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Protein

Collagen alpha-2(V) chain

Gene

COL5A2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Metal bindingi1314CalciumBy similarity1
Metal bindingi1316CalciumBy similarity1
Metal bindingi1317Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1322CalciumBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

LigandCalcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-1442490 Collagen degradation
R-HSA-1474244 Extracellular matrix organization
R-HSA-1650814 Collagen biosynthesis and modifying enzymes
R-HSA-186797 Signaling by PDGF
R-HSA-2022090 Assembly of collagen fibrils and other multimeric structures
R-HSA-216083 Integrin cell surface interactions
R-HSA-3000170 Syndecan interactions
R-HSA-3000171 Non-integrin membrane-ECM interactions
R-HSA-3000178 ECM proteoglycans
R-HSA-419037 NCAM1 interactions
R-HSA-8874081 MET activates PTK2 signaling
R-HSA-8948216 Collagen chain trimerization

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-2(V) chain
Gene namesi
Name:COL5A2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000204262.11
HGNCiHGNC:2210 COL5A2
MIMi120190 gene
neXtProtiNX_P05997

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Ehlers-Danlos syndrome, classic type, 2 (EDSCL2)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of Ehlers-Danlos syndrome, a group of connective tissue disorders characterized by skin hyperextensibility, articular hypermobility, and tissue fragility. The main features of classic Ehlers-Danlos syndrome are joint hypermobility and dislocation, and fragile, bruisable skin. EDSCL2 inheritance is autosomal dominant.
See also OMIM:130010
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078424228G → R in EDSCL2. 1 Publication1
Natural variantiVAR_013588963G → R in EDSCL2. 1 PublicationCorresponds to variant dbSNP:rs1186550791Ensembl.1

Keywords - Diseasei

Disease mutation, Ehlers-Danlos syndrome

Organism-specific databases

DisGeNETi1290
GeneReviewsiCOL5A2
MalaCardsiCOL5A2
MIMi130010 phenotype
OpenTargetsiENSG00000204262
Orphaneti90309 Ehlers-Danlos syndrome type 1
90318 Ehlers-Danlos syndrome type 2
PharmGKBiPA26725

Chemistry databases

ChEMBLiCHEMBL2364188

Polymorphism and mutation databases

BioMutaiCOL5A2
DMDMi143811378

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Add BLAST26
ChainiPRO_000000583027 – 1229Collagen alpha-2(V) chainAdd BLAST1203
PropeptideiPRO_00000058311230 – 1499C-terminal propeptideAdd BLAST270

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei290Hydroxyproline1 Publication1
Modified residuei293Hydroxyproline1 Publication1
Modified residuei296Hydroxyproline1 Publication1
Modified residuei611Hydroxyproline1 Publication1
Modified residuei617Hydroxyproline1 Publication1
Modified residuei9193-hydroxyproline; partial1 Publication1
Modified residuei11563-hydroxyproline; partial1 Publication1
Glycosylationi1262N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1296 ↔ 1328PROSITE-ProRule annotation
Disulfide bondi1336 ↔ 1497PROSITE-ProRule annotation
Glycosylationi1400N-linked (GlcNAc...) asparagineSequence analysis1
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

EPDiP05997
MaxQBiP05997
PaxDbiP05997
PeptideAtlasiP05997
PRIDEiP05997
ProteomicsDBi51866

PTM databases

GlyConnecti1136
iPTMnetiP05997
PhosphoSitePlusiP05997

Miscellaneous databases

PMAP-CutDBiP05997

Expressioni

Gene expression databases

BgeeiENSG00000204262 Expressed in 221 organ(s), highest expression level in tibia
ExpressionAtlasiP05997 baseline and differential
GenevisibleiP05997 HS

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.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi107687, 4 interactors
ComplexPortaliCPX-1727 Collagen type V trimer variant 1
CPX-1728 Collagen type V trimer variant 2
CPX-1751 Collagen type XI trimer variant 2
CPX-1752 Collagen type XI trimer variant 3
IntActiP05997, 2 interactors
STRINGi9606.ENSP00000364000

Structurei

3D structure databases

ProteinModelPortaliP05997
SMRiP05997
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini39 – 97VWFCPROSITE-ProRule annotationAdd BLAST59
Domaini1266 – 1499Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST234

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi506 – 508Cell attachment siteSequence analysis3
Motifi944 – 946Cell attachment siteSequence analysis3
Motifi1067 – 1069Cell attachment siteSequence analysis3
Motifi1070 – 1072Cell attachment siteSequence analysis3
Motifi1100 – 1102Cell attachment siteSequence analysis3
Motifi1127 – 1129Cell attachment siteSequence analysis3
Motifi1136 – 1138Cell attachment siteSequence analysis3

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

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3544 Eukaryota
ENOG4110XTV LUCA
GeneTreeiENSGT00900000140789
HOVERGENiHBG004933
InParanoidiP05997
KOiK19721
OMAiPNAAITQ
OrthoDBiEOG091G03LV
PhylomeDBiP05997
TreeFamiTF344135

Family and domain databases

InterProiView protein in InterPro
IPR008160 Collagen
IPR000885 Fib_collagen_C
IPR001007 VWF_dom
PfamiView protein in Pfam
PF01410 COLFI, 1 hit
PF01391 Collagen, 5 hits
PF00093 VWC, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD002078 Fib_collagen_C, 1 hit
SMARTiView protein in SMART
SM00038 COLFI, 1 hit
SM00214 VWC, 1 hit
PROSITEiView protein in PROSITE
PS51461 NC1_FIB, 1 hit
PS01208 VWFC_1, 1 hit
PS50184 VWFC_2, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WYX9A0A087WYX9_HUMAN
Collagen alpha-2(V) chain
COL5A2
1,112Annotation score:

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti292A → P AA sequence (PubMed:8181482).Curated1
Sequence conflicti361M → L in AAL13166 (PubMed:11566270).Curated1
Sequence conflicti430A → P in CAA75002 (Ref. 1) Curated1
Sequence conflicti430A → P in AAA51859 (PubMed:2914927).Curated1
Sequence conflicti430A → P in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti463 – 466IRGQ → NSGL in CAA75002 (Ref. 1) Curated4
Sequence conflicti463 – 466IRGQ → NSGL in CAA28454 (PubMed:3029669).Curated4
Sequence conflicti463I → N in AAA51859 (PubMed:2914927).Curated1
Sequence conflicti472 – 474Missing in CAA75002 (Ref. 1) Curated3
Sequence conflicti472 – 474Missing in CAA28454 (PubMed:3029669).Curated3
Sequence conflicti512V → L in CAA75002 (Ref. 1) Curated1
Sequence conflicti512V → L in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti608R → K in CAA75002 (Ref. 1) Curated1
Sequence conflicti608R → K in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti613S → T in CAA75002 (Ref. 1) Curated1
Sequence conflicti613S → T in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti623S → N in CAA75002 (Ref. 1) Curated1
Sequence conflicti623S → N in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti635A → P in CAA75002 (Ref. 1) Curated1
Sequence conflicti635A → P in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti649E → K in CAA75002 (Ref. 1) Curated1
Sequence conflicti649E → K in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti653S → Y in CAA75002 (Ref. 1) Curated1
Sequence conflicti653S → Y in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti656V → P in CAA75002 (Ref. 1) Curated1
Sequence conflicti656V → P in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti662A → R in CAA75002 (Ref. 1) Curated1
Sequence conflicti662A → R in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti679L → H in CAA75002 (Ref. 1) Curated1
Sequence conflicti679L → H in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti700D → G in CAA75002 (Ref. 1) Curated1
Sequence conflicti700D → G in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti797R → G in CAA75002 (Ref. 1) Curated1
Sequence conflicti797R → G in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti811 – 812PT → LL in CAA75002 (Ref. 1) Curated2
Sequence conflicti811 – 812PT → LL in CAA28454 (PubMed:3029669).Curated2
Sequence conflicti853P → S in CAA75002 (Ref. 1) Curated1
Sequence conflicti853P → S in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti943L → P in CAA75002 (Ref. 1) Curated1
Sequence conflicti943L → P in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti955D → V in CAA75002 (Ref. 1) Curated1
Sequence conflicti955D → V in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti1111 – 1112PP → HL in CAA75002 (Ref. 1) Curated2
Sequence conflicti1111 – 1112PP → HL in CAA28454 (PubMed:3029669).Curated2
Sequence conflicti1111 – 1112PP → HL in AAA52007 (PubMed:2985598).Curated2
Sequence conflicti1196I → L in CAA75002 (Ref. 1) Curated1
Sequence conflicti1196I → L in CAA28454 (PubMed:3029669).Curated1
Sequence conflicti1196I → L in AAA52007 (PubMed:2985598).Curated1
Sequence conflicti1421K → T in AAA52058 (PubMed:2411731).Curated1
Sequence conflicti1441F → S in AAA52058 (PubMed:2411731).Curated1
Sequence conflicti1467Q → E in AAA51858 (PubMed:3224983).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078424228G → R in EDSCL2. 1 Publication1
Natural variantiVAR_048799460P → S. Corresponds to variant dbSNP:rs35830636EnsemblClinVar.1
Natural variantiVAR_057910512V → A1 PublicationCorresponds to variant dbSNP:rs35852101EnsemblClinVar.1
Natural variantiVAR_057911833P → L1 PublicationCorresponds to variant dbSNP:rs116298748EnsemblClinVar.1
Natural variantiVAR_048800956R → P. Corresponds to variant dbSNP:rs6434313EnsemblClinVar.1
Natural variantiVAR_013588963G → R in EDSCL2. 1 PublicationCorresponds to variant dbSNP:rs1186550791Ensembl.1
Natural variantiVAR_0579121230T → S1 PublicationCorresponds to variant dbSNP:rs767234623Ensembl.1
Natural variantiVAR_0579131432D → V1 PublicationCorresponds to variant dbSNP:rs141777954EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_000393.4
UniGeneiHs.445827

Genome annotation databases

EnsembliENST00000374866; ENSP00000364000; ENSG00000204262
GeneIDi1290
KEGGihsa:1290
UCSCiuc002uqk.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_000393.4
UniGeneiHs.445827

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A9Amodel-B561-581[»]
ProteinModelPortaliP05997
SMRiP05997
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107687, 4 interactors
ComplexPortaliCPX-1727 Collagen type V trimer variant 1
CPX-1728 Collagen type V trimer variant 2
CPX-1751 Collagen type XI trimer variant 2
CPX-1752 Collagen type XI trimer variant 3
IntActiP05997, 2 interactors
STRINGi9606.ENSP00000364000

Chemistry databases

ChEMBLiCHEMBL2364188

PTM databases

GlyConnecti1136
iPTMnetiP05997
PhosphoSitePlusiP05997

Polymorphism and mutation databases

BioMutaiCOL5A2
DMDMi143811378

Proteomic databases

EPDiP05997
MaxQBiP05997
PaxDbiP05997
PeptideAtlasiP05997
PRIDEiP05997
ProteomicsDBi51866

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374866; ENSP00000364000; ENSG00000204262
GeneIDi1290
KEGGihsa:1290
UCSCiuc002uqk.4 human

Organism-specific databases

CTDi1290
DisGeNETi1290
EuPathDBiHostDB:ENSG00000204262.11
GeneCardsiCOL5A2
GeneReviewsiCOL5A2
HGNCiHGNC:2210 COL5A2
MalaCardsiCOL5A2
MIMi120190 gene
130010 phenotype
neXtProtiNX_P05997
OpenTargetsiENSG00000204262
Orphaneti90309 Ehlers-Danlos syndrome type 1
90318 Ehlers-Danlos syndrome type 2
PharmGKBiPA26725
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3544 Eukaryota
ENOG4110XTV LUCA
GeneTreeiENSGT00900000140789
HOVERGENiHBG004933
InParanoidiP05997
KOiK19721
OMAiPNAAITQ
OrthoDBiEOG091G03LV
PhylomeDBiP05997
TreeFamiTF344135

Enzyme and pathway databases

ReactomeiR-HSA-1442490 Collagen degradation
R-HSA-1474244 Extracellular matrix organization
R-HSA-1650814 Collagen biosynthesis and modifying enzymes
R-HSA-186797 Signaling by PDGF
R-HSA-2022090 Assembly of collagen fibrils and other multimeric structures
R-HSA-216083 Integrin cell surface interactions
R-HSA-3000170 Syndecan interactions
R-HSA-3000171 Non-integrin membrane-ECM interactions
R-HSA-3000178 ECM proteoglycans
R-HSA-419037 NCAM1 interactions
R-HSA-8874081 MET activates PTK2 signaling
R-HSA-8948216 Collagen chain trimerization

Miscellaneous databases

ChiTaRSiCOL5A2 human
GeneWikiiCOL5A2
GenomeRNAii1290
PMAP-CutDBiP05997
PROiPR:P05997
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000204262 Expressed in 221 organ(s), highest expression level in tibia
ExpressionAtlasiP05997 baseline and differential
GenevisibleiP05997 HS

Family and domain databases

InterProiView protein in InterPro
IPR008160 Collagen
IPR000885 Fib_collagen_C
IPR001007 VWF_dom
PfamiView protein in Pfam
PF01410 COLFI, 1 hit
PF01391 Collagen, 5 hits
PF00093 VWC, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD002078 Fib_collagen_C, 1 hit
SMARTiView protein in SMART
SM00038 COLFI, 1 hit
SM00214 VWC, 1 hit
PROSITEiView protein in PROSITE
PS51461 NC1_FIB, 1 hit
PS01208 VWFC_1, 1 hit
PS50184 VWFC_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiCO5A2_HUMAN
AccessioniPrimary (citable) accession number: P05997
Secondary accession number(s): P78440
, Q13908, Q53WR4, Q59GR4, Q6LDJ5, Q7KZ55, Q86XF6, Q96QB0, Q96QB3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 3, 2007
Last modified: November 7, 2018
This is version 204 of the entry and version 3 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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