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P20908 (CO5A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-1(V) chain
Gene names
Name:COL5A1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1838 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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. Ref.8

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Domain

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.

Post-translational modification

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.

Involvement in disease

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. Ref.9 Ref.11 Ref.14 Ref.15

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. Ref.9 Ref.13

Sequence similarities

Belongs to the fibrillar collagen family.

Contains 1 fibrillar collagen NC1 domain.

Contains 1 laminin G-like domain.

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Ehlers-Danlos syndrome
   DomainCollagen
Repeat
Signal
   LigandCalcium
Heparin-binding
Metal-binding
   PTMDisulfide bond
Hydroxylation
Sulfation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Traceable author statement. Source: Reactome

blood vessel development

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from mutant phenotype PubMed 18305566. Source: UniProtKB

cell migration

Inferred from mutant phenotype PubMed 18305566. Source: UniProtKB

collagen biosynthetic process

Inferred from mutant phenotype PubMed 11278977PubMed 15095409. Source: UniProtKB

collagen catabolic process

Traceable author statement. Source: Reactome

collagen fibril organization

Inferred from mutant phenotype PubMed 11278977PubMed 15095409PubMed 9683580. Source: UniProtKB

extracellular fibril organization

Inferred from mutant phenotype PubMed 14970208. Source: UniProtKB

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

eye morphogenesis

Inferred from mutant phenotype PubMed 16431952. Source: UniProtKB

heart morphogenesis

Inferred from electronic annotation. Source: Ensembl

integrin biosynthetic process

Inferred from mutant phenotype PubMed 18305566. Source: UniProtKB

regulation of cellular component organization

Inferred from electronic annotation. Source: Ensembl

skin development

Inferred from mutant phenotype PubMed 9683580. Source: UniProtKB

tendon development

Inferred from electronic annotation. Source: Ensembl

wound healing, spreading of epidermal cells

Inferred from mutant phenotype PubMed 18305566. Source: UniProtKB

   Cellular_componentbasement membrane

Inferred from electronic annotation. Source: Ensembl

collagen type V trimer

Inferred from mutant phenotype PubMed 9683580. Source: UniProtKB

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular matrix

Inferred from mutant phenotype PubMed 14970208. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

   Molecular_functionextracellular matrix structural constituent

Inferred from electronic annotation. Source: Ensembl

heparin binding

Inferred from direct assay Ref.5. Source: UniProtKB

integrin binding

Non-traceable author statement PubMed 14970208. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

platelet-derived growth factor binding

Inferred from direct assay PubMed 8900172. Source: MGI

proteoglycan binding

Inferred from physical interaction Ref.8. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3737 Potential
Chain38 – 16051568Collagen alpha-1(V) chain
PRO_0000005756
Propeptide1606 – 1838233C-terminal propeptide
PRO_0000005757

Regions

Domain72 – 244173Laminin G-like
Domain1609 – 1837229Fibrillar collagen NC1
Region231 – 443213Nonhelical region
Region444 – 558115Interrupted collagenous region
Region559 – 15701012Triple-helical region
Region1571 – 160535Nonhelical region

Sites

Metal binding16571Calcium By similarity
Metal binding16591Calcium By similarity
Metal binding16601Calcium; via carbonyl oxygen By similarity
Metal binding16621Calcium; via carbonyl oxygen By similarity
Metal binding16651Calcium By similarity

Amino acid modifications

Modified residue2341Sulfotyrosine Potential
Modified residue2361Sulfotyrosine Potential
Modified residue2401Sulfotyrosine Potential
Modified residue2621Sulfotyrosine Potential
Modified residue2631Sulfotyrosine Potential
Modified residue3381Sulfotyrosine Potential
Modified residue3401Sulfotyrosine Potential
Modified residue3461Sulfotyrosine Potential
Modified residue3471Sulfotyrosine Potential
Modified residue4161Sulfotyrosine Potential
Modified residue4171Sulfotyrosine Potential
Modified residue4201Sulfotyrosine Potential
Modified residue4211Sulfotyrosine Potential
Modified residue5701Hydroxyproline
Modified residue5761Hydroxyproline
Modified residue6211Hydroxyproline
Modified residue62715-hydroxylysine
Modified residue6391Hydroxyproline
Modified residue64215-hydroxylysine
Modified residue6481Hydroxyproline
Modified residue6541Hydroxyproline
Modified residue6571Hydroxyproline
Modified residue6751Hydroxyproline
Modified residue6781Hydroxyproline
Modified residue6801Hydroxyproline
Modified residue6861Hydroxyproline
Modified residue6901Hydroxyproline
Modified residue6961Hydroxyproline
Modified residue7051Hydroxyproline
Modified residue70815-hydroxylysine
Modified residue7171Hydroxyproline
Modified residue7201Hydroxyproline
Modified residue7261Hydroxyproline
Modified residue7321Hydroxyproline
Modified residue74415-hydroxylysine
Modified residue7501Hydroxyproline
Modified residue7561Hydroxyproline
Modified residue7621Hydroxyproline
Modified residue7651Hydroxyproline
Modified residue7711Hydroxyproline
Modified residue77415-hydroxylysine
Modified residue7801Hydroxyproline
Modified residue7891Hydroxyproline
Modified residue79515-hydroxylysine
Modified residue80415-hydroxylysine
Modified residue80715-hydroxylysine
Modified residue81015-hydroxylysine
Modified residue8161Hydroxyproline
Modified residue81915-hydroxylysine
Modified residue8341Hydroxyproline
Modified residue84615-hydroxylysine
Modified residue8611Hydroxyproline
Modified residue86415-hydroxylysine
Modified residue8701Hydroxyproline
Modified residue8731Hydroxyproline
Modified residue8761Hydroxyproline
Modified residue88215-hydroxylysine
Modified residue8881Hydroxyproline
Modified residue8911Hydroxyproline
Modified residue89715-hydroxylysine
Modified residue9031Hydroxyproline
Modified residue9061Hydroxyproline
Modified residue9301Hydroxyproline
Modified residue9451Hydroxyproline
Modified residue10171Hydroxyproline
Modified residue10201Hydroxyproline
Modified residue10231Hydroxyproline
Modified residue10291Hydroxyproline
Modified residue12211Hydroxyproline
Modified residue12241Hydroxyproline
Modified residue14671Hydroxyproline
Modified residue14701Hydroxyproline
Modified residue16011Sulfotyrosine Potential
Modified residue16041Sulfotyrosine Potential
Disulfide bond1639 ↔ 1671 By similarity
Disulfide bond1645Interchain (with C-1662) By similarity
Disulfide bond1662Interchain (with C-1645) By similarity
Disulfide bond1680 ↔ 1835 By similarity
Disulfide bond1746 ↔ 1789 By similarity

Natural variations

Natural variant251L → P in EDS1 and EDS2; not or less efficiently secreted into the extracellular matrix. Ref.15
VAR_057902
Natural variant251L → R in EDS1 and EDS2; not or less efficiently secreted into the extracellular matrix. Ref.15
VAR_057903
Natural variant1141A → D Unclassified mutation. Ref.14
VAR_057904
Natural variant1921D → N Unclassified mutation. Ref.14
Corresponds to variant rs138579182 [ dbSNP | Ensembl ].
VAR_057905
Natural variant2291D → N Associated with increased risk of cervical artery dissection. Ref.10
VAR_057906
Natural variant3931P → S Unclassified mutation. Ref.14
VAR_057907
Natural variant5301G → S in EDS1 and EDS2. Ref.11 Ref.13 Ref.14
Corresponds to variant rs61735045 [ dbSNP | Ensembl ].
VAR_015412
Natural variant9081P → L Found in a renal cell carcinoma case; somatic mutation. Ref.16
VAR_064702
Natural variant9511N → S Unclassified mutation. Ref.14
Corresponds to variant rs61736966 [ dbSNP | Ensembl ].
VAR_057908
Natural variant14861G → C in EDS1 and EDS2. Ref.14
VAR_057909
Natural variant14891G → D in EDS1. Ref.11
VAR_015413
Natural variant16391C → S in EDS1. Ref.9
VAR_001808

Experimental info

Sequence conflict82 – 832QL → HV in AAA59993. Ref.2
Sequence conflict3901A → R in AAA59993. Ref.2
Sequence conflict6411E → G AA sequence Ref.4
Sequence conflict6501P → L AA sequence Ref.4
Sequence conflict6631R → E AA sequence Ref.4
Sequence conflict6681E → Q AA sequence Ref.4
Sequence conflict6771E → K in BAA14323. Ref.1
Sequence conflict6771E → Q AA sequence Ref.4
Sequence conflict6841L → P AA sequence Ref.4
Sequence conflict692 – 6998PPGPPGVT → VTGEPGAP AA sequence Ref.4
Sequence conflict7271G → Q AA sequence Ref.4
Sequence conflict7411P → L AA sequence Ref.4
Sequence conflict7471L → Q AA sequence Ref.4
Sequence conflict7531P → A AA sequence Ref.4
Sequence conflict7591D → N AA sequence Ref.4
Sequence conflict776 – 7772GQ → QK AA sequence Ref.4
Sequence conflict849 – 8557GGPNGDP → IGPPGPR AA sequence Ref.5
Sequence conflict8941N → D AA sequence Ref.5
Sequence conflict1295 – 12995LPGEG → PSGRS in BAA14323. Ref.1
Sequence conflict15541K → R in BAA14323. Ref.1
Sequence conflict18131V → A in AAA59993. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P20908 [UniParc].

Last modified September 13, 2005. Version 3.
Checksum: 8F18AB0B91B3A0C7

FASTA1,838183,560
        10         20         30         40         50         60 
MDVHTRWKAR SALRPGAPLL PPLLLLLLWA PPPSRAAQPA DLLKVLDFHN LPDGITKTTG 

        70         80         90        100        110        120 
FCATRRSSKG PDVAYRVTKD AQLSAPTKQL YPASAFPEDF SILTTVKAKK GSQAFLVSIY 

       130        140        150        160        170        180 
NEQGIQQIGL ELGRSPVFLY EDHTGKPGPE DYPLFRGINL SDGKWHRIAL SVHKKNVTLI 

       190        200        210        220        230        240 
LDCKKKTTKF LDRSDHPMID INGIIVFGTR ILDEEVFEGD IQQLLFVSDH RAAYDYCEHY 

       250        260        270        280        290        300 
SPDCDTAVPD TPQSQDPNPD EYYTEGDGEG ETYYYEYPYY EDPEDLGKEP TPSKKPVEAA 

       310        320        330        340        350        360 
KETTEVPEEL TPTPTEAAPM PETSEGAGKE EDVGIGDYDY VPSEDYYTPS PYDDLTYGEG 

       370        380        390        400        410        420 
EENPDQPTDP GAGAEIPTST ADTSNSSNPA PPPGEGADDL EGEFTEETIR NLDENYYDPY 

       430        440        450        460        470        480 
YDPTSSPSEI GPGMPANQDT IYEGIGGPRG EKGQKGEPAI IEPGMLIEGP PGPEGPAGLP 

       490        500        510        520        530        540 
GPPGTMGPTG QVGDPGERGP PGRPGLPGAD GLPGPPGTML MLPFRFGGGG DAGSKGPMVS 

       550        560        570        580        590        600 
AQESQAQAIL QQARLALRGP AGPMGLTGRP GPVGPPGSGG LKGEPGDVGP QGPRGVQGPP 

       610        620        630        640        650        660 
GPAGKPGRRG RAGSDGARGM PGQTGPKGDR GFDGLAGLPG EKGHRGDPGP SGPPGPPGDD 

       670        680        690        700        710        720 
GERGDDGEVG PRGLPGEPGP RGLLGPKGPP GPPGPPGVTG MDGQPGPKGN VGPQGEPGPP 

       730        740        750        760        770        780 
GQQGNPGAQG LPGPQGAIGP PGEKGPLGKP GLPGMPGADG PPGHPGKEGP PGEKGGQGPP 

       790        800        810        820        830        840 
GPQGPIGYPG PRGVKGADGI RGLKGTKGEK GEDGFPGFKG DMGIKGDRGE IGPPGPRGED 

       850        860        870        880        890        900 
GPEGPKGRGG PNGDPGPLGP PGEKGKLGVP GLPGYPGRQG PKGSIGFPGF PGANGEKGGR 

       910        920        930        940        950        960 
GTPGKPGPRG QRGPTGPRGE RGPRGITGKP GPKGNSGGDG PAGPPGERGP NGPQGPTGFP 

       970        980        990       1000       1010       1020 
GPKGPPGPPG KDGLPGHPGQ RGETGFQGKT GPPGPPGVVG PQGPTGETGP MGERGHPGPP 

      1030       1040       1050       1060       1070       1080 
GPPGEQGLPG LAGKEGTKGD PGPAGLPGKD GPPGLRGFPG DRGLPGPVGA LGLKGNEGPP 

      1090       1100       1110       1120       1130       1140 
GPPGPAGSPG ERGPAGAAGP IGIPGRPGPQ GPPGPAGEKG APGEKGPQGP AGRDGLQGPV 

      1150       1160       1170       1180       1190       1200 
GLPGPAGPVG PPGEDGDKGE IGEPGQKGSK GDKGEQGPPG PTGPQGPIGQ PGPSGADGEP 

      1210       1220       1230       1240       1250       1260 
GPRGQQGLFG QKGDEGPRGF PGPPGPVGLQ GLPGPPGEKG ETGDVGQMGP PGPPGPRGPS 

      1270       1280       1290       1300       1310       1320 
GAPGADGPQG PPGGIGNPGA VGEKGEPGEA GEPGLPGEGG PPGPKGERGE KGESGPSGAA 

      1330       1340       1350       1360       1370       1380 
GPPGPKGPPG DDGPKGSPGP VGFPGDPGPP GEPGPAGQDG PPGDKGDDGE PGQTGSPGPT 

      1390       1400       1410       1420       1430       1440 
GEPGPSGPPG KRGPPGPAGP EGRQGEKGAK GEAGLEGPPG KTGPIGPQGA PGKPGPDGLR 

      1450       1460       1470       1480       1490       1500 
GIPGPVGEQG LPGSPGPDGP PGPMGPPGLP GLKGDSGPKG EKGHPGLIGL IGPPGEQGEK 

      1510       1520       1530       1540       1550       1560 
GDRGLPGPQG SSGPKGEQGI TGPSGPIGPP GPPGLPGPPG PKGAKGSSGP TGPKGEAGHP 

      1570       1580       1590       1600       1610       1620 
GPPGPPGPPG EVIQPLPIQA SRTRRNIDAS QLLDDGNGEN YVDYADGMEE IFGSLNSLKL 

      1630       1640       1650       1660       1670       1680 
EIEQMKRPLG TQQNPARTCK DLQLCHPDFP DGEYWVDPNQ GCSRDSFKVY CNFTAGGSTC 

      1690       1700       1710       1720       1730       1740 
VFPDKKSEGA RITSWPKENP GSWFSEFKRG KLLSYVDAEG NPVGVVQMTF LRLLSASAHQ 

      1750       1760       1770       1780       1790       1800 
NVTYHCYQSV AWQDAATGSY DKALRFLGSN DEEMSYDNNP YIRALVDGCA TKKGYQKTVL 

      1810       1820       1830 
EIDTPKVEQV PIVDIMFNDF GEASQKFGFE VGPACFMG 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
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]"Diversity in the processing events at the N-terminus of type-V collagen."
Moradi-Ameli M., Rousseau J.C., Kleman J.P., Champliaud M.-F., Boutillon M.-M., Bernillon J., Wallach J.M., van der Rest M.
Eur. J. Biochem. 221:987-995(1994) [PubMed] [Europe PMC] [Abstract]
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]"Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma."
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M. expand/collapse author list , Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.
Nature 469:539-542(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LEU-908.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS6982.1.
PIRCGHU1V. S18802.
RefSeqNP_000084.3. NM_000093.4.
UniGeneHs.210283.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A89model-A/B/C904-924[»]
1A9Amodel-A/C904-924[»]
ProteinModelPortalP20908.
SMRP20908. Positions 73-208, 1628-1837.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107686. 8 interactions.
IntActP20908. 1 interaction.
STRING9606.ENSP00000360882.

Chemistry

ChEMBLCHEMBL2364188.

PTM databases

PhosphoSiteP20908.

Polymorphism databases

DMDM85687376.

Proteomic databases

MaxQBP20908.
PaxDbP20908.
PRIDEP20908.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371817; ENSP00000360882; ENSG00000130635.
GeneID1289.
KEGGhsa:1289.
UCSCuc004cfe.4. human.

Organism-specific databases

CTD1289.
GeneCardsGC09P137533.
GeneReviewsCOL5A1.
H-InvDBHIX0008519.
HGNCHGNC:2209. COL5A1.
HPACAB002743.
HPA030769.
MIM120215. gene.
130000. phenotype.
130010. phenotype.
neXtProtNX_P20908.
Orphanet90309. Ehlers-Danlos syndrome type 1.
90318. Ehlers-Danlos syndrome type 2.
PharmGKBPA26724.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000085654.
HOVERGENHBG004933.
KOK06236.
OMAPIGVVQM.
OrthoDBEOG7XPZ4W.
PhylomeDBP20908.
TreeFamTF323987.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.
REACT_196873. Extracellular matrix organization.

Gene expression databases

ArrayExpressP20908.
BgeeP20908.
CleanExHS_COL5A1.
GenevestigatorP20908.

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008160. Collagen.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000885. Fib_collagen_C.
IPR001791. Laminin_G.
[Graphical view]
PfamPF01410. COLFI. 1 hit.
PF01391. Collagen. 5 hits.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
ProDomPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00038. COLFI. 1 hit.
SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS51461. NC1_FIB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOL5A1. human.
GeneWikiCollagen,_type_V,_alpha_1.
GenomeRNAi1289.
NextBio5219.
PMAP-CutDBP20908.
PROP20908.
SOURCESearch...

Entry information

Entry nameCO5A1_HUMAN
AccessionPrimary (citable) accession number: P20908
Secondary accession number(s): Q15094, Q5SUX4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: September 13, 2005
Last modified: July 9, 2014
This is version 161 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM