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CD18 (integrin beta-2, L-CAM beta, ITGB2, CD18, MFI7)

Function: - forms complexes with a) CD11a (integrin alpha-L) b) CD11b (integrin alpha-M) c) CD11c (integrin alpha-X) d) integrin alpha-D - interacts with COPS5 & RANBP9 - both Ser-745 & 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 Structure: - belongs to the integrin beta chain family - contains 1 VWFA domain Compartment: membrane Expression: leukocytes Pathology: - defects are associated with leukocyte adhesion deficiency type 1

General

cluster-of-differentiation antigen; cluster designation antigen; CD antigen integrin-beta

Properties

SIZE: entity length = 769 aa MW = 85 kD COMPARTMENT: cellular membrane MOTIF: signal sequence {1-22} cysteine residue {C25} MODIFICATION: cysteine residue {C447} cysteine residue {C33} MODIFICATION: cysteine residue {C43} cysteine residue {C36} MODIFICATION: cysteine residue {C73} cysteine residue {C43} MODIFICATION: cysteine residue {C33} cysteine residue {C46} MODIFICATION: cysteine residue {C62} N-glycosylation site {N50} cysteine residue {C62} MODIFICATION: cysteine residue {C46} cysteine residue {C73} MODIFICATION: cysteine residue {C36} N-glycosylation site {N116} VWFA domain {124-363} MOTIF: cysteine residue {C191} MODIFICATION: cysteine residue {C198} cysteine residue {C198} MODIFICATION: cysteine residue {C191} N-glycosylation site {N212} cysteine residue {C246} MODIFICATION: cysteine residue {C286} N-glycosylation site {N254} cysteine residue {C286} MODIFICATION: cysteine residue {C246} cysteine residue {C386} MODIFICATION: cysteine residue {C400} Cell attachment site {397-399} cysteine residue {C400} MODIFICATION: cysteine residue {C386} cysteine residue {C420} MODIFICATION: cysteine residue {C662} cysteine residue {C445} MODIFICATION: cysteine residue {C449} cysteine residue {C447} MODIFICATION: cysteine residue {C25} Cysteine-rich tandem repeats {449-617} MOTIF: I {449-496} cysteine residue {C449} MODIFICATION: cysteine residue {C445} cysteine residue {C459} MODIFICATION: cysteine residue {C470} cysteine residue {C467} MODIFICATION: cysteine residue {C506} cysteine residue {C470} MODIFICATION: cysteine residue {C459} cysteine residue {C472} MODIFICATION: cysteine residue {C481} cysteine residue {C481} MODIFICATION: cysteine residue {C472} cysteine residue {C483} MODIFICATION: cysteine residue {C497} II {497-540} cysteine residue {C497} MODIFICATION: cysteine residue {C483} N-glycosylation site {N501} cysteine residue {C506} MODIFICATION: cysteine residue {C467} cysteine residue {C512} MODIFICATION: cysteine residue {C517} cysteine residue {C514} MODIFICATION: cysteine residue {C549} cysteine residue {C517} MODIFICATION: cysteine residue {C512} cysteine residue {C519} MODIFICATION: cysteine residue {C534} cysteine residue {C534} MODIFICATION: cysteine residue {C519} cysteine residue {C536} MODIFICATION: cysteine residue {C541} III {541-581} cysteine residue {C541} MODIFICATION: cysteine residue {C536} cysteine residue {C549} MODIFICATION: cysteine residue {C514} cysteine residue {C557} MODIFICATION: cysteine residue {C562} cysteine residue {C559} MODIFICATION: cysteine residue {C590} cysteine residue {C562} MODIFICATION: cysteine residue {C557} cysteine residue {C564} MODIFICATION: cysteine residue {C573} cysteine residue {C573} MODIFICATION: cysteine residue {C564} cysteine residue {C575} MODIFICATION: cysteine residue {C582} IV {582-617} cysteine residue {C582} MODIFICATION: cysteine residue {C575} cysteine residue {C590} MODIFICATION: cysteine residue {C559} cysteine residue {C596} MODIFICATION: cysteine residue {C601} cysteine residue {C598} MODIFICATION: cysteine residue {C643} cysteine residue {C601} MODIFICATION: cysteine residue {C596} cysteine residue {C603} MODIFICATION: cysteine residue {C612} cysteine residue {C612} MODIFICATION: cysteine residue {C603} cysteine residue {C615} MODIFICATION: cysteine residue {C618} cysteine residue {C618} MODIFICATION: cysteine residue {C615} cysteine residue {C622} MODIFICATION: cysteine residue {C631} cysteine residue {C628} MODIFICATION: cysteine residue {C695} cysteine residue {C631} MODIFICATION: cysteine residue {C622} N-glycosylation site {N642} cysteine residue {C643} MODIFICATION: cysteine residue {C598} cysteine residue {C647} MODIFICATION: cysteine residue {C670} cysteine residue {C662} MODIFICATION: cysteine residue {C420} cysteine residue {C670} MODIFICATION: cysteine residue {C647} cysteine residue {C695} MODIFICATION: cysteine residue {C628} transmembrane domain {701-723} Ser phosphorylation site {S745} Ser phosphorylation site {S756} Thr phosphorylation site {T758} Thr phosphorylation site {T759} Thr phosphorylation site {T760}

Database Correlations

OMIM correlations MORBIDMAP 600065 UniProt P05107 PFAM correlations Entrez Gene 3689 Kegg hsa:3689

References

  1. Hobbs et al Science 251:1611 1991
  2. Molecular Cell Biology (2nd ed) Darnell J; Lodish H & Baltimore D (eds), Scientific American Books, WH Freeman, NY 1990, pg 921
  3. Clark EA & Brugge JS Integrins and signal transduction pathways: the road taken. Science 268:233 1995 PMID: 7716514
  4. UniProt :accession P05107
  5. Entrez Gene :accession 3689
  6. TGB2base; Note: ITGB2 mutation db http://bioinf.uta.fi/ITGB2base/
  7. GeneReviews https://www.genecards.org/cgi-bin/carddisp.pl?gene=ITGB2

Component-of

integrin alpha-M/beta-2 (CD11b/CD18, MAC1)