GO_REF:0000002
Gene Ontology annotation through association of InterPro records with GO terms
GO_REF:0000024
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
GO_REF:0000033
Annotation inferences using phylogenetic trees
GO_REF:0000107
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
GO_REF:0000117
Electronic Gene Ontology annotations created by ARBA machine learning models
GO_REF:0000120
Combined Automated Annotation using Multiple IEA Methods
PMID:16431952
Structural abnormalities of the cornea and lid resulting from collagen V mutations.
PMID:17666000
Downregulation of extracellular matrix-related gene clusters during osteogenic differentiation of human bone marrow- and adipose tissue-derived stromal cells.
PMID:17876790
The collagen family members as cell adhesion proteins.
PMID:21421911
The collagen family.
PMID:23154389
Regulation of endodermal differentiation of human embryonic stem cells through integrin-ECM interactions.
PMID:25037231
Extracellular matrix signatures of human primary metastatic colon cancers and their metastases to liver.
PMID:27068509
Extracellular matrix remodelling in response to venous hypertension: proteomics of human varicose veins.
PMID:27559042
Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin Activity in Human Atrial Fibrillation.
PMID:28327460
Comprehensive proteomic characterization of stem cell-derived extracellular matrices.
PMID:28344315
Proteomic characterization of human multiple myeloma bone marrow extracellular matrix.
PMID:28675934
Characterization of the Extracellular Matrix of Normal and Diseased Tissues Using Proteomics.
PMID:37158802
The Chemistry and Biology of Collagen Hybridization.
PMID:9425231
Mutations of the alpha2(V) chain of type V collagen impair matrix assembly and produce ehlers-danlos syndrome type I.
PMID:9783710
A single base mutation in COL5A2 causes Ehlers-Danlos syndrome type II.
Reactome:R-HSA-1474266
Formation of collagen fibrils
Reactome:R-HSA-1564164
Collagen type V degradation by MMP2,9,10
Reactome:R-HSA-2002428
Removal of fibrillar collagen N-propeptides
Reactome:R-HSA-2002440
Removal of fibrillar collagen C-propeptides
Reactome:R-HSA-2022073
Procollagen triple helix formation
Reactome:R-HSA-2089971
Secretion of collagens
Reactome:R-HSA-2213201
Formation of collagen fibres
Reactome:R-HSA-2327695
Collagen types III, IV, V, VI, VIII, IX, XVI bind integrins alpha1beta1 and alpha2beta1
Reactome:R-HSA-2327733
FN1 binds Collagen types I-V, VII
Reactome:R-HSA-2327738
DDR1 binds collagen type I, II, III, IV, V, XI fibrils
Reactome:R-HSA-2396370
VTN binds collagens II, III and V
Reactome:R-HSA-2465890
DDR2 binds collagen type I, II, III, V, X fibrils
Reactome:R-HSA-375151
Interaction of NCAM1 with collagens
Reactome:R-HSA-382054
PDGF binds to extracellular matrix proteins
Reactome:R-HSA-8944223
Association of procollagen type V
Reactome:R-HSA-9638561
MrkD binds Collagen V
Reactome:R-NUL-2731094
Syndecan-1 binds collagen types I, III, V
PMID:14559231
Interaction of Smads with collagen types I, III, and V.
PMID:15199158
Development of a functional skin matrix requires deposition of collagen V heterotrimers.