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P26010

- ITB7_HUMAN

UniProt

P26010 - ITB7_HUMAN

Protein

Integrin beta-7

Gene

ITGB7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 1 (01 May 1992)
      Previous versions | rss
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    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)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi159 – 1591Magnesium; MIDAS motifBy similarity
    Metal bindingi161 – 1611Magnesium; MIDAS motifBy similarity
    Metal bindingi163 – 1631Magnesium; MIDAS motifBy similarity
    Metal bindingi166 – 1661Magnesium or calcium; ADMIDAS motifBy similarity
    Metal bindingi167 – 1671Magnesium or calcium; ADMIDAS motifBy similarity
    Metal bindingi198 – 1981Magnesium; LIMBS motifBy similarity
    Metal bindingi254 – 2541Magnesium; LIMBS motifBy similarity
    Metal bindingi256 – 2561Magnesium; LIMBS motifBy similarity
    Metal bindingi259 – 2591Magnesium; LIMBS motifBy similarity
    Metal bindingi289 – 2891Magnesium; MIDAS motifBy similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. virus receptor activity Source: UniProtKB-KW

    GO - Biological processi

    1. cell adhesion Source: ProtInc
    2. cell-matrix adhesion Source: InterPro
    3. extracellular matrix organization Source: Reactome
    4. integrin-mediated signaling pathway Source: UniProtKB-KW
    5. leukocyte migration Source: Ensembl
    6. multicellular organismal development Source: InterPro
    7. regulation of immune response Source: Reactome

    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

    ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_13552. Integrin cell surface interactions.
    SignaLinkiP26010.

    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
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:6162. ITGB7.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. integrin complex Source: ProtInc
    3. membrane Source: UniProtKB
    4. plasma membrane Source: Reactome
    5. receptor complex Source: MGI

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi159 – 1591D → A: Loss of integrin alpha-E/beta-7 binding to E-cadherin and of integrin alpha-4/beta-7 binding to MADCAM1. 1 Publication

    Organism-specific databases

    PharmGKBiPA29961.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19192 PublicationsAdd
    BLAST
    Chaini20 – 798779Integrin beta-7PRO_0000016352Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi45 ↔ 476By similarity
    Disulfide bondi51 ↔ 61By similarity
    Disulfide bondi54 ↔ 91By similarity
    Disulfide bondi64 ↔ 80By similarity
    Glycosylationi68 – 681N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi216 ↔ 223By similarity
    Disulfide bondi271 ↔ 311By similarity
    Glycosylationi279 – 2791N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi412 ↔ 428By similarity
    Glycosylationi434 – 4341N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi448 ↔ 688By similarity
    Disulfide bondi474 ↔ 478By similarity
    Glycosylationi477 – 4771N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi488 ↔ 500By similarity
    Disulfide bondi497 ↔ 537By similarity
    Disulfide bondi502 ↔ 511By similarity
    Disulfide bondi513 ↔ 527By similarity
    Glycosylationi531 – 5311N-linked (GlcNAc...)Sequence Analysis
    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
    Glycosylationi590 – 5901N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi598 ↔ 605By similarity
    Disulfide bondi619 ↔ 624By similarity
    Disulfide bondi621 ↔ 666By similarity
    Disulfide bondi626 ↔ 635By similarity
    Disulfide bondi638 ↔ 641By similarity
    Disulfide bondi645 ↔ 654By similarity
    Glycosylationi665 – 6651N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi674 – 6741N-linked (GlcNAc...)Sequence Analysis
    Modified residuei778 – 7781Phosphotyrosine; by Tyr-kinasesBy similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP26010.
    PaxDbiP26010.
    PRIDEiP26010.

    PTM databases

    PhosphoSiteiP26010.

    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

    ArrayExpressiP26010.
    BgeeiP26010.
    CleanExiHS_ITGB7.
    GenevestigatoriP26010.

    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, VCAM, fibronectin, and may also interact with HIV-1 gp120.2 Publications

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi109901. 5 interactions.
    DIPiDIP-34970N.
    IntActiP26010. 3 interactions.
    MINTiMINT-258650.
    STRINGi9606.ENSP00000267082.

    Structurei

    Secondary structure

    1
    798
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi102 – 1054
    Turni114 – 1163
    Beta strandi117 – 1193
    Beta strandi127 – 1315
    Beta strandi138 – 1458
    Beta strandi152 – 1598
    Helixi162 – 1643
    Helixi165 – 1739
    Helixi176 – 1827
    Turni183 – 1853
    Beta strandi189 – 1968
    Turni202 – 2043
    Helixi209 – 2135
    Beta strandi219 – 2213
    Beta strandi228 – 23710
    Helixi240 – 2467
    Beta strandi255 – 2595
    Helixi261 – 27010
    Helixi272 – 2754
    Beta strandi279 – 29012
    Helixi297 – 2993
    Turni300 – 3023
    Beta strandi317 – 3193
    Helixi320 – 3245
    Helixi330 – 33910
    Beta strandi342 – 3487
    Beta strandi350 – 3523
    Helixi353 – 3608
    Beta strandi367 – 3704
    Helixi378 – 39013
    Beta strandi393 – 3964
    Beta strandi404 – 4085
    Beta strandi413 – 4153
    Beta strandi423 – 4286
    Beta strandi436 – 44510
    Beta strandi454 – 4607
    Beta strandi465 – 4695
    Beta strandi777 – 78610

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BRQX-ray2.10C/D768-798[»]
    3V4PX-ray3.15B/D20-512[»]
    3V4VX-ray3.10B/D20-512[»]
    ProteinModelPortaliP26010.
    SMRiP26010. Positions 50-691.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP26010.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 723704ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini747 – 79852CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei724 – 74623HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini150 – 389240VWFAAdd
    BLAST
    Repeati478 – 52649IAdd
    BLAST
    Repeati527 – 56539IIAdd
    BLAST
    Repeati566 – 60439IIIAdd
    BLAST
    Repeati605 – 64036IVAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni478 – 640163Cysteine-rich tandem repeatsAdd
    BLAST

    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

    eggNOGiNOG287997.
    HOGENOMiHOG000252936.
    HOVERGENiHBG006190.
    InParanoidiP26010.
    KOiK06590.
    OMAiDHTQAIV.
    OrthoDBiEOG7T7GSB.
    PhylomeDBiP26010.
    TreeFamiTF105392.

    Family and domain databases

    Gene3Di3.40.50.410. 1 hit.
    InterProiIPR015812. Integrin_bsu.
    IPR015437. Integrin_bsu-7.
    IPR014836. Integrin_bsu_cyt_dom.
    IPR002369. Integrin_bsu_N.
    IPR012896. Integrin_bsu_tail.
    IPR016201. Plexin-like_fold.
    IPR002035. VWF_A.
    [Graphical view]
    PANTHERiPTHR10082. PTHR10082. 1 hit.
    PTHR10082:SF36. PTHR10082:SF36. 1 hit.
    PfamiPF08725. Integrin_b_cyt. 1 hit.
    PF00362. Integrin_beta. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002512. Integrin_B. 1 hit.
    PRINTSiPR01186. INTEGRINB.
    SMARTiSM00187. INB. 1 hit.
    SM00423. PSI. 1 hit.
    SM00327. VWA. 1 hit.
    [Graphical view]
    SUPFAMiSSF103575. SSF103575. 1 hit.
    SSF53300. SSF53300. 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. Align

    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

    MVALPMVLVL LLVLSRGESE LDAKIPSTGD ATEWRNPHLS MLGSCQPAPS    50
    CQKCILSHPS CAWCKQLNFT ASGEAEARRC ARREELLARG CPLEELEEPR 100
    GQQEVLQDQP LSQGARGEGA TQLAPQRVRV TLRPGEPQQL QVRFLRAEGY 150
    PVDLYYLMDL SYSMKDDLER VRQLGHALLV RLQEVTHSVR IGFGSFVDKT 200
    VLPFVSTVPS KLRHPCPTRL ERCQSPFSFH HVLSLTGDAQ AFEREVGRQS 250
    VSGNLDSPEG GFDAILQAAL CQEQIGWRNV SRLLVFTSDD TFHTAGDGKL 300
    GGIFMPSDGH CHLDSNGLYS RSTEFDYPSV GQVAQALSAA NIQPIFAVTS 350
    AALPVYQELS KLIPKSAVGE LSEDSSNVVQ LIMDAYNSLS STVTLEHSSL 400
    PPGVHISYES QCEGPEKREG KAEDRGQCNH VRINQTVTFW VSLQATHCLP 450
    EPHLLRLRAL GFSEELIVEL HTLCDCNCSD TQPQAPHCSD GQGHLQCGVC 500
    SCAPGRLGRL CECSVAELSS PDLESGCRAP NGTGPLCSGK GHCQCGRCSC 550
    SGQSSGHLCE CDDASCERHE GILCGGFGRC QCGVCHCHAN RTGRACECSG 600
    DMDSCISPEG GLCSGHGRCK CNRCQCLDGY YGALCDQCPG CKTPCERHRD 650
    CAECGAFRTG PLATNCSTAC AHTNVTLALA PILDDGWCKE RTLDNQLFFF 700
    LVEDDARGTV VLRVRPQEKG ADHTQAIVLG CVGGIVAVGL GLVLAYRLSV 750
    EIYDRREYSR FEKEQQQLNW KQDSNPLYKS AITTTINPRF QEADSPTL 798
    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti34 – 341W → A AA sequence (PubMed:1750505)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti672 – 6721H → Y.
    Corresponds to variant rs11539433 [ dbSNP | Ensembl ].
    VAR_049637

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei501 – 648148Missing in isoform Short. 1 PublicationVSP_002753Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_005268851.1. [P26010-1]
    XP_005268909.1. XM_005268852.2. [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.3. human. [P26010-1]

    Polymorphism databases

    DMDMi124973.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS8849.1. [P26010-1 ]
    PIRi A40526.
    RefSeqi NP_000880.1. NM_000889.2. [P26010-1 ]
    XP_005268908.1. XM_005268851.1. [P26010-1 ]
    XP_005268909.1. XM_005268852.2. [P26010-1 ]
    UniGenei Hs.654470.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BRQ X-ray 2.10 C/D 768-798 [» ]
    3V4P X-ray 3.15 B/D 20-512 [» ]
    3V4V X-ray 3.10 B/D 20-512 [» ]
    ProteinModelPortali P26010.
    SMRi P26010. Positions 50-691.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109901. 5 interactions.
    DIPi DIP-34970N.
    IntActi P26010. 3 interactions.
    MINTi MINT-258650.
    STRINGi 9606.ENSP00000267082.

    Chemistry

    BindingDBi P26010.
    ChEMBLi CHEMBL2095184.

    PTM databases

    PhosphoSitei P26010.

    Polymorphism databases

    DMDMi 124973.

    Proteomic databases

    MaxQBi P26010.
    PaxDbi P26010.
    PRIDEi P26010.

    Protocols and materials databases

    DNASUi 3695.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000267082 ; ENSP00000267082 ; ENSG00000139626 . [P26010-1 ]
    ENST00000422257 ; ENSP00000408741 ; ENSG00000139626 . [P26010-1 ]
    ENST00000550743 ; ENSP00000455374 ; ENSG00000139626 . [P26010-2 ]
    GeneIDi 3695.
    KEGGi hsa:3695.
    UCSCi uc001scc.3. human. [P26010-1 ]

    Organism-specific databases

    CTDi 3695.
    GeneCardsi GC12M053585.
    HGNCi HGNC:6162. ITGB7.
    HPAi HPA042277.
    MIMi 147559. gene.
    neXtProti NX_P26010.
    PharmGKBi PA29961.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG287997.
    HOGENOMi HOG000252936.
    HOVERGENi HBG006190.
    InParanoidi P26010.
    KOi K06590.
    OMAi DHTQAIV.
    OrthoDBi EOG7T7GSB.
    PhylomeDBi P26010.
    TreeFami TF105392.

    Enzyme and pathway databases

    Reactomei REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_13552. Integrin cell surface interactions.
    SignaLinki P26010.

    Miscellaneous databases

    ChiTaRSi ITGB7. human.
    EvolutionaryTracei P26010.
    GeneWikii ITGB7.
    GenomeRNAii 3695.
    NextBioi 14483.
    PROi P26010.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P26010.
    Bgeei P26010.
    CleanExi HS_ITGB7.
    Genevestigatori P26010.

    Family and domain databases

    Gene3Di 3.40.50.410. 1 hit.
    InterProi IPR015812. Integrin_bsu.
    IPR015437. Integrin_bsu-7.
    IPR014836. Integrin_bsu_cyt_dom.
    IPR002369. Integrin_bsu_N.
    IPR012896. Integrin_bsu_tail.
    IPR016201. Plexin-like_fold.
    IPR002035. VWF_A.
    [Graphical view ]
    PANTHERi PTHR10082. PTHR10082. 1 hit.
    PTHR10082:SF36. PTHR10082:SF36. 1 hit.
    Pfami PF08725. Integrin_b_cyt. 1 hit.
    PF00362. Integrin_beta. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002512. Integrin_B. 1 hit.
    PRINTSi PR01186. INTEGRINB.
    SMARTi SM00187. INB. 1 hit.
    SM00423. PSI. 1 hit.
    SM00327. VWA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF103575. SSF103575. 1 hit.
    SSF53300. SSF53300. 1 hit.
    SSF69687. SSF69687. 1 hit.
    PROSITEi PS00022. EGF_1. 4 hits.
    PS01186. EGF_2. 1 hit.
    PS00243. INTEGRIN_BETA. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequence analysis of a novel beta 2-related integrin transcript from T lymphocytes: homology of integrin cysteine-rich repeats to domain III of laminin B chains."
      Yuan Q., Jiang W.-M., Krissansen G.W., Watson J.D.
      Int. Immunol. 2:1097-1108(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
      Tissue: T-cell.
    2. "Cloning and sequence analysis of a novel beta 2-related integrin transcript from T lymphocytes: homology of integrin cysteine-rich repeats to domain III of laminin B chains."
      Yuan Q., Jiang W.-M., Krissansen G.W., Watson J.D.
      Int. Immunol. 3:1373-1374(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    3. "Complete amino acid sequence of an integrin beta subunit (beta 7) identified in leukocytes."
      Erle D.J., Rueegg C., Sheppard D., Pytela R.
      J. Biol. Chem. 266:11009-11016(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
      Tissue: Leukocyte.
    4. "The gene organization of the human beta 7 subunit, the common beta subunit of the leukocyte integrins HML-1 and LPAM-1."
      Jiang W.-M., Jenkins D., Yuan Q., Leung E., Choo K.H., Watson J.D., Krissansen G.W.
      Int. Immunol. 4:1031-1040(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
      Tissue: Colon.
    6. Cited for: PROTEIN SEQUENCE OF 20-36, INTERACTION WITH INTEGRIN ALPHA-4 AND INTEGRIN ALPHA-E, INDUCTION.
    7. "HML-1 antigen on mucosa-associated T cells, activated cells, and hairy leukemic cells is a new integrin containing the beta 7 subunit."
      Micklem K.J., Dong Y., Willis A., Pulford K.A., Visser L., Duerkop H., Poppema S., Stein H., Mason D.Y.
      Am. J. Pathol. 139:1297-1301(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-34.
      Tissue: Leukemia.
    8. "The role of alpha and beta chains in ligand recognition by beta 7 integrins."
      Higgins J.M.G., Cernadas M., Tan K., Irie A., Wang J.-H., Takada Y., Brenner M.B.
      J. Biol. Chem. 275:25652-25664(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-159.
    9. "Integrins: bidirectional, allosteric signaling machines."
      Hynes R.O.
      Cell 110:673-687(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    10. "HIV-1 envelope protein binds to and signals through integrin alpha4beta7, the gut mucosal homing receptor for peripheral T cells."
      Arthos J., Cicala C., Martinelli E., Macleod K., Van Ryk D., Wei D., Xiao Z., Veenstra T.D., Conrad T.P., Lempicki R.A., McLaughlin S., Pascuccio M., Gopaul R., McNally J., Cruz C.C., Censoplano N., Chung E., Reitano K.N.
      , Kottilil S., Goode D.J., Fauci A.S.
      Nat. Immunol. 9:301-309(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 GP120.
    11. "The molecular basis of filamin binding to integrins and competition with talin."
      Kiema T., Lad Y., Jiang P., Oxley C.L., Baldassarre M., Wegener K.L., Campbell I.D., Ylanne J., Calderwood D.A.
      Mol. Cell 21:337-347(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 768-798.

    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: October 1, 2014
    This is version 153 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

    External Data

    Dasty 3