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P20908

- CO5A1_HUMAN

UniProt

P20908 - CO5A1_HUMAN

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Protein

Collagen alpha-1(V) chain

Gene

COL5A1

Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1657 – 16571CalciumBy similarity
Metal bindingi1659 – 16591CalciumBy similarity
Metal bindingi1660 – 16601Calcium; via carbonyl oxygenBy similarity
Metal bindingi1662 – 16621Calcium; via carbonyl oxygenBy similarity
Metal bindingi1665 – 16651CalciumBy similarity

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: Ensembl
  2. heparin binding Source: UniProtKB
  3. integrin binding Source: UniProtKB
  4. metal ion binding Source: UniProtKB-KW
  5. platelet-derived growth factor binding Source: MGI
  6. proteoglycan binding Source: UniProtKB

GO - Biological processi

  1. axon guidance Source: Reactome
  2. blood vessel development Source: Ensembl
  3. cell adhesion Source: UniProtKB
  4. cell migration Source: UniProtKB
  5. collagen biosynthetic process Source: UniProtKB
  6. collagen catabolic process Source: Reactome
  7. collagen fibril organization Source: UniProtKB
  8. extracellular fibril organization Source: UniProtKB
  9. extracellular matrix disassembly Source: Reactome
  10. extracellular matrix organization Source: Reactome
  11. eye morphogenesis Source: UniProtKB
  12. heart morphogenesis Source: Ensembl
  13. integrin biosynthetic process Source: UniProtKB
  14. negative regulation of endodermal cell differentiation Source: UniProtKB
  15. regulation of cellular component organization Source: Ensembl
  16. skin development Source: UniProtKB
  17. tendon development Source: Ensembl
  18. wound healing, spreading of epidermal cells Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calcium, Heparin-binding, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_118779. Extracellular matrix organization.
REACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_13552. Integrin cell surface interactions.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150401. Collagen degradation.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_163942. Syndecan interactions.
REACT_16888. Signaling by PDGF.
REACT_18312. NCAM1 interactions.
REACT_197897. Syndecan interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(V) chain
Gene namesi
Name:COL5A1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:2209. COL5A1.

Subcellular locationi

Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

GO - Cellular componenti

  1. basement membrane Source: Ensembl
  2. collagen type V trimer Source: UniProtKB
  3. endoplasmic reticulum lumen Source: Reactome
  4. extracellular matrix Source: UniProtKB
  5. extracellular region Source: Reactome
  6. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Ehlers-Danlos syndrome 1 (EDS1) [MIM:130000]: A connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS1 is the severe form of classic Ehlers-Danlos syndrome.4 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti25 – 251L → P in EDS1 and EDS2; not or less efficiently secreted into the extracellular matrix. 1 Publication
VAR_057902
Natural varianti25 – 251L → R in EDS1 and EDS2; not or less efficiently secreted into the extracellular matrix. 1 Publication
VAR_057903
Natural varianti530 – 5301G → S in EDS1 and EDS2. 3 Publications
Corresponds to variant rs61735045 [ dbSNP | Ensembl ].
VAR_015412
Natural varianti1486 – 14861G → C in EDS1 and EDS2. 1 Publication
VAR_057909
Natural varianti1489 – 14891G → D in EDS1. 1 Publication
VAR_015413
Natural varianti1639 – 16391C → S in EDS1. 1 Publication
VAR_001808
Ehlers-Danlos syndrome 2 (EDS2) [MIM:130010]: Mild form of classic Ehlers-Danlos syndrome.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti25 – 251L → P in EDS1 and EDS2; not or less efficiently secreted into the extracellular matrix. 1 Publication
VAR_057902
Natural varianti25 – 251L → R in EDS1 and EDS2; not or less efficiently secreted into the extracellular matrix. 1 Publication
VAR_057903
Natural varianti530 – 5301G → S in EDS1 and EDS2. 3 Publications
Corresponds to variant rs61735045 [ dbSNP | Ensembl ].
VAR_015412
Natural varianti1486 – 14861G → C in EDS1 and EDS2. 1 Publication
VAR_057909

Keywords - Diseasei

Disease mutation, Ehlers-Danlos syndrome

Organism-specific databases

MIMi130000. phenotype.
130010. phenotype.
Orphaneti90309. Ehlers-Danlos syndrome type 1.
90318. Ehlers-Danlos syndrome type 2.
PharmGKBiPA26724.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3737Sequence AnalysisAdd
BLAST
Chaini38 – 16051568Collagen alpha-1(V) chainPRO_0000005756Add
BLAST
Propeptidei1606 – 1838233C-terminal propeptidePRO_0000005757Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei234 – 2341SulfotyrosineSequence Analysis
Modified residuei236 – 2361SulfotyrosineSequence Analysis
Modified residuei240 – 2401SulfotyrosineSequence Analysis
Modified residuei262 – 2621SulfotyrosineSequence Analysis
Modified residuei263 – 2631SulfotyrosineSequence Analysis
Modified residuei338 – 3381SulfotyrosineSequence Analysis
Modified residuei340 – 3401SulfotyrosineSequence Analysis
Modified residuei346 – 3461SulfotyrosineSequence Analysis
Modified residuei347 – 3471SulfotyrosineSequence Analysis
Modified residuei416 – 4161SulfotyrosineSequence Analysis
Modified residuei417 – 4171SulfotyrosineSequence Analysis
Modified residuei420 – 4201SulfotyrosineSequence Analysis
Modified residuei421 – 4211SulfotyrosineSequence Analysis
Modified residuei570 – 5701Hydroxyproline1 Publication
Modified residuei576 – 5761Hydroxyproline1 Publication
Modified residuei621 – 6211Hydroxyproline1 Publication
Modified residuei627 – 62715-hydroxylysine1 Publication
Modified residuei639 – 6391Hydroxyproline1 Publication
Modified residuei642 – 64215-hydroxylysine1 Publication
Modified residuei648 – 6481Hydroxyproline1 Publication
Modified residuei654 – 6541Hydroxyproline1 Publication
Modified residuei657 – 6571Hydroxyproline1 Publication
Modified residuei675 – 6751Hydroxyproline1 Publication
Modified residuei678 – 6781Hydroxyproline1 Publication
Modified residuei680 – 6801Hydroxyproline1 Publication
Modified residuei686 – 6861Hydroxyproline1 Publication
Modified residuei690 – 6901Hydroxyproline1 Publication
Modified residuei696 – 6961Hydroxyproline1 Publication
Modified residuei705 – 7051Hydroxyproline1 Publication
Modified residuei708 – 70815-hydroxylysine1 Publication
Modified residuei717 – 7171Hydroxyproline1 Publication
Modified residuei720 – 7201Hydroxyproline1 Publication
Modified residuei726 – 7261Hydroxyproline1 Publication
Modified residuei732 – 7321Hydroxyproline1 Publication
Modified residuei744 – 74415-hydroxylysine1 Publication
Modified residuei750 – 7501Hydroxyproline1 Publication
Modified residuei756 – 7561Hydroxyproline1 Publication
Modified residuei762 – 7621Hydroxyproline1 Publication
Modified residuei765 – 7651Hydroxyproline1 Publication
Modified residuei771 – 7711Hydroxyproline1 Publication
Modified residuei774 – 77415-hydroxylysine1 Publication
Modified residuei780 – 7801Hydroxyproline1 Publication
Modified residuei789 – 7891Hydroxyproline1 Publication
Modified residuei795 – 79515-hydroxylysine1 Publication
Modified residuei804 – 80415-hydroxylysine1 Publication
Modified residuei807 – 80715-hydroxylysine1 Publication
Modified residuei810 – 81015-hydroxylysine1 Publication
Modified residuei816 – 8161Hydroxyproline1 Publication
Modified residuei819 – 81915-hydroxylysine1 Publication
Modified residuei834 – 8341Hydroxyproline1 Publication
Modified residuei846 – 84615-hydroxylysine1 Publication
Modified residuei861 – 8611Hydroxyproline1 Publication
Modified residuei864 – 86415-hydroxylysine1 Publication
Modified residuei870 – 8701Hydroxyproline1 Publication
Modified residuei873 – 8731Hydroxyproline1 Publication
Modified residuei876 – 8761Hydroxyproline1 Publication
Modified residuei882 – 88215-hydroxylysine1 Publication
Modified residuei888 – 8881Hydroxyproline1 Publication
Modified residuei891 – 8911Hydroxyproline1 Publication
Modified residuei897 – 89715-hydroxylysine1 Publication
Modified residuei903 – 9031Hydroxyproline1 Publication
Modified residuei906 – 9061Hydroxyproline1 Publication
Modified residuei930 – 9301Hydroxyproline1 Publication
Modified residuei945 – 9451Hydroxyproline1 Publication
Modified residuei1017 – 10171Hydroxyproline1 Publication
Modified residuei1020 – 10201Hydroxyproline1 Publication
Modified residuei1023 – 10231Hydroxyproline1 Publication
Modified residuei1029 – 10291Hydroxyproline1 Publication
Modified residuei1221 – 12211Hydroxyproline1 Publication
Modified residuei1224 – 12241Hydroxyproline1 Publication
Modified residuei1467 – 14671Hydroxyproline1 Publication
Modified residuei1470 – 14701Hydroxyproline1 Publication
Modified residuei1601 – 16011SulfotyrosineSequence Analysis
Modified residuei1604 – 16041SulfotyrosineSequence Analysis
Disulfide bondi1639 ↔ 1671PROSITE-ProRule annotation
Disulfide bondi1645 – 1645Interchain (with C-1662)PROSITE-ProRule annotation
Disulfide bondi1662 – 1662Interchain (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

MaxQBiP20908.
PaxDbiP20908.
PRIDEiP20908.

PTM databases

PhosphoSiteiP20908.

Miscellaneous databases

PMAP-CutDBP20908.

Expressioni

Gene expression databases

BgeeiP20908.
CleanExiHS_COL5A1.
ExpressionAtlasiP20908. baseline and differential.
GenevestigatoriP20908.

Organism-specific databases

HPAiCAB002743.
HPA030769.

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

Protein-protein interaction databases

BioGridi107686. 11 interactions.
IntActiP20908. 1 interaction.
STRINGi9606.ENSP00000360882.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A89model-A/B/C904-924[»]
1A9Amodel-A/C904-924[»]
ProteinModelPortaliP20908.
SMRiP20908. Positions 73-208, 1628-1837.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini72 – 244173Laminin G-likeAdd
BLAST
Domaini1609 – 1837229Fibrillar collagen NC1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni231 – 443213Nonhelical regionAdd
BLAST
Regioni444 – 558115Interrupted collagenous regionAdd
BLAST
Regioni559 – 15701012Triple-helical regionAdd
BLAST
Regioni1571 – 160535Nonhelical regionAdd
BLAST

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

eggNOGiNOG12793.
GeneTreeiENSGT00760000118776.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
InParanoidiP20908.
KOiK06236.
OMAiPIGVVQM.
OrthoDBiEOG7XPZ4W.
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.
PF02210. Laminin_G_2. 1 hit.
[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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 832QL → HV in AAA59993. (PubMed:1722213)Curated
Sequence conflicti390 – 3901A → R in AAA59993. (PubMed:1722213)Curated
Sequence conflicti641 – 6411E → G AA sequence (PubMed:2496661)Curated
Sequence conflicti650 – 6501P → L AA sequence (PubMed:2496661)Curated
Sequence conflicti663 – 6631R → E AA sequence (PubMed:2496661)Curated
Sequence conflicti668 – 6681E → Q AA sequence (PubMed:2496661)Curated
Sequence conflicti677 – 6771E → K in BAA14323. (PubMed:2071595)Curated
Sequence conflicti677 – 6771E → Q AA sequence (PubMed:2496661)Curated
Sequence conflicti684 – 6841L → P AA sequence (PubMed:2496661)Curated
Sequence conflicti692 – 6998PPGPPGVT → VTGEPGAP AA sequence (PubMed:2496661)Curated
Sequence conflicti727 – 7271G → Q AA sequence (PubMed:2496661)Curated
Sequence conflicti741 – 7411P → L AA sequence (PubMed:2496661)Curated
Sequence conflicti747 – 7471L → Q AA sequence (PubMed:2496661)Curated
Sequence conflicti753 – 7531P → A AA sequence (PubMed:2496661)Curated
Sequence conflicti759 – 7591D → N AA sequence (PubMed:2496661)Curated
Sequence conflicti776 – 7772GQ → QK AA sequence (PubMed:2496661)Curated
Sequence conflicti849 – 8557GGPNGDP → IGPPGPR AA sequence (PubMed:2203476)Curated
Sequence conflicti894 – 8941N → D AA sequence (PubMed:2203476)Curated
Sequence conflicti1295 – 12995LPGEG → PSGRS in BAA14323. (PubMed:2071595)Curated
Sequence conflicti1554 – 15541K → R in BAA14323. (PubMed:2071595)Curated
Sequence conflicti1813 – 18131V → A in AAA59993. (PubMed:1722213)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti25 – 251L → P in EDS1 and EDS2; not or less efficiently secreted into the extracellular matrix. 1 Publication
VAR_057902
Natural varianti25 – 251L → R in EDS1 and EDS2; not or less efficiently secreted into the extracellular matrix. 1 Publication
VAR_057903
Natural varianti114 – 1141A → D Unclassified mutation. 1 Publication
VAR_057904
Natural varianti192 – 1921D → N Unclassified mutation. 1 Publication
Corresponds to variant rs138579182 [ dbSNP | Ensembl ].
VAR_057905
Natural varianti229 – 2291D → N Associated with increased risk of cervical artery dissection. 1 Publication
VAR_057906
Natural varianti393 – 3931P → S Unclassified mutation. 1 Publication
VAR_057907
Natural varianti530 – 5301G → S in EDS1 and EDS2. 3 Publications
Corresponds to variant rs61735045 [ dbSNP | Ensembl ].
VAR_015412
Natural varianti908 – 9081P → L Found in a renal cell carcinoma case; somatic mutation. 1 Publication
VAR_064702
Natural varianti951 – 9511N → S Unclassified mutation. 1 Publication
Corresponds to variant rs61736966 [ dbSNP | Ensembl ].
VAR_057908
Natural varianti1486 – 14861G → C in EDS1 and EDS2. 1 Publication
VAR_057909
Natural varianti1489 – 14891G → D in EDS1. 1 Publication
VAR_015413
Natural varianti1639 – 16391C → S in EDS1. 1 Publication
VAR_001808

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.4. human.

Polymorphism databases

DMDMi85687376.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS6982.1.
PIRi S18802. CGHU1V.
RefSeqi NP_000084.3. NM_000093.4.
UniGenei Hs.210283.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A89 model - A/B/C 904-924 [» ]
1A9A model - A/C 904-924 [» ]
ProteinModelPortali P20908.
SMRi P20908. Positions 73-208, 1628-1837.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107686. 11 interactions.
IntActi P20908. 1 interaction.
STRINGi 9606.ENSP00000360882.

Chemistry

ChEMBLi CHEMBL2364188.

PTM databases

PhosphoSitei P20908.

Polymorphism databases

DMDMi 85687376.

Proteomic databases

MaxQBi P20908.
PaxDbi P20908.
PRIDEi P20908.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000371817 ; ENSP00000360882 ; ENSG00000130635 .
GeneIDi 1289.
KEGGi hsa:1289.
UCSCi uc004cfe.4. human.

Organism-specific databases

CTDi 1289.
GeneCardsi GC09P137533.
GeneReviewsi COL5A1.
H-InvDB HIX0008519.
HGNCi HGNC:2209. COL5A1.
HPAi CAB002743.
HPA030769.
MIMi 120215. gene.
130000. phenotype.
130010. phenotype.
neXtProti NX_P20908.
Orphaneti 90309. Ehlers-Danlos syndrome type 1.
90318. Ehlers-Danlos syndrome type 2.
PharmGKBi PA26724.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00760000118776.
HOGENOMi HOG000085654.
HOVERGENi HBG004933.
InParanoidi P20908.
KOi K06236.
OMAi PIGVVQM.
OrthoDBi EOG7XPZ4W.
PhylomeDBi P20908.
TreeFami TF323987.

Enzyme and pathway databases

Reactomei REACT_118779. Extracellular matrix organization.
REACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_13552. Integrin cell surface interactions.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150401. Collagen degradation.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_163942. Syndecan interactions.
REACT_16888. Signaling by PDGF.
REACT_18312. NCAM1 interactions.
REACT_197897. Syndecan interactions.

Miscellaneous databases

ChiTaRSi COL5A1. human.
GeneWikii Collagen,_type_V,_alpha_1.
GenomeRNAii 1289.
NextBioi 5219.
PMAP-CutDB P20908.
PROi P20908.
SOURCEi Search...

Gene expression databases

Bgeei P20908.
CleanExi HS_COL5A1.
ExpressionAtlasi P20908. baseline and differential.
Genevestigatori P20908.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR008160. Collagen.
IPR013320. ConA-like_dom.
IPR000885. Fib_collagen_C.
IPR001791. Laminin_G.
[Graphical view ]
Pfami PF01410. COLFI. 1 hit.
PF01391. Collagen. 5 hits.
PF02210. Laminin_G_2. 1 hit.
[Graphical view ]
ProDomi PD002078. Fib_collagen_C. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00038. COLFI. 1 hit.
SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
PROSITEi PS51461. NC1_FIB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complete primary structure of human collagen alpha 1 (V) chain."
    Takahara K., Seto Y., Okasawa K., Okamoto N., Noda A., Yaoi Y., Kato I.
    J. Biol. Chem. 266:13124-13129(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 556-565.
  2. "The pro-alpha-1(V) collagen chain: complete primary structure, distribution of expression, and comparison with the pro-alpha-1(XI) collagen chain."
    Greenspan D.S., Cheng W., Hoffman G.G.
    J. Biol. Chem. 266:24727-24733(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Covalent structure of collagen: amino acid sequence of three cyanogen bromide-derived peptides from human alpha 1(V) collagen chain."
    Seyer J.M., Kang A.H.
    Arch. Biochem. Biophys. 271:120-129(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 621-822, HYDROXYLATION.
    Tissue: Chorioamniotic membrane.
  5. "Primary structure of the heparin-binding site of type V collagen."
    Yaoi Y., Hashimoto K., Koitabashi H., Takahara K., Ito M., Kato I.
    Biochim. Biophys. Acta 1035:139-145(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 823-950, HEPARIN-BINDING.
  6. "Isolation of the alpha 3-chain of human type V collagen and characterization by partial sequencing."
    Mann K.
    Biol. Chem. Hoppe-Seyler 373:69-75(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 556-571.
    Tissue: Placenta.
  7. Cited for: PROTEIN SEQUENCE OF 565-576; 756-772; 1012-1029; 1219-1232 AND 1465-1477.
    Tissue: Chorioamniotic membrane.
  8. "The membrane-spanning proteoglycan NG2 binds to collagens V and VI through the central nonglobular domain of its core protein."
    Tillet E., Ruggiero F., Nishiyama A., Stallcup W.B.
    J. Biol. Chem. 272:10769-10776(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSPG4.
  9. "Mutations in the COL5A1 gene are causal in the Ehlers-Danlos syndromes I and II."
    de Paepe A., Nuytinck L., Hausser I., Anton-Lamprecht I., Naeyaert J.-M.
    Am. J. Hum. Genet. 60:547-554(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISEASE, VARIANT EDS1 SER-1639.
  10. "Mutations in the COL5A1 coding sequence are not common in patients with spontaneous cervical artery dissections."
    Grond-Ginsbach C., Weber R., Haas J., Orberk E., Kunz S., Busse O., Hausser I., Brandt T., Wildemann B.
    Stroke 30:1887-1890(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ASN-229, ASSOCIATION WITH INCREASED RISK OF CERVICAL ARTERY DISSECTION.
  11. "Compound heterozygosity for a disease-causing G1489E and disease-modifying G530S substitution in COL5A1 of a patient with the classical type of Ehlers-Danlos syndrome: an explanation of intrafamilial variability?"
    Giunta C., Steinmann B.
    Am. J. Med. Genet. 90:72-79(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS EDS1 SER-530 AND ASP-1489.
  12. Erratum
    Giunta C., Steinmann B.
    Am. J. Med. Genet. 93:342-342(2000)
  13. "Homozygous Gly530Ser substitution in COL5A1 causes mild classical Ehlers-Danlos syndrome."
    Giunta C., Nuytinck L., Raghunath M., Hausser I., De Paepe A., Steinmann B.
    Am. J. Med. Genet. 109:284-290(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT EDS2 SER-530.
  14. "The molecular basis of classic Ehlers-Danlos syndrome: a comprehensive study of biochemical and molecular findings in 48 unrelated patients."
    Malfait F., Coucke P., Symoens S., Loeys B., Nuytinck L., De Paepe A.
    Hum. Mutat. 25:28-37(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS EDS1/EDS2 SER-530 AND CYS-1486, VARIANTS ASP-114; ASN-192; SER-393 AND SER-951.
  15. "COL5A1 signal peptide mutations interfere with protein secretion and cause classic Ehlers-Danlos syndrome."
    Symoens S., Malfait F., Renard M., Andre J., Hausser I., Loeys B., Coucke P., De Paepe A.
    Hum. Mutat. 30:E395-E403(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS EDS1/EDS2 ARG-25 AND PRO-25, CHARACTERIZATION OF VARIANTS EDS1/EDS2 ARG-25 AND PRO-25.
  16. Cited for: VARIANT LEU-908.

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: October 29, 2014
This is version 164 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

External Data

Dasty 3