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Reviewed, UniProtKB/Swiss-Prot P05107 (ITB2_HUMAN)

Last modified June 16, 2009. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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)
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.

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 COPS5 and RANBP9. Ref.7 Ref.9

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.8

Involvement in disease

Defects in ITGB2 are the cause of leukocyte adhesion deficiency type I (LAD1) [MIM:116920]. LAD1 patients have recurrent bacterial infections and their leukocytes are deficient in a wide range of adhesion-dependent functions. Ref.6 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18

Sequence similarities

Belongs to the integrin beta chain family.

Contains 1 VWFA domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SYKP434051EBI-300173,EBI-78302

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 – 72323 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

Amino acid modifications

Modified residue231Pyrrolidone carboxylic acid
Modified residue7451Phosphoserine; by PKC Ref.8
Modified residue7561Phosphoserine Ref.8
Modified residue7581Phosphothreonine; by PKC; in vitro Ref.8
Modified residue7591Phosphothreonine Potential
Modified residue7601Phosphothreonine; by PKC/PRKCA; in vitro Ref.8
Glycosylation501N-linked (GlcNAc...)
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation2121N-linked (GlcNAc...) Ref.10
Glycosylation2541N-linked (GlcNAc...) Potential
Glycosylation5011N-linked (GlcNAc...) Potential
Glycosylation6421N-linked (GlcNAc...) Potential
Disulfide bond25 ↔ 447 By similarity
Disulfide bond33 ↔ 43 By similarity
Disulfide bond36 ↔ 73 By similarity
Disulfide bond46 ↔ 62 By similarity
Disulfide bond191 ↔ 198 By similarity
Disulfide bond246 ↔ 286 By similarity
Disulfide bond386 ↔ 400 By similarity
Disulfide bond420 ↔ 662 By similarity
Disulfide bond445 ↔ 449 By similarity
Disulfide bond459 ↔ 470 By similarity
Disulfide bond467 ↔ 506 By similarity
Disulfide bond472 ↔ 481 By similarity
Disulfide bond483 ↔ 497 By similarity
Disulfide bond512 ↔ 517 By similarity
Disulfide bond514 ↔ 549 By similarity
Disulfide bond519 ↔ 534 By similarity
Disulfide bond536 ↔ 541 By similarity
Disulfide bond557 ↔ 562 By similarity
Disulfide bond559 ↔ 590 By similarity
Disulfide bond564 ↔ 573 By similarity
Disulfide bond575 ↔ 582 By similarity
Disulfide bond596 ↔ 601 By similarity
Disulfide bond598 ↔ 643 By similarity
Disulfide bond603 ↔ 612 By similarity
Disulfide bond615 ↔ 618 By similarity
Disulfide bond622 ↔ 631 By similarity
Disulfide bond628 ↔ 695 By similarity
Disulfide bond647 ↔ 670 By similarity

Natural variations

Natural variant1281D → N in LAD1. Ref.16
VAR_003984
Natural variant1381S → P in LAD1. Ref.18
VAR_013402
Natural variant1491L → P in LAD1. Ref.12
VAR_003985
Natural variant1691G → R in LAD1. Ref.12 Ref.13
VAR_003986
Natural variant1781P → L in LAD1. Ref.15
VAR_003987
Natural variant1961K → T in LAD1. Ref.14
VAR_003988
Natural variant2731G → R in LAD1. Ref.18
VAR_013403
Natural variant2841G → S in LAD1. Ref.17
VAR_003989
Natural variant3511N → S in LAD1. Ref.6
VAR_003990
Natural variant3541Q → H: dbSNP rs235330. Ref.6 Ref.1 Ref.2 Ref.4 Ref.5
VAR_030035
Natural variant5861R → W in LAD1. dbSNP rs5030672. Ref.6
VAR_003991
Natural variant5931R → C in LAD1. Ref.14
VAR_003992

Experimental info

Sequence conflict1991Q → P in CAA68266. Ref.5

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P05107-1 [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: 3028646] [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: 1683838] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-354.
[3]"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: 10830953] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-354.
Tissue: Muscle.
[5]"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: 2954816] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-769, PARTIAL PROTEIN SEQUENCE, VARIANT HIS-354.
Tissue: Spleen.
[6]"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: 1346613] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 347-355, VARIANTS LAD1 SER-351 AND TRP-586, VARIANT HIS-354.
[7]"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: 10766246] [Abstract]
Cited for: INTERACTION WITH COPS5.
[8]"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: 11700305] [Abstract]
Cited for: PHOSPHORYLATION AT SER-745; SER-756; THR-758 AND THR-760.
[9]"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: 14722085] [Abstract]
Cited for: INTERACTION WITH RANBP9.
[10]"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: 16335952] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-212, MASS SPECTROMETRY.
Tissue: Plasma.
[11]"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: 19159218] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-50 AND ASN-212, MASS SPECTROMETRY.
Tissue: Liver.
[12]"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: 1694220] [Abstract]
Cited for: VARIANTS LAD1 PRO-149 AND ARG-169.
[13]"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: 1352501] [Abstract]
Cited for: VARIANT LAD1 ARG-169.
[14]"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: 1968911] [Abstract]
Cited for: VARIANTS LAD1 THR-196 AND CYS-593.
[15]"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: 1347532] [Abstract]
Cited for: VARIANT LAD1 LEU-178.
[16]"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: 1590804] [Abstract]
Cited for: VARIANT LAD1 ASN-128.
[17]"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: 7686755] [Abstract]
Cited for: VARIANT LAD1 SER-284.
[18]"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: 9884339] [Abstract]
Cited for: VARIANTS LAD1 PRO-138 AND ARG-273.
+Additional computationally mapped references.

Web resources

ITGB2base

ITGB2 mutation db

GeneReviews

Cross-references

Sequence databases

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.
AL163300 Genomic DNA. Translation: CAB90553.1.
BC005861 mRNA. Translation: AAH05861.1.
Y00057 mRNA. Translation: CAA68266.1.
S81234 mRNA. Translation: AAB21404.1.
IPIIPI00291792.
PIRIJHULM. A25967.
RefSeqNP_000202.2.
NP_001120963.1.
UniGeneHs.375957

3D structure databases

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[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:478N.
IntActP05107. 1 interaction.

PTM databases

PhosphoSiteP05107.

Proteomic databases

PRIDEP05107.

Genome annotation databases

EnsemblENSG00000160255. Homo sapiens. [Contig view]
GeneID3689.
KEGGhsa:3689.

Organism-specific databases

GeneCardsGC21M045130.
H-InvDBHIX0016175.
HGNCHGNC:6155. ITGB2.
HPAHPA008877.
HPA016894.
MIM116920. phenotype.
600065. gene.
Orphanet2968. Leukocyte adhesion deficiency.
PharmGKBPA29955.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP05107.
HOVERGENP05107.
OMAP05107. CHTSDVP.

Enzyme and pathway databases

Pathway_Interaction_DBamb2_neutrophils_pathway. amb2 Integrin signaling.
hif1_tfpathway. HIF-1-alpha transcription factor network.
a4b1_paxdep_pathway. Paxillin-dependent events mediated by a4b1.
ReactomeREACT_13552. Integrin cell surface interactions.
REACT_604. Hemostasis.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpressP05107.
BgeeP05107.
CleanExHS_ITGB2.
GermOnlineENSG00000160255. Homo sapiens.

Family and domain databases

InterProIPR013032. EGF-like_reg_CS.
IPR013111. EGF_extracell.
IPR015812. Integrin_bsu.
IPR015439. Integrin_bsu-2_C.
IPR001169. Integrin_bsu_C.
IPR014836. Integrin_bsu_cyt.
IPR002369. Integrin_bsu_N.
IPR012012. Integrin_bsu_subgr.
IPR012896. Integrin_bsu_tail.
IPR003659. Plexin-like.
IPR002035. VWF_A.
[Graphical view]
Gene3DG3DSA:1.20.5.630. Integrin_bsu_cyt. 1 hit.
PANTHERPTHR10082. Integrin_beta_C. 1 hit.
PTHR10082:SF15. Integrin_bsu-2_C. 1 hit.
PfamPF07974. EGF_2. 1 hit.
PF08725. 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]
PROSITEPS00022. EGF_1. 2 hits. Uncertain.
PS01186. EGF_2. 3 hits. Uncertain.
PS00243. INTEGRIN_BETA. 3 hits.
PS50234. VWFA. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00641. Simvastatin.
NextBio14449.
PMAP-CutDBP05107.
SOURCESearch...

Entry information

Entry nameITB2_HUMAN
AccessionPrimary (citable) accession number: P05107
Secondary accession number(s): Q16418
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human cell differentiation molecules

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

Human chromosome 21

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents