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P05997

- CO5A2_HUMAN

UniProt

P05997 - CO5A2_HUMAN

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Protein

Collagen alpha-2(V) chain

Gene

COL5A2

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1314 – 13141CalciumBy similarity
Metal bindingi1316 – 13161CalciumBy similarity
Metal bindingi1317 – 13171Calcium; via carbonyl oxygenBy similarity
Metal bindingi1322 – 13221CalciumBy similarity

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: InterPro
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. axon guidance Source: Reactome
  2. cellular response to amino acid stimulus Source: Ensembl
  3. collagen catabolic process Source: Reactome
  4. collagen fibril organization Source: UniProtKB
  5. extracellular matrix disassembly Source: Reactome
  6. extracellular matrix organization Source: Reactome
  7. eye morphogenesis Source: UniProtKB
  8. negative regulation of endodermal cell differentiation Source: UniProtKB
  9. skeletal system development Source: Ensembl
  10. skin development Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calcium, 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-2(V) chain
Gene namesi
Name:COL5A2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:2210. COL5A2.

Subcellular locationi

Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

GO - Cellular componenti

  1. collagen type V trimer Source: UniProtKB
  2. endoplasmic reticulum lumen Source: Reactome
  3. extracellular matrix Source: UniProtKB
  4. extracellular region Source: Reactome
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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 varianti963 – 9631G → R in EDS2. 1 Publication
VAR_013588

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.
PharmGKBiPA26725.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Add
BLAST
Chaini27 – 12291203Collagen alpha-2(V) chainPRO_0000005830Add
BLAST
Propeptidei1230 – 1499270C-terminal propeptidePRO_0000005831Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei290 – 2901Hydroxyproline1 Publication
Modified residuei293 – 2931Hydroxyproline1 Publication
Modified residuei296 – 2961Hydroxyproline1 Publication
Modified residuei611 – 6111Hydroxyproline1 Publication
Modified residuei617 – 6171Hydroxyproline1 Publication
Modified residuei919 – 91913-hydroxyproline; partial1 Publication
Modified residuei1156 – 115613-hydroxyproline; partial1 Publication
Glycosylationi1262 – 12621N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1296 ↔ 1328PROSITE-ProRule annotation
Disulfide bondi1336 ↔ 1497PROSITE-ProRule annotation
Glycosylationi1400 – 14001N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1405 ↔ 1450PROSITE-ProRule annotation

Post-translational modificationi

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 LEPREL1.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

MaxQBiP05997.
PaxDbiP05997.
PRIDEiP05997.

PTM databases

PhosphoSiteiP05997.

Miscellaneous databases

PMAP-CutDBP05997.

Expressioni

Gene expression databases

BgeeiP05997.
ExpressionAtlasiP05997. baseline and differential.
GenevestigatoriP05997.

Organism-specific databases

HPAiHPA047922.

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.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A9Amodel-B561-581[»]
ProteinModelPortaliP05997.
SMRiP05997. Positions 35-96, 1284-1499.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 9759VWFCPROSITE-ProRule annotationAdd
BLAST
Domaini1266 – 1499234Fibrillar collagen NC1PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi506 – 5083Cell attachment siteSequence Analysis
Motifi944 – 9463Cell attachment siteSequence Analysis
Motifi1067 – 10693Cell attachment siteSequence Analysis
Motifi1070 – 10723Cell attachment siteSequence Analysis
Motifi1100 – 11023Cell attachment siteSequence Analysis
Motifi1127 – 11293Cell attachment siteSequence Analysis
Motifi1136 – 11383Cell attachment siteSequence Analysis

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 VWFC domain.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00760000118776.
HOVERGENiHBG004933.
InParanoidiP05997.
KOiK06236.
OMAiIGIRGQP.
OrthoDBiEOG7TJ3HH.
PhylomeDBiP05997.
TreeFamiTF344135.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 9 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEiPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P05997-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMANWAEARP LLILIVLLGQ FVSIKAQEED EDEGYGEEIA CTQNGQMYLN
60 70 80 90 100
RDIWKPAPCQ ICVCDNGAIL CDKIECQDVL DCADPVTPPG ECCPVCSQTP
110 120 130 140 150
GGGNTNFGRG RKGQKGEPGL VPVVTGIRGR PGPAGPPGSQ GPRGERGPKG
160 170 180 190 200
RPGPRGPQGI DGEPGVPGQP GAPGPPGHPS HPGPDGLSRP FSAQMAGLDE
210 220 230 240 250
KSGLGSQVGL MPGSVGPVGP RGPQGLQGQQ GGAGPTGPPG EPGDPGPMGP
260 270 280 290 300
IGSRGPEGPP GKPGEDGEPG RNGNPGEVGF AGSPGARGFP GAPGLPGLKG
310 320 330 340 350
HRGHKGLEGP KGEVGAPGSK GEAGPTGPMG AMGPLGPRGM PGERGRLGPQ
360 370 380 390 400
GAPGQRGAHG MPGKPGPMGP LGIPGSSGFP GNPGMKGEAG PTGARGPEGP
410 420 430 440 450
QGQRGETGPP GPVGSPGLPG AIGTDGTPGA KGPTGSPGTS GPPGSAGPPG
460 470 480 490 500
SPGPQGSTGP QGIRGQPGDP GVPGFKGEAG PKGEPGPHGI QGPIGPPGEE
510 520 530 540 550
GKRGPRGDPG TVGPPGPVGE RGAPGNRGFP GSDGLPGPKG AQGERGPVGS
560 570 580 590 600
SGPKGSQGDP GRPGEPGLPG ARGLTGNPGV QGPEGKLGPL GAPGEDGRPG
610 620 630 640 650
PPGSIGIRGQ PGSMGLPGPK GSSGDPGKPG EAGNAGVPGQ RGAPGKDGEV
660 670 680 690 700
GPSGPVGPPG LAGERGEQGP PGPTGFQGLP GPPGPPGEGG KPGDQGVPGD
710 720 730 740 750
PGAVGPLGPR GERGNPGERG EPGITGLPGE KGMAGGHGPD GPKGSPGPSG
760 770 780 790 800
TPGDTGPPGL QGMPGERGIA GTPGPKGDRG GIGEKGAEGT AGNDGARGLP
810 820 830 840 850
GPLGPPGPAG PTGEKGEPGP RGLVGPPGSR GNPGSRGENG PTGAVGFAGP
860 870 880 890 900
QGPDGQPGVK GEPGEPGQKG DAGSPGPQGL AGSPGPHGPN GVPGLKGGRG
910 920 930 940 950
TQGPPGATGF PGSAGRVGPP GPAGAPGPAG PLGEPGKEGP PGLRGDPGSH
960 970 980 990 1000
GRVGDRGPAG PPGGPGDKGD PGEDGQPGPD GPPGPAGTTG QRGIVGMPGQ
1010 1020 1030 1040 1050
RGERGMPGLP GPAGTPGKVG PTGATGDKGP PGPVGPPGSN GPVGEPGPEG
1060 1070 1080 1090 1100
PAGNDGTPGR DGAVGERGDR GDPGPAGLPG SQGAPGTPGP VGAPGDAGQR
1110 1120 1130 1140 1150
GDPGSRGPIG PPGRAGKRGL PGPQGPRGDK GDHGDRGDRG QKGHRGFTGL
1160 1170 1180 1190 1200
QGLPGPPGPN GEQGSAGIPG PFGPRGPPGP VGPSGKEGNP GPLGPIGPPG
1210 1220 1230 1240 1250
VRGSVGEAGP EGPPGEPGPP GPPGPPGHLT AALGDIMGHY DESMPDPLPE
1260 1270 1280 1290 1300
FTEDQAAPDD KNKTDPGVHA TLKSLSSQIE TMRSPDGSKK HPARTCDDLK
1310 1320 1330 1340 1350
LCHSAKQSGE YWIDPNQGSV EDAIKVYCNM ETGETCISAN PSSVPRKTWW
1360 1370 1380 1390 1400
ASKSPDNKPV WYGLDMNRGS QFAYGDHQSP NTAITQMTFL RLLSKEASQN
1410 1420 1430 1440 1450
ITYICKNSVG YMDDQAKNLK KAVVLKGAND LDIKAEGNIR FRYIVLQDTC
1460 1470 1480 1490
SKRNGNVGKT VFEYRTQNVA RLPIIDLAPV DVGGTDQEFG VEIGPVCFV
Length:1,499
Mass (Da):144,910
Last modified:April 3, 2007 - v3
Checksum:iE8C92BF5E749EC97
GO

Sequence cautioni

The sequence AAH43613.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAD92282.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence AAY24185.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti292 – 2921A → P AA sequence (PubMed:8181482)Curated
Sequence conflicti361 – 3611M → L in AAL13166. (PubMed:11566270)Curated
Sequence conflicti430 – 4301A → P in CAA75002. 1 PublicationCurated
Sequence conflicti430 – 4301A → P in AAA51859. (PubMed:2914927)Curated
Sequence conflicti430 – 4301A → P in CAA28454. (PubMed:3029669)Curated
Sequence conflicti463 – 4664IRGQ → NSGL in CAA75002. 1 PublicationCurated
Sequence conflicti463 – 4664IRGQ → NSGL in CAA28454. (PubMed:3029669)Curated
Sequence conflicti463 – 4631I → N in AAA51859. (PubMed:2914927)Curated
Sequence conflicti472 – 4743Missing in CAA75002. 1 PublicationCurated
Sequence conflicti472 – 4743Missing in CAA28454. (PubMed:3029669)Curated
Sequence conflicti512 – 5121V → L in CAA75002. 1 PublicationCurated
Sequence conflicti512 – 5121V → L in CAA28454. (PubMed:3029669)Curated
Sequence conflicti608 – 6081R → K in CAA75002. 1 PublicationCurated
Sequence conflicti608 – 6081R → K in CAA28454. (PubMed:3029669)Curated
Sequence conflicti613 – 6131S → T in CAA75002. 1 PublicationCurated
Sequence conflicti613 – 6131S → T in CAA28454. (PubMed:3029669)Curated
Sequence conflicti623 – 6231S → N in CAA75002. 1 PublicationCurated
Sequence conflicti623 – 6231S → N in CAA28454. (PubMed:3029669)Curated
Sequence conflicti635 – 6351A → P in CAA75002. 1 PublicationCurated
Sequence conflicti635 – 6351A → P in CAA28454. (PubMed:3029669)Curated
Sequence conflicti649 – 6491E → K in CAA75002. 1 PublicationCurated
Sequence conflicti649 – 6491E → K in CAA28454. (PubMed:3029669)Curated
Sequence conflicti653 – 6531S → Y in CAA75002. 1 PublicationCurated
Sequence conflicti653 – 6531S → Y in CAA28454. (PubMed:3029669)Curated
Sequence conflicti656 – 6561V → P in CAA75002. 1 PublicationCurated
Sequence conflicti656 – 6561V → P in CAA28454. (PubMed:3029669)Curated
Sequence conflicti662 – 6621A → R in CAA75002. 1 PublicationCurated
Sequence conflicti662 – 6621A → R in CAA28454. (PubMed:3029669)Curated
Sequence conflicti679 – 6791L → H in CAA75002. 1 PublicationCurated
Sequence conflicti679 – 6791L → H in CAA28454. (PubMed:3029669)Curated
Sequence conflicti700 – 7001D → G in CAA75002. 1 PublicationCurated
Sequence conflicti700 – 7001D → G in CAA28454. (PubMed:3029669)Curated
Sequence conflicti797 – 7971R → G in CAA75002. 1 PublicationCurated
Sequence conflicti797 – 7971R → G in CAA28454. (PubMed:3029669)Curated
Sequence conflicti811 – 8122PT → LL in CAA75002. 1 PublicationCurated
Sequence conflicti811 – 8122PT → LL in CAA28454. (PubMed:3029669)Curated
Sequence conflicti853 – 8531P → S in CAA75002. 1 PublicationCurated
Sequence conflicti853 – 8531P → S in CAA28454. (PubMed:3029669)Curated
Sequence conflicti943 – 9431L → P in CAA75002. 1 PublicationCurated
Sequence conflicti943 – 9431L → P in CAA28454. (PubMed:3029669)Curated
Sequence conflicti955 – 9551D → V in CAA75002. 1 PublicationCurated
Sequence conflicti955 – 9551D → V in CAA28454. (PubMed:3029669)Curated
Sequence conflicti1111 – 11122PP → HL in CAA75002. 1 PublicationCurated
Sequence conflicti1111 – 11122PP → HL in CAA28454. (PubMed:3029669)Curated
Sequence conflicti1111 – 11122PP → HL in AAA52007. (PubMed:2985598)Curated
Sequence conflicti1196 – 11961I → L in CAA75002. 1 PublicationCurated
Sequence conflicti1196 – 11961I → L in CAA28454. (PubMed:3029669)Curated
Sequence conflicti1196 – 11961I → L in AAA52007. (PubMed:2985598)Curated
Sequence conflicti1421 – 14211K → T in AAA52058. (PubMed:2411731)Curated
Sequence conflicti1441 – 14411F → S in AAA52058. (PubMed:2411731)Curated
Sequence conflicti1467 – 14671Q → E in AAA51858. (PubMed:3224983)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti460 – 4601P → S.
Corresponds to variant rs35830636 [ dbSNP | Ensembl ].
VAR_048799
Natural varianti512 – 5121V → A.1 Publication
Corresponds to variant rs35852101 [ dbSNP | Ensembl ].
VAR_057910
Natural varianti833 – 8331P → L.1 Publication
Corresponds to variant rs116298748 [ dbSNP | Ensembl ].
VAR_057911
Natural varianti956 – 9561R → P.
Corresponds to variant rs6434313 [ dbSNP | Ensembl ].
VAR_048800
Natural varianti963 – 9631G → R in EDS2. 1 Publication
VAR_013588
Natural varianti1230 – 12301T → S.1 Publication
VAR_057912
Natural varianti1432 – 14321D → V.1 Publication
VAR_057913

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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
, 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.
CCDSiCCDS33350.1.
PIRiA31427. CGHU2V.
RefSeqiNP_000384.2. NM_000393.3.
UniGeneiHs.445827.

Genome annotation databases

EnsembliENST00000374866; ENSP00000364000; ENSG00000204262.
GeneIDi1290.
KEGGihsa:1290.
UCSCiuc002uqk.3. human.

Polymorphism databases

DMDMi143811378.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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
, 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 .
CCDSi CCDS33350.1.
PIRi A31427. CGHU2V.
RefSeqi NP_000384.2. NM_000393.3.
UniGenei Hs.445827.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A9A model - B 561-581 [» ]
ProteinModelPortali P05997.
SMRi P05997. Positions 35-96, 1284-1499.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL2364188.

PTM databases

PhosphoSitei P05997.

Polymorphism databases

DMDMi 143811378.

Proteomic databases

MaxQBi P05997.
PaxDbi P05997.
PRIDEi P05997.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000374866 ; ENSP00000364000 ; ENSG00000204262 .
GeneIDi 1290.
KEGGi hsa:1290.
UCSCi uc002uqk.3. human.

Organism-specific databases

CTDi 1290.
GeneCardsi GC02M189861.
GeneReviewsi COL5A2.
HGNCi HGNC:2210. COL5A2.
HPAi HPA047922.
MIMi 120190. gene.
130000. phenotype.
130010. phenotype.
neXtProti NX_P05997.
Orphaneti 90309. Ehlers-Danlos syndrome type 1.
90318. Ehlers-Danlos syndrome type 2.
PharmGKBi PA26725.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00760000118776.
HOVERGENi HBG004933.
InParanoidi P05997.
KOi K06236.
OMAi IGIRGQP.
OrthoDBi EOG7TJ3HH.
PhylomeDBi P05997.
TreeFami TF344135.

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 COL5A2. human.
GeneWikii COL5A2.
GenomeRNAii 1290.
NextBioi 5223.
PMAP-CutDB P05997.
PROi P05997.
SOURCEi Search...

Gene expression databases

Bgeei P05997.
ExpressionAtlasi P05997. baseline and differential.
Genevestigatori P05997.

Family and domain databases

InterProi IPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view ]
Pfami PF01410. COLFI. 1 hit.
PF01391. Collagen. 9 hits.
PF00093. VWC. 1 hit.
[Graphical view ]
ProDomi PD002078. Fib_collagen_C. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view ]
PROSITEi PS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: PROTEIN SEQUENCE OF 288-297 AND 609-620, HYDROXYLATION AT PRO-290; PRO-293; PRO-296; PRO-611 AND PRO-617.
    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.

Entry informationi

Entry nameiCO5A2_HUMAN
AccessioniPrimary (citable) accession number: P05997
Secondary accession number(s): P78440
, Q13908, Q53WR4, Q59GR4, Q6LDJ5, Q7KZ55, Q86XF6, Q96QB0, Q96QB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 3, 2007
Last modified: October 29, 2014
This is version 167 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 2
    Human chromosome 2: 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