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P05107

- ITB2_HUMAN

UniProt

P05107 - ITB2_HUMAN

Protein

Integrin beta-2

Gene

ITGB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 193 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Integrin alpha-L/beta-2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. Integrins alpha-M/beta-2 and alpha-X/beta-2 are receptors for the iC3b fragment of the third complement component and for fibrinogen. Integrin alpha-X/beta-2 recognizes the sequence G-P-R in fibrinogen alpha-chain. Integrin alpha-M/beta-2 recognizes P1 and P2 peptides of fibrinogen gamma chain. Integrin alpha-M/beta-2 is also a receptor for factor X. Integrin alpha-D/beta-2 is a receptor for ICAM3 and VCAM1. Triggers neutrophil transmigration during lung injury through PTK2B/PYK2-mediated activation.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi138 – 1381Calcium; via carbonyl oxygen
    Metal bindingi141 – 1411Calcium
    Metal bindingi142 – 1421Calcium
    Metal bindingi347 – 3471Calcium

    GO - Molecular functioni

    1. glycoprotein binding Source: BHF-UCL
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. protein kinase binding Source: UniProtKB
    5. receptor activity Source: InterPro

    GO - Biological processi

    1. apoptotic process Source: UniProtKB
    2. blood coagulation Source: Reactome
    3. cell adhesion Source: ProtInc
    4. cell-cell signaling Source: UniProtKB
    5. cell-matrix adhesion Source: InterPro
    6. extracellular matrix organization Source: Reactome
    7. inflammatory response Source: UniProtKB
    8. innate immune response Source: Reactome
    9. integrin-mediated signaling pathway Source: UniProtKB
    10. leukocyte cell-cell adhesion Source: UniProtKB
    11. leukocyte migration Source: Reactome
    12. multicellular organismal development Source: InterPro
    13. neutrophil chemotaxis Source: UniProtKB
    14. regulation of cell shape Source: UniProtKB
    15. regulation of immune response Source: Reactome
    16. regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
    17. toll-like receptor 4 signaling pathway Source: Reactome
    18. toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Integrin, Receptor

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_12051. Cell surface interactions at the vascular wall.
    REACT_13552. Integrin cell surface interactions.
    REACT_6894. Toll Like Receptor 4 (TLR4) Cascade.
    SignaLinkiP05107.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Integrin beta-2
    Alternative name(s):
    Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta
    Complement receptor C3 subunit beta
    CD_antigen: CD18
    Gene namesi
    Name:ITGB2
    Synonyms:CD18, MFI7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:6155. ITGB2.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Leukocyte adhesion deficiency 1 (LAD1) [MIM:116920]: LAD1 patients have recurrent bacterial infections and their leukocytes are deficient in a wide range of adhesion-dependent functions.11 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti128 – 1281D → N in LAD1. 1 Publication
    Corresponds to variant rs137852615 [ dbSNP | Ensembl ].
    VAR_003984
    Natural varianti128 – 1281D → Y in LAD1. 1 Publication
    Corresponds to variant rs137852615 [ dbSNP | Ensembl ].
    VAR_065661
    Natural varianti138 – 1381S → P in LAD1. 1 Publication
    Corresponds to variant rs137852617 [ dbSNP | Ensembl ].
    VAR_013402
    Natural varianti149 – 1491L → P in LAD1. 1 Publication
    Corresponds to variant rs137852611 [ dbSNP | Ensembl ].
    VAR_003985
    Natural varianti169 – 1691G → R in LAD1. 2 Publications
    Corresponds to variant rs137852612 [ dbSNP | Ensembl ].
    VAR_003986
    Natural varianti178 – 1781P → L in LAD1. 2 Publications
    Corresponds to variant rs137852614 [ dbSNP | Ensembl ].
    VAR_003987
    Natural varianti196 – 1961K → T in LAD1. 1 Publication
    Corresponds to variant rs137852610 [ dbSNP | Ensembl ].
    VAR_003988
    Natural varianti239 – 2391A → T in LAD1. 1 Publication
    Corresponds to variant rs179363873 [ dbSNP | Ensembl ].
    VAR_065662
    Natural varianti273 – 2731G → R in LAD1. 1 Publication
    Corresponds to variant rs137852618 [ dbSNP | Ensembl ].
    VAR_013403
    Natural varianti284 – 2841G → S in LAD1. 1 Publication
    Corresponds to variant rs137852616 [ dbSNP | Ensembl ].
    VAR_003989
    Natural varianti300 – 3001D → V in LAD1. 1 Publication
    Corresponds to variant rs179363874 [ dbSNP | Ensembl ].
    VAR_065663
    Natural varianti351 – 3511N → S in LAD1. 1 Publication
    Corresponds to variant rs137852613 [ dbSNP | Ensembl ].
    VAR_003990
    Natural varianti586 – 5861R → W in LAD1. 1 Publication
    Corresponds to variant rs5030672 [ dbSNP | Ensembl ].
    VAR_003991
    Natural varianti593 – 5931R → C in LAD1. 1 Publication
    Corresponds to variant rs137852609 [ dbSNP | Ensembl ].
    VAR_003992
    Natural varianti716 – 7161G → A in LAD1. 1 Publication
    Corresponds to variant rs179363872 [ dbSNP | Ensembl ].
    VAR_065664

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi116920. phenotype.
    Orphaneti99842. Leukocyte adhesion deficiency type I.
    PharmGKBiPA29955.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Add
    BLAST
    Chaini23 – 769747Integrin beta-2PRO_0000016341Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei23 – 231Pyrrolidone carboxylic acid1 Publication
    Disulfide bondi25 ↔ 431 Publication
    Disulfide bondi33 ↔ 4471 Publication
    Disulfide bondi36 ↔ 621 Publication
    Disulfide bondi46 ↔ 731 Publication
    Glycosylationi50 – 501N-linked (GlcNAc...)2 Publications
    Glycosylationi116 – 1161N-linked (GlcNAc...)2 Publications
    Disulfide bondi191 ↔ 1981 Publication
    Glycosylationi212 – 2121N-linked (GlcNAc...)3 Publications
    Glycosylationi213 – 2131N-linked (GlcNAc...); atypical1 Publication
    Glycosylationi215 – 2151N-linked (GlcNAc...); atypical1 Publication
    Disulfide bondi246 ↔ 2861 Publication
    Glycosylationi254 – 2541N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi386 ↔ 4001 Publication
    Disulfide bondi420 ↔ 4451 Publication
    Disulfide bondi449 ↔ 4671 Publication
    Disulfide bondi459 ↔ 4701 Publication
    Disulfide bondi472 ↔ 4811 Publication
    Disulfide bondi483 ↔ 5141 Publication
    Disulfide bondi497 ↔ 5121 Publication
    Glycosylationi501 – 5011N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi506 ↔ 5171 Publication
    Disulfide bondi519 ↔ 5341 Publication
    Disulfide bondi536 ↔ 5591 Publication
    Disulfide bondi541 ↔ 5571 Publication
    Disulfide bondi549 ↔ 5621 Publication
    Disulfide bondi564 ↔ 5731 Publication
    Disulfide bondi575 ↔ 5981 Publication
    Disulfide bondi582 ↔ 5961 Publication
    Disulfide bondi590 ↔ 6011 Publication
    Disulfide bondi603 ↔ 6121 Publication
    Disulfide bondi615 ↔ 6181 Publication
    Disulfide bondi622 ↔ 6621 Publication
    Disulfide bondi628 ↔ 6471 Publication
    Disulfide bondi631 ↔ 6431 Publication
    Glycosylationi642 – 6421N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi670 ↔ 6951 Publication
    Modified residuei745 – 7451Phosphoserine; by PKC1 Publication
    Modified residuei756 – 7561Phosphoserine1 Publication
    Modified residuei758 – 7581Phosphothreonine; by PKC; in vitro1 Publication
    Modified residuei759 – 7591PhosphothreonineSequence Analysis
    Modified residuei760 – 7601Phosphothreonine; by PKC/PRKCA; in vitro1 Publication

    Post-translational modificationi

    Both Ser-745 and Ser-756 become phosphorylated when T-cells are exposed to phorbol esters. Phosphorylation on Thr-758 (but not on Ser-756) allows interaction with 14-3-3 proteins.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Pyrrolidone carboxylic acid

    Proteomic databases

    MaxQBiP05107.
    PaxDbiP05107.
    PRIDEiP05107.

    PTM databases

    PhosphoSiteiP05107.

    Miscellaneous databases

    PMAP-CutDBP05107.

    Expressioni

    Gene expression databases

    ArrayExpressiP05107.
    BgeeiP05107.
    CleanExiHS_ITGB2.
    GenevestigatoriP05107.

    Organism-specific databases

    HPAiHPA008877.
    HPA016894.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta subunit. Beta-2 associates with either alpha-L, alpha-M, alpha-X or alpha-D. Interacts with FGR By similarity. Interacts with COPS5 and RANBP9.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABL1P005194EBI-300173,EBI-375543
    RDXP352412EBI-300173,EBI-2514878
    TLN2Q9Y4G65EBI-300173,EBI-1220811

    Protein-protein interaction databases

    BioGridi109895. 25 interactions.
    DIPiDIP-478N.
    IntActiP05107. 14 interactions.
    MINTiMINT-129139.
    STRINGi9606.ENSP00000303242.

    Structurei

    Secondary structure

    1
    769
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi33 – 375
    Beta strandi44 – 463
    Helixi49 – 513
    Helixi58 – 614
    Helixi65 – 706
    Helixi75 – 773
    Beta strandi84 – 885
    Beta strandi91 – 944
    Beta strandi96 – 994
    Beta strandi101 – 1077
    Beta strandi113 – 1197
    Beta strandi127 – 1348
    Helixi137 – 1393
    Turni140 – 1423
    Helixi146 – 16015
    Beta strandi162 – 17110
    Turni177 – 1793
    Helixi184 – 1885
    Beta strandi196 – 1983
    Beta strandi203 – 21210
    Helixi214 – 2229
    Beta strandi230 – 2356
    Helixi236 – 24510
    Helixi247 – 2504
    Beta strandi254 – 26512
    Helixi272 – 2765
    Beta strandi289 – 2924
    Helixi294 – 2974
    Helixi304 – 31310
    Beta strandi316 – 3238
    Helixi324 – 3263
    Helixi327 – 3315
    Helixi333 – 3364
    Beta strandi337 – 3393
    Beta strandi341 – 3455
    Helixi352 – 36413
    Beta strandi365 – 3717
    Beta strandi378 – 3858
    Beta strandi387 – 3893
    Beta strandi391 – 40212
    Beta strandi409 – 41911
    Beta strandi424 – 4307
    Beta strandi437 – 4437
    Beta strandi452 – 4543
    Helixi458 – 4614
    Beta strandi462 – 4665
    Beta strandi469 – 4724
    Beta strandi476 – 4783
    Beta strandi483 – 4875
    Helixi490 – 4956
    Beta strandi498 – 5003
    Helixi505 – 5084
    Beta strandi509 – 5135
    Beta strandi516 – 5194
    Beta strandi528 – 5314
    Beta strandi536 – 5394
    Beta strandi544 – 5507
    Turni552 – 5543
    Beta strandi555 – 5584
    Beta strandi561 – 5644
    Beta strandi568 – 5703
    Beta strandi575 – 5773
    Turni580 – 5823
    Beta strandi593 – 5975
    Beta strandi600 – 6034
    Turni609 – 6113
    Beta strandi616 – 6183
    Helixi622 – 6243
    Helixi626 – 6349
    Helixi637 – 6393
    Turni640 – 6423
    Helixi643 – 6464
    Beta strandi650 – 6556
    Beta strandi658 – 6658
    Beta strandi667 – 6693
    Beta strandi671 – 6799
    Turni680 – 6834
    Beta strandi684 – 6896
    Beta strandi754 – 7629

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JX3model-A126-364[»]
    1L3YNMR-A535-574[»]
    1YUKX-ray1.80A23-125[»]
    B365-482[»]
    2JF1X-ray2.20T735-769[»]
    2P26X-ray1.75A23-535[»]
    2P28X-ray2.20A23-122[»]
    B362-574[»]
    2V7DX-ray2.50P/Q/R/S755-764[»]
    3K6SX-ray3.50B/D/F/H23-699[»]
    3K71X-ray3.95B/D/F/H23-699[»]
    3K72X-ray3.70B/D23-699[»]
    4NEHX-ray2.75B23-695[»]
    4NENX-ray2.90B23-696[»]
    ProteinModelPortaliP05107.
    SMRiP05107. Positions 23-696, 698-763.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05107.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 700678ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini724 – 76946CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei701 – 72323HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini124 – 363240VWFAAdd
    BLAST
    Repeati449 – 49648IAdd
    BLAST
    Repeati497 – 54044IIAdd
    BLAST
    Repeati541 – 58141IIIAdd
    BLAST
    Repeati582 – 61736IVAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni449 – 617169Cysteine-rich tandem repeatsAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi397 – 3993Cell attachment siteSequence Analysis

    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.
    InParanoidiP05107.
    KOiK06464.
    OMAiRGRCRCN.
    OrthoDBiEOG7T7GSB.
    PhylomeDBiP05107.
    TreeFamiTF105392.

    Family and domain databases

    Gene3Di3.40.50.410. 1 hit.
    InterProiIPR015812. Integrin_bsu.
    IPR015439. Integrin_bsu-2.
    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:SF15. PTHR10082:SF15. 1 hit.
    PfamiPF08725. Integrin_b_cyt. 1 hit.
    PF07965. Integrin_B_tail. 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. 2 hits.
    PS01186. EGF_2. 3 hits.
    PS00243. INTEGRIN_BETA. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P05107-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLGLRPPLLA LVGLLSLGCV LSQECTKFKV SSCRECIESG PGCTWCQKLN    50
    FTGPGDPDSI RCDTRPQLLM RGCAADDIMD PTSLAETQED HNGGQKQLSP 100
    QKVTLYLRPG QAAAFNVTFR RAKGYPIDLY YLMDLSYSML DDLRNVKKLG 150
    GDLLRALNEI TESGRIGFGS FVDKTVLPFV NTHPDKLRNP CPNKEKECQP 200
    PFAFRHVLKL TNNSNQFQTE VGKQLISGNL DAPEGGLDAM MQVAACPEEI 250
    GWRNVTRLLV FATDDGFHFA GDGKLGAILT PNDGRCHLED NLYKRSNEFD 300
    YPSVGQLAHK LAENNIQPIF AVTSRMVKTY EKLTEIIPKS AVGELSEDSS 350
    NVVQLIKNAY NKLSSRVFLD HNALPDTLKV TYDSFCSNGV THRNQPRGDC 400
    DGVQINVPIT FQVKVTATEC IQEQSFVIRA LGFTDIVTVQ VLPQCECRCR 450
    DQSRDRSLCH GKGFLECGIC RCDTGYIGKN CECQTQGRSS QELEGSCRKD 500
    NNSIICSGLG DCVCGQCLCH TSDVPGKLIY GQYCECDTIN CERYNGQVCG 550
    GPGRGLCFCG KCRCHPGFEG SACQCERTTE GCLNPRRVEC SGRGRCRCNV 600
    CECHSGYQLP LCQECPGCPS PCGKYISCAE CLKFEKGPFG KNCSAACPGL 650
    QLSNNPVKGR TCKERDSEGC WVAYTLEQQD GMDRYLIYVD ESRECVAGPN 700
    IAAIVGGTVA GIVLIGILLL VIWKALIHLS DLREYRRFEK EKLKSQWNND 750
    NPLFKSATTT VMNPKFAES 769
    Length:769
    Mass (Da):84,782
    Last modified:January 23, 2007 - v2
    Checksum:iEB9F3C3DF338B4E1
    GO

    Sequence cautioni

    The sequence BAD96225.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti199 – 1991Q → P in CAA68266. (PubMed:2954816)Curated
    Sequence conflicti279 – 2791L → P in BAD96225. 1 PublicationCurated
    Sequence conflicti526 – 5261G → C in BAG53190. (PubMed:14702039)Curated
    Sequence conflicti630 – 6301E → K in BAG53190. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti128 – 1281D → N in LAD1. 1 Publication
    Corresponds to variant rs137852615 [ dbSNP | Ensembl ].
    VAR_003984
    Natural varianti128 – 1281D → Y in LAD1. 1 Publication
    Corresponds to variant rs137852615 [ dbSNP | Ensembl ].
    VAR_065661
    Natural varianti138 – 1381S → P in LAD1. 1 Publication
    Corresponds to variant rs137852617 [ dbSNP | Ensembl ].
    VAR_013402
    Natural varianti149 – 1491L → P in LAD1. 1 Publication
    Corresponds to variant rs137852611 [ dbSNP | Ensembl ].
    VAR_003985
    Natural varianti169 – 1691G → R in LAD1. 2 Publications
    Corresponds to variant rs137852612 [ dbSNP | Ensembl ].
    VAR_003986
    Natural varianti178 – 1781P → L in LAD1. 2 Publications
    Corresponds to variant rs137852614 [ dbSNP | Ensembl ].
    VAR_003987
    Natural varianti196 – 1961K → T in LAD1. 1 Publication
    Corresponds to variant rs137852610 [ dbSNP | Ensembl ].
    VAR_003988
    Natural varianti239 – 2391A → T in LAD1. 1 Publication
    Corresponds to variant rs179363873 [ dbSNP | Ensembl ].
    VAR_065662
    Natural varianti273 – 2731G → R in LAD1. 1 Publication
    Corresponds to variant rs137852618 [ dbSNP | Ensembl ].
    VAR_013403
    Natural varianti284 – 2841G → S in LAD1. 1 Publication
    Corresponds to variant rs137852616 [ dbSNP | Ensembl ].
    VAR_003989
    Natural varianti300 – 3001D → V in LAD1. 1 Publication
    Corresponds to variant rs179363874 [ dbSNP | Ensembl ].
    VAR_065663
    Natural varianti351 – 3511N → S in LAD1. 1 Publication
    Corresponds to variant rs137852613 [ dbSNP | Ensembl ].
    VAR_003990
    Natural varianti354 – 3541Q → H.8 Publications
    Corresponds to variant rs235330 [ dbSNP | Ensembl ].
    VAR_030035
    Natural varianti586 – 5861R → W in LAD1. 1 Publication
    Corresponds to variant rs5030672 [ dbSNP | Ensembl ].
    VAR_003991
    Natural varianti593 – 5931R → C in LAD1. 1 Publication
    Corresponds to variant rs137852609 [ dbSNP | Ensembl ].
    VAR_003992
    Natural varianti716 – 7161G → A in LAD1. 1 Publication
    Corresponds to variant rs179363872 [ dbSNP | Ensembl ].
    VAR_065664

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15395 mRNA. Translation: AAA59490.1.
    X64072
    , X64073, X64074, X64075, X64076, X64077, X64078, X64079, X64080, X64081, X64082, X64083, X63924, X63925, X63926 Genomic DNA. Translation: CAA45427.1.
    AK095992 mRNA. Translation: BAG53190.1.
    AK222505 mRNA. Translation: BAD96225.1. Different initiation.
    AL163300 Genomic DNA. Translation: CAB90553.1.
    CH471079 Genomic DNA. Translation: EAX09381.1.
    CH471079 Genomic DNA. Translation: EAX09382.1.
    CH471079 Genomic DNA. Translation: EAX09385.1.
    BC005861 mRNA. Translation: AAH05861.1.
    Y00057 mRNA. Translation: CAA68266.1.
    S81234 mRNA. Translation: AAB21404.1.
    CCDSiCCDS13716.1.
    PIRiA25967. IJHULM.
    RefSeqiNP_000202.2. NM_000211.3.
    NP_001120963.1. NM_001127491.1.
    UniGeneiHs.375957.

    Genome annotation databases

    EnsembliENST00000302347; ENSP00000303242; ENSG00000160255.
    ENST00000355153; ENSP00000347279; ENSG00000160255.
    ENST00000397850; ENSP00000380948; ENSG00000160255.
    ENST00000397852; ENSP00000380950; ENSG00000160255.
    ENST00000397857; ENSP00000380955; ENSG00000160255.
    GeneIDi3689.
    KEGGihsa:3689.
    UCSCiuc002zgd.2. human.

    Polymorphism databases

    DMDMi124056465.

    Cross-referencesi

    Web resourcesi

    ITGB2base

    ITGB2 mutation db

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15395 mRNA. Translation: AAA59490.1 .
    X64072
    , X64073 , X64074 , X64075 , X64076 , X64077 , X64078 , X64079 , X64080 , X64081 , X64082 , X64083 , X63924 , X63925 , X63926 Genomic DNA. Translation: CAA45427.1 .
    AK095992 mRNA. Translation: BAG53190.1 .
    AK222505 mRNA. Translation: BAD96225.1 . Different initiation.
    AL163300 Genomic DNA. Translation: CAB90553.1 .
    CH471079 Genomic DNA. Translation: EAX09381.1 .
    CH471079 Genomic DNA. Translation: EAX09382.1 .
    CH471079 Genomic DNA. Translation: EAX09385.1 .
    BC005861 mRNA. Translation: AAH05861.1 .
    Y00057 mRNA. Translation: CAA68266.1 .
    S81234 mRNA. Translation: AAB21404.1 .
    CCDSi CCDS13716.1.
    PIRi A25967. IJHULM.
    RefSeqi NP_000202.2. NM_000211.3.
    NP_001120963.1. NM_001127491.1.
    UniGenei Hs.375957.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JX3 model - A 126-364 [» ]
    1L3Y NMR - A 535-574 [» ]
    1YUK X-ray 1.80 A 23-125 [» ]
    B 365-482 [» ]
    2JF1 X-ray 2.20 T 735-769 [» ]
    2P26 X-ray 1.75 A 23-535 [» ]
    2P28 X-ray 2.20 A 23-122 [» ]
    B 362-574 [» ]
    2V7D X-ray 2.50 P/Q/R/S 755-764 [» ]
    3K6S X-ray 3.50 B/D/F/H 23-699 [» ]
    3K71 X-ray 3.95 B/D/F/H 23-699 [» ]
    3K72 X-ray 3.70 B/D 23-699 [» ]
    4NEH X-ray 2.75 B 23-695 [» ]
    4NEN X-ray 2.90 B 23-696 [» ]
    ProteinModelPortali P05107.
    SMRi P05107. Positions 23-696, 698-763.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109895. 25 interactions.
    DIPi DIP-478N.
    IntActi P05107. 14 interactions.
    MINTi MINT-129139.
    STRINGi 9606.ENSP00000303242.

    Chemistry

    BindingDBi P05107.
    ChEMBLi CHEMBL2096661.
    DrugBanki DB00641. Simvastatin.

    PTM databases

    PhosphoSitei P05107.

    Polymorphism databases

    DMDMi 124056465.

    Proteomic databases

    MaxQBi P05107.
    PaxDbi P05107.
    PRIDEi P05107.

    Protocols and materials databases

    DNASUi 3689.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000302347 ; ENSP00000303242 ; ENSG00000160255 .
    ENST00000355153 ; ENSP00000347279 ; ENSG00000160255 .
    ENST00000397850 ; ENSP00000380948 ; ENSG00000160255 .
    ENST00000397852 ; ENSP00000380950 ; ENSG00000160255 .
    ENST00000397857 ; ENSP00000380955 ; ENSG00000160255 .
    GeneIDi 3689.
    KEGGi hsa:3689.
    UCSCi uc002zgd.2. human.

    Organism-specific databases

    CTDi 3689.
    GeneCardsi GC21M046305.
    HGNCi HGNC:6155. ITGB2.
    HPAi HPA008877.
    HPA016894.
    MIMi 116920. phenotype.
    600065. gene.
    neXtProti NX_P05107.
    Orphaneti 99842. Leukocyte adhesion deficiency type I.
    PharmGKBi PA29955.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG287997.
    HOGENOMi HOG000252936.
    HOVERGENi HBG006190.
    InParanoidi P05107.
    KOi K06464.
    OMAi RGRCRCN.
    OrthoDBi EOG7T7GSB.
    PhylomeDBi P05107.
    TreeFami TF105392.

    Enzyme and pathway databases

    Reactomei REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_12051. Cell surface interactions at the vascular wall.
    REACT_13552. Integrin cell surface interactions.
    REACT_6894. Toll Like Receptor 4 (TLR4) Cascade.
    SignaLinki P05107.

    Miscellaneous databases

    ChiTaRSi ITGB2. human.
    EvolutionaryTracei P05107.
    GeneWikii CD18.
    GenomeRNAii 3689.
    NextBioi 14449.
    PMAP-CutDB P05107.
    PROi P05107.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P05107.
    Bgeei P05107.
    CleanExi HS_ITGB2.
    Genevestigatori P05107.

    Family and domain databases

    Gene3Di 3.40.50.410. 1 hit.
    InterProi IPR015812. Integrin_bsu.
    IPR015439. Integrin_bsu-2.
    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:SF15. PTHR10082:SF15. 1 hit.
    Pfami PF08725. Integrin_b_cyt. 1 hit.
    PF07965. Integrin_B_tail. 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. 2 hits.
    PS01186. EGF_2. 3 hits.
    PS00243. INTEGRIN_BETA. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of the beta subunit of the leukocyte adhesion proteins: homology to an extracellular matrix receptor defines a novel supergene family."
      Kishimoto T.K., O'Connor K., Lee A., Roberts T.M., Springer T.A.
      Cell 48:681-690(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT HIS-354.
    2. "The gene organisation of the human beta 2 integrin subunit (CD18)."
      Weitzman J.B., Wells C.E., Wright A.H., Clark P.A., Law S.K.A.
      FEBS Lett. 294:97-103(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-354.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-354.
      Tissue: Synovial cell.
    4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-354.
      Tissue: Adipose tissue.
    5. "The DNA sequence of human chromosome 21."
      Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
      , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
      Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT HIS-354.
    7. "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], VARIANT HIS-354.
      Tissue: Muscle.
    8. "The primary structure of the beta-subunit of the cell surface adhesion glycoproteins LFA-1, CR3 and p150,95 and its relationship to the fibronectin receptor."
      Law S.K.A., Gagnon J., Hildreth J.E., Wells C.E., Willis A.C., Wong A.J.
      EMBO J. 6:915-919(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-769, PARTIAL PROTEIN SEQUENCE, PYROGLUTAMATE FORMATION AT GLN-23, VARIANT HIS-354.
      Tissue: Spleen.
    9. "Familial genetic defect in a case of leukocyte adhesion deficiency."
      Ohashi Y., Yambe T., Tsuchiya S., Kikuchi H., Konno T.
      Hum. Mutat. 2:458-467(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 124-199, VARIANT LAD1 LEU-178.
      Tissue: Lymphoblast.
    10. "Genetic cause of leukocyte adhesion molecule deficiency. Abnormal splicing and a missense mutation in a conserved region of CD18 impair cell surface expression of beta 2 integrins."
      Nelson C., Rabb H., Arnaout M.A.
      J. Biol. Chem. 267:3351-3357(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 347-355, VARIANTS LAD1 SER-351 AND TRP-586, VARIANT HIS-354.
    11. "Integrin LFA-1 interacts with the transcriptional co-activator JAB1 to modulate AP-1 activity."
      Bianchi E., Denti S., Granata A., Bossi G., Geginat J., Villa A., Rogge L., Pardi R.
      Nature 404:617-621(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH COPS5.
    12. "Phosphorylation of the cytoplasmic domain of the integrin CD18 chain by protein kinase C isoforms in leukocytes."
      Fagerholm S., Morrice N., Gahmberg C.G., Cohen P.
      J. Biol. Chem. 277:1728-1738(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-745; SER-756; THR-758 AND THR-760.
    13. "RanBPM is a phosphoprotein that associates with the plasma membrane and interacts with the integrin LFA-1."
      Denti S., Sirri A., Cheli A., Rogge L., Innamorati G., Putignano S., Fabbri M., Pardi R., Bianchi E.
      J. Biol. Chem. 279:13027-13034(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RANBP9.
    14. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-212.
      Tissue: Plasma.
    15. "Nonmuscle myosin light-chain kinase mediates neutrophil transmigration in sepsis-induced lung inflammation by activating beta2 integrins."
      Xu J., Gao X.-P., Ramchandran R., Zhao Y.-Y., Vogel S.M., Malik A.B.
      Nat. Immunol. 9:880-886(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION DURING LUNG INJURY.
    16. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-50 AND ASN-212.
      Tissue: Liver.
    17. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-50; ASN-116; ASN-212; ASN-213 AND ASN-215.
      Tissue: Leukemic T-cell.
    18. "Structure of an integrin with an alphaI domain, complement receptor type 4."
      Xie C., Zhu J., Chen X., Mi L., Nishida N., Springer T.A.
      EMBO J. 29:666-679(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 23-699 IN COMPLEX WITH ITGAX, GLYCOSYLATION AT ASN-116, DISULFIDE BONDS, CALCIUM-BINDING SITES, SUBUNIT.
    19. "Point mutations impairing cell surface expression of the common beta subunit (CD18) in a patient with leukocyte adhesion molecule (Leu-CAM) deficiency."
      Arnaout M.A., Dana N., Gupta S.K., Tenen D.G., Fathallah D.M.
      J. Clin. Invest. 85:977-981(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS LAD1 THR-196 AND CYS-593.
    20. "Distinct mutations in two patients with leukocyte adhesion deficiency and their functional correlates."
      Wardlaw A.J., Hibbs M.L., Stacker S.A., Springer T.A.
      J. Exp. Med. 172:335-345(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS LAD1 PRO-149 AND ARG-169.
    21. "Leukocyte adhesion deficiency: identification of novel mutations in two Japanese patients with a severe form."
      Matsuura S., Kishi F., Tsukahara M., Nunoi H., Matsuda I., Kobayashi K., Kajii T.
      Biochem. Biophys. Res. Commun. 184:1460-1467(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LAD1 ASN-128.
    22. "Molecular basis for a severe case of leukocyte adhesion deficiency."
      Corbi A., Vara A., Ursa A., Rodriguez M.C.G., Fontan G., Sanchez-Madrid F.
      Eur. J. Immunol. 22:1877-1881(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LAD1 ARG-169.
    23. "Identification of two molecular defects in a child with leukocyte adherence deficiency."
      Back L.L., Kwok W.W., Hickstein D.D.
      J. Biol. Chem. 267:5482-5487(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LAD1 LEU-178.
    24. "A point mutation associated with leukocyte adhesion deficiency type 1 of moderate severity."
      Back L.A., Kerkering M., Baker D., Bauer T.R., Embree L.J., Hickstein D.D.
      Biochem. Biophys. Res. Commun. 193:912-918(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LAD1 SER-284.
    25. "A novel leukocyte adhesion deficiency caused by expressed but nonfunctional beta2 integrins Mac-1 and LFA-1."
      Hogg N., Stewart M.P., Scarth S.L., Newton R., Shaw J.M., Law S.K.A., Klein N.
      J. Clin. Invest. 103:97-106(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS LAD1 PRO-138 AND ARG-273.
    26. "A novel point mutation in CD18 causing leukocyte adhesion deficiency in a Chinese patient."
      Li L., Jin Y.Y., Cao R.M., Chen T.X.
      Chin. Med. J. 123:1278-1282(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LAD1 VAL-300.
    27. "Characterization of 11 new cases of leukocyte adhesion deficiency type 1 with seven novel mutations in the ITGB2 gene."
      Parvaneh N., Mamishi S., Rezaei A., Rezaei N., Tamizifar B., Parvaneh L., Sherkat R., Ghalehbaghi B., Kashef S., Chavoshzadeh Z., Isaeian A., Ashrafi F., Aghamohammadi A.
      J. Clin. Immunol. 30:756-760(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS LAD1 TYR-128; THR-239 AND ALA-716.

    Entry informationi

    Entry nameiITB2_HUMAN
    AccessioniPrimary (citable) accession number: P05107
    Secondary accession number(s): B3KTS8
    , D3DSM1, Q16418, Q53HS5, Q9UD72
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 193 of the entry and version 2 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 21
      Human chromosome 21: 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

    External Data

    Dasty 3