SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P20908

- CO5A1_HUMAN

UniProt

P20908 - CO5A1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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 – 16571Calcium By similarity
Metal bindingi1659 – 16591Calcium By similarity
Metal bindingi1660 – 16601Calcium; via carbonyl oxygen By similarity
Metal bindingi1662 – 16621Calcium; via carbonyl oxygen By similarity
Metal bindingi1665 – 16651Calcium By 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
Complete GO annotation...

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. regulation of cellular component organization Source: Ensembl
  15. skin development Source: UniProtKB
  16. tendon development Source: Ensembl
  17. 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

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.4 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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 – 3737 Reviewed prediction
Add
BLAST
Chaini38 – 16051568Collagen alpha-1(V) chain
PRO_0000005756Add
BLAST
Propeptidei1606 – 1838233C-terminal propeptide
PRO_0000005757Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei234 – 2341Sulfotyrosine Reviewed prediction
Modified residuei236 – 2361Sulfotyrosine Reviewed prediction
Modified residuei240 – 2401Sulfotyrosine Reviewed prediction
Modified residuei262 – 2621Sulfotyrosine Reviewed prediction
Modified residuei263 – 2631Sulfotyrosine Reviewed prediction
Modified residuei338 – 3381Sulfotyrosine Reviewed prediction
Modified residuei340 – 3401Sulfotyrosine Reviewed prediction
Modified residuei346 – 3461Sulfotyrosine Reviewed prediction
Modified residuei347 – 3471Sulfotyrosine Reviewed prediction
Modified residuei416 – 4161Sulfotyrosine Reviewed prediction
Modified residuei417 – 4171Sulfotyrosine Reviewed prediction
Modified residuei420 – 4201Sulfotyrosine Reviewed prediction
Modified residuei421 – 4211Sulfotyrosine Reviewed prediction
Modified residuei570 – 5701Hydroxyproline
Modified residuei576 – 5761Hydroxyproline
Modified residuei621 – 6211Hydroxyproline
Modified residuei627 – 62715-hydroxylysine
Modified residuei639 – 6391Hydroxyproline
Modified residuei642 – 64215-hydroxylysine
Modified residuei648 – 6481Hydroxyproline
Modified residuei654 – 6541Hydroxyproline
Modified residuei657 – 6571Hydroxyproline
Modified residuei675 – 6751Hydroxyproline
Modified residuei678 – 6781Hydroxyproline
Modified residuei680 – 6801Hydroxyproline
Modified residuei686 – 6861Hydroxyproline
Modified residuei690 – 6901Hydroxyproline
Modified residuei696 – 6961Hydroxyproline
Modified residuei705 – 7051Hydroxyproline
Modified residuei708 – 70815-hydroxylysine
Modified residuei717 – 7171Hydroxyproline
Modified residuei720 – 7201Hydroxyproline
Modified residuei726 – 7261Hydroxyproline
Modified residuei732 – 7321Hydroxyproline
Modified residuei744 – 74415-hydroxylysine
Modified residuei750 – 7501Hydroxyproline
Modified residuei756 – 7561Hydroxyproline
Modified residuei762 – 7621Hydroxyproline
Modified residuei765 – 7651Hydroxyproline
Modified residuei771 – 7711Hydroxyproline
Modified residuei774 – 77415-hydroxylysine
Modified residuei780 – 7801Hydroxyproline
Modified residuei789 – 7891Hydroxyproline
Modified residuei795 – 79515-hydroxylysine
Modified residuei804 – 80415-hydroxylysine
Modified residuei807 – 80715-hydroxylysine
Modified residuei810 – 81015-hydroxylysine
Modified residuei816 – 8161Hydroxyproline
Modified residuei819 – 81915-hydroxylysine
Modified residuei834 – 8341Hydroxyproline
Modified residuei846 – 84615-hydroxylysine
Modified residuei861 – 8611Hydroxyproline
Modified residuei864 – 86415-hydroxylysine
Modified residuei870 – 8701Hydroxyproline
Modified residuei873 – 8731Hydroxyproline
Modified residuei876 – 8761Hydroxyproline
Modified residuei882 – 88215-hydroxylysine
Modified residuei888 – 8881Hydroxyproline
Modified residuei891 – 8911Hydroxyproline
Modified residuei897 – 89715-hydroxylysine
Modified residuei903 – 9031Hydroxyproline
Modified residuei906 – 9061Hydroxyproline
Modified residuei930 – 9301Hydroxyproline
Modified residuei945 – 9451Hydroxyproline
Modified residuei1017 – 10171Hydroxyproline
Modified residuei1020 – 10201Hydroxyproline
Modified residuei1023 – 10231Hydroxyproline
Modified residuei1029 – 10291Hydroxyproline
Modified residuei1221 – 12211Hydroxyproline
Modified residuei1224 – 12241Hydroxyproline
Modified residuei1467 – 14671Hydroxyproline
Modified residuei1470 – 14701Hydroxyproline
Modified residuei1601 – 16011Sulfotyrosine Reviewed prediction
Modified residuei1604 – 16041Sulfotyrosine Reviewed prediction
Disulfide bondi1639 ↔ 1671 By similarity
Disulfide bondi1645 – 1645Interchain (with C-1662) By similarity
Disulfide bondi1662 – 1662Interchain (with C-1645) By similarity
Disulfide bondi1680 ↔ 1835 By similarity
Disulfide bondi1746 ↔ 1789 By similarity

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.
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

ArrayExpressiP20908.
BgeeiP20908.
CleanExiHS_COL5A1.
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. 8 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini72 – 244173Laminin G-like
Add
BLAST
Domaini1609 – 1837229Fibrillar collagen NC1
Add
BLAST

Region

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

Sequence similaritiesi

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000085654.
HOVERGENiHBG004933.
KOiK06236.
OMAiPIGVVQM.
OrthoDBiEOG7XPZ4W.
PhylomeDBiP20908.
TreeFamiTF323987.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR008160. Collagen.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
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

MDVHTRWKAR SALRPGAPLL PPLLLLLLWA PPPSRAAQPA DLLKVLDFHN     50
LPDGITKTTG FCATRRSSKG PDVAYRVTKD AQLSAPTKQL YPASAFPEDF 100
SILTTVKAKK GSQAFLVSIY NEQGIQQIGL ELGRSPVFLY EDHTGKPGPE 150
DYPLFRGINL SDGKWHRIAL SVHKKNVTLI LDCKKKTTKF LDRSDHPMID 200
INGIIVFGTR ILDEEVFEGD IQQLLFVSDH RAAYDYCEHY SPDCDTAVPD 250
TPQSQDPNPD EYYTEGDGEG ETYYYEYPYY EDPEDLGKEP TPSKKPVEAA 300
KETTEVPEEL TPTPTEAAPM PETSEGAGKE EDVGIGDYDY VPSEDYYTPS 350
PYDDLTYGEG EENPDQPTDP GAGAEIPTST ADTSNSSNPA PPPGEGADDL 400
EGEFTEETIR NLDENYYDPY YDPTSSPSEI GPGMPANQDT IYEGIGGPRG 450
EKGQKGEPAI IEPGMLIEGP PGPEGPAGLP GPPGTMGPTG QVGDPGERGP 500
PGRPGLPGAD GLPGPPGTML MLPFRFGGGG DAGSKGPMVS AQESQAQAIL 550
QQARLALRGP AGPMGLTGRP GPVGPPGSGG LKGEPGDVGP QGPRGVQGPP 600
GPAGKPGRRG RAGSDGARGM PGQTGPKGDR GFDGLAGLPG EKGHRGDPGP 650
SGPPGPPGDD GERGDDGEVG PRGLPGEPGP RGLLGPKGPP GPPGPPGVTG 700
MDGQPGPKGN VGPQGEPGPP GQQGNPGAQG LPGPQGAIGP PGEKGPLGKP 750
GLPGMPGADG PPGHPGKEGP PGEKGGQGPP GPQGPIGYPG PRGVKGADGI 800
RGLKGTKGEK GEDGFPGFKG DMGIKGDRGE IGPPGPRGED GPEGPKGRGG 850
PNGDPGPLGP PGEKGKLGVP GLPGYPGRQG PKGSIGFPGF PGANGEKGGR 900
GTPGKPGPRG QRGPTGPRGE RGPRGITGKP GPKGNSGGDG PAGPPGERGP 950
NGPQGPTGFP GPKGPPGPPG KDGLPGHPGQ RGETGFQGKT GPPGPPGVVG 1000
PQGPTGETGP MGERGHPGPP GPPGEQGLPG LAGKEGTKGD PGPAGLPGKD 1050
GPPGLRGFPG DRGLPGPVGA LGLKGNEGPP GPPGPAGSPG ERGPAGAAGP 1100
IGIPGRPGPQ GPPGPAGEKG APGEKGPQGP AGRDGLQGPV GLPGPAGPVG 1150
PPGEDGDKGE IGEPGQKGSK GDKGEQGPPG PTGPQGPIGQ PGPSGADGEP 1200
GPRGQQGLFG QKGDEGPRGF PGPPGPVGLQ GLPGPPGEKG ETGDVGQMGP 1250
PGPPGPRGPS GAPGADGPQG PPGGIGNPGA VGEKGEPGEA GEPGLPGEGG 1300
PPGPKGERGE KGESGPSGAA GPPGPKGPPG DDGPKGSPGP VGFPGDPGPP 1350
GEPGPAGQDG PPGDKGDDGE PGQTGSPGPT GEPGPSGPPG KRGPPGPAGP 1400
EGRQGEKGAK GEAGLEGPPG KTGPIGPQGA PGKPGPDGLR GIPGPVGEQG 1450
LPGSPGPDGP PGPMGPPGLP GLKGDSGPKG EKGHPGLIGL IGPPGEQGEK 1500
GDRGLPGPQG SSGPKGEQGI TGPSGPIGPP GPPGLPGPPG PKGAKGSSGP 1550
TGPKGEAGHP GPPGPPGPPG EVIQPLPIQA SRTRRNIDAS QLLDDGNGEN 1600
YVDYADGMEE IFGSLNSLKL EIEQMKRPLG TQQNPARTCK DLQLCHPDFP 1650
DGEYWVDPNQ GCSRDSFKVY CNFTAGGSTC VFPDKKSEGA RITSWPKENP 1700
GSWFSEFKRG KLLSYVDAEG NPVGVVQMTF LRLLSASAHQ NVTYHCYQSV 1750
AWQDAATGSY DKALRFLGSN DEEMSYDNNP YIRALVDGCA TKKGYQKTVL 1800
EIDTPKVEQV PIVDIMFNDF GEASQKFGFE VGPACFMG 1838
Length:1,838
Mass (Da):183,560
Last modified:September 13, 2005 - v3
Checksum:i8F18AB0B91B3A0C7
GO

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 832QL → HV in AAA59993. 1 Publication
Sequence conflicti390 – 3901A → R in AAA59993. 1 Publication
Sequence conflicti641 – 6411E → G AA sequence 1 Publication
Sequence conflicti650 – 6501P → L AA sequence 1 Publication
Sequence conflicti663 – 6631R → E AA sequence 1 Publication
Sequence conflicti668 – 6681E → Q AA sequence 1 Publication
Sequence conflicti677 – 6771E → K in BAA14323. 1 Publication
Sequence conflicti677 – 6771E → Q AA sequence 1 Publication
Sequence conflicti684 – 6841L → P AA sequence 1 Publication
Sequence conflicti692 – 6998PPGPPGVT → VTGEPGAP AA sequence 1 Publication
Sequence conflicti727 – 7271G → Q AA sequence 1 Publication
Sequence conflicti741 – 7411P → L AA sequence 1 Publication
Sequence conflicti747 – 7471L → Q AA sequence 1 Publication
Sequence conflicti753 – 7531P → A AA sequence 1 Publication
Sequence conflicti759 – 7591D → N AA sequence 1 Publication
Sequence conflicti776 – 7772GQ → QK AA sequence 1 Publication
Sequence conflicti849 – 8557GGPNGDP → IGPPGPR AA sequence 1 Publication
Sequence conflicti894 – 8941N → D AA sequence 1 Publication
Sequence conflicti1295 – 12995LPGEG → PSGRS in BAA14323. 1 Publication
Sequence conflicti1554 – 15541K → R in BAA14323. 1 Publication
Sequence conflicti1813 – 18131V → A in AAA59993. 1 Publication

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...

Protein-protein interaction databases

BioGridi 107686. 8 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.
HOGENOMi HOG000085654.
HOVERGENi HBG004933.
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

ArrayExpressi P20908.
Bgeei P20908.
CleanExi HS_COL5A1.
Genevestigatori P20908.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR008160. Collagen.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
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: September 3, 2014
This is version 162 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

Similar proteinsi