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Protein

Integrin beta-2

Gene

ITGB2

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

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. Contributes to natural killer cell cytotoxicity (PubMed:15356110). Involved in leukocyte adhesion and transmigration of leukocytes including T-cells and neutrophils (PubMed:11812992). Triggers neutrophil transmigration during lung injury through PTK2B/PYK2-mediated activation (PubMed:18587400). Integrin alpha-L/beta-2 in association with ICAM3, contributes to apoptotic neutrophil phagocytosis by macrophages (PubMed:23775590).4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi138Calcium; via carbonyl oxygen1
Metal bindingi141Calcium1
Metal bindingi142Calcium1
Metal bindingi347Calcium1

GO - Molecular functioni

  • cell adhesion molecule binding Source: UniProtKB
  • glycoprotein binding Source: BHF-UCL
  • ICAM-3 receptor activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • protein kinase binding Source: UniProtKB

GO - Biological processi

  • aging Source: Ensembl
  • apoptotic process Source: UniProtKB
  • cell adhesion Source: ProtInc
  • cell-cell signaling Source: UniProtKB
  • cell-matrix adhesion Source: UniProtKB
  • cellular extravasation Source: Ensembl
  • cellular response to low-density lipoprotein particle stimulus Source: UniProtKB
  • endodermal cell differentiation Source: UniProtKB
  • endothelial cell migration Source: Ensembl
  • extracellular matrix organization Source: Reactome
  • heterotypic cell-cell adhesion Source: UniProtKB
  • inflammatory response Source: UniProtKB
  • integrin-mediated signaling pathway Source: UniProtKB
  • leukocyte cell-cell adhesion Source: UniProtKB
  • leukocyte migration Source: Reactome
  • leukocyte migration involved in inflammatory response Source: Ensembl
  • natural killer cell activation Source: Ensembl
  • neutrophil chemotaxis Source: UniProtKB
  • phagocytosis Source: UniProtKB-KW
  • positive regulation of angiogenesis Source: Ensembl
  • positive regulation of NF-kappaB transcription factor activity Source: Ensembl
  • positive regulation of nitric oxide biosynthetic process Source: Ensembl
  • receptor clustering Source: UniProtKB
  • receptor internalization Source: UniProtKB
  • regulation of cell shape Source: UniProtKB
  • regulation of immune response Source: Reactome
  • regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
  • toll-like receptor 4 signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Integrin, Receptor

Keywords - Biological processi

Cell adhesion, Phagocytosis

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000160255-MONOMER.
ReactomeiR-HSA-166016. Toll Like Receptor 4 (TLR4) Cascade.
R-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.
R-HSA-6798695. Neutrophil degranulation.
SignaLinkiP05107.
SIGNORiP05107.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 21

Organism-specific databases

HGNCiHGNC:6155. ITGB2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini23 – 700ExtracellularSequence analysisAdd BLAST678
Transmembranei701 – 723HelicalSequence analysisAdd BLAST23
Topological domaini724 – 769CytoplasmicSequence analysisAdd BLAST46

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular vesicle Source: UniProtKB
  • integrin alphaL-beta2 complex Source: UniProtKB
  • integrin complex Source: UniProtKB
  • membrane Source: UniProtKB
  • plasma membrane Source: Reactome
  • receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Leukocyte adhesion deficiency 1 (LAD1)11 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionLAD1 patients have recurrent bacterial infections and their leukocytes are deficient in a wide range of adhesion-dependent functions.
See also OMIM:116920
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_003984128D → N in LAD1. 1 PublicationCorresponds to variant rs137852615dbSNPEnsembl.1
Natural variantiVAR_065661128D → Y in LAD1. 1 PublicationCorresponds to variant rs137852615dbSNPEnsembl.1
Natural variantiVAR_013402138S → P in LAD1. 1 PublicationCorresponds to variant rs137852617dbSNPEnsembl.1
Natural variantiVAR_003985149L → P in LAD1. 1 PublicationCorresponds to variant rs137852611dbSNPEnsembl.1
Natural variantiVAR_003986169G → R in LAD1. 2 PublicationsCorresponds to variant rs137852612dbSNPEnsembl.1
Natural variantiVAR_003987178P → L in LAD1. 2 PublicationsCorresponds to variant rs137852614dbSNPEnsembl.1
Natural variantiVAR_003988196K → T in LAD1. 1 PublicationCorresponds to variant rs137852610dbSNPEnsembl.1
Natural variantiVAR_065662239A → T in LAD1. 1 PublicationCorresponds to variant rs179363873dbSNPEnsembl.1
Natural variantiVAR_013403273G → R in LAD1. 1 PublicationCorresponds to variant rs137852618dbSNPEnsembl.1
Natural variantiVAR_003989284G → S in LAD1. 1 PublicationCorresponds to variant rs137852616dbSNPEnsembl.1
Natural variantiVAR_065663300D → V in LAD1. 1 PublicationCorresponds to variant rs179363874dbSNPEnsembl.1
Natural variantiVAR_003990351N → S in LAD1. 1 PublicationCorresponds to variant rs137852613dbSNPEnsembl.1
Natural variantiVAR_003991586R → W in LAD1. 1 PublicationCorresponds to variant rs5030672dbSNPEnsembl.1
Natural variantiVAR_003992593R → C in LAD1. 1 PublicationCorresponds to variant rs137852609dbSNPEnsembl.1
Natural variantiVAR_065664716G → A in LAD1. 1 PublicationCorresponds to variant rs179363872dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi758T → A: Abolishes phosphorylation. Reduces COS cell adhesion to ICAM1. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi3689.
MalaCardsiITGB2.
MIMi116920. phenotype.
Orphaneti99842. Leukocyte adhesion deficiency type I.
PharmGKBiPA29955.

Chemistry databases

ChEMBLiCHEMBL2096661.
DrugBankiDB00641. Simvastatin.

Polymorphism and mutation databases

BioMutaiITGB2.
DMDMi124056465.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Add BLAST22
ChainiPRO_000001634123 – 769Integrin beta-2Add BLAST747

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei23Pyrrolidone carboxylic acid1 Publication1
Disulfide bondi25 ↔ 431 Publication
Disulfide bondi33 ↔ 4471 Publication
Disulfide bondi36 ↔ 621 Publication
Disulfide bondi46 ↔ 731 Publication
Glycosylationi50N-linked (GlcNAc...)2 Publications1
Glycosylationi116N-linked (GlcNAc...)2 Publications1
Disulfide bondi191 ↔ 1981 Publication
Glycosylationi212N-linked (GlcNAc...)3 Publications1
Glycosylationi213N-linked (GlcNAc...); atypical1 Publication1
Glycosylationi215N-linked (GlcNAc...); atypical1 Publication1
Disulfide bondi246 ↔ 2861 Publication
Glycosylationi254N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi501N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi642N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi670 ↔ 6951 Publication
Modified residuei745Phosphoserine; by PKC1 Publication1
Modified residuei756Phosphoserine1 Publication1
Modified residuei758Phosphothreonine; by PKC; in vitro2 Publications1
Modified residuei759PhosphothreonineSequence analysis1
Modified residuei760Phosphothreonine; by PKC/PRKCA; in vitro1 Publication1

Post-translational modificationi

Both Ser-745 and Ser-756 become phosphorylated when T-cells are exposed to phorbol esters (PubMed:11700305). Phosphorylation on Thr-758 (but not on Ser-756) allows interaction with 14-3-3 proteins (PubMed:11700305, PubMed:16301335).2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Pyrrolidone carboxylic acid

Proteomic databases

EPDiP05107.
MaxQBiP05107.
PaxDbiP05107.
PeptideAtlasiP05107.
PRIDEiP05107.

PTM databases

iPTMnetiP05107.
PhosphoSitePlusiP05107.

Miscellaneous databases

PMAP-CutDBP05107.

Expressioni

Tissue specificityi

Leukocytes.1 Publication

Gene expression databases

BgeeiENSG00000160255.
CleanExiHS_ITGB2.
ExpressionAtlasiP05107. baseline and differential.
GenevisibleiP05107. HS.

Organism-specific databases

HPAiHPA008877.
HPA016894.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit (PubMed:20033057). Beta-2 associates with either alpha-L, alpha-M, alpha-X or alpha-D. Interacts with FGR (By similarity). Interacts with COPS5 and RANBP9 (PubMed:10766246, PubMed:14722085). Interacts with FLNA (via filamin repeats 4, 9, 12, 17, 19, 21, and 23) (PubMed:19828450). Interacts with THBD (PubMed:27055590).By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABL1P005194EBI-300173,EBI-375543
NOTCH2NLQ7Z3S95EBI-300173,EBI-945833
RDXP352412EBI-300173,EBI-2514878
TLN2Q9Y4G65EBI-300173,EBI-1220811

GO - Molecular functioni

  • cell adhesion molecule binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109895. 28 interactors.
DIPiDIP-478N.
IntActiP05107. 22 interactors.
MINTiMINT-129139.
STRINGi9606.ENSP00000303242.

Chemistry databases

BindingDBiP05107.

Structurei

Secondary structure

1769
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi33 – 37Combined sources5
Beta strandi44 – 46Combined sources3
Helixi49 – 51Combined sources3
Beta strandi54 – 56Combined sources3
Helixi58 – 61Combined sources4
Helixi65 – 70Combined sources6
Helixi75 – 77Combined sources3
Beta strandi84 – 88Combined sources5
Beta strandi91 – 94Combined sources4
Beta strandi96 – 99Combined sources4
Beta strandi101 – 107Combined sources7
Beta strandi113 – 119Combined sources7
Beta strandi127 – 134Combined sources8
Helixi137 – 139Combined sources3
Helixi140 – 146Combined sources7
Helixi150 – 160Combined sources11
Beta strandi161 – 163Combined sources3
Beta strandi165 – 171Combined sources7
Turni177 – 179Combined sources3
Helixi184 – 188Combined sources5
Beta strandi196 – 198Combined sources3
Beta strandi203 – 212Combined sources10
Helixi214 – 222Combined sources9
Beta strandi230 – 234Combined sources5
Helixi236 – 245Combined sources10
Helixi247 – 250Combined sources4
Beta strandi254 – 265Combined sources12
Helixi272 – 276Combined sources5
Beta strandi289 – 292Combined sources4
Helixi294 – 297Combined sources4
Helixi304 – 313Combined sources10
Beta strandi316 – 322Combined sources7
Helixi324 – 326Combined sources3
Helixi327 – 331Combined sources5
Helixi333 – 336Combined sources4
Beta strandi337 – 339Combined sources3
Beta strandi341 – 344Combined sources4
Helixi352 – 364Combined sources13
Beta strandi365 – 371Combined sources7
Beta strandi378 – 385Combined sources8
Beta strandi387 – 389Combined sources3
Beta strandi391 – 402Combined sources12
Beta strandi409 – 419Combined sources11
Beta strandi424 – 430Combined sources7
Beta strandi437 – 443Combined sources7
Beta strandi452 – 454Combined sources3
Helixi458 – 461Combined sources4
Beta strandi462 – 466Combined sources5
Beta strandi469 – 472Combined sources4
Beta strandi476 – 478Combined sources3
Beta strandi483 – 487Combined sources5
Helixi490 – 495Combined sources6
Beta strandi498 – 500Combined sources3
Helixi505 – 508Combined sources4
Beta strandi509 – 513Combined sources5
Beta strandi516 – 519Combined sources4
Beta strandi528 – 531Combined sources4
Beta strandi536 – 539Combined sources4
Beta strandi544 – 550Combined sources7
Turni552 – 554Combined sources3
Beta strandi555 – 558Combined sources4
Beta strandi561 – 564Combined sources4
Beta strandi568 – 570Combined sources3
Beta strandi575 – 577Combined sources3
Turni580 – 582Combined sources3
Turni590 – 592Combined sources3
Beta strandi593 – 597Combined sources5
Beta strandi600 – 603Combined sources4
Turni609 – 611Combined sources3
Beta strandi616 – 618Combined sources3
Helixi622 – 624Combined sources3
Helixi626 – 634Combined sources9
Helixi637 – 639Combined sources3
Turni640 – 642Combined sources3
Helixi643 – 646Combined sources4
Beta strandi650 – 655Combined sources6
Beta strandi658 – 665Combined sources8
Beta strandi667 – 669Combined sources3
Beta strandi671 – 679Combined sources9
Turni680 – 683Combined sources4
Beta strandi684 – 689Combined sources6
Beta strandi754 – 762Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5E6RX-ray2.90B23-482[»]
5E6SX-ray2.15B/D/F23-482[»]
5E6UX-ray2.50B23-482[»]
5E6VX-ray1.80A24-482[»]
5E6WX-ray2.20A23-118[»]
A362-574[»]
5E6XX-ray1.75A23-535[»]
5ES4X-ray3.30B/D/F/H23-696[»]
ProteinModelPortaliP05107.
SMRiP05107.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05107.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini124 – 363VWFAAdd BLAST240
Repeati449 – 496IAdd BLAST48
Repeati497 – 540IIAdd BLAST44
Repeati541 – 581IIIAdd BLAST41
Repeati582 – 617IVAdd BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni449 – 617Cysteine-rich tandem repeatsAdd BLAST169

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi397 – 399Cell attachment siteSequence analysis3

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.
HOGENOMiHOG000252936.
HOVERGENiHBG006190.
InParanoidiP05107.
KOiK06464.
OrthoDBiEOG091G029W.
PhylomeDBiP05107.
TreeFamiTF105392.

Family and domain databases

Gene3Di3.40.50.410. 1 hit.
InterProiIPR033760. Integin_beta_N.
IPR015812. Integrin_bsu.
IPR015439. Integrin_bsu-2.
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:SF15. PTHR10082:SF15. 1 hit.
PfamiPF08725. Integrin_b_cyt. 1 hit.
PF07965. Integrin_B_tail. 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. 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

        10         20         30         40         50
MLGLRPPLLA LVGLLSLGCV LSQECTKFKV SSCRECIESG PGCTWCQKLN
60 70 80 90 100
FTGPGDPDSI RCDTRPQLLM RGCAADDIMD PTSLAETQED HNGGQKQLSP
110 120 130 140 150
QKVTLYLRPG QAAAFNVTFR RAKGYPIDLY YLMDLSYSML DDLRNVKKLG
160 170 180 190 200
GDLLRALNEI TESGRIGFGS FVDKTVLPFV NTHPDKLRNP CPNKEKECQP
210 220 230 240 250
PFAFRHVLKL TNNSNQFQTE VGKQLISGNL DAPEGGLDAM MQVAACPEEI
260 270 280 290 300
GWRNVTRLLV FATDDGFHFA GDGKLGAILT PNDGRCHLED NLYKRSNEFD
310 320 330 340 350
YPSVGQLAHK LAENNIQPIF AVTSRMVKTY EKLTEIIPKS AVGELSEDSS
360 370 380 390 400
NVVQLIKNAY NKLSSRVFLD HNALPDTLKV TYDSFCSNGV THRNQPRGDC
410 420 430 440 450
DGVQINVPIT FQVKVTATEC IQEQSFVIRA LGFTDIVTVQ VLPQCECRCR
460 470 480 490 500
DQSRDRSLCH GKGFLECGIC RCDTGYIGKN CECQTQGRSS QELEGSCRKD
510 520 530 540 550
NNSIICSGLG DCVCGQCLCH TSDVPGKLIY GQYCECDTIN CERYNGQVCG
560 570 580 590 600
GPGRGLCFCG KCRCHPGFEG SACQCERTTE GCLNPRRVEC SGRGRCRCNV
610 620 630 640 650
CECHSGYQLP LCQECPGCPS PCGKYISCAE CLKFEKGPFG KNCSAACPGL
660 670 680 690 700
QLSNNPVKGR TCKERDSEGC WVAYTLEQQD GMDRYLIYVD ESRECVAGPN
710 720 730 740 750
IAAIVGGTVA GIVLIGILLL VIWKALIHLS DLREYRRFEK EKLKSQWNND
760
NPLFKSATTT VMNPKFAES
Length:769
Mass (Da):84,782
Last modified:January 23, 2007 - v2
Checksum:iEB9F3C3DF338B4E1
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti199Q → P in CAA68266 (PubMed:2954816).Curated1
Sequence conflicti279L → P in BAD96225 (Ref. 4) Curated1
Sequence conflicti526G → C in BAG53190 (PubMed:14702039).Curated1
Sequence conflicti630E → K in BAG53190 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_003984128D → N in LAD1. 1 PublicationCorresponds to variant rs137852615dbSNPEnsembl.1
Natural variantiVAR_065661128D → Y in LAD1. 1 PublicationCorresponds to variant rs137852615dbSNPEnsembl.1
Natural variantiVAR_013402138S → P in LAD1. 1 PublicationCorresponds to variant rs137852617dbSNPEnsembl.1
Natural variantiVAR_003985149L → P in LAD1. 1 PublicationCorresponds to variant rs137852611dbSNPEnsembl.1
Natural variantiVAR_003986169G → R in LAD1. 2 PublicationsCorresponds to variant rs137852612dbSNPEnsembl.1
Natural variantiVAR_003987178P → L in LAD1. 2 PublicationsCorresponds to variant rs137852614dbSNPEnsembl.1
Natural variantiVAR_003988196K → T in LAD1. 1 PublicationCorresponds to variant rs137852610dbSNPEnsembl.1
Natural variantiVAR_065662239A → T in LAD1. 1 PublicationCorresponds to variant rs179363873dbSNPEnsembl.1
Natural variantiVAR_013403273G → R in LAD1. 1 PublicationCorresponds to variant rs137852618dbSNPEnsembl.1
Natural variantiVAR_003989284G → S in LAD1. 1 PublicationCorresponds to variant rs137852616dbSNPEnsembl.1
Natural variantiVAR_065663300D → V in LAD1. 1 PublicationCorresponds to variant rs179363874dbSNPEnsembl.1
Natural variantiVAR_003990351N → S in LAD1. 1 PublicationCorresponds to variant rs137852613dbSNPEnsembl.1
Natural variantiVAR_030035354Q → H.8 PublicationsCorresponds to variant rs235330dbSNPEnsembl.1
Natural variantiVAR_003991586R → W in LAD1. 1 PublicationCorresponds to variant rs5030672dbSNPEnsembl.1
Natural variantiVAR_003992593R → C in LAD1. 1 PublicationCorresponds to variant rs137852609dbSNPEnsembl.1
Natural variantiVAR_065664716G → A in LAD1. 1 PublicationCorresponds to variant rs179363872dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_000202.3. NM_000211.4.
NP_001120963.2. NM_001127491.2.
NP_001290167.1. NM_001303238.1.
UniGeneiHs.375957.

Genome annotation databases

EnsembliENST00000302347; ENSP00000303242; ENSG00000160255.
ENST00000355153; ENSP00000347279; ENSG00000160255.
ENST00000397850; ENSP00000380948; ENSG00000160255.
ENST00000397852; ENSP00000380950; ENSG00000160255.
ENST00000397857; ENSP00000380955; ENSG00000160255.
GeneIDi3689.
KEGGihsa:3689.
UCSCiuc002zgd.4. human.

Cross-referencesi

Web resourcesi

ITGB2base

ITGB2 mutation db

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_000202.3. NM_000211.4.
NP_001120963.2. NM_001127491.2.
NP_001290167.1. NM_001303238.1.
UniGeneiHs.375957.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5E6RX-ray2.90B23-482[»]
5E6SX-ray2.15B/D/F23-482[»]
5E6UX-ray2.50B23-482[»]
5E6VX-ray1.80A24-482[»]
5E6WX-ray2.20A23-118[»]
A362-574[»]
5E6XX-ray1.75A23-535[»]
5ES4X-ray3.30B/D/F/H23-696[»]
ProteinModelPortaliP05107.
SMRiP05107.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109895. 28 interactors.
DIPiDIP-478N.
IntActiP05107. 22 interactors.
MINTiMINT-129139.
STRINGi9606.ENSP00000303242.

Chemistry databases

BindingDBiP05107.
ChEMBLiCHEMBL2096661.
DrugBankiDB00641. Simvastatin.

PTM databases

iPTMnetiP05107.
PhosphoSitePlusiP05107.

Polymorphism and mutation databases

BioMutaiITGB2.
DMDMi124056465.

Proteomic databases

EPDiP05107.
MaxQBiP05107.
PaxDbiP05107.
PeptideAtlasiP05107.
PRIDEiP05107.

Protocols and materials databases

DNASUi3689.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302347; ENSP00000303242; ENSG00000160255.
ENST00000355153; ENSP00000347279; ENSG00000160255.
ENST00000397850; ENSP00000380948; ENSG00000160255.
ENST00000397852; ENSP00000380950; ENSG00000160255.
ENST00000397857; ENSP00000380955; ENSG00000160255.
GeneIDi3689.
KEGGihsa:3689.
UCSCiuc002zgd.4. human.

Organism-specific databases

CTDi3689.
DisGeNETi3689.
GeneCardsiITGB2.
HGNCiHGNC:6155. ITGB2.
HPAiHPA008877.
HPA016894.
MalaCardsiITGB2.
MIMi116920. phenotype.
600065. gene.
neXtProtiNX_P05107.
Orphaneti99842. Leukocyte adhesion deficiency type I.
PharmGKBiPA29955.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1226. Eukaryota.
ENOG410XP60. LUCA.
HOGENOMiHOG000252936.
HOVERGENiHBG006190.
InParanoidiP05107.
KOiK06464.
OrthoDBiEOG091G029W.
PhylomeDBiP05107.
TreeFamiTF105392.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000160255-MONOMER.
ReactomeiR-HSA-166016. Toll Like Receptor 4 (TLR4) Cascade.
R-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.
R-HSA-6798695. Neutrophil degranulation.
SignaLinkiP05107.
SIGNORiP05107.

Miscellaneous databases

ChiTaRSiITGB2. human.
EvolutionaryTraceiP05107.
GeneWikiiCD18.
GenomeRNAii3689.
PMAP-CutDBP05107.
PROiP05107.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000160255.
CleanExiHS_ITGB2.
ExpressionAtlasiP05107. baseline and differential.
GenevisibleiP05107. HS.

Family and domain databases

Gene3Di3.40.50.410. 1 hit.
InterProiIPR033760. Integin_beta_N.
IPR015812. Integrin_bsu.
IPR015439. Integrin_bsu-2.
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:SF15. PTHR10082:SF15. 1 hit.
PfamiPF08725. Integrin_b_cyt. 1 hit.
PF07965. Integrin_B_tail. 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. 2 hits.
PS01186. EGF_2. 3 hits.
PS00243. INTEGRIN_BETA. 3 hits.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 216 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

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.