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Protein

Collagen alpha-2(IV) chain

Gene

COL4A2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.
Canstatin, a cleavage product corresponding to the collagen alpha 2(IV) NC1 domain, possesses both anti-angiogenic and anti-tumor cell activity. It inhibits proliferation and migration of endothelial cells, reduces mitochondrial membrane potential, and induces apoptosis. Specifically induces Fas-dependent apoptosis and activates procaspase-8 and -9 activity. Ligand for alphavbeta3 and alphavbeta5 integrins.

GO - Molecular functioni

  • extracellular matrix structural constituent Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Angiogenesis

Enzyme and pathway databases

BioCyciZFISH:ENSG00000134871-MONOMER.
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-2214320. Anchoring fibril formation.
R-HSA-3000157. Laminin interactions.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-3000480. Scavenging by Class A Receptors.
R-HSA-419037. NCAM1 interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-2(IV) chain
Cleaved into the following chain:
Gene namesi
Name:COL4A2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:2203. COL4A2.

Subcellular locationi

GO - Cellular componenti

  • collagen type IV trimer Source: UniProtKB
  • endoplasmic reticulum lumen Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: UniProtKB
  • extracellular region Source: Reactome
  • intracellular membrane-bounded organelle Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Porencephaly 2 (POREN2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA neurologic disorder characterized by a fluid-filled cysts or cavities within the cerebral hemispheres. Affected individuals typically have hemiplegia, seizures, and intellectual disability. Porencephaly type 2, or schizencephalic porencephaly, is usually symmetric and represents a primary defect in the development of the cerebral ventricles.
See also OMIM:614483
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0678371037G → E in POREN2. 1 PublicationCorresponds to variant rs387906603dbSNPEnsembl.1
Natural variantiVAR_0678381152G → D in POREN2; incomplete penetrance. 1 PublicationCorresponds to variant rs387906602dbSNPEnsembl.1
Intracerebral hemorrhage (ICH)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA pathological condition characterized by bleeding into one or both cerebral hemispheres including the basal ganglia and the cerebral cortex. It is often associated with hypertension and craniocerebral trauma. Intracerebral bleeding is a common cause of stroke.
See also OMIM:614519
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0675541123E → G Associated with ICH susceptibility; results in a significantly decreased extracellular-to-intracellular ratio of COL4A2 and COL4A1 proteins, indicating interference with the proper secretion of both these proteins. 1 PublicationCorresponds to variant rs117412802dbSNPEnsembl.1
Natural variantiVAR_0675551150Q → K Associated with ICH susceptibility; results in a significantly decreased extracellular-to-intracellular ratio of COL4A2 and COL4A1 proteins, indicating interference with the proper secretion of both these proteins. 1 PublicationCorresponds to variant rs62621875dbSNPEnsembl.1
Natural variantiVAR_0675581690A → T Associated with ICH susceptibility; results in a significantly decreased extracellular-to-intracellular ratio of COL4A2 and COL4A1 proteins, indicating interference with the proper secretion of both these proteins. 1 PublicationCorresponds to variant rs201105747dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi1284.
MalaCardsiCOL4A2.
MIMi614483. phenotype.
614519. phenotype.
OpenTargetsiENSG00000134871.
Orphaneti99810. Familial porencephaly.
PharmGKBiPA26718.

Chemistry databases

ChEMBLiCHEMBL2364188.

Polymorphism and mutation databases

BioMutaiCOL4A2.
DMDMi143811377.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Add BLAST25
PropeptideiPRO_000000582426 – 183N-terminal propeptide (7S domain)Add BLAST158
ChainiPRO_0000005825184 – 1712Collagen alpha-2(IV) chainAdd BLAST1529
ChainiPRO_00002837751486 – 1712CanstatinAdd BLAST227

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi138N-linked (GlcNAc...)1 Publication1
Disulfide bondi1504 ↔ 1593
Disulfide bondi1537 ↔ 1590
Disulfide bondi1549 ↔ 1555
Disulfide bondi1612 ↔ 1708
Disulfide bondi1646 ↔ 1705
Disulfide bondi1658 ↔ 1665

Post-translational modificationi

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens.
The trimeric structure of the NC1 domains is stabilized by covalent bonds between Lys and Met residues.By similarity
Proteolytic processing produces the C-terminal NC1 peptide, canstatin.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

EPDiP08572.
MaxQBiP08572.
PaxDbiP08572.
PeptideAtlasiP08572.
PRIDEiP08572.

PTM databases

iPTMnetiP08572.
PhosphoSitePlusiP08572.
SwissPalmiP08572.

Miscellaneous databases

PMAP-CutDBP08572.

Expressioni

Gene expression databases

BgeeiENSG00000134871.
CleanExiHS_COL4A2.
ExpressionAtlasiP08572. baseline and differential.
GenevisibleiP08572. HS.

Organism-specific databases

HPAiCAB010751.
HPA029118.

Interactioni

Subunit structurei

There are six type IV collagen isoforms, alpha 1(IV)-alpha 6(IV), each of which can form a triple helix structure with 2 other chains to generate type IV collagen network.

Binary interactionsi

WithEntry#Exp.IntActNotes
COL4A1P024622EBI-2432506,EBI-2432478

Protein-protein interaction databases

BioGridi107681. 37 interactors.
IntActiP08572. 19 interactors.
MINTiMINT-1180068.
STRINGi9606.ENSP00000353654.

Structurei

Secondary structure

11712
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1490 – 1495Combined sources6
Beta strandi1497 – 1500Combined sources4
Beta strandi1509 – 1522Combined sources14
Beta strandi1525 – 1528Combined sources4
Helixi1534 – 1536Combined sources3
Beta strandi1537 – 1540Combined sources4
Beta strandi1546 – 1550Combined sources5
Turni1551 – 1553Combined sources3
Beta strandi1554 – 1558Combined sources5
Beta strandi1563 – 1568Combined sources6
Helixi1580 – 1586Combined sources7
Beta strandi1589 – 1597Combined sources9
Beta strandi1599 – 1603Combined sources5
Beta strandi1605 – 1608Combined sources4
Beta strandi1616 – 1629Combined sources14
Beta strandi1635 – 1637Combined sources3
Helixi1643 – 1645Combined sources3
Beta strandi1646 – 1649Combined sources4
Beta strandi1655 – 1659Combined sources5
Turni1660 – 1663Combined sources4
Beta strandi1664 – 1666Combined sources3
Beta strandi1672 – 1677Combined sources6
Beta strandi1680 – 1684Combined sources5
Beta strandi1691 – 1694Combined sources4
Helixi1699 – 1701Combined sources3
Beta strandi1704 – 1710Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LI1X-ray1.90C/F1485-1712[»]
ProteinModelPortaliP08572.
SMRiP08572.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08572.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1489 – 1712Collagen IV NC1PROSITE-ProRule annotationAdd BLAST224

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni184 – 1484Triple-helical regionAdd BLAST1301

Domaini

Alpha chains of type IV collagen have a non-collagenous domain (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats in the long central triple-helical domain (which may cause flexibility in the triple helix), and a short N-terminal triple-helical 7S domain.

Sequence similaritiesi

Belongs to the type IV collagen family.PROSITE-ProRule annotation
Contains 1 collagen IV NC1 (C-terminal non-collagenous) domain.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
GeneTreeiENSGT00840000129673.
HOGENOMiHOG000085652.
HOVERGENiHBG004933.
InParanoidiP08572.
KOiK06237.
OMAiKGDSGWP.
OrthoDBiEOG091G0613.
PhylomeDBiP08572.
TreeFamiTF344135.

Family and domain databases

Gene3Di2.170.240.10. 1 hit.
InterProiIPR008160. Collagen.
IPR001442. Collagen_VI_NC.
IPR016187. CTDL_fold.
[Graphical view]
PfamiPF01413. C4. 2 hits.
PF01391. Collagen. 17 hits.
[Graphical view]
SMARTiSM00111. C4. 2 hits.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 2 hits.
PROSITEiPS51403. NC1_IV. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P08572-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRDQRAVAG PALRRWLLLG TVTVGFLAQS VLAGVKKFDV PCGGRDCSGG
60 70 80 90 100
CQCYPEKGGR GQPGPVGPQG YNGPPGLQGF PGLQGRKGDK GERGAPGVTG
110 120 130 140 150
PKGDVGARGV SGFPGADGIP GHPGQGGPRG RPGYDGCNGT QGDSGPQGPP
160 170 180 190 200
GSEGFTGPPG PQGPKGQKGE PYALPKEERD RYRGEPGEPG LVGFQGPPGR
210 220 230 240 250
PGHVGQMGPV GAPGRPGPPG PPGPKGQQGN RGLGFYGVKG EKGDVGQPGP
260 270 280 290 300
NGIPSDTLHP IIAPTGVTFH PDQYKGEKGS EGEPGIRGIS LKGEEGIMGF
310 320 330 340 350
PGLRGYPGLS GEKGSPGQKG SRGLDGYQGP DGPRGPKGEA GDPGPPGLPA
360 370 380 390 400
YSPHPSLAKG ARGDPGFPGA QGEPGSQGEP GDPGLPGPPG LSIGDGDQRR
410 420 430 440 450
GLPGEMGPKG FIGDPGIPAL YGGPPGPDGK RGPPGPPGLP GPPGPDGFLF
460 470 480 490 500
GLKGAKGRAG FPGLPGSPGA RGPKGWKGDA GECRCTEGDE AIKGLPGLPG
510 520 530 540 550
PKGFAGINGE PGRKGDRGDP GQHGLPGFPG LKGVPGNIGA PGPKGAKGDS
560 570 580 590 600
RTITTKGERG QPGVPGVPGM KGDDGSPGRD GLDGFPGLPG PPGDGIKGPP
610 620 630 640 650
GDPGYPGIPG TKGTPGEMGP PGLGLPGLKG QRGFPGDAGL PGPPGFLGPP
660 670 680 690 700
GPAGTPGQID CDTDVKRAVG GDRQEAIQPG CIGGPKGLPG LPGPPGPTGA
710 720 730 740 750
KGLRGIPGFA GADGGPGPRG LPGDAGREGF PGPPGFIGPR GSKGAVGLPG
760 770 780 790 800
PDGSPGPIGL PGPDGPPGER GLPGEVLGAQ PGPRGDAGVP GQPGLKGLPG
810 820 830 840 850
DRGPPGFRGS QGMPGMPGLK GQPGLPGPSG QPGLYGPPGL HGFPGAPGQE
860 870 880 890 900
GPLGLPGIPG REGLPGDRGD PGDTGAPGPV GMKGLSGDRG DAGFTGEQGH
910 920 930 940 950
PGSPGFKGID GMPGTPGLKG DRGSPGMDGF QGMPGLKGRP GFPGSKGEAG
960 970 980 990 1000
FFGIPGLKGL AGEPGFKGSR GDPGPPGPPP VILPGMKDIK GEKGDEGPMG
1010 1020 1030 1040 1050
LKGYLGAKGI QGMPGIPGLS GIPGLPGRPG HIKGVKGDIG VPGIPGLPGF
1060 1070 1080 1090 1100
PGVAGPPGIT GFPGFIGSRG DKGAPGRAGL YGEIGATGDF GDIGDTINLP
1110 1120 1130 1140 1150
GRPGLKGERG TTGIPGLKGF FGEKGTEGDI GFPGITGVTG VQGPPGLKGQ
1160 1170 1180 1190 1200
TGFPGLTGPP GSQGELGRIG LPGGKGDDGW PGAPGLPGFP GLRGIRGLHG
1210 1220 1230 1240 1250
LPGTKGFPGS PGSDIHGDPG FPGPPGERGD PGEANTLPGP VGVPGQKGDQ
1260 1270 1280 1290 1300
GAPGERGPPG SPGLQGFPGI TPPSNISGAP GDKGAPGIFG LKGYRGPPGP
1310 1320 1330 1340 1350
PGSAALPGSK GDTGNPGAPG TPGTKGWAGD SGPQGRPGVF GLPGEKGPRG
1360 1370 1380 1390 1400
EQGFMGNTGP TGAVGDRGPK GPKGDPGFPG APGTVGAPGI AGIPQKIAVQ
1410 1420 1430 1440 1450
PGTVGPQGRR GPPGAPGEMG PQGPPGEPGF RGAPGKAGPQ GRGGVSAVPG
1460 1470 1480 1490 1500
FRGDEGPIGH QGPIGQEGAP GRPGSPGLPG MPGRSVSIGY LLVKHSQTDQ
1510 1520 1530 1540 1550
EPMCPVGMNK LWSGYSLLYF EGQEKAHNQD LGLAGSCLAR FSTMPFLYCN
1560 1570 1580 1590 1600
PGDVCYYASR NDKSYWLSTT APLPMMPVAE DEIKPYISRC SVCEAPAIAI
1610 1620 1630 1640 1650
AVHSQDVSIP HCPAGWRSLW IGYSFLMHTA AGDEGGGQSL VSPGSCLEDF
1660 1670 1680 1690 1700
RATPFIECNG GRGTCHYYAN KYSFWLTTIP EQSFQGSPSA DTLKAGLIRT
1710
HISRCQVCMK NL
Length:1,712
Mass (Da):167,553
Last modified:April 3, 2007 - v4
Checksum:iE0DABEEAB349D8AF
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti471R → P in CAA29076 (PubMed:3345760).Curated1
Sequence conflicti1041V → L in AAA52043 (PubMed:3692475).Curated1
Sequence conflicti1419M → I in CAA29098 (PubMed:3582677).Curated1
Sequence conflicti1575M → I in AAA58422 (PubMed:2439508).Curated1
Sequence conflicti1636G → V in AAA52043 (PubMed:3692475).Curated1
Sequence conflicti1663G → H AA sequence (PubMed:2844531).Curated1
Sequence conflicti1701H → G AA sequence (PubMed:2844531).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_067551192V → F Polymorphism; does not affect COL4A2 and COL4A1 secretion. 2 PublicationsCorresponds to variant rs62621885dbSNPEnsembl.1
Natural variantiVAR_048796517R → K.3 PublicationsCorresponds to variant rs7990383dbSNPEnsembl.1
Natural variantiVAR_048797683G → A.3 PublicationsCorresponds to variant rs3803230dbSNPEnsembl.1
Natural variantiVAR_067552701K → R Polymorphism; does not affect COL4A2 and COL4A1 secretion. 2 PublicationsCorresponds to variant rs78829338dbSNPEnsembl.1
Natural variantiVAR_067836718P → S Polymorphism; does not affect COL4A2 and COL4A1 secretion. 2 PublicationsCorresponds to variant rs9583500dbSNPEnsembl.1
Natural variantiVAR_0678371037G → E in POREN2. 1 PublicationCorresponds to variant rs387906603dbSNPEnsembl.1
Natural variantiVAR_0675531109R → Q Polymorphism; does not affect COL4A2 and COL4A1 secretion. 1 PublicationCorresponds to variant rs184812559dbSNPEnsembl.1
Natural variantiVAR_0675541123E → G Associated with ICH susceptibility; results in a significantly decreased extracellular-to-intracellular ratio of COL4A2 and COL4A1 proteins, indicating interference with the proper secretion of both these proteins. 1 PublicationCorresponds to variant rs117412802dbSNPEnsembl.1
Natural variantiVAR_0675551150Q → K Associated with ICH susceptibility; results in a significantly decreased extracellular-to-intracellular ratio of COL4A2 and COL4A1 proteins, indicating interference with the proper secretion of both these proteins. 1 PublicationCorresponds to variant rs62621875dbSNPEnsembl.1
Natural variantiVAR_0678381152G → D in POREN2; incomplete penetrance. 1 PublicationCorresponds to variant rs387906602dbSNPEnsembl.1
Natural variantiVAR_0675561389G → R Probable disease-associated mutation found in a family with porencephaly and small-vessel disease in the form of scattered white matter lesions; impairs COL4A2 and COL4A1 secretion; the mutant protein is retained in the endoplasmic reticulum. 1 Publication1
Natural variantiVAR_0675571399V → I.2 PublicationsCorresponds to variant rs45520539dbSNPEnsembl.1
Natural variantiVAR_0675581690A → T Associated with ICH susceptibility; results in a significantly decreased extracellular-to-intracellular ratio of COL4A2 and COL4A1 proteins, indicating interference with the proper secretion of both these proteins. 1 PublicationCorresponds to variant rs201105747dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL139385, AL159153, AL161773 Genomic DNA. Translation: CAI17005.2.
AL159153, AL139385, AL161773 Genomic DNA. Translation: CAH72050.2.
AL161773, AL139385, AL159153 Genomic DNA. Translation: CAH71366.2.
X05562 mRNA. Translation: CAA29076.1.
M36963 Genomic DNA. Translation: AAA53099.1.
J04217 Genomic DNA. Translation: AAA53097.1.
X12784 Genomic DNA. Translation: CAA31275.1.
M24766 mRNA. Translation: AAA52043.1.
X05610 mRNA. Translation: CAA29098.1.
BC080644 mRNA. Translation: AAH80644.1.
J02760 mRNA. Translation: AAA58422.1.
AF258350 mRNA. Translation: AAF72631.1.
AF400430 mRNA. Translation: AAK92479.1.
AY450357 mRNA. Translation: AAR20245.1.
AY455978 mRNA. Translation: AAR18250.1.
CCDSiCCDS41907.1.
PIRiA32024. CGHU2B.
RefSeqiNP_001837.2. NM_001846.3.
UniGeneiHs.508716.

Genome annotation databases

EnsembliENST00000360467; ENSP00000353654; ENSG00000134871.
GeneIDi1284.
KEGGihsa:1284.
UCSCiuc001vqx.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL139385, AL159153, AL161773 Genomic DNA. Translation: CAI17005.2.
AL159153, AL139385, AL161773 Genomic DNA. Translation: CAH72050.2.
AL161773, AL139385, AL159153 Genomic DNA. Translation: CAH71366.2.
X05562 mRNA. Translation: CAA29076.1.
M36963 Genomic DNA. Translation: AAA53099.1.
J04217 Genomic DNA. Translation: AAA53097.1.
X12784 Genomic DNA. Translation: CAA31275.1.
M24766 mRNA. Translation: AAA52043.1.
X05610 mRNA. Translation: CAA29098.1.
BC080644 mRNA. Translation: AAH80644.1.
J02760 mRNA. Translation: AAA58422.1.
AF258350 mRNA. Translation: AAF72631.1.
AF400430 mRNA. Translation: AAK92479.1.
AY450357 mRNA. Translation: AAR20245.1.
AY455978 mRNA. Translation: AAR18250.1.
CCDSiCCDS41907.1.
PIRiA32024. CGHU2B.
RefSeqiNP_001837.2. NM_001846.3.
UniGeneiHs.508716.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LI1X-ray1.90C/F1485-1712[»]
ProteinModelPortaliP08572.
SMRiP08572.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107681. 37 interactors.
IntActiP08572. 19 interactors.
MINTiMINT-1180068.
STRINGi9606.ENSP00000353654.

Chemistry databases

ChEMBLiCHEMBL2364188.

PTM databases

iPTMnetiP08572.
PhosphoSitePlusiP08572.
SwissPalmiP08572.

Polymorphism and mutation databases

BioMutaiCOL4A2.
DMDMi143811377.

Proteomic databases

EPDiP08572.
MaxQBiP08572.
PaxDbiP08572.
PeptideAtlasiP08572.
PRIDEiP08572.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360467; ENSP00000353654; ENSG00000134871.
GeneIDi1284.
KEGGihsa:1284.
UCSCiuc001vqx.4. human.

Organism-specific databases

CTDi1284.
DisGeNETi1284.
GeneCardsiCOL4A2.
H-InvDBHIX0011454.
HGNCiHGNC:2203. COL4A2.
HPAiCAB010751.
HPA029118.
MalaCardsiCOL4A2.
MIMi120090. gene.
614483. phenotype.
614519. phenotype.
neXtProtiNX_P08572.
OpenTargetsiENSG00000134871.
Orphaneti99810. Familial porencephaly.
PharmGKBiPA26718.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
GeneTreeiENSGT00840000129673.
HOGENOMiHOG000085652.
HOVERGENiHBG004933.
InParanoidiP08572.
KOiK06237.
OMAiKGDSGWP.
OrthoDBiEOG091G0613.
PhylomeDBiP08572.
TreeFamiTF344135.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000134871-MONOMER.
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-2214320. Anchoring fibril formation.
R-HSA-3000157. Laminin interactions.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-3000480. Scavenging by Class A Receptors.
R-HSA-419037. NCAM1 interactions.

Miscellaneous databases

ChiTaRSiCOL4A2. human.
EvolutionaryTraceiP08572.
GeneWikiiCOL4A2.
GenomeRNAii1284.
PMAP-CutDBP08572.
PROiP08572.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000134871.
CleanExiHS_COL4A2.
ExpressionAtlasiP08572. baseline and differential.
GenevisibleiP08572. HS.

Family and domain databases

Gene3Di2.170.240.10. 1 hit.
InterProiIPR008160. Collagen.
IPR001442. Collagen_VI_NC.
IPR016187. CTDL_fold.
[Graphical view]
PfamiPF01413. C4. 2 hits.
PF01391. Collagen. 17 hits.
[Graphical view]
SMARTiSM00111. C4. 2 hits.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 2 hits.
PROSITEiPS51403. NC1_IV. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCO4A2_HUMAN
AccessioniPrimary (citable) accession number: P08572
Secondary accession number(s): Q14052
, Q548C3, Q5VZA9, Q66K23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: April 3, 2007
Last modified: November 30, 2016
This is version 186 of the entry and version 4 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 13
    Human chromosome 13: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.