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P05997 (CO5A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-2(V) chain
Gene names
Name:COL5A2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1499 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. Type V collagen is a key determinant in the assembly of tissue-specific matrices By similarity.

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.

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-P) are hydroxylated in some or all of the chains. Probably 3-hydroxylated on Pro-919 and Pro-1156 by LEPREL1.

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.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.17

Sequence similarities

Belongs to the fibrillar collagen family.

Contains 1 fibrillar collagen NC1 domain.

Contains 1 VWFC domain.

Sequence caution

The sequence AAH43613.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAY24185.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence BAD92282.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

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

Traceable author statement. Source: Reactome

cellular response to amino acid stimulus

Inferred from electronic annotation. Source: Ensembl

collagen catabolic process

Traceable author statement. Source: Reactome

collagen fibril organization

Inferred from mutant phenotype Ref.15. 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

skeletal system development

Inferred from electronic annotation. Source: Ensembl

skin development

Inferred from mutant phenotype Ref.15. Source: UniProtKB

   Cellular_componentcollagen type V

Inferred from mutant phenotype Ref.15Ref.17. Source: UniProtKB

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular matrix

Non-traceable author statement PubMed 17666000. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

   Molecular_functionextracellular matrix structural constituent

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626
Chain27 – 12291203Collagen alpha-2(V) chain
PRO_0000005830
Propeptide1230 – 1499270C-terminal propeptide
PRO_0000005831

Regions

Domain39 – 9759VWFC
Domain1266 – 1499234Fibrillar collagen NC1
Motif506 – 5083Cell attachment site Potential
Motif944 – 9463Cell attachment site Potential
Motif1067 – 10693Cell attachment site Potential
Motif1070 – 10723Cell attachment site Potential
Motif1100 – 11023Cell attachment site Potential
Motif1127 – 11293Cell attachment site Potential
Motif1136 – 11383Cell attachment site Potential

Sites

Metal binding13141Calcium By similarity
Metal binding13161Calcium By similarity
Metal binding13171Calcium; via carbonyl oxygen By similarity
Metal binding13221Calcium By similarity

Amino acid modifications

Modified residue2901Hydroxyproline
Modified residue2931Hydroxyproline
Modified residue2961Hydroxyproline
Modified residue6111Hydroxyproline
Modified residue6171Hydroxyproline
Modified residue91913-hydroxyproline; partial Ref.16
Modified residue115613-hydroxyproline; partial Ref.16
Glycosylation12621N-linked (GlcNAc...) Potential
Glycosylation14001N-linked (GlcNAc...) Potential
Disulfide bond1296 ↔ 1328 By similarity
Disulfide bond1336 ↔ 1497 By similarity
Disulfide bond1405 ↔ 1450 By similarity

Natural variations

Natural variant4601P → S.
Corresponds to variant rs35830636 [ dbSNP | Ensembl ].
VAR_048799
Natural variant5121V → A. Ref.18
Corresponds to variant rs35852101 [ dbSNP | Ensembl ].
VAR_057910
Natural variant8331P → L. Ref.18
Corresponds to variant rs116298748 [ dbSNP | Ensembl ].
VAR_057911
Natural variant9561R → P.
Corresponds to variant rs6434313 [ dbSNP | Ensembl ].
VAR_048800
Natural variant9631G → R in EDS2. Ref.17
VAR_013588
Natural variant12301T → S. Ref.18
VAR_057912
Natural variant14321D → V. Ref.18
VAR_057913

Experimental info

Sequence conflict2921A → P AA sequence Ref.8
Sequence conflict3611M → L in AAL13166. Ref.5
Sequence conflict4301A → P in CAA75002. Ref.1
Sequence conflict4301A → P in AAA51859. Ref.4
Sequence conflict4301A → P in CAA28454. Ref.9
Sequence conflict463 – 4664IRGQ → NSGL in CAA75002. Ref.1
Sequence conflict463 – 4664IRGQ → NSGL in CAA28454. Ref.9
Sequence conflict4631I → N in AAA51859. Ref.4
Sequence conflict472 – 4743Missing in CAA75002. Ref.1
Sequence conflict472 – 4743Missing in CAA28454. Ref.9
Sequence conflict5121V → L in CAA75002. Ref.1
Sequence conflict5121V → L in CAA28454. Ref.9
Sequence conflict6081R → K in CAA75002. Ref.1
Sequence conflict6081R → K in CAA28454. Ref.9
Sequence conflict6131S → T in CAA75002. Ref.1
Sequence conflict6131S → T in CAA28454. Ref.9
Sequence conflict6231S → N in CAA75002. Ref.1
Sequence conflict6231S → N in CAA28454. Ref.9
Sequence conflict6351A → P in CAA75002. Ref.1
Sequence conflict6351A → P in CAA28454. Ref.9
Sequence conflict6491E → K in CAA75002. Ref.1
Sequence conflict6491E → K in CAA28454. Ref.9
Sequence conflict6531S → Y in CAA75002. Ref.1
Sequence conflict6531S → Y in CAA28454. Ref.9
Sequence conflict6561V → P in CAA75002. Ref.1
Sequence conflict6561V → P in CAA28454. Ref.9
Sequence conflict6621A → R in CAA75002. Ref.1
Sequence conflict6621A → R in CAA28454. Ref.9
Sequence conflict6791L → H in CAA75002. Ref.1
Sequence conflict6791L → H in CAA28454. Ref.9
Sequence conflict7001D → G in CAA75002. Ref.1
Sequence conflict7001D → G in CAA28454. Ref.9
Sequence conflict7971R → G in CAA75002. Ref.1
Sequence conflict7971R → G in CAA28454. Ref.9
Sequence conflict811 – 8122PT → LL in CAA75002. Ref.1
Sequence conflict811 – 8122PT → LL in CAA28454. Ref.9
Sequence conflict8531P → S in CAA75002. Ref.1
Sequence conflict8531P → S in CAA28454. Ref.9
Sequence conflict9431L → P in CAA75002. Ref.1
Sequence conflict9431L → P in CAA28454. Ref.9
Sequence conflict9551D → V in CAA75002. Ref.1
Sequence conflict9551D → V in CAA28454. Ref.9
Sequence conflict1111 – 11122PP → HL in CAA75002. Ref.1
Sequence conflict1111 – 11122PP → HL in CAA28454. Ref.9
Sequence conflict1111 – 11122PP → HL in AAA52007. Ref.11
Sequence conflict11961I → L in CAA75002. Ref.1
Sequence conflict11961I → L in CAA28454. Ref.9
Sequence conflict11961I → L in AAA52007. Ref.11
Sequence conflict14211K → T in AAA52058. Ref.13
Sequence conflict14411F → S in AAA52058. Ref.13
Sequence conflict14671Q → E in AAA51858. Ref.14

Sequences

Sequence LengthMass (Da)Tools
P05997 [UniParc].

Last modified April 3, 2007. Version 3.
Checksum: E8C92BF5E749EC97

FASTA1,499144,910
        10         20         30         40         50         60 
MMANWAEARP LLILIVLLGQ FVSIKAQEED EDEGYGEEIA CTQNGQMYLN RDIWKPAPCQ 

        70         80         90        100        110        120 
ICVCDNGAIL CDKIECQDVL DCADPVTPPG ECCPVCSQTP GGGNTNFGRG RKGQKGEPGL 

       130        140        150        160        170        180 
VPVVTGIRGR PGPAGPPGSQ GPRGERGPKG RPGPRGPQGI DGEPGVPGQP GAPGPPGHPS 

       190        200        210        220        230        240 
HPGPDGLSRP FSAQMAGLDE KSGLGSQVGL MPGSVGPVGP RGPQGLQGQQ GGAGPTGPPG 

       250        260        270        280        290        300 
EPGDPGPMGP IGSRGPEGPP GKPGEDGEPG RNGNPGEVGF AGSPGARGFP GAPGLPGLKG 

       310        320        330        340        350        360 
HRGHKGLEGP KGEVGAPGSK GEAGPTGPMG AMGPLGPRGM PGERGRLGPQ GAPGQRGAHG 

       370        380        390        400        410        420 
MPGKPGPMGP LGIPGSSGFP GNPGMKGEAG PTGARGPEGP QGQRGETGPP GPVGSPGLPG 

       430        440        450        460        470        480 
AIGTDGTPGA KGPTGSPGTS GPPGSAGPPG SPGPQGSTGP QGIRGQPGDP GVPGFKGEAG 

       490        500        510        520        530        540 
PKGEPGPHGI QGPIGPPGEE GKRGPRGDPG TVGPPGPVGE RGAPGNRGFP GSDGLPGPKG 

       550        560        570        580        590        600 
AQGERGPVGS SGPKGSQGDP GRPGEPGLPG ARGLTGNPGV QGPEGKLGPL GAPGEDGRPG 

       610        620        630        640        650        660 
PPGSIGIRGQ PGSMGLPGPK GSSGDPGKPG EAGNAGVPGQ RGAPGKDGEV GPSGPVGPPG 

       670        680        690        700        710        720 
LAGERGEQGP PGPTGFQGLP GPPGPPGEGG KPGDQGVPGD PGAVGPLGPR GERGNPGERG 

       730        740        750        760        770        780 
EPGITGLPGE KGMAGGHGPD GPKGSPGPSG TPGDTGPPGL QGMPGERGIA GTPGPKGDRG 

       790        800        810        820        830        840 
GIGEKGAEGT AGNDGARGLP GPLGPPGPAG PTGEKGEPGP RGLVGPPGSR GNPGSRGENG 

       850        860        870        880        890        900 
PTGAVGFAGP QGPDGQPGVK GEPGEPGQKG DAGSPGPQGL AGSPGPHGPN GVPGLKGGRG 

       910        920        930        940        950        960 
TQGPPGATGF PGSAGRVGPP GPAGAPGPAG PLGEPGKEGP PGLRGDPGSH GRVGDRGPAG 

       970        980        990       1000       1010       1020 
PPGGPGDKGD PGEDGQPGPD GPPGPAGTTG QRGIVGMPGQ RGERGMPGLP GPAGTPGKVG 

      1030       1040       1050       1060       1070       1080 
PTGATGDKGP PGPVGPPGSN GPVGEPGPEG PAGNDGTPGR DGAVGERGDR GDPGPAGLPG 

      1090       1100       1110       1120       1130       1140 
SQGAPGTPGP VGAPGDAGQR GDPGSRGPIG PPGRAGKRGL PGPQGPRGDK GDHGDRGDRG 

      1150       1160       1170       1180       1190       1200 
QKGHRGFTGL QGLPGPPGPN GEQGSAGIPG PFGPRGPPGP VGPSGKEGNP GPLGPIGPPG 

      1210       1220       1230       1240       1250       1260 
VRGSVGEAGP EGPPGEPGPP GPPGPPGHLT AALGDIMGHY DESMPDPLPE FTEDQAAPDD 

      1270       1280       1290       1300       1310       1320 
KNKTDPGVHA TLKSLSSQIE TMRSPDGSKK HPARTCDDLK LCHSAKQSGE YWIDPNQGSV 

      1330       1340       1350       1360       1370       1380 
EDAIKVYCNM ETGETCISAN PSSVPRKTWW ASKSPDNKPV WYGLDMNRGS QFAYGDHQSP 

      1390       1400       1410       1420       1430       1440 
NTAITQMTFL RLLSKEASQN ITYICKNSVG YMDDQAKNLK KAVVLKGAND LDIKAEGNIR 

      1450       1460       1470       1480       1490 
FRYIVLQDTC SKRNGNVGKT VFEYRTQNVA RLPIIDLAPV DVGGTDQEFG VEIGPVCFV 

« Hide

References

« Hide 'large scale' references
[1]Richards A.J.
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Amino-terminal propeptide of human pro-alpha 2(V) collagen conforms to the structural criteria of a fibrillar procollagen molecule."
Woodbury D., Benson-Chanda V., Ramirez F.
J. Biol. Chem. 264:2735-2738(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-463.
[5]"Genomic organization of the human COL3A1 and COL5A2 genes: COL5A2 has evolved differently than the other minor fibrillar collagen genes."
Valkkila M., Melkoniemi M., Kvist L., Kuivaniemi H., Tromp G., Ala-Kokko L.
Matrix Biol. 20:357-366(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-104 AND 153-1499.
[6]"Homology between alpha 2(V) and alpha 1(III) collagen promoters and evidence for negatively acting elements in the alpha 2(V) first intron and 5' flanking sequences."
Greenspan D.S., Lee S.T., Lee B.S., Hoffman G.G.
Gene Expr. 1:29-39(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
[7]"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 208-227.
Tissue: Placenta.
[8]"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 288-297 AND 609-620.
Tissue: Bone.
[9]"The pro alpha 2(V) collagen gene is evolutionarily related to the major fibrillar-forming collagens."
Weil D., Bernard M.P., Gargano S., Ramirez F.
Nucleic Acids Res. 15:181-198(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 398-1499.
[10]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 878-1499.
Tissue: Skin.
[11]"Partial covalent structure of the human alpha 2 type V collagen chain."
Myers J.C., Loidl H.R., Stolle C.A., Seyer J.M.
J. Biol. Chem. 260:5533-5541(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1005-1229, PROTEIN SEQUENCE OF 1006-1036.
[12]"Human alpha 1(III) and alpha 2(V) procollagen genes are located on the long arm of chromosome 2."
Emanuel B.S., Cannizzaro L.A., Seyer J.M., Myers J.C.
Proc. Natl. Acad. Sci. U.S.A. 82:3385-3389(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1006-1037.
[13]"Complete primary structure of the human alpha 2 type V procollagen COOH-terminal propeptide."
Myers J.C., Loidl H.R., Seyer J.M., Dion A.S.
J. Biol. Chem. 260:11216-11222(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1230-1499.
[14]"Genetic distance of two fibrillar collagen loci, COL3A1 and COL5A2, located on the long arm of human chromosome 2."
Tsipouras P., Schwartz R.C., Liddell A.C., Salkeld C.S., Weil D., Ramirez F.
Genomics 3:275-277(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1452-1499.
[15]"Mutations of the alpha2(V) chain of type V collagen impair matrix assembly and produce Ehlers-Danlos syndrome type I."
Michalickova K., Susic M., Willing M.C., Wenstrup R.J., Cole W.G.
Hum. Mol. Genet. 7:249-255(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN EDS1.
[16]"A role for prolyl 3-hydroxylase 2 in post-translational modification of fibril-forming collagens."
Fernandes R.J., Farnand A.W., Traeger G.R., Weis M.A., Eyre D.R.
J. Biol. Chem. 286:30662-30669(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: HYDROXYLATION AT PRO-919 AND PRO-1156, IDENTIFICATION BY MASS SPECTROMETRY.
[17]"A single base mutation in COL5A2 causes Ehlers-Danlos syndrome type II."
Richards A.J., Martin S., Nicholls A.C., Harrison J.B., Pope F.M., Burrows N.P.
J. Med. Genet. 35:846-848(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EDS2 ARG-963.
[18]"Sequence analysis of the COL5A2 gene in patients with spontaneous cervical artery dissections."
Grond-Ginsbach C., Wigger F., Morcher M., von Pein F., Grau A., Hausser I., Brandt T.
Neurology 58:1103-1105(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALA-512; LEU-833; SER-1230 AND VAL-1432.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y14690 mRNA. Translation: CAA75002.1.
AB209045 mRNA. Translation: BAD92282.1. Different initiation.
AC064833 Genomic DNA. No translation available.
AC133106 Genomic DNA. Translation: AAY24185.1. Sequence problems.
J04478 mRNA. Translation: AAA51859.1.
AY016288, AY016287 Genomic DNA. Translation: AAL13165.1.
AY016295 expand/collapse EMBL AC list , AY016289, AY016290, AY016291, AY016292, AY016293, AY016294 Genomic DNA. Translation: AAL13166.1.
M58529 Genomic DNA. Translation: AAC41699.1.
X04758 mRNA. Translation: CAA28454.1.
BC043613 mRNA. Translation: AAH43613.1. Different initiation.
M10956 mRNA. Translation: AAA52007.1.
M11135 mRNA. Translation: AAA51857.1.
M11718 mRNA. Translation: AAA52058.1.
J03051 Genomic DNA. Translation: AAA51858.1.
PIRCGHU2V. A31427.
RefSeqNP_000384.2. NM_000393.3.
UniGeneHs.445827.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A9Amodel-B561-581[»]
ProteinModelPortalP05997.
SMRP05997. Positions 35-96, 213-248, 1284-1499.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL2364188.

PTM databases

PhosphoSiteP05997.

Polymorphism databases

DMDM143811378.

Proteomic databases

PaxDbP05997.
PRIDEP05997.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374866; ENSP00000364000; ENSG00000204262.
GeneID1290.
KEGGhsa:1290.
UCSCuc002uqk.3. human.

Organism-specific databases

CTD1290.
GeneCardsGC02M189861.
HGNCHGNC:2210. COL5A2.
HPAHPA047922.
MIM120190. gene.
130000. phenotype.
130010. phenotype.
neXtProtNX_P05997.
Orphanet90309. Ehlers-Danlos syndrome type 1.
90318. Ehlers-Danlos syndrome type 2.
PharmGKBPA26725.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG004933.
InParanoidP05997.
KOK06236.
OMAPDHKPVW.
OrthoDBEOG7TJ3HH.
PhylomeDBP05997.
TreeFamTF344135.

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

ArrayExpressP05997.
BgeeP05997.
GenevestigatorP05997.

Family and domain databases

InterProIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]
PfamPF01410. COLFI. 1 hit.
PF01391. Collagen. 9 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOL5A2. human.
GeneWikiCOL5A2.
GenomeRNAi1290.
NextBio5223.
PMAP-CutDBP05997.
PROP05997.
SOURCESearch...

Entry information

Entry nameCO5A2_HUMAN
AccessionPrimary (citable) accession number: P05997
Secondary accession number(s): P78440 expand/collapse secondary AC list , Q13908, Q53WR4, Q59GR4, Q6LDJ5, Q7KZ55, Q86XF6, Q96QB0, Q96QB3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 3, 2007
Last modified: April 16, 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.

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SIMILARITY comments

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PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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

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