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Protein

Integrin alpha-4

Gene

ITGA4

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

Functioni

Integrins alpha-4/beta-1 (VLA-4) and alpha-4/beta-7 are receptors for fibronectin. They recognize one or more domains within the alternatively spliced CS-1 and CS-5 regions of fibronectin. They are also receptors for VCAM1. Integrin alpha-4/beta-1 recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-4/beta-7 is also a receptor for MADCAM1. It recognizes the sequence L-D-T in MADCAM1. On activated endothelial cells integrin VLA-4 triggers homotypic aggregation for most VLA-4-positive leukocyte cell lines. It may also participate in cytolytic T-cell interactions with target cells. ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-dependent fractalkine signaling (PubMed:23125415). ITGA4:ITGB1 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ligand binding to site 1 (PubMed:18635536, PubMed:25398877).4 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi314 – 322Sequence analysis9
Calcium bindingi377 – 385Sequence analysis9
Calcium bindingi439 – 447Sequence analysis9

GO - Molecular functioni

  • antigen binding Source: Ensembl
  • cell adhesion molecule binding Source: UniProtKB
  • coreceptor activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • B cell differentiation Source: BHF-UCL
  • cell-matrix adhesion Source: UniProtKB
  • cell-matrix adhesion involved in ameboidal cell migration Source: UniProtKB
  • cellular response to cytokine stimulus Source: Ensembl
  • clathrin-dependent extracellular exosome endocytosis Source: Ensembl
  • diapedesis Source: Ensembl
  • endodermal cell differentiation Source: UniProtKB
  • extracellular matrix organization Source: Reactome
  • heterotypic cell-cell adhesion Source: UniProtKB
  • import into cell Source: Ensembl
  • integrin-mediated signaling pathway Source: UniProtKB-KW
  • leukocyte cell-cell adhesion Source: BHF-UCL
  • leukocyte migration Source: Reactome
  • leukocyte tethering or rolling Source: UniProtKB
  • negative regulation of protein homodimerization activity Source: UniProtKB
  • positive regulation of leukocyte tethering or rolling Source: Ensembl
  • positive regulation of T cell migration Source: Ensembl
  • receptor clustering Source: UniProtKB
  • regulation of immune response Source: Reactome
  • substrate adhesion-dependent cell spreading Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Integrin, Receptor

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000115232-MONOMER.
ReactomeiR-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-HSA-202733. Cell surface interactions at the vascular wall.
R-HSA-216083. Integrin cell surface interactions.
SignaLinkiP13612.
SIGNORiP13612.

Names & Taxonomyi

Protein namesi
Recommended name:
Integrin alpha-4
Alternative name(s):
CD49 antigen-like family member D
Integrin alpha-IV
VLA-4 subunit alpha
CD_antigen: CD49d
Gene namesi
Name:ITGA4
Synonyms:CD49D
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:6140. ITGA4.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini35 – 977ExtracellularSequence analysisAdd BLAST943
Transmembranei978 – 1001HelicalSequence analysisAdd BLAST24
Topological domaini1002 – 1032CytoplasmicSequence analysisAdd BLAST31

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • integrin alpha4-beta7 complex Source: UniProtKB
  • membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi222T → A: Blocks binding to PLA2G2A. 1 Publication1
Mutagenesisi223G → A: Blocks binding to PLA2G2A. 1 Publication1
Mutagenesisi590K → Q: Abolishes almost completely cleavage. 1 Publication1
Mutagenesisi591R → L: Abolishes completely cleavage. 1 Publication1
Mutagenesisi1021S → A: Abolishes phosphorylation. 1 Publication1
Mutagenesisi1021S → D: Reduces PXN binding. 1 Publication1
Mutagenesisi1024Y → A: Disrupts PXN binding. 1 Publication1

Organism-specific databases

DisGeNETi3676.
OpenTargetsiENSG00000115232.
PharmGKBiPA29940.

Chemistry databases

ChEMBLiCHEMBL278.
DrugBankiDB00108. Natalizumab.
DB06822. Tinzaparin.
DB09033. Vedolizumab.

Polymorphism and mutation databases

BioMutaiITGA4.
DMDMi311033436.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 331 PublicationAdd BLAST33
ChainiPRO_000001624434 – 1032Integrin alpha-4Add BLAST999

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi79N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi91 ↔ 101By similarity
Glycosylationi138N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi144 ↔ 165By similarity
Disulfide bondi183 ↔ 198By similarity
Glycosylationi229N-linked (GlcNAc...)Sequence analysis1
Glycosylationi480N-linked (GlcNAc...)1 Publication1
Disulfide bondi486 ↔ 495By similarity
Disulfide bondi501 ↔ 557By similarity
Glycosylationi518N-linked (GlcNAc...)1 Publication1
Glycosylationi538N-linked (GlcNAc...)1 Publication1
Disulfide bondi622 ↔ 627By similarity
Glycosylationi626N-linked (GlcNAc...)Sequence analysis1
Glycosylationi645N-linked (GlcNAc...)1 Publication1
Glycosylationi660N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi698 ↔ 711By similarity
Glycosylationi806N-linked (GlcNAc...)Sequence analysis1
Glycosylationi821N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi852 ↔ 890By similarity
Disulfide bondi897 ↔ 902By similarity
Modified residuei1021PhosphoserineCombined sources1 Publication1

Post-translational modificationi

Phosphorylation on Ser-1027 inhibits PXN binding.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei591 – 592Cleavage2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP13612.
MaxQBiP13612.
PaxDbiP13612.
PeptideAtlasiP13612.
PRIDEiP13612.

PTM databases

iPTMnetiP13612.
PhosphoSitePlusiP13612.

Expressioni

Gene expression databases

BgeeiENSG00000115232.
CleanExiHS_ITGA4.
ExpressionAtlasiP13612. baseline and differential.
GenevisibleiP13612. HS.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. The alpha subunit can sometimes be cleaved into two non-covalently associated fragments. Alpha-4 associates with either beta-1 or beta-7. Alpha-4 interacts with PXN, LPXN, and TGFB1I1/HIC5. Interacts with CSPG4 through CSPG4 chondroitin sulfate glycosaminoglycan. Interacts with JAML; integrin alpha-4/beta-1 may regulate leukocyte to endothelial cells adhesion by controlling JAML homodimerization. ITGA4:ITGB1 is found in a ternary complex with CX3CR1 and CX3CL1 (PubMed:23125415).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ITGB1P055564EBI-703044,EBI-703066
ITGB7P260106EBI-703044,EBI-702932
PXNP490233EBI-703044,EBI-702209
TGFB1I1O432942EBI-703044,EBI-1051449

GO - Molecular functioni

  • cell adhesion molecule binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109883. 509 interactors.
DIPiDIP-34971N.
IntActiP13612. 11 interactors.
MINTiMINT-4098849.
STRINGi9606.ENSP00000380227.

Chemistry databases

BindingDBiP13612.

Structurei

Secondary structure

11032
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi42 – 45Combined sources4
Beta strandi54 – 61Combined sources8
Beta strandi64 – 71Combined sources8
Beta strandi87 – 95Combined sources9
Beta strandi102 – 104Combined sources3
Beta strandi127 – 133Combined sources7
Beta strandi141 – 145Combined sources5
Turni152 – 156Combined sources5
Beta strandi165 – 168Combined sources4
Helixi174 – 176Combined sources3
Beta strandi178 – 180Combined sources3
Turni193 – 197Combined sources5
Beta strandi202 – 206Combined sources5
Beta strandi208 – 215Combined sources8
Helixi218 – 221Combined sources4
Beta strandi223 – 229Combined sources7
Turni230 – 233Combined sources4
Beta strandi234 – 237Combined sources4
Beta strandi253 – 258Combined sources6
Beta strandi267 – 272Combined sources6
Helixi275 – 277Combined sources3
Beta strandi280 – 286Combined sources7
Beta strandi288 – 298Combined sources11
Beta strandi308 – 313Combined sources6
Beta strandi318 – 320Combined sources3
Beta strandi322 – 327Combined sources6
Beta strandi332 – 334Combined sources3
Beta strandi338 – 344Combined sources7
Beta strandi346 – 349Combined sources4
Beta strandi351 – 353Combined sources3
Beta strandi381 – 383Combined sources3
Beta strandi386 – 390Combined sources5
Helixi393 – 396Combined sources4
Beta strandi398 – 403Combined sources6
Beta strandi415 – 419Combined sources5
Helixi420 – 422Combined sources3
Beta strandi429 – 438Combined sources10
Beta strandi440 – 445Combined sources6
Beta strandi447 – 452Combined sources6
Helixi453 – 455Combined sources3
Beta strandi457 – 461Combined sources5
Beta strandi466 – 474Combined sources9
Beta strandi495 – 505Combined sources11
Beta strandi511 – 522Combined sources12
Beta strandi532 – 534Combined sources3
Beta strandi536 – 538Combined sources3
Beta strandi542 – 554Combined sources13
Beta strandi556 – 564Combined sources9
Beta strandi575 – 583Combined sources9
Beta strandi610 – 617Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3V4PX-ray3.15A/C34-620[»]
3V4VX-ray3.10A/C34-620[»]
4HKCX-ray2.20B1003-1032[»]
5C7ZX-ray2.77B1008-1015[»]
5FPIX-ray2.77B1008-1015[»]
ProteinModelPortaliP13612.
SMRiP13612.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati35 – 100FG-GAP 1PROSITE-ProRule annotationAdd BLAST66
Repeati110 – 177FG-GAP 2PROSITE-ProRule annotationAdd BLAST68
Repeati185 – 237FG-GAP 3PROSITE-ProRule annotationAdd BLAST53
Repeati238 – 291FG-GAP 4PROSITE-ProRule annotationAdd BLAST54
Repeati292 – 351FG-GAP 5PROSITE-ProRule annotationAdd BLAST60
Repeati355 – 412FG-GAP 6PROSITE-ProRule annotationAdd BLAST58
Repeati416 – 478FG-GAP 7PROSITE-ProRule annotationAdd BLAST63

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi606 – 616SG1Add BLAST11
Motifi1003 – 1007GFFKR motif5

Domaini

The SG1 motif is involved in binding to chondroitin sulfate glycosaminoglycan and cell adhesion.1 Publication

Sequence similaritiesi

Belongs to the integrin alpha chain family.Curated
Contains 7 FG-GAP repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IPB2. Eukaryota.
ENOG410XTAR. LUCA.
GeneTreeiENSGT00760000118782.
HOGENOMiHOG000088626.
HOVERGENiHBG004538.
InParanoidiP13612.
KOiK06483.
OMAiEKQINCE.
OrthoDBiEOG091G011V.
PhylomeDBiP13612.
TreeFamiTF105391.

Family and domain databases

InterProiIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
IPR032695. Integrin_dom.
[Graphical view]
PfamiPF01839. FG-GAP. 2 hits.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSiPR01185. INTEGRINA.
SMARTiSM00191. Int_alpha. 5 hits.
[Graphical view]
SUPFAMiSSF69179. SSF69179. 3 hits.
PROSITEiPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P13612-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAWEARREPG PRRAAVRETV MLLLCLGVPT GRPYNVDTES ALLYQGPHNT
60 70 80 90 100
LFGYSVVLHS HGANRWLLVG APTANWLANA SVINPGAIYR CRIGKNPGQT
110 120 130 140 150
CEQLQLGSPN GEPCGKTCLE ERDNQWLGVT LSRQPGENGS IVTCGHRWKN
160 170 180 190 200
IFYIKNENKL PTGGCYGVPP DLRTELSKRI APCYQDYVKK FGENFASCQA
210 220 230 240 250
GISSFYTKDL IVMGAPGSSY WTGSLFVYNI TTNKYKAFLD KQNQVKFGSY
260 270 280 290 300
LGYSVGAGHF RSQHTTEVVG GAPQHEQIGK AYIFSIDEKE LNILHEMKGK
310 320 330 340 350
KLGSYFGASV CAVDLNADGF SDLLVGAPMQ STIREEGRVF VYINSGSGAV
360 370 380 390 400
MNAMETNLVG SDKYAARFGE SIVNLGDIDN DGFEDVAIGA PQEDDLQGAI
410 420 430 440 450
YIYNGRADGI SSTFSQRIEG LQISKSLSMF GQSISGQIDA DNNGYVDVAV
460 470 480 490 500
GAFRSDSAVL LRTRPVVIVD ASLSHPESVN RTKFDCVENG WPSVCIDLTL
510 520 530 540 550
CFSYKGKEVP GYIVLFYNMS LDVNRKAESP PRFYFSSNGT SDVITGSIQV
560 570 580 590 600
SSREANCRTH QAFMRKDVRD ILTPIQIEAA YHLGPHVISK RSTEEFPPLQ
610 620 630 640 650
PILQQKKEKD IMKKTINFAR FCAHENCSAD LQVSAKIGFL KPHENKTYLA
660 670 680 690 700
VGSMKTLMLN VSLFNAGDDA YETTLHVKLP VGLYFIKILE LEEKQINCEV
710 720 730 740 750
TDNSGVVQLD CSIGYIYVDH LSRIDISFLL DVSSLSRAEE DLSITVHATC
760 770 780 790 800
ENEEEMDNLK HSRVTVAIPL KYEVKLTVHG FVNPTSFVYG SNDENEPETC
810 820 830 840 850
MVEKMNLTFH VINTGNSMAP NVSVEIMVPN SFSPQTDKLF NILDVQTTTG
860 870 880 890 900
ECHFENYQRV CALEQQKSAM QTLKGIVRFL SKTDKRLLYC IKADPHCLNF
910 920 930 940 950
LCNFGKMESG KEASVHIQLE GRPSILEMDE TSALKFEIRA TGFPEPNPRV
960 970 980 990 1000
IELNKDENVA HVLLEGLHHQ RPKRYFTIVI ISSSLLLGLI VLLLISYVMW
1010 1020 1030
KAGFFKRQYK SILQEENRRD SWSYINSKSN DD
Length:1,032
Mass (Da):114,900
Last modified:November 2, 2010 - v3
Checksum:i73EC1204DE78CD35
GO
Isoform 2 (identifier: P13612-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     186-195: DYVKKFGENF → GSISKYRART
     196-1032: Missing.

Note: No experimental confirmation available.
Show »
Length:195
Mass (Da):21,536
Checksum:iD8F8CBE554E5DE6B
GO

Sequence cautioni

The sequence AAB59613 differs from that shown. Reason: Frameshift at position 13.Curated
The sequence CAA34852 differs from that shown. Reason: Frameshift at position 13.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_047423634S → T.Corresponds to variant rs35322532dbSNPEnsembl.1
Natural variantiVAR_047424824V → A.Corresponds to variant rs1143675dbSNPEnsembl.1
Natural variantiVAR_003978878R → Q.2 PublicationsCorresponds to variant rs1143676dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_056612186 – 195DYVKKFGENF → GSISKYRART in isoform 2. 1 Publication10
Alternative sequenceiVSP_056613196 – 1032Missing in isoform 2. 1 PublicationAdd BLAST837

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16983 mRNA. Translation: CAA34852.1. Frameshift.
L12002 mRNA. Translation: AAB59613.1. Frameshift.
AC020595 Genomic DNA. No translation available.
CH471058 Genomic DNA. Translation: EAX10985.1.
CH471058 Genomic DNA. Translation: EAX10987.1.
BC055419 mRNA. Translation: AAH55419.1.
CCDSiCCDS42788.1. [P13612-1]
CCDS82540.1. [P13612-2]
PIRiS06046.
RefSeqiNP_000876.3. NM_000885.5. [P13612-1]
NP_001303241.1. NM_001316312.1. [P13612-2]
UniGeneiHs.440955.
Hs.72981.

Genome annotation databases

EnsembliENST00000339307; ENSP00000340149; ENSG00000115232. [P13612-2]
ENST00000397033; ENSP00000380227; ENSG00000115232. [P13612-1]
GeneIDi3676.
KEGGihsa:3676.
UCSCiuc002unu.4. human. [P13612-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16983 mRNA. Translation: CAA34852.1. Frameshift.
L12002 mRNA. Translation: AAB59613.1. Frameshift.
AC020595 Genomic DNA. No translation available.
CH471058 Genomic DNA. Translation: EAX10985.1.
CH471058 Genomic DNA. Translation: EAX10987.1.
BC055419 mRNA. Translation: AAH55419.1.
CCDSiCCDS42788.1. [P13612-1]
CCDS82540.1. [P13612-2]
PIRiS06046.
RefSeqiNP_000876.3. NM_000885.5. [P13612-1]
NP_001303241.1. NM_001316312.1. [P13612-2]
UniGeneiHs.440955.
Hs.72981.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3V4PX-ray3.15A/C34-620[»]
3V4VX-ray3.10A/C34-620[»]
4HKCX-ray2.20B1003-1032[»]
5C7ZX-ray2.77B1008-1015[»]
5FPIX-ray2.77B1008-1015[»]
ProteinModelPortaliP13612.
SMRiP13612.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109883. 509 interactors.
DIPiDIP-34971N.
IntActiP13612. 11 interactors.
MINTiMINT-4098849.
STRINGi9606.ENSP00000380227.

Chemistry databases

BindingDBiP13612.
ChEMBLiCHEMBL278.
DrugBankiDB00108. Natalizumab.
DB06822. Tinzaparin.
DB09033. Vedolizumab.

PTM databases

iPTMnetiP13612.
PhosphoSitePlusiP13612.

Polymorphism and mutation databases

BioMutaiITGA4.
DMDMi311033436.

Proteomic databases

EPDiP13612.
MaxQBiP13612.
PaxDbiP13612.
PeptideAtlasiP13612.
PRIDEiP13612.

Protocols and materials databases

DNASUi3676.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000339307; ENSP00000340149; ENSG00000115232. [P13612-2]
ENST00000397033; ENSP00000380227; ENSG00000115232. [P13612-1]
GeneIDi3676.
KEGGihsa:3676.
UCSCiuc002unu.4. human. [P13612-1]

Organism-specific databases

CTDi3676.
DisGeNETi3676.
GeneCardsiITGA4.
HGNCiHGNC:6140. ITGA4.
MIMi192975. gene.
neXtProtiNX_P13612.
OpenTargetsiENSG00000115232.
PharmGKBiPA29940.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IPB2. Eukaryota.
ENOG410XTAR. LUCA.
GeneTreeiENSGT00760000118782.
HOGENOMiHOG000088626.
HOVERGENiHBG004538.
InParanoidiP13612.
KOiK06483.
OMAiEKQINCE.
OrthoDBiEOG091G011V.
PhylomeDBiP13612.
TreeFamiTF105391.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000115232-MONOMER.
ReactomeiR-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-HSA-202733. Cell surface interactions at the vascular wall.
R-HSA-216083. Integrin cell surface interactions.
SignaLinkiP13612.
SIGNORiP13612.

Miscellaneous databases

ChiTaRSiITGA4. human.
GeneWikiiCD49d.
GenomeRNAii3676.
PROiP13612.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000115232.
CleanExiHS_ITGA4.
ExpressionAtlasiP13612. baseline and differential.
GenevisibleiP13612. HS.

Family and domain databases

InterProiIPR013517. FG-GAP.
IPR013519. Int_alpha_beta-p.
IPR000413. Integrin_alpha.
IPR013649. Integrin_alpha-2.
IPR018184. Integrin_alpha_C_CS.
IPR032695. Integrin_dom.
[Graphical view]
PfamiPF01839. FG-GAP. 2 hits.
PF08441. Integrin_alpha2. 1 hit.
[Graphical view]
PRINTSiPR01185. INTEGRINA.
SMARTiSM00191. Int_alpha. 5 hits.
[Graphical view]
SUPFAMiSSF69179. SSF69179. 3 hits.
PROSITEiPS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiITA4_HUMAN
AccessioniPrimary (citable) accession number: P13612
Secondary accession number(s): D3DPG4, Q7Z4L6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 2, 2010
Last modified: November 2, 2016
This is version 179 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 cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  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
  7. 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.