UniProtKB - P08572 (CO4A2_HUMAN)
Protein
Collagen alpha-2(IV) chain
Gene
COL4A2
Organism
Homo sapiens (Human)
Status
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: GO_Central
- extracellular matrix structural constituent conferring tensile strength Source: BHF-UCL
GO - Biological processi
- aging Source: Ensembl
- angiogenesis Source: UniProtKB-KW
- cellular response to transforming growth factor beta stimulus Source: Ensembl
- collagen-activated tyrosine kinase receptor signaling pathway Source: GO_Central
- endodermal cell differentiation Source: UniProtKB
- extracellular matrix organization Source: GO_Central
- negative regulation of angiogenesis Source: UniProtKB
- response to activity Source: Ensembl
- transcription, DNA-templated Source: Ensembl
Keywordsi
Biological process | Angiogenesis |
Enzyme and pathway databases
Reactomei | R-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-2243919 Crosslinking of collagen fibrils 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 R-HSA-8948216 Collagen chain trimerization |
SIGNORi | P08572 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:COL4A2 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:2203 COL4A2 |
MIMi | 120090 gene |
neXtProti | NX_P08572 |
Subcellular locationi
Extracellular region or secreted
Endoplasmic reticulum
- endoplasmic reticulum lumen Source: Reactome
Extracellular region or secreted
- collagen type IV trimer Source: GO_Central
- collagen-containing extracellular matrix Source: UniProtKB
- extracellular exosome Source: UniProtKB
- extracellular matrix Source: GO_Central
- extracellular region Source: Reactome
- extracellular space Source: GO_Central
Keywords - Cellular componenti
Basement membrane, Extracellular matrix, SecretedPathology & Biotechi
Involvement in diseasei
Brain small vessel disease 2 (BSVD2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant cerebrovascular disorder with variable manifestations reflecting the location and severity of the vascular defect. BSVD2 features include intracranial hemorrage, fluid-filled cysts or cavities within the cerebral hemispheres, delayed psychomotor development, hemiplegia, spasticity and seizures.
Related information in OMIMFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_067837 | 1037 | G → E in BSVD2. 1 PublicationCorresponds to variant dbSNP:rs387906603EnsemblClinVar. | 1 | |
Natural variantiVAR_067838 | 1152 | G → D in BSVD2; incomplete penetrance. 1 PublicationCorresponds to variant dbSNP:rs387906602EnsemblClinVar. | 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.
Related information in OMIMKeywords - Diseasei
Disease mutationOrganism-specific databases
DisGeNETi | 1284 |
MalaCardsi | COL4A2 |
MIMi | 614483 phenotype 614519 phenotype |
OpenTargetsi | ENSG00000134871 |
Orphaneti | 99810 Familial porencephaly |
PharmGKBi | PA26718 |
Miscellaneous databases
Pharosi | P08572 |
Chemistry databases
ChEMBLi | CHEMBL2364188 |
Polymorphism and mutation databases
BioMutai | COL4A2 |
DMDMi | 143811377 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 25 | Add BLAST | 25 | |
PropeptideiPRO_0000005824 | 26 – 183 | N-terminal propeptide (7S domain)Add BLAST | 158 | |
ChainiPRO_0000005825 | 184 – 1712 | Collagen alpha-2(IV) chainAdd BLAST | 1529 | |
ChainiPRO_0000283775 | 1486 – 1712 | CanstatinAdd BLAST | 227 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 138 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Disulfide bondi | 1504 ↔ 1593 | |||
Disulfide bondi | 1537 ↔ 1590 | |||
Disulfide bondi | 1549 ↔ 1555 | |||
Disulfide bondi | 1612 ↔ 1708 | |||
Disulfide bondi | 1646 ↔ 1705 | |||
Disulfide bondi | 1658 ↔ 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, HydroxylationProteomic databases
EPDi | P08572 |
jPOSTi | P08572 |
MassIVEi | P08572 |
MaxQBi | P08572 |
PaxDbi | P08572 |
PeptideAtlasi | P08572 |
PRIDEi | P08572 |
ProteomicsDBi | 52123 |
PTM databases
iPTMneti | P08572 |
PhosphoSitePlusi | P08572 |
SwissPalmi | P08572 |
Miscellaneous databases
PMAP-CutDBi | P08572 |
Expressioni
Gene expression databases
Bgeei | ENSG00000134871 Expressed in 238 organ(s), highest expression level in placenta |
ExpressionAtlasi | P08572 baseline and differential |
Genevisiblei | P08572 HS |
Organism-specific databases
HPAi | CAB010751 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
With | Entry | #Exp. | IntAct | Notes |
---|---|---|---|---|
P02462 | 2 | EBI-2432506,EBI-2432478 |
Protein-protein interaction databases
BioGridi | 107681, 42 interactors |
ComplexPortali | CPX-1723 Collagen type IV trimer variant 1 |
IntActi | P08572, 36 interactors |
MINTi | P08572 |
STRINGi | 9606.ENSP00000353654 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P08572 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P08572 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1489 – 1712 | Collagen IV NC1PROSITE-ProRule annotationAdd BLAST | 224 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 184 – 1484 | Triple-helical regionAdd BLAST | 1301 |
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
Keywords - Domaini
Collagen, Repeat, SignalPhylogenomic databases
eggNOGi | KOG3544 Eukaryota ENOG410XNMM LUCA |
GeneTreei | ENSGT00940000157234 |
HOGENOMi | HOG000085652 |
InParanoidi | P08572 |
KOi | K06237 |
OMAi | NPGTKGW |
OrthoDBi | 63831at2759 |
PhylomeDBi | P08572 |
TreeFami | TF344135 |
Family and domain databases
Gene3Di | 2.170.240.10, 1 hit |
InterProi | View protein in InterPro IPR008160 Collagen IPR001442 Collagen_IV_NC IPR036954 Collagen_IV_NC_sf IPR016187 CTDL_fold |
Pfami | View protein in Pfam PF01413 C4, 2 hits PF01391 Collagen, 17 hits |
SMARTi | View protein in SMART SM00111 C4, 2 hits |
SUPFAMi | SSF56436 SSF56436, 2 hits |
PROSITEi | View protein in PROSITE PS51403 NC1_IV, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 8 potential isoforms that are computationally mapped.Show allAlign All
P08572-1 [UniParc]FASTAAdd to basket
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
Computationally mapped potential isoform sequencesi
There are 8 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A3B3ITQ8 | A0A3B3ITQ8_HUMAN | Collagen alpha-2(IV) chain | COL4A2 | 361 | Annotation score: | ||
A2A352 | A2A352_HUMAN | Collagen alpha-2(IV) chain | COL4A2 | 102 | Annotation score: | ||
A0A087WY39 | A0A087WY39_HUMAN | Collagen alpha-2(IV) chain | COL4A2 | 311 | Annotation score: | ||
A0A3B3IT80 | A0A3B3IT80_HUMAN | Collagen alpha-2(IV) chain | COL4A2 | 121 | Annotation score: | ||
A0A3B3IS47 | A0A3B3IS47_HUMAN | Collagen alpha-2(IV) chain | COL4A2 | 166 | Annotation score: | ||
A0A3B3ITN7 | A0A3B3ITN7_HUMAN | Collagen alpha-2(IV) chain | COL4A2 | 79 | Annotation score: | ||
A0A3B3IRV2 | A0A3B3IRV2_HUMAN | Collagen alpha-2(IV) chain | COL4A2 | 93 | Annotation score: | ||
A0A3B3IS04 | A0A3B3IS04_HUMAN | Collagen alpha-2(IV) chain | COL4A2 | 47 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 471 | R → P in CAA29076 (PubMed:3345760).Curated | 1 | |
Sequence conflicti | 1041 | V → L in AAA52043 (PubMed:3692475).Curated | 1 | |
Sequence conflicti | 1419 | M → I in CAA29098 (PubMed:3582677).Curated | 1 | |
Sequence conflicti | 1575 | M → I in AAA58422 (PubMed:2439508).Curated | 1 | |
Sequence conflicti | 1636 | G → V in AAA52043 (PubMed:3692475).Curated | 1 | |
Sequence conflicti | 1663 | G → H AA sequence (PubMed:2844531).Curated | 1 | |
Sequence conflicti | 1701 | H → G AA sequence (PubMed:2844531).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_067551 | 192 | V → F Polymorphism; does not affect COL4A2 and COL4A1 secretion. 2 PublicationsCorresponds to variant dbSNP:rs62621885EnsemblClinVar. | 1 | |
Natural variantiVAR_048796 | 517 | R → K3 PublicationsCorresponds to variant dbSNP:rs7990383EnsemblClinVar. | 1 | |
Natural variantiVAR_048797 | 683 | G → A3 PublicationsCorresponds to variant dbSNP:rs3803230EnsemblClinVar. | 1 | |
Natural variantiVAR_067552 | 701 | K → R Polymorphism; does not affect COL4A2 and COL4A1 secretion. 2 PublicationsCorresponds to variant dbSNP:rs78829338EnsemblClinVar. | 1 | |
Natural variantiVAR_067836 | 718 | P → S Polymorphism; does not affect COL4A2 and COL4A1 secretion. 2 PublicationsCorresponds to variant dbSNP:rs9583500EnsemblClinVar. | 1 | |
Natural variantiVAR_067837 | 1037 | G → E in BSVD2. 1 PublicationCorresponds to variant dbSNP:rs387906603EnsemblClinVar. | 1 | |
Natural variantiVAR_067553 | 1109 | R → Q Polymorphism; does not affect COL4A2 and COL4A1 secretion. 1 PublicationCorresponds to variant dbSNP:rs184812559EnsemblClinVar. | 1 | |
Natural variantiVAR_067554 | 1123 | E → 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 dbSNP:rs117412802EnsemblClinVar. | 1 | |
Natural variantiVAR_067555 | 1150 | Q → 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 dbSNP:rs62621875EnsemblClinVar. | 1 | |
Natural variantiVAR_067838 | 1152 | G → D in BSVD2; incomplete penetrance. 1 PublicationCorresponds to variant dbSNP:rs387906602EnsemblClinVar. | 1 | |
Natural variantiVAR_067556 | 1389 | G → 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 Publication | 1 | |
Natural variantiVAR_067557 | 1399 | V → I2 PublicationsCorresponds to variant dbSNP:rs45520539EnsemblClinVar. | 1 | |
Natural variantiVAR_067558 | 1690 | A → 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 dbSNP:rs201105747EnsemblClinVar. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL139385 Genomic DNA No translation available. AL159153 Genomic DNA No translation available. AL161773 Genomic DNA No translation available. 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 |
CCDSi | CCDS41907.1 |
PIRi | A32024 CGHU2B |
RefSeqi | NP_001837.2, NM_001846.3 |
Genome annotation databases
Ensembli | ENST00000360467; ENSP00000353654; ENSG00000134871 |
GeneIDi | 1284 |
KEGGi | hsa:1284 |
UCSCi | uc001vqx.4 human |
Keywords - Coding sequence diversityi
PolymorphismSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL139385 Genomic DNA No translation available. AL159153 Genomic DNA No translation available. AL161773 Genomic DNA No translation available. 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 |
CCDSi | CCDS41907.1 |
PIRi | A32024 CGHU2B |
RefSeqi | NP_001837.2, NM_001846.3 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1LI1 | X-ray | 1.90 | C/F | 1485-1712 | [»] | |
5NAX | X-ray | 2.82 | C/E | 1485-1712 | [»] | |
5NB2 | X-ray | 2.50 | A/B | 1485-1712 | [»] | |
6MPX | X-ray | 1.90 | A | 1489-1709 | [»] | |
SMRi | P08572 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGridi | 107681, 42 interactors |
ComplexPortali | CPX-1723 Collagen type IV trimer variant 1 |
IntActi | P08572, 36 interactors |
MINTi | P08572 |
STRINGi | 9606.ENSP00000353654 |
Chemistry databases
ChEMBLi | CHEMBL2364188 |
PTM databases
iPTMneti | P08572 |
PhosphoSitePlusi | P08572 |
SwissPalmi | P08572 |
Polymorphism and mutation databases
BioMutai | COL4A2 |
DMDMi | 143811377 |
Proteomic databases
EPDi | P08572 |
jPOSTi | P08572 |
MassIVEi | P08572 |
MaxQBi | P08572 |
PaxDbi | P08572 |
PeptideAtlasi | P08572 |
PRIDEi | P08572 |
ProteomicsDBi | 52123 |
Genome annotation databases
Ensembli | ENST00000360467; ENSP00000353654; ENSG00000134871 |
GeneIDi | 1284 |
KEGGi | hsa:1284 |
UCSCi | uc001vqx.4 human |
Organism-specific databases
CTDi | 1284 |
DisGeNETi | 1284 |
GeneCardsi | COL4A2 |
HGNCi | HGNC:2203 COL4A2 |
HPAi | CAB010751 HPA029118 |
MalaCardsi | COL4A2 |
MIMi | 120090 gene 614483 phenotype 614519 phenotype |
neXtProti | NX_P08572 |
OpenTargetsi | ENSG00000134871 |
Orphaneti | 99810 Familial porencephaly |
PharmGKBi | PA26718 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG3544 Eukaryota ENOG410XNMM LUCA |
GeneTreei | ENSGT00940000157234 |
HOGENOMi | HOG000085652 |
InParanoidi | P08572 |
KOi | K06237 |
OMAi | NPGTKGW |
OrthoDBi | 63831at2759 |
PhylomeDBi | P08572 |
TreeFami | TF344135 |
Enzyme and pathway databases
Reactomei | R-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-2243919 Crosslinking of collagen fibrils 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 R-HSA-8948216 Collagen chain trimerization |
SIGNORi | P08572 |
Miscellaneous databases
ChiTaRSi | COL4A2 human |
EvolutionaryTracei | P08572 |
GeneWikii | COL4A2 |
GenomeRNAii | 1284 |
Pharosi | P08572 |
PMAP-CutDBi | P08572 |
PROi | PR:P08572 |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000134871 Expressed in 238 organ(s), highest expression level in placenta |
ExpressionAtlasi | P08572 baseline and differential |
Genevisiblei | P08572 HS |
Family and domain databases
Gene3Di | 2.170.240.10, 1 hit |
InterProi | View protein in InterPro IPR008160 Collagen IPR001442 Collagen_IV_NC IPR036954 Collagen_IV_NC_sf IPR016187 CTDL_fold |
Pfami | View protein in Pfam PF01413 C4, 2 hits PF01391 Collagen, 17 hits |
SMARTi | View protein in SMART SM00111 C4, 2 hits |
SUPFAMi | SSF56436 SSF56436, 2 hits |
PROSITEi | View protein in PROSITE PS51403 NC1_IV, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | CO4A2_HUMAN | |
Accessioni | P08572Primary (citable) accession number: P08572 Secondary accession number(s): Q14052 Q66K23 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1988 |
Last sequence update: | April 3, 2007 | |
Last modified: | November 13, 2019 | |
This is version 213 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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 proteomeDocuments
- Human chromosome 13
Human chromosome 13: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - SIMILARITY comments
Index of protein domains and families - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references