the alpha2 type I chain; it is not itself a new stoichiometric measurement. Independent assembly and official product evidence support this precise complex membership. |
| GO:0005783 endoplasmic reticulum | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: ER localization is a biosynthetic compartment for procollagen. Reason: The curated immunofluorescence source is retained and is consistent with signal-directed entry and procollagen assembly in the ER. The exact original image was not independently retrieved, so no new image-specific claim is made. This is not an ER-resident mature structural protein. |
| GO:0005788 endoplasmic reticulum lumen | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: The current ARBA prediction correctly includes the ER lumen during biosynthesis. Reason: Three current rule branches match the authentic target: IPR050149 plus PTHR24023:SF1082 and Haplorrhini; IPR000885 plus Catarrhini; and exact FunFam 2.60.120.1000:FF:000001 plus Haplorrhini. Signal-directed precursor entry and assembly support the location, which remains non-core rather than permanent residence. |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-1650808 | KEEP AS NON CORE | Summary: The modeled alpha2 precursor occupies the ER lumen during synthesis and assembly. Reason: Reactome:R-HSA-1650808 (Prolyl 4-hydroxylase converts collagen prolines to 4-hydroxyprolines) explicitly reaches the P08123 precursor in the ER lumen. Preserve the biosynthetic location. The collagen is a substrate of hydroxylases and chaperones and an assembling structural chain; its presence does not transfer their catalytic functions or the transcription factors' activities to COL1A2. Supporting Evidence: Reactome:R-HSA-1650808 |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-2002460 | KEEP AS NON CORE | Summary: The modeled alpha2 precursor occupies the ER lumen during synthesis and assembly. Reason: Reactome:R-HSA-2002460 (P4HB binds Collagen chains) explicitly reaches the P08123 precursor in the ER lumen. Preserve the biosynthetic location. The collagen is a substrate of hydroxylases and chaperones and an assembling structural chain; its presence does not transfer their catalytic functions or the transcription factors' activities to COL1A2. Supporting Evidence: Reactome:R-HSA-2002460 |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-2022073 | KEEP AS NON CORE | Summary: The modeled alpha2 precursor occupies the ER lumen during synthesis and assembly. Reason: Reactome:R-HSA-2022073 (Procollagen triple helix formation) explicitly reaches the P08123 precursor in the ER lumen. Preserve the biosynthetic location. The collagen is a substrate of hydroxylases and chaperones and an assembling structural chain; its presence does not transfer their catalytic functions or the transcription factors' activities to COL1A2. Supporting Evidence: Reactome:R-HSA-2022073 |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-2089971 | KEEP AS NON CORE | Summary: The modeled alpha2 precursor occupies the ER lumen during synthesis and assembly. Reason: Reactome:R-HSA-2089971 (Secretion of collagens) explicitly reaches the P08123 precursor in the ER lumen. Preserve the biosynthetic location. The collagen is a substrate of hydroxylases and chaperones and an assembling structural chain; its presence does not transfer their catalytic functions or the transcription factors' activities to COL1A2. Supporting Evidence: Reactome:R-HSA-2089971 |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-8944214 | KEEP AS NON CORE | Summary: The modeled alpha2 precursor occupies the ER lumen during synthesis and assembly. Reason: Reactome:R-HSA-8944214 (Association of procollagen type I) explicitly reaches the P08123 precursor in the ER lumen. Preserve the biosynthetic location. The collagen is a substrate of hydroxylases and chaperones and an assembling structural chain; its presence does not transfer their catalytic functions or the transcription factors' activities to COL1A2. Supporting Evidence: Reactome:R-HSA-8944214 |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-9733216 | KEEP AS NON CORE | Summary: The modeled alpha2 precursor occupies the ER lumen during synthesis and assembly. Reason: Reactome:R-HSA-9733216 (COL1A2 gene expression is stimulated by p-2S-SMAD3:p-2S-SMAD3:SMAD4) explicitly reaches the P08123 precursor in the ER lumen. Preserve the biosynthetic location. The collagen is a substrate of hydroxylases and chaperones and an assembling structural chain; its presence does not transfer their catalytic functions or the transcription factors' activities to COL1A2. Supporting Evidence: Reactome:R-HSA-9733216 |
| GO:0007179 transforming growth factor beta receptor signaling pathway | IDA PMID:17217948 Inhibition of RhoA/Rho-kinase pathway suppresses the express... | UNDECIDED | Summary: The signaling-process attribution is not resolved by the available promoter-response evidence. Reason: The genuine abstract reports RhoA/ROCK-dependent TGF-beta2 induction of COL1A2 transcripts and promoter reporters in human ARPE-19 cells. Those are positive upstream regulation observations, not an assay demonstrating that the COL1A2 protein relays the signal. The full source was not recovered, so the prior categorical REMOVE is replaced by a source-scoped undecided judgment rather than an assertion of absence. Supporting Evidence: |
| GO:0007266 Rho protein signal transduction | IDA PMID:17217948 Inhibition of RhoA/Rho-kinase pathway suppresses the express... | UNDECIDED | Summary: The signaling-process attribution is not resolved by the available promoter-response evidence. Reason: The genuine abstract reports RhoA/ROCK-dependent TGF-beta2 induction of COL1A2 transcripts and promoter reporters in human ARPE-19 cells. Those are positive upstream regulation observations, not an assay demonstrating that the COL1A2 protein relays the signal. The full source was not recovered, so the prior categorical REMOVE is replaced by a source-scoped undecided judgment rather than an assertion of absence. Supporting Evidence: |
| GO:0008217 regulation of blood pressure | IMP PMID:17334644 Association of gene polymorphisms with blood pressure and th... | MARK AS OVER ANNOTATED | Summary: The original genotype–blood-pressure association does not establish COL1A2 protein participation in blood-pressure regulation. Reason: The authentic original PMID:17334644, recovered in an official Japanese grant-repository PDF, was inspected beyond its abstract. Table VIII includes 854 untreated men: SS versus SL+LL groups have systolic blood pressure 123.1 versus 120.5 mmHg (nominal P=0.0460) and diastolic pressure 76.8 versus 74.9 mmHg (P=0.0178). Those positive associations are retained. Male hypertension prevalence and female blood-pressure associations were not significant. The paper tests genotypes and clinical measurements; its Discussion leaves effects on transcription/protein structure/function unresolved and acknowledges possible linked variants and false positives. This source therefore does not establish the annotated protein-performed regulatory process. The assessment does not deny a vascular structural contribution by collagen or require a catalytic mechanism. The selected cache remains abstract-only; the external original is separately identified by URL, PDF hash and journal pages 675–683. Supporting Evidence: |
| GO:0030020 extracellular matrix structural constituent conferring tensile strength | HDA PMID:28344315 Proteomic characterization of human multiple myeloma bone ma... | ACCEPT | Summary: The tensile structural function is consistent with the target’s fibrillar collagen role. Reason: Original S2/S3 workbooks identify COL1A2/P08123; the summary and detailed MGUS presentations differ and are both retained without inventing a uniform condition effect. These proteomic/classification sources detect or classify matrix components; they are not direct tensile-force measurements. Independent type I collagen composition and fibril evidence supports the molecular function and the official term comment permits ECM collagen proteins. |
| GO:0030020 extracellular matrix structural constituent conferring tensile strength | IBA GO_REF:0000033 | ACCEPT | Summary: The tensile-strength IBA is retained as the core structural activity. Reason: The broad ancestral collagen assertion has authentic current descendant premises; no historical PAINT tree/IBD placement was independently recovered. Neither the distinct collagen subtype nor the number of donors is a biological refutation. The target itself forms type I collagen matrix fibrils, supporting the inherited structural activity. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN001166351 UNRESOLVED Original node identifier preserved. Current exact descendant/target records were resolved separately, but the historical PAINT tree, alignment and IBD placement were not reconstructed; target-function confidence is not a claim to have inspected that placement. Supporting Evidence: file:human/COL1A2/COL1A2-uniprot.txt Forms the fibrils of tendon, ligaments and bones. |
| GO:0030020 extracellular matrix structural constituent conferring tensile strength | RCA PMID:20551380 Proteomics characterization of extracellular space component... | ACCEPT | Summary: The tensile structural function is consistent with the target’s fibrillar collagen role. Reason: Original Table II identifies CO1A2_HUMAN in human aortic guanidine extracts (12 unique peptides, 15 unique spectra, 70 total spectra). These proteomic/classification sources detect or classify matrix components; they are not direct tensile-force measurements. Independent type I collagen composition and fibril evidence supports the molecular function and the official term comment permits ECM collagen proteins. |
| GO:0030020 extracellular matrix structural constituent conferring tensile strength | RCA PMID:25037231 Extracellular matrix signatures of human primary metastatic ... | ACCEPT | Summary: The tensile structural function is consistent with the target’s fibrillar collagen role. Reason: Both supplemental sheets row97 identify the same P08123/legacy-accession group across human colon/liver samples; they are duplicate presentations, not independent experiments. These proteomic/classification sources detect or classify matrix components; they are not direct tensile-force measurements. Independent type I collagen composition and fibril evidence supports the molecular function and the official term comment permits ECM collagen proteins. |
| GO:0030020 extracellular matrix structural constituent conferring tensile strength | RCA PMID:27559042 Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin... | ACCEPT | Summary: The tensile structural function is consistent with the target’s fibrillar collagen role. Reason: The exact target-level supplement remains uninspected; the selected source scope and that access limit are retained. These proteomic/classification sources detect or classify matrix components; they are not direct tensile-force measurements. Independent type I collagen composition and fibril evidence supports the molecular function and the official term comment permits ECM collagen proteins. |
| GO:0030020 extracellular matrix structural constituent conferring tensile strength | RCA PMID:28327460 Comprehensive proteomic characterization of stem cell-derive... | ACCEPT | Summary: The tensile structural function is consistent with the target’s fibrillar collagen role. Reason: The exact target-level supplement remains uninspected; the selected source scope and that access limit are retained. These proteomic/classification sources detect or classify matrix components; they are not direct tensile-force measurements. Independent type I collagen composition and fibril evidence supports the molecular function and the official term comment permits ECM collagen proteins. |
| GO:0030020 extracellular matrix structural constituent conferring tensile strength | RCA PMID:28675934 Characterization of the Extracellular Matrix of Normal and D... | ACCEPT | Summary: The tensile structural function is consistent with the target’s fibrillar collagen role. Reason: The exact target-level supplement remains uninspected; the selected source scope and that access limit are retained. These proteomic/classification sources detect or classify matrix components; they are not direct tensile-force measurements. Independent type I collagen composition and fibril evidence supports the molecular function and the official term comment permits ECM collagen proteins. |
| GO:0030199 collagen fibril organization | IBA GO_REF:0000033 | ACCEPT | Summary: Alpha2-containing type I collagen contributes structure to collagen fibril organization. Reason: The assembling collagen chain performs structural work rather than merely being consumed by an external processing step. Current experimental descendant and target records support the inherited process; the historical PAINT placement remains a separately unresolved provenance question, not a basis for rejection. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN009074843 UNRESOLVED Original node identifier preserved. Current exact descendant/target records were resolved separately, but the historical PAINT tree, alignment and IBD placement were not reconstructed; target-function confidence is not a claim to have inspected that placement. |
| GO:0030199 collagen fibril organization | IEA GO_REF:0000117 | ACCEPT | Summary: The collagen-fibril-organization prediction is biologically supported. Reason: The current ARBA branch matches exact FunFam 2.60.120.1000:FF:000001 and Primates. Alpha2 contributes an assembling structural chain to type I collagen, with C-propeptide-mediated heterotrimer formation upstream of fibril organization. This is not transfer of a processing protease activity. |
| GO:0030199 collagen fibril organization | IMP PMID:17211858 Three arginine to cysteine substitutions in the pro-alpha (I... | ACCEPT | Summary: Fibril organization is retained with the original citation’s chain limitation. Reason: The available PMID:17211858 abstract reports alpha1 mutations and abnormal dermal fibrils; its full alpha2-specific experimental scope remains unverified. Independent alpha2 assembly and type I collagen evidence supports the target process. Do not describe the cited abstract as an alpha2-mutant fibril-imaging experiment. |
| GO:0030199 collagen fibril organization | IMP PMID:18375391 Defective C-propeptides of the proalpha2(I) chain of type I ... | ACCEPT | Summary: Intrinsic alpha2 chain-association work supports the collagen assembly process. Reason: The authentic original source tests proalpha2 C-propeptide-dependent association and trimer incorporation. This is positive intrinsic assembly participation, but the assay is not direct imaging of fibril organization. The broader established organization of type I collagen provides the process context. |
| GO:0030199 collagen fibril organization | NAS PMID:1916105 Collagen family of proteins. | ACCEPT | Summary: The collagen-family synthesis supports organization of fibrillar type I collagen. Reason: The genuine review abstract identifies type I among fibrillar collagens and describes homo/heterotrimeric assemblies and supramolecular interactions. Combined with target-specific alpha2 assembly, this supports structural participation rather than catalysis of collagen processing. |
| GO:0030674 protein-macromolecule adaptor activity | IMP PMID:18375391 Defective C-propeptides of the proalpha2(I) chain of type I ... | MARK AS OVER ANNOTATED | Summary: The source establishes intrinsic procollagen assembly but not a separate adaptor activity. Reason: Alpha2 is not an inert assembly substrate: its C-propeptide performs genuine chain-selection/association work and enables trimer incorporation. However, GO:0030674 describes an adaptor coordinating macromolecules and explicitly directs integral protein-complex scaffolds to a separate term. The cited trimer-incorporation experiments do not establish a distinct adaptor mechanism beyond the collagen chain’s integral structural assembly. Retain over-annotation for this MF without a blanket exclusion of subunits or a requirement for different protein species; no new scaffold activity is inferred. Supporting Evidence: |
| GO:0031012 extracellular matrix | HDA PMID:20551380 Proteomics characterization of extracellular space component... | ACCEPT | Summary: COL1A2 is an extracellular-matrix collagen chain. Reason: Original aortic Table II explicitly identifies the alpha2(I) target in ECM-enriched guanidine extracts. Matrix-fraction detection does not itself measure tensile mechanics or prove each processed form has identical localization. |
| GO:0031012 extracellular matrix | HDA PMID:23658023 Comparative proteomic analysis of supportive and unsupportiv... | ACCEPT | Summary: COL1A2 is an extracellular-matrix collagen chain. Reason: Original Table1 identifies COL1A2, including 18.1 normalized spectra in feeder-free HUES1-derived ECM; mouse/human feeder columns are kept separate. Matrix-fraction detection does not itself measure tensile mechanics or prove each processed form has identical localization. |
| GO:0031012 extracellular matrix | HDA PMID:25037231 Extracellular matrix signatures of human primary metastatic ... | ACCEPT | Summary: COL1A2 is an extracellular-matrix collagen chain. Reason: Original supplemental row97 identifies the same COL1A2 protein group in both sheets across human colon/liver samples. Matrix-fraction detection does not itself measure tensile mechanics or prove each processed form has identical localization. |
| GO:0031012 extracellular matrix | HDA PMID:27559042 Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin... | ACCEPT | Summary: COL1A2 is an extracellular-matrix collagen chain. Reason: The exact source target supplement was not independently recovered; separate human target-specific studies support the established matrix location. Matrix-fraction detection does not itself measure tensile mechanics or prove each processed form has identical localization. |
| GO:0031012 extracellular matrix | HDA PMID:28327460 Comprehensive proteomic characterization of stem cell-derive... | ACCEPT | Summary: COL1A2 is an extracellular-matrix collagen chain. Reason: The exact source target supplement was not independently recovered; separate human target-specific studies support the established matrix location. Matrix-fraction detection does not itself measure tensile mechanics or prove each processed form has identical localization. |
| GO:0031012 extracellular matrix | HDA PMID:28344315 Proteomic characterization of human multiple myeloma bone ma... | ACCEPT | Summary: COL1A2 is an extracellular-matrix collagen chain. Reason: Authentic original bone-marrow S2/S3 workbooks contain the target; condition-specific values and the summary-table discrepancy are retained. Matrix-fraction detection does not itself measure tensile mechanics or prove each processed form has identical localization. |
| GO:0031012 extracellular matrix | HDA PMID:28675934 Characterization of the Extracellular Matrix of Normal and D... | ACCEPT | Summary: COL1A2 is an extracellular-matrix collagen chain. Reason: The exact source target supplement was not independently recovered; separate human target-specific studies support the established matrix location. Matrix-fraction detection does not itself measure tensile mechanics or prove each processed form has identical localization. |
| GO:0031012 extracellular matrix | IBA GO_REF:0000033 | ACCEPT | Summary: COL1A2 is an extracellular-matrix collagen chain. Reason: Current descendant and target ECM records support the inherited location without reconstruction of the historical PAINT node. Matrix-fraction detection does not itself measure tensile mechanics or prove each processed form has identical localization. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN008390299 UNRESOLVED Original node identifier preserved. Current exact descendant/target records were resolved separately, but the historical PAINT tree, alignment and IBD placement were not reconstructed; target-function confidence is not a claim to have inspected that placement. |
| GO:0031012 extracellular matrix | IEA GO_REF:0000107 | ACCEPT | Summary: COL1A2 is an extracellular-matrix collagen chain. Reason: The mouse alpha2 source is consistent with independent human matrix detection. Matrix-fraction detection does not itself measure tensile mechanics or prove each processed form has identical localization. |
| GO:0042476 odontogenesis | NAS PMID:1740554 Expression of type I collagen pro-alpha 2 chain mRNA in adul... | UNDECIDED | Summary: The adult dental-expression finding does not resolve tooth formation-to-maturation participation. Reason: The authentic abstract measures human proalpha2(I) mRNA in fully developed teeth, including odontoblasts depositing dentin in response to caries. Those are positive adult expression and repair observations. GO:0042476 specifies progression of teeth from formation to mature structures; the inspected source does not resolve that process for COL1A2, and its full text remains unavailable. Preserve the NAS assertion as undecided without denying structural participation or requiring a signaling mechanism. Supporting Evidence: |
| GO:0042802 identical protein binding | IDA PMID:17211858 Three arginine to cysteine substitutions in the pro-alpha (I... | UNDECIDED | Summary: Source-specific identical-protein binding remains unresolved. Reason: The available abstract describes disulfide-linked mutant alpha1 dimers. The full alpha2 assay scope is unavailable, so neither alpha2 self-binding nor its absence is inferred. Normal type I heterotrimer composition alone does not disprove every alpha2 self-association condition. Supporting Evidence: |
| GO:0043588 skin development | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: The inherited skin-development context is compatible with the structural collagen role. Reason: Type I collagen contributes the dermal matrix, and current target experimental premises remain part of the inherited source. The historical ancestral placement was not inspected. Preserve the tissue-level process without a separate developmental signaling core. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN002770820 UNRESOLVED Original node identifier preserved. Current exact descendant/target records were resolved separately, but the historical PAINT tree, alignment and IBD placement were not reconstructed; target-function confidence is not a claim to have inspected that placement. |
| GO:0043589 skin morphogenesis | IMP PMID:17211858 Three arginine to cysteine substitutions in the pro-alpha (I... | KEEP AS NON CORE | Summary: Skin morphogenesis is retained with source-specific experimental limits. Reason: The original abstract reports alpha1-mutant dermal fibril abnormalities. Its alpha2-specific full-text scope remains unresolved, while the established contribution of alpha2-containing type I collagen to dermal structure supports the broad target context. No direct alpha2 mutation assay is newly attributed to this paper. |
| GO:0046332 SMAD binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse alpha2–SMAD association supports qualified non-core retention. Reason: The current Q01149 mouse Col1a2 record maps the stated Ensembl protein and has three explicit MGI IPI premises for SMAD binding from PMID:14559231. The genuine abstract reports fetal-murine-library interaction screening and translated collagen/GST-SMAD-domain assays, but the full alpha2 construct boundaries were not recovered. The donor-chain identity therefore rests on current curator records, not an independently read construct. The term denotes binding to a SMAD protein. An ER/extracellular location by itself does not contradict these positive assay and curator premises; native human physiological significance remains unresolved. Retain the existing IEA orthology projection as qualified non-core binding, without equating it with direct human IPI or assigning a human TGF-beta signaling function. Supporting Evidence: PMID:14559231 MH2 domain of Smad 3 fused to GST interacted strongly with in vitro translated, 35S-labeled collagen types I, III, and V. |
| GO:0048407 platelet-derived growth factor binding | IDA PMID:8900172 Type I, II, III, IV, V, and VI collagens serve as extracellu... | KEEP AS NON CORE | Summary: Collagen–PDGF binding is retained as a contextual matrix-ligand interaction. Reason: The authentic abstract reports binding of PDGF isoforms to type I and other collagens and constituent chains, with activity of collagen-bound PDGF in fibroblast assays. Full preparation/alpha2-chain boundaries remain unverified. Retain the positive IDA association without converting COL1A2 into a PDGF receptor or an autonomous mitogenic signaling protein. Supporting Evidence: |
| GO:0048513 animal organ development | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Broad organ development is compatible with the structural collagen contribution. Reason: The current ARBA branch matches exact target FunFam 2.60.120.1000:FF:000001 and Primates. Structural contributions to developing skeletal and connective tissues support the broad context. Generality and overlap with specific developmental annotations are not evidence that the assertion is false; retain it outside the molecular core. |
| GO:0070062 extracellular exosome | HDA PMID:21362503 Protein profile of exosomes from trabecular meshwork cells. | KEEP AS NON CORE | Summary: COL1A2 is detected in the isolated human trabecular-meshwork exosome fraction. Reason: The authentic original Table1 identifies COL1A2/P08123 with normalized spectra 96.4 in TM-cell exosomes and 1.7 in the urine comparison. The study uses exosome-depleted medium, serial centrifugation and pellet washing. This directly supports the reported fraction association and supersedes the earlier contamination-based rationale. It does not establish intraluminal sorting, exosome biogenesis or target-specific flotation/marker validation, which were not shown for COL1A2. Supporting Evidence: |
| GO:0140151 solid phase of interstitial matrix | IEA GO_REF:0000117 | ACCEPT | Summary: Type I collagen contributes the solid interstitial matrix. Reason: The current ARBA branch matches the authentic target FunFam and Primates condition. The alpha2-containing fibril is an integral matrix component, not merely a soluble extracellular ligand. Preserve the original located_in qualifier; the separately modeled complex membership does not rewrite it. |
| GO:0098643 fibrillar collagen complex | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The inherited reviewer-authored fibril-membership assertion is preserved as historical context. Reason: This source object came from the earlier review’s NEW proposal and is absent from the authentic current 133-row GOA seed. Its original IEA/GO_REF:0000107 fields are preserved as historical provenance, not represented as a newly fetched or independently reconstructed transfer. General fibril membership is biologically consistent, but current GO:0005584 is_a GO:0005583 part_of GO:0098643 already supplies the assembly context. Do not count this reassessment as a fresh NEW or claim it adds independent nonredundant coverage. The retired flag withdraws this redundant historical synthetic proposal from the active assertion set; it does not claim that GOA retired an annotation. All pre-existing field values remain intact. |
Loading supporting content…
Download this section (compressed HTML)Q: How does the alpha2 chain alter fibril packing, cross-link distribution and tensile behavior relative to alpha1 homotrimers in mineralized bone versus unmineralized tendon?
Q: Which precursor processing states, if any, mediate the COL1A2 associations with cytosolic proteostasis proteins during secretion stress?
Q: Is COL1A2 in trabecular-meshwork extracellular-vesicle fractions surface associated, lumenal or carried by co-isolated matrix assemblies, and does this distribution affect matrix turnover?
Experiment: Compare purified human type I heterotrimers and alpha1 homotrimers with matched propeptide removal and cross-linking conditions. Quantify fibril diameter and packing by microscopy, tensile response by single-fibril mechanics, and protease susceptibility; measure assembly yield separately from the properties of assembled fibrils.
Hypothesis: At matched collagen amount and processing, incorporation of alpha2 changes fibril architecture and mechanical response relative to alpha1 homotrimers.
Type: Controlled collagen assembly and mechanical characterization
Experiment: Use endogenous tagging, pulse-chase labeling and compartment-resolved crosslinking in collagen-producing cells before and after a reversible secretion perturbation. Resolve signal/propeptide processing and compare SGTA association with ER entry, secretion and degradation, including tag-only and unrelated secretory-protein controls.
Hypothesis: Some screen associations depend on an intracellular precursor state exposed during secretion stress rather than persisting on extracellular mature collagen.
Type: Precursor-resolved interaction and trafficking analysis
Experiment: Combine density flotation and particle markers with COL1A2 protease protection in the presence or absence of detergent, immunogold localization and matrix-only controls in human trabecular-meshwork conditioned medium. Test fraction association independently of any effect on vesicle biogenesis.
Hypothesis: The positive COL1A2 vesicle-fraction signal includes a separable surface-associated pool whose distribution differs from protected lumenal cargo.
Type: Extracellular-vesicle topology and fractionation
Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)