Gene Details | GeDiPNet - Complete Gene Info, Disease Associations & Pathways

Gene Gene miRNA Gene ontology Other IDs Protein Pathways Associated diseases
Entrez ID Entrez Gene ID - the GENE ID in NCBI Gene database.	50509
Gene name Gene Name - the full gene name approved by the HGNC.	Collagen type V alpha 3 chain
Gene symbol Gene Symbol - the official gene symbol approved by the HGNC.	COL5A3
Synonyms (NCBI Gene) Gene synonyms aliases	-
Chromosome Chromosome number	19
Chromosome location Chromosomal Location - indicates the cytogenetic location of the gene or region on the chromosome.	19p13.2
Summary Summary of gene provided in NCBI Entrez Gene.	This gene encodes an alpha chain for one of the low abundance fibrillar collagens. Fibrillar collagen molecules are trimers that can be composed of one or more types of alpha chains. Type V collagen is found in tissues containing type I collagen and appea

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miRTarBase ID	miRNA	Experiments	Reference
MIRT005822	hsa-miR-204-5p	Microarray	21282569
MIRT000098	hsa-miR-29b-3p	Luciferase reporter assay	23478036
MIRT724417	hsa-miR-9500	HITS-CLIP	19536157
MIRT724416	hsa-miR-2114-5p	HITS-CLIP	19536157
MIRT724415	hsa-miR-6892-3p	HITS-CLIP	19536157
MIRT724414	hsa-miR-2276-5p	HITS-CLIP	19536157
MIRT724413	hsa-miR-877-3p	HITS-CLIP	19536157
MIRT724412	hsa-miR-1236-3p	HITS-CLIP	19536157
MIRT724411	hsa-miR-3137	HITS-CLIP	19536157
MIRT724410	hsa-miR-20b-3p	HITS-CLIP	19536157
MIRT724409	hsa-miR-6723-5p	HITS-CLIP	19536157
MIRT724408	hsa-miR-642a-5p	HITS-CLIP	19536157
MIRT440915	hsa-miR-323a-5p	HITS-CLIP	24374217
MIRT440915	hsa-miR-323a-5p	HITS-CLIP	24374217
MIRT724417	hsa-miR-9500	HITS-CLIP	19536157
MIRT724416	hsa-miR-2114-5p	HITS-CLIP	19536157
MIRT724415	hsa-miR-6892-3p	HITS-CLIP	19536157
MIRT724414	hsa-miR-2276-5p	HITS-CLIP	19536157
MIRT724413	hsa-miR-877-3p	HITS-CLIP	19536157
MIRT724412	hsa-miR-1236-3p	HITS-CLIP	19536157
MIRT724411	hsa-miR-3137	HITS-CLIP	19536157
MIRT724410	hsa-miR-20b-3p	HITS-CLIP	19536157
MIRT724409	hsa-miR-6723-5p	HITS-CLIP	19536157
MIRT724408	hsa-miR-642a-5p	HITS-CLIP	19536157
MIRT903100	hsa-miR-1256	CLIP-seq
MIRT903101	hsa-miR-1273f	CLIP-seq
MIRT903102	hsa-miR-1275	CLIP-seq
MIRT903103	hsa-miR-1283	CLIP-seq
MIRT903104	hsa-miR-143	CLIP-seq
MIRT903105	hsa-miR-204	CLIP-seq
MIRT903106	hsa-miR-211	CLIP-seq
MIRT903107	hsa-miR-3119	CLIP-seq
MIRT903108	hsa-miR-3140-3p	CLIP-seq
MIRT903109	hsa-miR-4328	CLIP-seq
MIRT903110	hsa-miR-4330	CLIP-seq
MIRT903111	hsa-miR-4446-5p	CLIP-seq
MIRT903112	hsa-miR-4447	CLIP-seq
MIRT903113	hsa-miR-4472	CLIP-seq
MIRT903114	hsa-miR-4651	CLIP-seq
MIRT903115	hsa-miR-4652-5p	CLIP-seq
MIRT903116	hsa-miR-4665-5p	CLIP-seq
MIRT903117	hsa-miR-4708-5p	CLIP-seq
MIRT903118	hsa-miR-4755-5p	CLIP-seq
MIRT903119	hsa-miR-4770	CLIP-seq
MIRT903120	hsa-miR-608	CLIP-seq
MIRT903121	hsa-miR-623	CLIP-seq
MIRT1547251	hsa-miR-4728-5p	CLIP-seq
MIRT2203623	hsa-miR-3065-3p	CLIP-seq
MIRT2203624	hsa-miR-361-3p	CLIP-seq
MIRT2203625	hsa-miR-3620	CLIP-seq
MIRT2203626	hsa-miR-3978	CLIP-seq
MIRT2203627	hsa-miR-4308	CLIP-seq
MIRT2203628	hsa-miR-4428	CLIP-seq
MIRT2203629	hsa-miR-4434	CLIP-seq
MIRT903112	hsa-miR-4447	CLIP-seq
MIRT903113	hsa-miR-4472	CLIP-seq
MIRT2203630	hsa-miR-4516	CLIP-seq
MIRT903114	hsa-miR-4651	CLIP-seq
MIRT903120	hsa-miR-608	CLIP-seq
MIRT2203631	hsa-miR-875-3p	CLIP-seq
MIRT2386347	hsa-miR-642a	CLIP-seq
MIRT2427785	hsa-miR-1206	CLIP-seq
MIRT2427786	hsa-miR-3921	CLIP-seq
MIRT2427787	hsa-miR-4424	CLIP-seq
MIRT2427788	hsa-miR-4653-5p	CLIP-seq
MIRT2427789	hsa-miR-4682	CLIP-seq
MIRT2506685	hsa-miR-1276	CLIP-seq
MIRT2506686	hsa-miR-1321	CLIP-seq
MIRT2506687	hsa-miR-3175	CLIP-seq
MIRT2506688	hsa-miR-4419a	CLIP-seq
MIRT2506689	hsa-miR-4510	CLIP-seq
MIRT1547251	hsa-miR-4728-5p	CLIP-seq
MIRT2506690	hsa-miR-4739	CLIP-seq
MIRT2506691	hsa-miR-4756-5p	CLIP-seq
MIRT2506685	hsa-miR-1276	CLIP-seq
MIRT2506686	hsa-miR-1321	CLIP-seq
MIRT2506687	hsa-miR-3175	CLIP-seq
MIRT2506688	hsa-miR-4419a	CLIP-seq
MIRT2506689	hsa-miR-4510	CLIP-seq
MIRT1547251	hsa-miR-4728-5p	CLIP-seq
MIRT2506690	hsa-miR-4739	CLIP-seq
MIRT2506691	hsa-miR-4756-5p	CLIP-seq

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GO ID	Ontology	Definition	Evidence	Reference
GO:0005201	Function	Extracellular matrix structural constituent	IBA	21873635
GO:0005201	Function	Extracellular matrix structural constituent	NAS	10722718
GO:0005518	Function	Collagen binding	NAS	10722718
GO:0005576	Component	Extracellular region	TAS
GO:0005588	Component	Collagen type V trimer	NAS	1571108, 10722718
GO:0005615	Component	Extracellular space	IBA	21873635
GO:0005788	Component	Endoplasmic reticulum lumen	TAS
GO:0007160	Process	Cell-matrix adhesion	IEA
GO:0008201	Function	Heparin binding	IEA
GO:0030020	Function	Extracellular matrix structural constituent conferring tensile strength	HDA	28344315
GO:0030020	Function	Extracellular matrix structural constituent conferring tensile strength	RCA	27559042, 28675934
GO:0030198	Process	Extracellular matrix organization	IBA	21873635
GO:0030198	Process	Extracellular matrix organization	TAS
GO:0030199	Process	Collagen fibril organization	NAS	10722718
GO:0031012	Component	Extracellular matrix	IBA	21873635
GO:0043394	Function	Proteoglycan binding	IEA
GO:0043588	Process	Skin development	NAS	10722718
GO:0062023	Component	Collagen-containing extracellular matrix	HDA	27559042, 28344315, 28675934

MIM	HGNC	e!Ensembl
120216	14864	ENSG00000080573

Protein

UniProt ID

P25940

Protein name

Collagen alpha-3(V) chain

Protein function

Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin.

Family and domains

Pfam

Accession	ID	Position in sequence	Description	Type
PF01391	Collagen	476 → 539	Collagen triple helix repeat (20 copies)	Repeat
PF01391	Collagen	1430 → 1492	Collagen triple helix repeat (20 copies)	Repeat
PF01410	COLFI	1512 → 1743	Fibrillar collagen C-terminal domain	Family

Tissue specificity

TISSUE SPECIFICITY: Detected in fibroblasts (at protein level) (PubMed:36213313). Detected in urine (at protein level) (PubMed:37453717). {ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}.

Sequence

MGNRRDLGQPRAGLCLLLAALQLLPGTQADPVDVLKALGVQGGQAGVPEGPGFCPQRTPE
GDRAFRIGQASTLGIPTWELFPEGHFPENFSLLITLRGQPANQSVLLSIYDERGARQLGL
ALGPALGLLGDPFRPLPQQVNLTDGRWHRVAVSIDGEMVTLVADCEAQPPVLGHGPRFIS
IAGLTVLGTQDLGEKTFEGDIQELLISPDPQAAFQACERYLPDCDNLAPAATVAPQGEPE
TPRPRRKGKGKGRKKGRGRKGKGRKKNKEIWTSSPPPDSAENQTSTDIPKTETPAPNLPP
TPTPLVVTSTVTTGLNATILERSLDPDSGTELGTLETKAAREDEEGDDSTMGPDFRAAEY
PSRTQFQIFPGAGEKGAKGEPAVIEKGQQFEGPPGAPGPQGVVGPSGPPGPPGFPGDPGP
PGPAGLPGIPGIDGIRGPPGTVIMMPFQFAGGSFKGPPVSFQQAQAQAVLQQTQLSMKGP
PGPVGLTGRPGPVGLPGHPGLKGEEGAEGPQGPRGLQGPHGPPGRVGKMGRPGADGARGL
PGDTGPKGDRGFDGLPGLPGEKGQRGDFGHVGQPGPPGEDGERGAEGPPGPTGQAGEPGP
RGLLGPRGSPGPTGRPGVTGIDGAPGAKGNVGPPGEPGPPGQQGNHGSQGLPGPQGLIGT
PGEKGPPGNPGIPGLPGSDGPLGHPGHEGPTGEKGAQGPPGSAGPPGYPGPRGVKGTSGN
RGLQGEKGEKGEDGFPGFKGDVGLKGDQGKPGAPGPRGEDGPEGPKGQAGQAGEEGPPGS
AGEKGKLGVPGLPGYPGRPGPKGSIGFPGPLGPIGEKGKSGKTGQPGLEGERGPPGSRGE
RGQPGATGQPGPKGDVGQDGAPGIPGEKGLPGLQGPPGFPGPKGPPGHQGKDGRPGHPGQ
RGELGFQGQTGPPGPAGVLGPQGKTGEVGPLGERGPPGPPGPPGEQGLPGLEGREGAKGE
LGPPGPLGKEGPAGLRGFPGPKGGPGDPGPTGLKGDKGPPGPVGANGSPGERGPLGPAGG
IGLPGQSGSEGPVGPAGKKGSRGERGPPGPTGKDGIPGPLGPLGPPGAAGPSGEEGDKGD
VGAPGHKGSKGDKGDAGPPGQPGIRGPAGHPGPPGADGAQGRRGPPGLFGQKGDDGVRGF
VGVIGPPGLQGLPGPPGEKGEVGDVGSMGPHGAPGPRGPQGPTGSEGTPGLPGGVGQPGA
VGEKGERGDAGDPGPPGAPGIPGPKGDIGEKGDSGPSGAAGPPGKKGPPGEDGAKGSVGP
TGLPGDLGPPGDPGVSGIDGSPGEKGDPGDVGGPGPPGASGEPGAPGPPGKRGPSGHMGR
EGREGEKGAKGEPGPDGPPGRTGPMGARGPPGRVGPEGLRGIPGPVGEPGLLGAPGQMGP
PGPLGPSGLPGLKGDTGPKGEKGHIGLIGLIGPPGEAGEKGDQGLPGVQGPPGPKGDPGP
PGPIGSLGHPGPPGVAGPLGQKGSKGSPGSMGPRGDTGPAGPPGPPGAPAELHGLRRRRR
FVPVPLPVVEGGLEEVLASLTSLSLELEQLRRPPGTAERPGLVCHELHRNHPHLPDGEYW
IDPNQGCARDSFRVFCNFTAGGETCLYPDKKFEIVKLASWSKEKPGGWYSTFRRGKKFSY
VDADGSPVNVVQLNFLKLLSATARQNFTYSCQNAAAWLDEATGDYSHSARFLGTNGEELS
FNQTTAATVSVPQDGCRLRKGQTKTLFEFSSSRAGFLPLWDVAATDFGQTNQKFGFELGP
VCFSS

Sequence length

1745

Interactions

View interactions

	KEGG		Reactome
	Cytoskeleton in muscle cells Protein digestion and absorption		Collagen degradation Extracellular matrix organization Collagen biosynthesis and modifying enzymes Signaling by PDGF Assembly of collagen fibrils and other multimeric structures Integrin cell surface interactions Non-integrin membrane-ECM interactions ECM proteoglycans NCAM1 interactions MET activates PTK2 signaling Collagen chain trimerization

Show/Hide Causal Diseases (1)

Disease term	Disease name	dbSNP ID	References
Causal
Prostate cancer	Malignant neoplasm of prostate	rs121909139, rs121909140, rs121909141, rs121909142, rs121909143, rs606231169, rs606231170, rs137852584, rs137852578, rs137852580, rs137852581, rs137852582	29610475

Show/Hide Text Mining Associations (7)

Disease Name	Relationship Type	References
Associations from Text Mining
Breast Neoplasms	Associate	34541602
Erythema elevatum diutinum	Associate	36012487
Inflammation	Associate	34256840
Neoplasms	Stimulate	37284741
Personality Disorders	Associate	33450964
Prostatic Neoplasms	Associate	33450964
Urinary Bladder Neoplasms	Associate	35450397

COL5A3 (collagen type V alpha 3 chain)