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Protein

Integrin beta-7

Gene

ITGB7

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

Functioni

Integrin alpha-4/beta-7 (Peyer patches-specific homing receptor LPAM-1) is an adhesion molecule that mediates lymphocyte migration and homing to gut-associated lymphoid tissue (GALT). Integrin alpha-4/beta-7 interacts with the cell surface adhesion molecules MADCAM1 which is normally expressed by the vascular endothelium of the gastrointestinal tract. Interacts also with VCAM1 and fibronectin, an extracellular matrix component. It recognizes one or more domains within the alternatively spliced CS-1 region of fibronectin. Interactions involves the tripeptide L-D-T in MADCAM1, and L-D-V in fibronectin. Binds to HIV-1 gp120, thereby allowing the virus to enter GALT, which is thought to be the major trigger of AIDS disease. Interaction would involve a tripeptide L-D-I in HIV-1 gp120. Integrin alpha-E/beta-7 (HML-1) is a receptor for E-cadherin.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi159Magnesium; MIDAS motifBy similarity1
Metal bindingi161Magnesium; MIDAS motifBy similarity1
Metal bindingi163Magnesium; MIDAS motifBy similarity1
Metal bindingi166Magnesium or calcium; ADMIDAS motifBy similarity1
Metal bindingi167Magnesium or calcium; ADMIDAS motifBy similarity1
Metal bindingi198Magnesium; LIMBS motifBy similarity1
Metal bindingi254Magnesium; LIMBS motifBy similarity1
Metal bindingi256Magnesium; LIMBS motifBy similarity1
Metal bindingi259Magnesium; LIMBS motifBy similarity1
Metal bindingi289Magnesium; MIDAS motifBy similarity1

GO - Molecular functioni

  • cell adhesion molecule binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • virus receptor activity Source: UniProtKB-KW

GO - Biological processi

  • cell adhesion Source: ProtInc
  • cell-matrix adhesion Source: UniProtKB
  • cell-matrix adhesion involved in ameboidal cell migration Source: UniProtKB
  • extracellular matrix organization Source: Reactome
  • heterotypic cell-cell adhesion Source: UniProtKB
  • integrin-mediated signaling pathway Source: UniProtKB
  • leukocyte tethering or rolling Source: UniProtKB
  • receptor clustering Source: UniProtKB
  • regulation of immune response Source: Reactome
  • substrate adhesion-dependent cell spreading Source: UniProtKB
  • T cell migration Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Host cell receptor for virus entry, Integrin, Receptor

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000139626-MONOMER.
ReactomeiR-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-HSA-216083. Integrin cell surface interactions.
SignaLinkiP26010.
SIGNORiP26010.

Names & Taxonomyi

Protein namesi
Recommended name:
Integrin beta-7
Alternative name(s):
Gut homing receptor beta subunit
Gene namesi
Name:ITGB7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:6162. ITGB7.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini20 – 723ExtracellularSequence analysisAdd BLAST704
Transmembranei724 – 746HelicalSequence analysisAdd BLAST23
Topological domaini747 – 798CytoplasmicSequence analysisAdd BLAST52

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • integrin alpha4-beta7 complex Source: UniProtKB
  • integrin complex Source: ProtInc
  • membrane Source: UniProtKB
  • plasma membrane Source: Reactome
  • receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi159D → A: Loss of integrin alpha-E/beta-7 binding to E-cadherin and of integrin alpha-4/beta-7 binding to MADCAM1. 1 Publication1

Organism-specific databases

DisGeNETi3695.
OpenTargetsiENSG00000139626.
PharmGKBiPA29961.

Chemistry databases

ChEMBLiCHEMBL2979.
DrugBankiDB09033. Vedolizumab.

Polymorphism and mutation databases

BioMutaiITGB7.
DMDMi124973.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 192 PublicationsAdd BLAST19
ChainiPRO_000001635220 – 798Integrin beta-7Add BLAST779

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi45 ↔ 476By similarity
Disulfide bondi51 ↔ 61By similarity
Disulfide bondi54 ↔ 91By similarity
Disulfide bondi64 ↔ 80By similarity
Glycosylationi68N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi216 ↔ 223By similarity
Disulfide bondi271 ↔ 311By similarity
Glycosylationi279N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi412 ↔ 428By similarity
Glycosylationi434N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi448 ↔ 688By similarity
Disulfide bondi474 ↔ 478By similarity
Glycosylationi477N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi488 ↔ 500By similarity
Disulfide bondi497 ↔ 537By similarity
Disulfide bondi502 ↔ 511By similarity
Disulfide bondi513 ↔ 527By similarity
Glycosylationi531N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi543 ↔ 548By similarity
Disulfide bondi545 ↔ 574By similarity
Disulfide bondi550 ↔ 559By similarity
Disulfide bondi561 ↔ 566By similarity
Disulfide bondi580 ↔ 585By similarity
Disulfide bondi582 ↔ 613By similarity
Disulfide bondi587 ↔ 596By similarity
Glycosylationi590N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi598 ↔ 605By similarity
Disulfide bondi619 ↔ 624By similarity
Disulfide bondi621 ↔ 666By similarity
Disulfide bondi626 ↔ 635By similarity
Disulfide bondi638 ↔ 641By similarity
Disulfide bondi645 ↔ 654By similarity
Glycosylationi665N-linked (GlcNAc...)Sequence analysis1
Glycosylationi674N-linked (GlcNAc...)Sequence analysis1
Modified residuei778Phosphotyrosine; by Tyr-kinasesBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP26010.
PaxDbiP26010.
PeptideAtlasiP26010.
PRIDEiP26010.

PTM databases

iPTMnetiP26010.
PhosphoSitePlusiP26010.

Expressioni

Tissue specificityi

Expressed in a variety of leukocyte lines.

Inductioni

Integrin alpha-E/beta-7 is induced by TGFB1.1 Publication

Gene expression databases

BgeeiENSG00000139626.
CleanExiHS_ITGB7.
ExpressionAtlasiP26010. baseline and differential.
GenevisibleiP26010. HS.

Organism-specific databases

HPAiHPA042277.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. Beta-7 associates with either alpha-4 or alpha-E. Integrin alpha-4/beta-7 interacts with MADCAM1, VCAM1, fibronectin, and may also interact with HIV-1 gp120. Interacts with FLNA (via filamin repeats 4, 9, 12, 17, 19, 21, and 23) (PubMed:19828450).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FLNAP213336EBI-702932,EBI-350432
ITGA4P136126EBI-702932,EBI-703044

GO - Molecular functioni

  • cell adhesion molecule binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109901. 4 interactors.
DIPiDIP-34970N.
IntActiP26010. 3 interactors.
MINTiMINT-258650.
STRINGi9606.ENSP00000267082.

Chemistry databases

BindingDBiP26010.

Structurei

Secondary structure

1798
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi102 – 105Combined sources4
Turni114 – 116Combined sources3
Beta strandi117 – 119Combined sources3
Beta strandi127 – 131Combined sources5
Beta strandi138 – 145Combined sources8
Beta strandi152 – 159Combined sources8
Helixi162 – 164Combined sources3
Helixi165 – 173Combined sources9
Helixi176 – 182Combined sources7
Turni183 – 185Combined sources3
Beta strandi189 – 196Combined sources8
Turni202 – 204Combined sources3
Helixi209 – 213Combined sources5
Beta strandi219 – 221Combined sources3
Beta strandi228 – 237Combined sources10
Helixi240 – 246Combined sources7
Beta strandi255 – 259Combined sources5
Helixi261 – 270Combined sources10
Helixi272 – 275Combined sources4
Beta strandi279 – 290Combined sources12
Helixi297 – 299Combined sources3
Turni300 – 302Combined sources3
Beta strandi317 – 319Combined sources3
Helixi320 – 324Combined sources5
Helixi330 – 339Combined sources10
Beta strandi342 – 348Combined sources7
Beta strandi350 – 352Combined sources3
Helixi353 – 360Combined sources8
Beta strandi367 – 370Combined sources4
Helixi378 – 390Combined sources13
Beta strandi393 – 396Combined sources4
Beta strandi404 – 408Combined sources5
Beta strandi413 – 415Combined sources3
Beta strandi423 – 428Combined sources6
Beta strandi436 – 445Combined sources10
Beta strandi454 – 460Combined sources7
Beta strandi465 – 469Combined sources5
Beta strandi777 – 786Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BRQX-ray2.10C/D768-798[»]
3V4PX-ray3.15B/D20-512[»]
3V4VX-ray3.10B/D20-512[»]
ProteinModelPortaliP26010.
SMRiP26010.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26010.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini150 – 389VWFAAdd BLAST240
Repeati478 – 526IAdd BLAST49
Repeati527 – 565IIAdd BLAST39
Repeati566 – 604IIIAdd BLAST39
Repeati605 – 640IVAdd BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni478 – 640Cysteine-rich tandem repeatsAdd BLAST163

Domaini

Domain I contains three cation-binding sites: the ligand-integrin-binding site (LIMBS), the metal ion-dependent adhesion site (MIDAS), and the adjacent to MIDAS site (ADMIDAS). In the absence of a ligand or in calcium-dependent binding, only ADMIDAS is occupied. In magnesium-dependent binding all three sites bind metal ions. LIMBS positively modify ligand binding whereas ADMIDAS negatively modify ligand binding.

Sequence similaritiesi

Belongs to the integrin beta chain family.Curated
Contains 1 VWFA domain.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1226. Eukaryota.
ENOG410XP60. LUCA.
GeneTreeiENSGT00760000119064.
HOGENOMiHOG000252936.
HOVERGENiHBG006190.
InParanoidiP26010.
KOiK06590.
OMAiDHTQAIV.
OrthoDBiEOG091G029W.
PhylomeDBiP26010.
TreeFamiTF105392.

Family and domain databases

Gene3Di3.40.50.410. 1 hit.
InterProiIPR013111. EGF_extracell.
IPR033760. Integin_beta_N.
IPR015812. Integrin_bsu.
IPR015437. Integrin_bsu-7.
IPR014836. Integrin_bsu_cyt_dom.
IPR012896. Integrin_bsu_tail.
IPR002369. Integrin_bsu_VWA.
IPR032695. Integrin_dom.
IPR016201. PSI.
IPR002035. VWF_A.
[Graphical view]
PANTHERiPTHR10082. PTHR10082. 1 hit.
PTHR10082:SF36. PTHR10082:SF36. 1 hit.
PfamiPF07974. EGF_2. 1 hit.
PF08725. Integrin_b_cyt. 1 hit.
PF00362. Integrin_beta. 1 hit.
PF17205. PSI_integrin. 1 hit.
[Graphical view]
PIRSFiPIRSF002512. Integrin_B. 1 hit.
PRINTSiPR01186. INTEGRINB.
SMARTiSM00187. INB. 1 hit.
SM01241. Integrin_b_cyt. 1 hit.
SM01242. Integrin_B_tail. 1 hit.
SM00423. PSI. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
SSF69179. SSF69179. 1 hit.
SSF69687. SSF69687. 1 hit.
PROSITEiPS00022. EGF_1. 4 hits.
PS01186. EGF_2. 1 hit.
PS00243. INTEGRIN_BETA. 3 hits.
[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 Long (identifier: P26010-1) [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
MVALPMVLVL LLVLSRGESE LDAKIPSTGD ATEWRNPHLS MLGSCQPAPS
60 70 80 90 100
CQKCILSHPS CAWCKQLNFT ASGEAEARRC ARREELLARG CPLEELEEPR
110 120 130 140 150
GQQEVLQDQP LSQGARGEGA TQLAPQRVRV TLRPGEPQQL QVRFLRAEGY
160 170 180 190 200
PVDLYYLMDL SYSMKDDLER VRQLGHALLV RLQEVTHSVR IGFGSFVDKT
210 220 230 240 250
VLPFVSTVPS KLRHPCPTRL ERCQSPFSFH HVLSLTGDAQ AFEREVGRQS
260 270 280 290 300
VSGNLDSPEG GFDAILQAAL CQEQIGWRNV SRLLVFTSDD TFHTAGDGKL
310 320 330 340 350
GGIFMPSDGH CHLDSNGLYS RSTEFDYPSV GQVAQALSAA NIQPIFAVTS
360 370 380 390 400
AALPVYQELS KLIPKSAVGE LSEDSSNVVQ LIMDAYNSLS STVTLEHSSL
410 420 430 440 450
PPGVHISYES QCEGPEKREG KAEDRGQCNH VRINQTVTFW VSLQATHCLP
460 470 480 490 500
EPHLLRLRAL GFSEELIVEL HTLCDCNCSD TQPQAPHCSD GQGHLQCGVC
510 520 530 540 550
SCAPGRLGRL CECSVAELSS PDLESGCRAP NGTGPLCSGK GHCQCGRCSC
560 570 580 590 600
SGQSSGHLCE CDDASCERHE GILCGGFGRC QCGVCHCHAN RTGRACECSG
610 620 630 640 650
DMDSCISPEG GLCSGHGRCK CNRCQCLDGY YGALCDQCPG CKTPCERHRD
660 670 680 690 700
CAECGAFRTG PLATNCSTAC AHTNVTLALA PILDDGWCKE RTLDNQLFFF
710 720 730 740 750
LVEDDARGTV VLRVRPQEKG ADHTQAIVLG CVGGIVAVGL GLVLAYRLSV
760 770 780 790
EIYDRREYSR FEKEQQQLNW KQDSNPLYKS AITTTINPRF QEADSPTL
Length:798
Mass (Da):86,903
Last modified:May 1, 1992 - v1
Checksum:iCBE275E0E9992385
GO
Isoform Short (identifier: P26010-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     501-648: Missing.

Show »
Length:650
Mass (Da):71,582
Checksum:iB247895C3772178D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti34W → A AA sequence (PubMed:1750505).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_049637672H → Y.Corresponds to variant rs11539433dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_002753501 – 648Missing in isoform Short. 1 PublicationAdd BLAST148

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M68892 mRNA. Translation: AAA59184.1.
S80335 mRNA. Translation: AAB21332.1.
M62880 mRNA. Translation: AAA59185.1.
L23823
, L23810, L23811, L23812, L23813, L23814, L23815, L23816, L23817, L23818, L23819, L23820, L23821, L23822 Genomic DNA. Translation: AAA36118.1.
S49378
, S49364, S49365, S49366, S49367, S49368, S49369, S49370, S49371, S49373, S49374, S49375, S49376, S49377 Genomic DNA. Translation: AAB23688.1.
BC015916 mRNA. Translation: AAH15916.1.
CCDSiCCDS8849.1. [P26010-1]
PIRiA40526.
RefSeqiNP_000880.1. NM_000889.2. [P26010-1]
XP_005268908.1. XM_005268851.3. [P26010-1]
XP_005268909.1. XM_005268852.4. [P26010-1]
UniGeneiHs.654470.

Genome annotation databases

EnsembliENST00000267082; ENSP00000267082; ENSG00000139626. [P26010-1]
ENST00000422257; ENSP00000408741; ENSG00000139626. [P26010-1]
ENST00000550743; ENSP00000455374; ENSG00000139626. [P26010-2]
GeneIDi3695.
KEGGihsa:3695.
UCSCiuc001scc.4. human. [P26010-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M68892 mRNA. Translation: AAA59184.1.
S80335 mRNA. Translation: AAB21332.1.
M62880 mRNA. Translation: AAA59185.1.
L23823
, L23810, L23811, L23812, L23813, L23814, L23815, L23816, L23817, L23818, L23819, L23820, L23821, L23822 Genomic DNA. Translation: AAA36118.1.
S49378
, S49364, S49365, S49366, S49367, S49368, S49369, S49370, S49371, S49373, S49374, S49375, S49376, S49377 Genomic DNA. Translation: AAB23688.1.
BC015916 mRNA. Translation: AAH15916.1.
CCDSiCCDS8849.1. [P26010-1]
PIRiA40526.
RefSeqiNP_000880.1. NM_000889.2. [P26010-1]
XP_005268908.1. XM_005268851.3. [P26010-1]
XP_005268909.1. XM_005268852.4. [P26010-1]
UniGeneiHs.654470.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BRQX-ray2.10C/D768-798[»]
3V4PX-ray3.15B/D20-512[»]
3V4VX-ray3.10B/D20-512[»]
ProteinModelPortaliP26010.
SMRiP26010.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109901. 4 interactors.
DIPiDIP-34970N.
IntActiP26010. 3 interactors.
MINTiMINT-258650.
STRINGi9606.ENSP00000267082.

Chemistry databases

BindingDBiP26010.
ChEMBLiCHEMBL2979.
DrugBankiDB09033. Vedolizumab.

PTM databases

iPTMnetiP26010.
PhosphoSitePlusiP26010.

Polymorphism and mutation databases

BioMutaiITGB7.
DMDMi124973.

Proteomic databases

MaxQBiP26010.
PaxDbiP26010.
PeptideAtlasiP26010.
PRIDEiP26010.

Protocols and materials databases

DNASUi3695.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000267082; ENSP00000267082; ENSG00000139626. [P26010-1]
ENST00000422257; ENSP00000408741; ENSG00000139626. [P26010-1]
ENST00000550743; ENSP00000455374; ENSG00000139626. [P26010-2]
GeneIDi3695.
KEGGihsa:3695.
UCSCiuc001scc.4. human. [P26010-1]

Organism-specific databases

CTDi3695.
DisGeNETi3695.
GeneCardsiITGB7.
HGNCiHGNC:6162. ITGB7.
HPAiHPA042277.
MIMi147559. gene.
neXtProtiNX_P26010.
OpenTargetsiENSG00000139626.
PharmGKBiPA29961.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1226. Eukaryota.
ENOG410XP60. LUCA.
GeneTreeiENSGT00760000119064.
HOGENOMiHOG000252936.
HOVERGENiHBG006190.
InParanoidiP26010.
KOiK06590.
OMAiDHTQAIV.
OrthoDBiEOG091G029W.
PhylomeDBiP26010.
TreeFamiTF105392.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000139626-MONOMER.
ReactomeiR-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-HSA-216083. Integrin cell surface interactions.
SignaLinkiP26010.
SIGNORiP26010.

Miscellaneous databases

ChiTaRSiITGB7. human.
EvolutionaryTraceiP26010.
GeneWikiiITGB7.
GenomeRNAii3695.
PROiP26010.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000139626.
CleanExiHS_ITGB7.
ExpressionAtlasiP26010. baseline and differential.
GenevisibleiP26010. HS.

Family and domain databases

Gene3Di3.40.50.410. 1 hit.
InterProiIPR013111. EGF_extracell.
IPR033760. Integin_beta_N.
IPR015812. Integrin_bsu.
IPR015437. Integrin_bsu-7.
IPR014836. Integrin_bsu_cyt_dom.
IPR012896. Integrin_bsu_tail.
IPR002369. Integrin_bsu_VWA.
IPR032695. Integrin_dom.
IPR016201. PSI.
IPR002035. VWF_A.
[Graphical view]
PANTHERiPTHR10082. PTHR10082. 1 hit.
PTHR10082:SF36. PTHR10082:SF36. 1 hit.
PfamiPF07974. EGF_2. 1 hit.
PF08725. Integrin_b_cyt. 1 hit.
PF00362. Integrin_beta. 1 hit.
PF17205. PSI_integrin. 1 hit.
[Graphical view]
PIRSFiPIRSF002512. Integrin_B. 1 hit.
PRINTSiPR01186. INTEGRINB.
SMARTiSM00187. INB. 1 hit.
SM01241. Integrin_b_cyt. 1 hit.
SM01242. Integrin_B_tail. 1 hit.
SM00423. PSI. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
SSF69179. SSF69179. 1 hit.
SSF69687. SSF69687. 1 hit.
PROSITEiPS00022. EGF_1. 4 hits.
PS01186. EGF_2. 1 hit.
PS00243. INTEGRIN_BETA. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiITB7_HUMAN
AccessioniPrimary (citable) accession number: P26010
Secondary accession number(s): Q9UCP7, Q9UCS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: November 30, 2016
This is version 173 of the entry and version 1 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 12
    Human chromosome 12: 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.