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P05107

- ITB2_HUMAN

UniProt

P05107 - ITB2_HUMAN

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Protein

Integrin beta-2

Gene

ITGB2

Organism
Homo sapiens (Human)
Status
Reviewed - 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. 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. cell adhesion molecule binding Source: UniProtKB
  2. glycoprotein binding Source: BHF-UCL
  3. ICAM-3 receptor activity Source: UniProtKB
  4. metal ion binding Source: UniProtKB-KW
  5. protein kinase binding Source: UniProtKB

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: UniProtKB
  6. endodermal cell differentiation Source: UniProtKB
  7. extracellular matrix organization Source: Reactome
  8. heterotypic cell-cell adhesion Source: UniProtKB
  9. inflammatory response Source: UniProtKB
  10. innate immune response Source: Reactome
  11. integrin-mediated signaling pathway Source: UniProtKB
  12. leukocyte cell-cell adhesion Source: UniProtKB
  13. leukocyte migration Source: Reactome
  14. neutrophil chemotaxis Source: UniProtKB
  15. receptor clustering Source: UniProtKB
  16. regulation of cell shape Source: UniProtKB
  17. regulation of immune response Source: Reactome
  18. regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
  19. toll-like receptor 4 signaling pathway Source: Reactome
  20. toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

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 alphaL-beta2 complex Source: UniProtKB
  4. integrin complex Source: UniProtKB
  5. membrane Source: UniProtKB
  6. plasma membrane Source: Reactome
  7. receptor complex Source: MGI
  8. vesicle Source: UniProtKB
Complete GO annotation...

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

BgeeiP05107.
CleanExiHS_ITGB2.
ExpressionAtlasiP05107. baseline and differential.
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. 26 interactions.
DIPiDIP-478N.
IntActiP05107. 16 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.
GeneTreeiENSGT00760000119064.
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

        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 BAD96225.1 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. 26 interactions.
DIPi DIP-478N.
IntActi P05107. 16 interactions.
MINTi MINT-129139.
STRINGi 9606.ENSP00000303242.

Chemistry

BindingDBi P05107.
ChEMBLi CHEMBL2111362.
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.
GeneTreei ENSGT00760000119064.
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

Bgeei P05107.
CleanExi HS_ITGB2.
ExpressionAtlasi P05107. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 194 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