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Protein

Collagen alpha-2(V) chain

Gene

COL5A2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Type V collagen is a key determinant in the assembly of tissue-specific matrices (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi1314CalciumBy similarity1
Metal bindingi1316CalciumBy similarity1
Metal bindingi1317Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1322CalciumBy similarity1

GO - Molecular functioni

GO - Biological processi

  • cellular response to amino acid stimulus Source: Ensembl
  • collagen catabolic process Source: Reactome
  • collagen fibril organization Source: UniProtKB
  • extracellular matrix organization Source: Reactome
  • eye morphogenesis Source: UniProtKB
  • negative regulation of endodermal cell differentiation Source: UniProtKB
  • ossification Source: Ensembl
  • skeletal system development Source: Ensembl
  • skin development Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:G66-31757-MONOMER.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1474244. Extracellular matrix organization.
R-HSA-1650814. Collagen biosynthesis and modifying enzymes.
R-HSA-186797. Signaling by PDGF.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-3000170. Syndecan interactions.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-419037. NCAM1 interactions.
R-HSA-8874081. MET activates PTK2 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-2(V) chain
Gene namesi
Name:COL5A2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:2210. COL5A2.

Subcellular locationi

GO - Cellular componenti

  • collagen type V trimer Source: UniProtKB
  • endoplasmic reticulum lumen Source: Reactome
  • extracellular matrix Source: UniProtKB
  • extracellular region Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Ehlers-Danlos syndrome, classic type (EDS)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity.
See also OMIM:130000
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_013588963G → R in EDS. 1 Publication1

Keywords - Diseasei

Disease mutation, Ehlers-Danlos syndrome

Organism-specific databases

DisGeNETi1290.
MalaCardsiCOL5A2.
MIMi130000. phenotype.
OpenTargetsiENSG00000204262.
Orphaneti90309. Ehlers-Danlos syndrome type 1.
90318. Ehlers-Danlos syndrome type 2.
PharmGKBiPA26725.

Chemistry databases

ChEMBLiCHEMBL2364188.

Polymorphism and mutation databases

BioMutaiCOL5A2.
DMDMi143811378.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Add BLAST26
ChainiPRO_000000583027 – 1229Collagen alpha-2(V) chainAdd BLAST1203
PropeptideiPRO_00000058311230 – 1499C-terminal propeptideAdd BLAST270

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei290Hydroxyproline1 Publication1
Modified residuei293Hydroxyproline1 Publication1
Modified residuei296Hydroxyproline1 Publication1
Modified residuei611Hydroxyproline1 Publication1
Modified residuei617Hydroxyproline1 Publication1
Modified residuei9193-hydroxyproline; partial1 Publication1
Modified residuei11563-hydroxyproline; partial1 Publication1
Glycosylationi1262N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1296 ↔ 1328PROSITE-ProRule annotation
Disulfide bondi1336 ↔ 1497PROSITE-ProRule annotation
Glycosylationi1400N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1405 ↔ 1450PROSITE-ProRule annotation

Post-translational modificationi

Prolines at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Probably 3-hydroxylated on Pro-919 and Pro-1156 by LEPREL1.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

EPDiP05997.
MaxQBiP05997.
PaxDbiP05997.
PeptideAtlasiP05997.
PRIDEiP05997.

PTM databases

iPTMnetiP05997.
PhosphoSitePlusiP05997.

Miscellaneous databases

PMAP-CutDBP05997.

Expressioni

Gene expression databases

BgeeiENSG00000204262.
ExpressionAtlasiP05997. baseline and differential.
GenevisibleiP05997. HS.

Organism-specific databases

HPAiHPA047922.

Interactioni

Subunit structurei

Trimers of two alpha 1(V) and one alpha 2(V) chains in most tissues and trimers of one alpha 1(V), one alpha 2(V), and one alpha 3(V) chains in placenta.

Protein-protein interaction databases

BioGridi107687. 3 interactors.
IntActiP05997. 2 interactors.
STRINGi9606.ENSP00000364000.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A9Amodel-B561-581[»]
ProteinModelPortaliP05997.
SMRiP05997.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini39 – 97VWFCPROSITE-ProRule annotationAdd BLAST59
Domaini1266 – 1499Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST234

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi506 – 508Cell attachment siteSequence analysis3
Motifi944 – 946Cell attachment siteSequence analysis3
Motifi1067 – 1069Cell attachment siteSequence analysis3
Motifi1070 – 1072Cell attachment siteSequence analysis3
Motifi1100 – 1102Cell attachment siteSequence analysis3
Motifi1127 – 1129Cell attachment siteSequence analysis3
Motifi1136 – 1138Cell attachment siteSequence analysis3

Domaini

The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function (By similarity).By similarity

Sequence similaritiesi

Belongs to the fibrillar collagen family.PROSITE-ProRule annotation
Contains 1 fibrillar collagen NC1 domain.PROSITE-ProRule annotation
Contains 1 VWFC domain.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG4110XTV. LUCA.
GeneTreeiENSGT00840000129673.
HOVERGENiHBG004933.
InParanoidiP05997.
KOiK19721.
OMAiIGIRGQP.
OrthoDBiEOG091G03LV.
PhylomeDBiP05997.
TreeFamiTF344135.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR001007. VWF_dom.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 5 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEiPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05997-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMANWAEARP LLILIVLLGQ FVSIKAQEED EDEGYGEEIA CTQNGQMYLN
60 70 80 90 100
RDIWKPAPCQ ICVCDNGAIL CDKIECQDVL DCADPVTPPG ECCPVCSQTP
110 120 130 140 150
GGGNTNFGRG RKGQKGEPGL VPVVTGIRGR PGPAGPPGSQ GPRGERGPKG
160 170 180 190 200
RPGPRGPQGI DGEPGVPGQP GAPGPPGHPS HPGPDGLSRP FSAQMAGLDE
210 220 230 240 250
KSGLGSQVGL MPGSVGPVGP RGPQGLQGQQ GGAGPTGPPG EPGDPGPMGP
260 270 280 290 300
IGSRGPEGPP GKPGEDGEPG RNGNPGEVGF AGSPGARGFP GAPGLPGLKG
310 320 330 340 350
HRGHKGLEGP KGEVGAPGSK GEAGPTGPMG AMGPLGPRGM PGERGRLGPQ
360 370 380 390 400
GAPGQRGAHG MPGKPGPMGP LGIPGSSGFP GNPGMKGEAG PTGARGPEGP
410 420 430 440 450
QGQRGETGPP GPVGSPGLPG AIGTDGTPGA KGPTGSPGTS GPPGSAGPPG
460 470 480 490 500
SPGPQGSTGP QGIRGQPGDP GVPGFKGEAG PKGEPGPHGI QGPIGPPGEE
510 520 530 540 550
GKRGPRGDPG TVGPPGPVGE RGAPGNRGFP GSDGLPGPKG AQGERGPVGS
560 570 580 590 600
SGPKGSQGDP GRPGEPGLPG ARGLTGNPGV QGPEGKLGPL GAPGEDGRPG
610 620 630 640 650
PPGSIGIRGQ PGSMGLPGPK GSSGDPGKPG EAGNAGVPGQ RGAPGKDGEV
660 670 680 690 700
GPSGPVGPPG LAGERGEQGP PGPTGFQGLP GPPGPPGEGG KPGDQGVPGD
710 720 730 740 750
PGAVGPLGPR GERGNPGERG EPGITGLPGE KGMAGGHGPD GPKGSPGPSG
760 770 780 790 800
TPGDTGPPGL QGMPGERGIA GTPGPKGDRG GIGEKGAEGT AGNDGARGLP
810 820 830 840 850
GPLGPPGPAG PTGEKGEPGP RGLVGPPGSR GNPGSRGENG PTGAVGFAGP
860 870 880 890 900
QGPDGQPGVK GEPGEPGQKG DAGSPGPQGL AGSPGPHGPN GVPGLKGGRG
910 920 930 940 950
TQGPPGATGF PGSAGRVGPP GPAGAPGPAG PLGEPGKEGP PGLRGDPGSH
960 970 980 990 1000
GRVGDRGPAG PPGGPGDKGD PGEDGQPGPD GPPGPAGTTG QRGIVGMPGQ
1010 1020 1030 1040 1050
RGERGMPGLP GPAGTPGKVG PTGATGDKGP PGPVGPPGSN GPVGEPGPEG
1060 1070 1080 1090 1100
PAGNDGTPGR DGAVGERGDR GDPGPAGLPG SQGAPGTPGP VGAPGDAGQR
1110 1120 1130 1140 1150
GDPGSRGPIG PPGRAGKRGL PGPQGPRGDK GDHGDRGDRG QKGHRGFTGL
1160 1170 1180 1190 1200
QGLPGPPGPN GEQGSAGIPG PFGPRGPPGP VGPSGKEGNP GPLGPIGPPG
1210 1220 1230 1240 1250
VRGSVGEAGP EGPPGEPGPP GPPGPPGHLT AALGDIMGHY DESMPDPLPE
1260 1270 1280 1290 1300
FTEDQAAPDD KNKTDPGVHA TLKSLSSQIE TMRSPDGSKK HPARTCDDLK
1310 1320 1330 1340 1350
LCHSAKQSGE YWIDPNQGSV EDAIKVYCNM ETGETCISAN PSSVPRKTWW
1360 1370 1380 1390 1400
ASKSPDNKPV WYGLDMNRGS QFAYGDHQSP NTAITQMTFL RLLSKEASQN
1410 1420 1430 1440 1450
ITYICKNSVG YMDDQAKNLK KAVVLKGAND LDIKAEGNIR FRYIVLQDTC
1460 1470 1480 1490
SKRNGNVGKT VFEYRTQNVA RLPIIDLAPV DVGGTDQEFG VEIGPVCFV
Length:1,499
Mass (Da):144,910
Last modified:April 3, 2007 - v3
Checksum:iE8C92BF5E749EC97
GO

Sequence cautioni

The sequence AAH43613 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAY24185 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence BAD92282 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti292A → P AA sequence (PubMed:8181482).Curated1
Sequence conflicti361M → L in AAL13166 (PubMed:11566270).Curated1
Sequence conflicti430A → P in CAA75002 (Ref. 1) Curated1
Sequence conflicti430A → P in AAA51859 (PubMed:2914927).Curated1
Sequence conflicti430A → P in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti463 – 466IRGQ → NSGL in CAA75002 (Ref. 1) Curated4
Sequence conflicti463 – 466IRGQ → NSGL in CAA28454 (PubMed:3029669).Curated4
Sequence conflicti463I → N in AAA51859 (PubMed:2914927).Curated1
Sequence conflicti472 – 474Missing in CAA75002 (Ref. 1) Curated3
Sequence conflicti472 – 474Missing in CAA28454 (PubMed:3029669).Curated3
Sequence conflicti512V → L in CAA75002 (Ref. 1) Curated1
Sequence conflicti512V → L in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti608R → K in CAA75002 (Ref. 1) Curated1
Sequence conflicti608R → K in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti613S → T in CAA75002 (Ref. 1) Curated1
Sequence conflicti613S → T in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti623S → N in CAA75002 (Ref. 1) Curated1
Sequence conflicti623S → N in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti635A → P in CAA75002 (Ref. 1) Curated1
Sequence conflicti635A → P in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti649E → K in CAA75002 (Ref. 1) Curated1
Sequence conflicti649E → K in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti653S → Y in CAA75002 (Ref. 1) Curated1
Sequence conflicti653S → Y in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti656V → P in CAA75002 (Ref. 1) Curated1
Sequence conflicti656V → P in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti662A → R in CAA75002 (Ref. 1) Curated1
Sequence conflicti662A → R in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti679L → H in CAA75002 (Ref. 1) Curated1
Sequence conflicti679L → H in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti700D → G in CAA75002 (Ref. 1) Curated1
Sequence conflicti700D → G in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti797R → G in CAA75002 (Ref. 1) Curated1
Sequence conflicti797R → G in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti811 – 812PT → LL in CAA75002 (Ref. 1) Curated2
Sequence conflicti811 – 812PT → LL in CAA28454 (PubMed:3029669).Curated2
Sequence conflicti853P → S in CAA75002 (Ref. 1) Curated1
Sequence conflicti853P → S in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti943L → P in CAA75002 (Ref. 1) Curated1
Sequence conflicti943L → P in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti955D → V in CAA75002 (Ref. 1) Curated1
Sequence conflicti955D → V in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti1111 – 1112PP → HL in CAA75002 (Ref. 1) Curated2
Sequence conflicti1111 – 1112PP → HL in CAA28454 (PubMed:3029669).Curated2
Sequence conflicti1111 – 1112PP → HL in AAA52007 (PubMed:2985598).Curated2
Sequence conflicti1196I → L in CAA75002 (Ref. 1) Curated1
Sequence conflicti1196I → L in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti1196I → L in AAA52007 (PubMed:2985598).Curated1
Sequence conflicti1421K → T in AAA52058 (PubMed:2411731).Curated1
Sequence conflicti1441F → S in AAA52058 (PubMed:2411731).Curated1
Sequence conflicti1467Q → E in AAA51858 (PubMed:3224983).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_048799460P → S.Corresponds to variant rs35830636dbSNPEnsembl.1
Natural variantiVAR_057910512V → A.1 PublicationCorresponds to variant rs35852101dbSNPEnsembl.1
Natural variantiVAR_057911833P → L.1 PublicationCorresponds to variant rs116298748dbSNPEnsembl.1
Natural variantiVAR_048800956R → P.Corresponds to variant rs6434313dbSNPEnsembl.1
Natural variantiVAR_013588963G → R in EDS. 1 Publication1
Natural variantiVAR_0579121230T → S.1 PublicationCorresponds to variant rs767234623dbSNPEnsembl.1
Natural variantiVAR_0579131432D → V.1 PublicationCorresponds to variant rs141777954dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y14690 mRNA. Translation: CAA75002.1.
AB209045 mRNA. Translation: BAD92282.1. Different initiation.
AC064833 Genomic DNA. No translation available.
AC133106 Genomic DNA. Translation: AAY24185.1. Sequence problems.
J04478 mRNA. Translation: AAA51859.1.
AY016288, AY016287 Genomic DNA. Translation: AAL13165.1.
AY016295
, AY016289, AY016290, AY016291, AY016292, AY016293, AY016294 Genomic DNA. Translation: AAL13166.1.
M58529 Genomic DNA. Translation: AAC41699.1.
X04758 mRNA. Translation: CAA28454.1.
BC043613 mRNA. Translation: AAH43613.1. Different initiation.
M10956 mRNA. Translation: AAA52007.1.
M11135 mRNA. Translation: AAA51857.1.
M11718 mRNA. Translation: AAA52058.1.
J03051 Genomic DNA. Translation: AAA51858.1.
CCDSiCCDS33350.1.
PIRiA31427. CGHU2V.
RefSeqiNP_000384.2. NM_000393.3.
UniGeneiHs.445827.

Genome annotation databases

EnsembliENST00000374866; ENSP00000364000; ENSG00000204262.
GeneIDi1290.
KEGGihsa:1290.
UCSCiuc002uqk.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y14690 mRNA. Translation: CAA75002.1.
AB209045 mRNA. Translation: BAD92282.1. Different initiation.
AC064833 Genomic DNA. No translation available.
AC133106 Genomic DNA. Translation: AAY24185.1. Sequence problems.
J04478 mRNA. Translation: AAA51859.1.
AY016288, AY016287 Genomic DNA. Translation: AAL13165.1.
AY016295
, AY016289, AY016290, AY016291, AY016292, AY016293, AY016294 Genomic DNA. Translation: AAL13166.1.
M58529 Genomic DNA. Translation: AAC41699.1.
X04758 mRNA. Translation: CAA28454.1.
BC043613 mRNA. Translation: AAH43613.1. Different initiation.
M10956 mRNA. Translation: AAA52007.1.
M11135 mRNA. Translation: AAA51857.1.
M11718 mRNA. Translation: AAA52058.1.
J03051 Genomic DNA. Translation: AAA51858.1.
CCDSiCCDS33350.1.
PIRiA31427. CGHU2V.
RefSeqiNP_000384.2. NM_000393.3.
UniGeneiHs.445827.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A9Amodel-B561-581[»]
ProteinModelPortaliP05997.
SMRiP05997.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107687. 3 interactors.
IntActiP05997. 2 interactors.
STRINGi9606.ENSP00000364000.

Chemistry databases

ChEMBLiCHEMBL2364188.

PTM databases

iPTMnetiP05997.
PhosphoSitePlusiP05997.

Polymorphism and mutation databases

BioMutaiCOL5A2.
DMDMi143811378.

Proteomic databases

EPDiP05997.
MaxQBiP05997.
PaxDbiP05997.
PeptideAtlasiP05997.
PRIDEiP05997.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374866; ENSP00000364000; ENSG00000204262.
GeneIDi1290.
KEGGihsa:1290.
UCSCiuc002uqk.4. human.

Organism-specific databases

CTDi1290.
DisGeNETi1290.
GeneCardsiCOL5A2.
GeneReviewsiCOL5A2.
HGNCiHGNC:2210. COL5A2.
HPAiHPA047922.
MalaCardsiCOL5A2.
MIMi120190. gene.
130000. phenotype.
neXtProtiNX_P05997.
OpenTargetsiENSG00000204262.
Orphaneti90309. Ehlers-Danlos syndrome type 1.
90318. Ehlers-Danlos syndrome type 2.
PharmGKBiPA26725.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG4110XTV. LUCA.
GeneTreeiENSGT00840000129673.
HOVERGENiHBG004933.
InParanoidiP05997.
KOiK19721.
OMAiIGIRGQP.
OrthoDBiEOG091G03LV.
PhylomeDBiP05997.
TreeFamiTF344135.

Enzyme and pathway databases

BioCyciZFISH:G66-31757-MONOMER.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1474244. Extracellular matrix organization.
R-HSA-1650814. Collagen biosynthesis and modifying enzymes.
R-HSA-186797. Signaling by PDGF.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-3000170. Syndecan interactions.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-419037. NCAM1 interactions.
R-HSA-8874081. MET activates PTK2 signaling.

Miscellaneous databases

ChiTaRSiCOL5A2. human.
GeneWikiiCOL5A2.
GenomeRNAii1290.
PMAP-CutDBP05997.
PROiP05997.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000204262.
ExpressionAtlasiP05997. baseline and differential.
GenevisibleiP05997. HS.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR001007. VWF_dom.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 5 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEiPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCO5A2_HUMAN
AccessioniPrimary (citable) accession number: P05997
Secondary accession number(s): P78440
, Q13908, Q53WR4, Q59GR4, Q6LDJ5, Q7KZ55, Q86XF6, Q96QB0, Q96QB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 3, 2007
Last modified: November 30, 2016
This is version 190 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.