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Protein

Collagen alpha-1(V) chain

Gene

COL5A1

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi1657CalciumBy similarity1
Metal bindingi1659CalciumBy similarity1
Metal bindingi1660Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1662Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1665CalciumBy similarity1

GO - Molecular functioni

  • extracellular matrix structural constituent Source: Ensembl
  • heparin binding Source: UniProtKB
  • integrin binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • platelet-derived growth factor binding Source: MGI
  • proteoglycan binding Source: UniProtKB

GO - Biological processi

  • blood vessel development Source: Ensembl
  • cell adhesion Source: UniProtKB
  • cell migration Source: UniProtKB
  • collagen biosynthetic process Source: UniProtKB
  • collagen catabolic process Source: Reactome
  • collagen fibril organization Source: UniProtKB
  • extracellular fibril organization Source: UniProtKB
  • extracellular matrix organization Source: Reactome
  • eye morphogenesis Source: UniProtKB
  • heart morphogenesis Source: Ensembl
  • integrin biosynthetic process Source: UniProtKB
  • negative regulation of endodermal cell differentiation Source: UniProtKB
  • regulation of cellular component organization Source: Ensembl
  • skin development Source: UniProtKB
  • tendon development Source: Ensembl
  • wound healing, spreading of epidermal cells Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calcium, Heparin-binding, Metal-binding

Enzyme and pathway databases

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-1(V) chain
Gene namesi
Name:COL5A1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:2209. COL5A1.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: Ensembl
  • collagen type V trimer Source: UniProtKB
  • endoplasmic reticulum lumen Source: Reactome
  • extracellular exosome Source: UniProtKB
  • 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)5 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_05790225L → P in EDS; not or less efficiently secreted into the extracellular matrix. 1 Publication1
Natural variantiVAR_05790325L → R in EDS; not or less efficiently secreted into the extracellular matrix. 1 Publication1
Natural variantiVAR_015412530G → S in EDS. 3 PublicationsCorresponds to variant rs61735045dbSNPEnsembl.1
Natural variantiVAR_0579091486G → C in EDS. 1 Publication1
Natural variantiVAR_0154131489G → D in EDS. 1 Publication1
Natural variantiVAR_0018081639C → S in EDS. 1 PublicationCorresponds to variant rs80338764dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Ehlers-Danlos syndrome

Organism-specific databases

DisGeNETi1289.
MalaCardsiCOL5A1.
MIMi130000. phenotype.
OpenTargetsiENSG00000130635.
Orphaneti90309. Ehlers-Danlos syndrome type 1.
90318. Ehlers-Danlos syndrome type 2.
PharmGKBiPA26724.

Chemistry databases

ChEMBLiCHEMBL2364188.

Polymorphism and mutation databases

DMDMi85687376.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 37Sequence analysisAdd BLAST37
ChainiPRO_000000575638 – 1605Collagen alpha-1(V) chainAdd BLAST1568
PropeptideiPRO_00000057571606 – 1838C-terminal propeptideAdd BLAST233

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei234SulfotyrosineSequence analysis1
Modified residuei236SulfotyrosineSequence analysis1
Modified residuei240SulfotyrosineSequence analysis1
Modified residuei262SulfotyrosineSequence analysis1
Modified residuei263SulfotyrosineSequence analysis1
Modified residuei338SulfotyrosineSequence analysis1
Modified residuei340SulfotyrosineSequence analysis1
Modified residuei346SulfotyrosineSequence analysis1
Modified residuei347SulfotyrosineSequence analysis1
Modified residuei416SulfotyrosineSequence analysis1
Modified residuei417SulfotyrosineSequence analysis1
Modified residuei420SulfotyrosineSequence analysis1
Modified residuei421SulfotyrosineSequence analysis1
Modified residuei570Hydroxyproline1 Publication1
Modified residuei576Hydroxyproline1 Publication1
Modified residuei621Hydroxyproline1 Publication1
Modified residuei6275-hydroxylysine1 Publication1
Modified residuei639Hydroxyproline1 Publication1
Modified residuei6425-hydroxylysine1 Publication1
Modified residuei648Hydroxyproline1 Publication1
Modified residuei654Hydroxyproline1 Publication1
Modified residuei657Hydroxyproline1 Publication1
Modified residuei675Hydroxyproline1 Publication1
Modified residuei678Hydroxyproline1 Publication1
Modified residuei680Hydroxyproline1 Publication1
Modified residuei686Hydroxyproline1 Publication1
Modified residuei690Hydroxyproline1 Publication1
Modified residuei696Hydroxyproline1 Publication1
Modified residuei705Hydroxyproline1 Publication1
Modified residuei7085-hydroxylysine1 Publication1
Modified residuei717Hydroxyproline1 Publication1
Modified residuei720Hydroxyproline1 Publication1
Modified residuei726Hydroxyproline1 Publication1
Modified residuei732Hydroxyproline1 Publication1
Modified residuei7445-hydroxylysine1 Publication1
Modified residuei750Hydroxyproline1 Publication1
Modified residuei756Hydroxyproline1 Publication1
Modified residuei762Hydroxyproline1 Publication1
Modified residuei765Hydroxyproline1 Publication1
Modified residuei771Hydroxyproline1 Publication1
Modified residuei7745-hydroxylysine1 Publication1
Modified residuei780Hydroxyproline1 Publication1
Modified residuei789Hydroxyproline1 Publication1
Modified residuei7955-hydroxylysine1 Publication1
Modified residuei8045-hydroxylysine1 Publication1
Modified residuei8075-hydroxylysine1 Publication1
Modified residuei8105-hydroxylysine1 Publication1
Modified residuei816Hydroxyproline1 Publication1
Modified residuei8195-hydroxylysine1 Publication1
Modified residuei834Hydroxyproline1 Publication1
Modified residuei8465-hydroxylysine1 Publication1
Modified residuei861Hydroxyproline1 Publication1
Modified residuei8645-hydroxylysine1 Publication1
Modified residuei870Hydroxyproline1 Publication1
Modified residuei873Hydroxyproline1 Publication1
Modified residuei876Hydroxyproline1 Publication1
Modified residuei8825-hydroxylysine1 Publication1
Modified residuei888Hydroxyproline1 Publication1
Modified residuei891Hydroxyproline1 Publication1
Modified residuei8975-hydroxylysine1 Publication1
Modified residuei903Hydroxyproline1 Publication1
Modified residuei906Hydroxyproline1 Publication1
Modified residuei930Hydroxyproline1 Publication1
Modified residuei945Hydroxyproline1 Publication1
Modified residuei1017Hydroxyproline1 Publication1
Modified residuei1020Hydroxyproline1 Publication1
Modified residuei1023Hydroxyproline1 Publication1
Modified residuei1029Hydroxyproline1 Publication1
Modified residuei1221Hydroxyproline1 Publication1
Modified residuei1224Hydroxyproline1 Publication1
Modified residuei1467Hydroxyproline1 Publication1
Modified residuei1470Hydroxyproline1 Publication1
Modified residuei1601SulfotyrosineSequence analysis1
Modified residuei1604SulfotyrosineSequence analysis1
Disulfide bondi1639 ↔ 1671PROSITE-ProRule annotation
Disulfide bondi1645Interchain (with C-1662)PROSITE-ProRule annotation
Disulfide bondi1662Interchain (with C-1645)PROSITE-ProRule annotation
Disulfide bondi1680 ↔ 1835PROSITE-ProRule annotation
Disulfide bondi1746 ↔ 1789PROSITE-ProRule annotation

Post-translational modificationi

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.1 Publication
Sulfated on 40% of tyrosines.

Keywords - PTMi

Disulfide bond, Hydroxylation, Sulfation

Proteomic databases

EPDiP20908.
MaxQBiP20908.
PaxDbiP20908.
PeptideAtlasiP20908.
PRIDEiP20908.

PTM databases

iPTMnetiP20908.
PhosphoSitePlusiP20908.

Miscellaneous databases

PMAP-CutDBP20908.

Expressioni

Gene expression databases

BgeeiENSG00000130635.
CleanExiHS_COL5A1.
ExpressionAtlasiP20908. baseline and differential.
GenevisibleiP20908. HS.

Organism-specific databases

HPAiHPA030769.

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. Interacts with CSPG4.1 Publication

GO - Molecular functioni

  • integrin binding Source: UniProtKB
  • platelet-derived growth factor binding Source: MGI

Protein-protein interaction databases

BioGridi107686. 23 interactors.
IntActiP20908. 10 interactors.
STRINGi9606.ENSP00000360882.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A89model-A/B/C904-924[»]
1A9Amodel-A/C904-924[»]
ProteinModelPortaliP20908.
SMRiP20908.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini72 – 244Laminin G-likeAdd BLAST173
Domaini1609 – 1837Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST229

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni231 – 443Nonhelical regionAdd BLAST213
Regioni444 – 558Interrupted collagenous regionAdd BLAST115
Regioni559 – 1570Triple-helical regionAdd BLAST1012
Regioni1571 – 1605Nonhelical regionAdd BLAST35

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 laminin G-like domain.Curated

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
GeneTreeiENSGT00840000129673.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiP20908.
KOiK19721.
OMAiPIGVVQM.
PhylomeDBiP20908.
TreeFamiTF323987.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR008160. Collagen.
IPR013320. ConA-like_dom.
IPR000885. Fib_collagen_C.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 5 hits.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS51461. NC1_FIB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P20908-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDVHTRWKAR SALRPGAPLL PPLLLLLLWA PPPSRAAQPA DLLKVLDFHN
60 70 80 90 100
LPDGITKTTG FCATRRSSKG PDVAYRVTKD AQLSAPTKQL YPASAFPEDF
110 120 130 140 150
SILTTVKAKK GSQAFLVSIY NEQGIQQIGL ELGRSPVFLY EDHTGKPGPE
160 170 180 190 200
DYPLFRGINL SDGKWHRIAL SVHKKNVTLI LDCKKKTTKF LDRSDHPMID
210 220 230 240 250
INGIIVFGTR ILDEEVFEGD IQQLLFVSDH RAAYDYCEHY SPDCDTAVPD
260 270 280 290 300
TPQSQDPNPD EYYTEGDGEG ETYYYEYPYY EDPEDLGKEP TPSKKPVEAA
310 320 330 340 350
KETTEVPEEL TPTPTEAAPM PETSEGAGKE EDVGIGDYDY VPSEDYYTPS
360 370 380 390 400
PYDDLTYGEG EENPDQPTDP GAGAEIPTST ADTSNSSNPA PPPGEGADDL
410 420 430 440 450
EGEFTEETIR NLDENYYDPY YDPTSSPSEI GPGMPANQDT IYEGIGGPRG
460 470 480 490 500
EKGQKGEPAI IEPGMLIEGP PGPEGPAGLP GPPGTMGPTG QVGDPGERGP
510 520 530 540 550
PGRPGLPGAD GLPGPPGTML MLPFRFGGGG DAGSKGPMVS AQESQAQAIL
560 570 580 590 600
QQARLALRGP AGPMGLTGRP GPVGPPGSGG LKGEPGDVGP QGPRGVQGPP
610 620 630 640 650
GPAGKPGRRG RAGSDGARGM PGQTGPKGDR GFDGLAGLPG EKGHRGDPGP
660 670 680 690 700
SGPPGPPGDD GERGDDGEVG PRGLPGEPGP RGLLGPKGPP GPPGPPGVTG
710 720 730 740 750
MDGQPGPKGN VGPQGEPGPP GQQGNPGAQG LPGPQGAIGP PGEKGPLGKP
760 770 780 790 800
GLPGMPGADG PPGHPGKEGP PGEKGGQGPP GPQGPIGYPG PRGVKGADGI
810 820 830 840 850
RGLKGTKGEK GEDGFPGFKG DMGIKGDRGE IGPPGPRGED GPEGPKGRGG
860 870 880 890 900
PNGDPGPLGP PGEKGKLGVP GLPGYPGRQG PKGSIGFPGF PGANGEKGGR
910 920 930 940 950
GTPGKPGPRG QRGPTGPRGE RGPRGITGKP GPKGNSGGDG PAGPPGERGP
960 970 980 990 1000
NGPQGPTGFP GPKGPPGPPG KDGLPGHPGQ RGETGFQGKT GPPGPPGVVG
1010 1020 1030 1040 1050
PQGPTGETGP MGERGHPGPP GPPGEQGLPG LAGKEGTKGD PGPAGLPGKD
1060 1070 1080 1090 1100
GPPGLRGFPG DRGLPGPVGA LGLKGNEGPP GPPGPAGSPG ERGPAGAAGP
1110 1120 1130 1140 1150
IGIPGRPGPQ GPPGPAGEKG APGEKGPQGP AGRDGLQGPV GLPGPAGPVG
1160 1170 1180 1190 1200
PPGEDGDKGE IGEPGQKGSK GDKGEQGPPG PTGPQGPIGQ PGPSGADGEP
1210 1220 1230 1240 1250
GPRGQQGLFG QKGDEGPRGF PGPPGPVGLQ GLPGPPGEKG ETGDVGQMGP
1260 1270 1280 1290 1300
PGPPGPRGPS GAPGADGPQG PPGGIGNPGA VGEKGEPGEA GEPGLPGEGG
1310 1320 1330 1340 1350
PPGPKGERGE KGESGPSGAA GPPGPKGPPG DDGPKGSPGP VGFPGDPGPP
1360 1370 1380 1390 1400
GEPGPAGQDG PPGDKGDDGE PGQTGSPGPT GEPGPSGPPG KRGPPGPAGP
1410 1420 1430 1440 1450
EGRQGEKGAK GEAGLEGPPG KTGPIGPQGA PGKPGPDGLR GIPGPVGEQG
1460 1470 1480 1490 1500
LPGSPGPDGP PGPMGPPGLP GLKGDSGPKG EKGHPGLIGL IGPPGEQGEK
1510 1520 1530 1540 1550
GDRGLPGPQG SSGPKGEQGI TGPSGPIGPP GPPGLPGPPG PKGAKGSSGP
1560 1570 1580 1590 1600
TGPKGEAGHP GPPGPPGPPG EVIQPLPIQA SRTRRNIDAS QLLDDGNGEN
1610 1620 1630 1640 1650
YVDYADGMEE IFGSLNSLKL EIEQMKRPLG TQQNPARTCK DLQLCHPDFP
1660 1670 1680 1690 1700
DGEYWVDPNQ GCSRDSFKVY CNFTAGGSTC VFPDKKSEGA RITSWPKENP
1710 1720 1730 1740 1750
GSWFSEFKRG KLLSYVDAEG NPVGVVQMTF LRLLSASAHQ NVTYHCYQSV
1760 1770 1780 1790 1800
AWQDAATGSY DKALRFLGSN DEEMSYDNNP YIRALVDGCA TKKGYQKTVL
1810 1820 1830
EIDTPKVEQV PIVDIMFNDF GEASQKFGFE VGPACFMG
Length:1,838
Mass (Da):183,560
Last modified:September 13, 2005 - v3
Checksum:i8F18AB0B91B3A0C7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti82 – 83QL → HV in AAA59993 (PubMed:1722213).Curated2
Sequence conflicti390A → R in AAA59993 (PubMed:1722213).Curated1
Sequence conflicti641E → G AA sequence (PubMed:2496661).Curated1
Sequence conflicti650P → L AA sequence (PubMed:2496661).Curated1
Sequence conflicti663R → E AA sequence (PubMed:2496661).Curated1
Sequence conflicti668E → Q AA sequence (PubMed:2496661).Curated1
Sequence conflicti677E → K in BAA14323 (PubMed:2071595).Curated1
Sequence conflicti677E → Q AA sequence (PubMed:2496661).Curated1
Sequence conflicti684L → P AA sequence (PubMed:2496661).Curated1
Sequence conflicti692 – 699PPGPPGVT → VTGEPGAP AA sequence (PubMed:2496661).Curated8
Sequence conflicti727G → Q AA sequence (PubMed:2496661).Curated1
Sequence conflicti741P → L AA sequence (PubMed:2496661).Curated1
Sequence conflicti747L → Q AA sequence (PubMed:2496661).Curated1
Sequence conflicti753P → A AA sequence (PubMed:2496661).Curated1
Sequence conflicti759D → N AA sequence (PubMed:2496661).Curated1
Sequence conflicti776 – 777GQ → QK AA sequence (PubMed:2496661).Curated2
Sequence conflicti849 – 855GGPNGDP → IGPPGPR AA sequence (PubMed:2203476).Curated7
Sequence conflicti894N → D AA sequence (PubMed:2203476).Curated1
Sequence conflicti1295 – 1299LPGEG → PSGRS in BAA14323 (PubMed:2071595).Curated5
Sequence conflicti1554K → R in BAA14323 (PubMed:2071595).Curated1
Sequence conflicti1813V → A in AAA59993 (PubMed:1722213).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05790225L → P in EDS; not or less efficiently secreted into the extracellular matrix. 1 Publication1
Natural variantiVAR_05790325L → R in EDS; not or less efficiently secreted into the extracellular matrix. 1 Publication1
Natural variantiVAR_057904114A → D Unclassified mutation. 1 PublicationCorresponds to variant rs147589613dbSNPEnsembl.1
Natural variantiVAR_057905192D → N Unclassified mutation. 1 PublicationCorresponds to variant rs138579182dbSNPEnsembl.1
Natural variantiVAR_057906229D → N Associated with increased risk of cervical artery dissection. 1 Publication1
Natural variantiVAR_057907393P → S Unclassified mutation. 1 Publication1
Natural variantiVAR_015412530G → S in EDS. 3 PublicationsCorresponds to variant rs61735045dbSNPEnsembl.1
Natural variantiVAR_075702863E → V Found in a patient with Joubert syndrome; unknown pathological significance. 1 PublicationCorresponds to variant rs139788610dbSNPEnsembl.1
Natural variantiVAR_064702908P → L Found in a renal cell carcinoma case; somatic mutation. 1 PublicationCorresponds to variant rs772211736dbSNPEnsembl.1
Natural variantiVAR_057908951N → S Unclassified mutation. 1 PublicationCorresponds to variant rs61736966dbSNPEnsembl.1
Natural variantiVAR_0757031140V → M Found in a patient with Joubert syndrome; unknown pathological significance. 1 PublicationCorresponds to variant rs149616140dbSNPEnsembl.1
Natural variantiVAR_0579091486G → C in EDS. 1 Publication1
Natural variantiVAR_0154131489G → D in EDS. 1 Publication1
Natural variantiVAR_0018081639C → S in EDS. 1 PublicationCorresponds to variant rs80338764dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90279 mRNA. Translation: BAA14323.1.
M76729 mRNA. Translation: AAA59993.1.
AL591890, AL603650, AL645768 Genomic DNA. Translation: CAI15483.1.
AL645768, AL591890, AL603650 Genomic DNA. Translation: CAI17261.1.
AL603650, AL591890, AL645768 Genomic DNA. Translation: CAI39859.1.
CCDSiCCDS6982.1.
PIRiS18802. CGHU1V.
RefSeqiNP_000084.3. NM_000093.4.
UniGeneiHs.210283.

Genome annotation databases

EnsembliENST00000371817; ENSP00000360882; ENSG00000130635.
GeneIDi1289.
KEGGihsa:1289.
UCSCiuc004cfe.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90279 mRNA. Translation: BAA14323.1.
M76729 mRNA. Translation: AAA59993.1.
AL591890, AL603650, AL645768 Genomic DNA. Translation: CAI15483.1.
AL645768, AL591890, AL603650 Genomic DNA. Translation: CAI17261.1.
AL603650, AL591890, AL645768 Genomic DNA. Translation: CAI39859.1.
CCDSiCCDS6982.1.
PIRiS18802. CGHU1V.
RefSeqiNP_000084.3. NM_000093.4.
UniGeneiHs.210283.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A89model-A/B/C904-924[»]
1A9Amodel-A/C904-924[»]
ProteinModelPortaliP20908.
SMRiP20908.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107686. 23 interactors.
IntActiP20908. 10 interactors.
STRINGi9606.ENSP00000360882.

Chemistry databases

ChEMBLiCHEMBL2364188.

PTM databases

iPTMnetiP20908.
PhosphoSitePlusiP20908.

Polymorphism and mutation databases

DMDMi85687376.

Proteomic databases

EPDiP20908.
MaxQBiP20908.
PaxDbiP20908.
PeptideAtlasiP20908.
PRIDEiP20908.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371817; ENSP00000360882; ENSG00000130635.
GeneIDi1289.
KEGGihsa:1289.
UCSCiuc004cfe.5. human.

Organism-specific databases

CTDi1289.
DisGeNETi1289.
GeneCardsiCOL5A1.
GeneReviewsiCOL5A1.
H-InvDBHIX0008519.
HGNCiHGNC:2209. COL5A1.
HPAiHPA030769.
MalaCardsiCOL5A1.
MIMi120215. gene.
130000. phenotype.
neXtProtiNX_P20908.
OpenTargetsiENSG00000130635.
Orphaneti90309. Ehlers-Danlos syndrome type 1.
90318. Ehlers-Danlos syndrome type 2.
PharmGKBiPA26724.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
GeneTreeiENSGT00840000129673.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiP20908.
KOiK19721.
OMAiPIGVVQM.
PhylomeDBiP20908.
TreeFamiTF323987.

Enzyme and pathway databases

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

ChiTaRSiCOL5A1. human.
GeneWikiiCollagen,_type_V,_alpha_1.
GenomeRNAii1289.
PMAP-CutDBP20908.
PROiP20908.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000130635.
CleanExiHS_COL5A1.
ExpressionAtlasiP20908. baseline and differential.
GenevisibleiP20908. HS.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR008160. Collagen.
IPR013320. ConA-like_dom.
IPR000885. Fib_collagen_C.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 5 hits.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS51461. NC1_FIB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCO5A1_HUMAN
AccessioniPrimary (citable) accession number: P20908
Secondary accession number(s): Q15094, Q5SUX4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: September 13, 2005
Last modified: November 30, 2016
This is version 186 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 9
    Human chromosome 9: 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.