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P05107 (ITB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 188. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ITGB2
Synonyms:CD18, MFI7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length769 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.15

Subunit structure

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. Ref.11 Ref.13 Ref.18

Subcellular location

Membrane; Single-pass type I membrane protein.

Post-translational modification

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. Ref.12

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.10 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27

Sequence similarities

Belongs to the integrin beta chain family.

Contains 1 VWFA domain.

Sequence caution

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

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentMembrane
   DiseaseDisease mutation
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandMetal-binding
   Molecular functionIntegrin
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Non-traceable author statement PubMed 12885943. Source: UniProtKB

blood coagulation

Traceable author statement. Source: Reactome

cell adhesion

Traceable author statement Ref.20. Source: ProtInc

cell-cell signaling

Non-traceable author statement PubMed 12885943. Source: UniProtKB

cell-matrix adhesion

Inferred from electronic annotation. Source: InterPro

extracellular matrix organization

Traceable author statement. Source: Reactome

inflammatory response

Non-traceable author statement PubMed 12885943. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

integrin-mediated signaling pathway

Non-traceable author statement PubMed 12885943. Source: UniProtKB

leukocyte cell-cell adhesion

Inferred from direct assay PubMed 12885943. Source: UniProtKB

leukocyte migration

Traceable author statement. Source: Reactome

multicellular organismal development

Inferred from electronic annotation. Source: InterPro

neutrophil chemotaxis

Inferred from direct assay PubMed 12885943. Source: UniProtKB

regulation of cell shape

Non-traceable author statement PubMed 12885943. Source: UniProtKB

regulation of immune response

Traceable author statement. Source: Reactome

regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 12885943. Source: UniProtKB

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentextracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

integrin complex

Non-traceable author statement PubMed 12885943. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

receptor complex

Inferred from direct assay PubMed 23382219. Source: MGI

   Molecular_functionglycoprotein binding

Inferred from physical interaction PubMed 16831868. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase binding

Inferred from physical interaction PubMed 12885943. Source: UniProtKB

receptor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222
Chain23 – 769747Integrin beta-2
PRO_0000016341

Regions

Topological domain23 – 700678Extracellular Potential
Transmembrane701 – 72323Helical; Potential
Topological domain724 – 76946Cytoplasmic Potential
Domain124 – 363240VWFA
Repeat449 – 49648I
Repeat497 – 54044II
Repeat541 – 58141III
Repeat582 – 61736IV
Region449 – 617169Cysteine-rich tandem repeats
Motif397 – 3993Cell attachment site Potential

Sites

Metal binding1381Calcium; via carbonyl oxygen
Metal binding1411Calcium
Metal binding1421Calcium
Metal binding3471Calcium

Amino acid modifications

Modified residue231Pyrrolidone carboxylic acid Probable
Modified residue7451Phosphoserine; by PKC Ref.12
Modified residue7561Phosphoserine Ref.12
Modified residue7581Phosphothreonine; by PKC; in vitro Ref.12
Modified residue7591Phosphothreonine Potential
Modified residue7601Phosphothreonine; by PKC/PRKCA; in vitro Ref.12
Glycosylation501N-linked (GlcNAc...) Ref.16 Ref.17
Glycosylation1161N-linked (GlcNAc...) Ref.17 Ref.18
Glycosylation2121N-linked (GlcNAc...) Ref.14 Ref.16 Ref.17
Glycosylation2131N-linked (GlcNAc...); atypical Ref.17
Glycosylation2151N-linked (GlcNAc...); atypical Ref.17
Glycosylation2541N-linked (GlcNAc...) Potential
Glycosylation5011N-linked (GlcNAc...) Potential
Glycosylation6421N-linked (GlcNAc...) Potential
Disulfide bond25 ↔ 43 Ref.18
Disulfide bond33 ↔ 447 Ref.18
Disulfide bond36 ↔ 62 Ref.18
Disulfide bond46 ↔ 73 Ref.18
Disulfide bond191 ↔ 198 Ref.18
Disulfide bond246 ↔ 286 Ref.18
Disulfide bond386 ↔ 400 Ref.18
Disulfide bond420 ↔ 445 Ref.18
Disulfide bond449 ↔ 467 Ref.18
Disulfide bond459 ↔ 470 Ref.18
Disulfide bond472 ↔ 481 Ref.18
Disulfide bond483 ↔ 514 Ref.18
Disulfide bond497 ↔ 512 Ref.18
Disulfide bond506 ↔ 517 Ref.18
Disulfide bond519 ↔ 534 Ref.18
Disulfide bond536 ↔ 559 Ref.18
Disulfide bond541 ↔ 557 Ref.18
Disulfide bond549 ↔ 562 Ref.18
Disulfide bond564 ↔ 573 Ref.18
Disulfide bond575 ↔ 598 Ref.18
Disulfide bond582 ↔ 596 Ref.18
Disulfide bond590 ↔ 601 Ref.18
Disulfide bond603 ↔ 612 Ref.18
Disulfide bond615 ↔ 618 Ref.18
Disulfide bond622 ↔ 662 Ref.18
Disulfide bond628 ↔ 647 Ref.18
Disulfide bond631 ↔ 643 Ref.18
Disulfide bond670 ↔ 695 Ref.18

Natural variations

Natural variant1281D → N in LAD1. Ref.21
Corresponds to variant rs137852615 [ dbSNP | Ensembl ].
VAR_003984
Natural variant1281D → Y in LAD1. Ref.27
Corresponds to variant rs137852615 [ dbSNP | Ensembl ].
VAR_065661
Natural variant1381S → P in LAD1. Ref.25
Corresponds to variant rs137852617 [ dbSNP | Ensembl ].
VAR_013402
Natural variant1491L → P in LAD1. Ref.20
Corresponds to variant rs137852611 [ dbSNP | Ensembl ].
VAR_003985
Natural variant1691G → R in LAD1. Ref.20 Ref.22
Corresponds to variant rs137852612 [ dbSNP | Ensembl ].
VAR_003986
Natural variant1781P → L in LAD1. Ref.9 Ref.23
Corresponds to variant rs137852614 [ dbSNP | Ensembl ].
VAR_003987
Natural variant1961K → T in LAD1. Ref.19
Corresponds to variant rs137852610 [ dbSNP | Ensembl ].
VAR_003988
Natural variant2391A → T in LAD1. Ref.27
Corresponds to variant rs179363873 [ dbSNP | Ensembl ].
VAR_065662
Natural variant2731G → R in LAD1. Ref.25
Corresponds to variant rs137852618 [ dbSNP | Ensembl ].
VAR_013403
Natural variant2841G → S in LAD1. Ref.24
Corresponds to variant rs137852616 [ dbSNP | Ensembl ].
VAR_003989
Natural variant3001D → V in LAD1. Ref.26
Corresponds to variant rs179363874 [ dbSNP | Ensembl ].
VAR_065663
Natural variant3511N → S in LAD1. Ref.10
Corresponds to variant rs137852613 [ dbSNP | Ensembl ].
VAR_003990
Natural variant3541Q → H. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6 Ref.7 Ref.8 Ref.10
Corresponds to variant rs235330 [ dbSNP | Ensembl ].
VAR_030035
Natural variant5861R → W in LAD1. Ref.10
Corresponds to variant rs5030672 [ dbSNP | Ensembl ].
VAR_003991
Natural variant5931R → C in LAD1. Ref.19
Corresponds to variant rs137852609 [ dbSNP | Ensembl ].
VAR_003992
Natural variant7161G → A in LAD1. Ref.27
Corresponds to variant rs179363872 [ dbSNP | Ensembl ].
VAR_065664

Experimental info

Sequence conflict1991Q → P in CAA68266. Ref.8
Sequence conflict2791L → P in BAD96225. Ref.4
Sequence conflict5261G → C in BAG53190. Ref.3
Sequence conflict6301E → K in BAG53190. Ref.3

Secondary structure

.................................................................................................................................................. 769
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05107 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: EB9F3C3DF338B4E1

FASTA76984,782
        10         20         30         40         50         60 
MLGLRPPLLA LVGLLSLGCV LSQECTKFKV SSCRECIESG PGCTWCQKLN FTGPGDPDSI 

        70         80         90        100        110        120 
RCDTRPQLLM RGCAADDIMD PTSLAETQED HNGGQKQLSP QKVTLYLRPG QAAAFNVTFR 

       130        140        150        160        170        180 
RAKGYPIDLY YLMDLSYSML DDLRNVKKLG GDLLRALNEI TESGRIGFGS FVDKTVLPFV 

       190        200        210        220        230        240 
NTHPDKLRNP CPNKEKECQP PFAFRHVLKL TNNSNQFQTE VGKQLISGNL DAPEGGLDAM 

       250        260        270        280        290        300 
MQVAACPEEI GWRNVTRLLV FATDDGFHFA GDGKLGAILT PNDGRCHLED NLYKRSNEFD 

       310        320        330        340        350        360 
YPSVGQLAHK LAENNIQPIF AVTSRMVKTY EKLTEIIPKS AVGELSEDSS NVVQLIKNAY 

       370        380        390        400        410        420 
NKLSSRVFLD HNALPDTLKV TYDSFCSNGV THRNQPRGDC DGVQINVPIT FQVKVTATEC 

       430        440        450        460        470        480 
IQEQSFVIRA LGFTDIVTVQ VLPQCECRCR DQSRDRSLCH GKGFLECGIC RCDTGYIGKN 

       490        500        510        520        530        540 
CECQTQGRSS QELEGSCRKD NNSIICSGLG DCVCGQCLCH TSDVPGKLIY GQYCECDTIN 

       550        560        570        580        590        600 
CERYNGQVCG GPGRGLCFCG KCRCHPGFEG SACQCERTTE GCLNPRRVEC SGRGRCRCNV 

       610        620        630        640        650        660 
CECHSGYQLP LCQECPGCPS PCGKYISCAE CLKFEKGPFG KNCSAACPGL QLSNNPVKGR 

       670        680        690        700        710        720 
TCKERDSEGC WVAYTLEQQD GMDRYLIYVD ESRECVAGPN IAAIVGGTVA GIVLIGILLL 

       730        740        750        760 
VIWKALIHLS DLREYRRFEK EKLKSQWNND NPLFKSATTT VMNPKFAES 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Web resources

ITGB2base

ITGB2 mutation db

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M15395 mRNA. Translation: AAA59490.1.
X64072 expand/collapse EMBL AC list , 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.
PIRIJHULM. A25967.
RefSeqNP_000202.2. NM_000211.3.
NP_001120963.1. NM_001127491.1.
UniGeneHs.375957.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP05107.
SMRP05107. Positions 23-696, 698-763.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109895. 25 interactions.
DIPDIP-478N.
IntActP05107. 14 interactions.
MINTMINT-129139.
STRING9606.ENSP00000303242.

Chemistry

BindingDBP05107.
ChEMBLCHEMBL2096661.
DrugBankDB00641. Simvastatin.

PTM databases

PhosphoSiteP05107.

Polymorphism databases

DMDM124056465.

Proteomic databases

PaxDbP05107.
PRIDEP05107.

Protocols and materials databases

DNASU3689.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302347; ENSP00000303242; ENSG00000160255.
ENST00000355153; ENSP00000347279; ENSG00000160255.
ENST00000397850; ENSP00000380948; ENSG00000160255.
ENST00000397852; ENSP00000380950; ENSG00000160255.
ENST00000397857; ENSP00000380955; ENSG00000160255.
GeneID3689.
KEGGhsa:3689.
UCSCuc002zgd.2. human.

Organism-specific databases

CTD3689.
GeneCardsGC21M046305.
HGNCHGNC:6155. ITGB2.
HPAHPA008877.
HPA016894.
MIM116920. phenotype.
600065. gene.
neXtProtNX_P05107.
Orphanet99842. Leukocyte adhesion deficiency type I.
PharmGKBPA29955.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG287997.
HOGENOMHOG000252936.
HOVERGENHBG006190.
InParanoidP05107.
KOK06464.
OMARGRCRCN.
OrthoDBEOG7T7GSB.
PhylomeDBP05107.
TreeFamTF105392.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP05107.

Gene expression databases

ArrayExpressP05107.
BgeeP05107.
CleanExHS_ITGB2.
GenevestigatorP05107.

Family and domain databases

Gene3D3.40.50.410. 1 hit.
InterProIPR015812. 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]
PANTHERPTHR10082. PTHR10082. 1 hit.
PTHR10082:SF15. PTHR10082:SF15. 1 hit.
PfamPF08725. Integrin_b_cyt. 1 hit.
PF07965. Integrin_B_tail. 1 hit.
PF00362. Integrin_beta. 1 hit.
[Graphical view]
PIRSFPIRSF002512. Integrin_B. 1 hit.
PRINTSPR01186. INTEGRINB.
SMARTSM00187. INB. 1 hit.
SM00423. PSI. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF103575. SSF103575. 1 hit.
SSF53300. SSF53300. 1 hit.
SSF69687. SSF69687. 1 hit.
PROSITEPS00022. EGF_1. 2 hits.
PS01186. EGF_2. 3 hits.
PS00243. INTEGRIN_BETA. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSITGB2. human.
EvolutionaryTraceP05107.
GeneWikiCD18.
GenomeRNAi3689.
NextBio14449.
PMAP-CutDBP05107.
PROP05107.
SOURCESearch...

Entry information

Entry nameITB2_HUMAN
AccessionPrimary (citable) accession number: P05107
Secondary accession number(s): B3KTS8 expand/collapse secondary AC list , D3DSM1, Q16418, Q53HS5, Q9UD72
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 188 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries