SymbolsCD2 ; LFA-2; SRBC; T11
External IDsOMIM186990 MGI88320 HomoloGene1338 IUPHAR: 2600 ChEMBL: 2040 GeneCards: CD2 Gene
RNA expression pattern
File:PBB GE CD2 205831 at tn.png
More reference expression data
RefSeq (mRNA)NM_001767NM_013486
RefSeq (protein)NP_001758NP_038514
Location (UCSC)Chr 1:
117.3 – 117.31 Mb
Chr 3:
101.28 – 101.29 Mb
PubMed search[1][2]

CD2 (cluster of differentiation 2) is a cell adhesion molecule found on the surface of T cells and natural killer (NK) cells. It has also been called T-cell surface antigen T11/Leu-5, LFA-2,[1] LFA-3 receptor, erythrocyte receptor and rosette receptor.[2]


It interacts with other adhesion molecules, such as lymphocyte function-associated antigen-3 (LFA-3/CD58) in humans, or CD48 in rodents, which are expressed on the surfaces of other cells.[3]

In addition to its adhesive properties, CD2 also acts as a co-stimulatory molecule on T and NK cells.[4]

Diagnostic relevance

CD2 is a specific marker for T cells and NK cells, and can therefore be used in immunohistochemistry to identify the presence of such cells in tissue sections. The great majority of T cell lymphomas and leukaemias also express CD2, making it possible to use the presence of the antigen to distinguish these conditions from B cell neoplasms.[5]


Due to its structural characteristics, CD2 is a member of the immunoglobulin superfamily; it possesses two immunoglobulin-like domains in its extracellular portion.[4]


CD2 has been shown to interact with CD2BP2,[6] Lck[7] and PSTPIP1.[8]


  1. ^ Sanchez-Madrid F, Krensky AM, Ware CF, Robbins E, Strominger JL, Burakoff SJ et al. (1982). "Three distinct antigens associated with human T-lymphocyte-mediated cytolysis: LFA-1, LFA-2, and LFA-3". Proc Natl Acad Sci U S A 79 (23): 7489–93. PMC 347365. PMID 6984191. doi:10.1073/pnas.79.23.7489. 
  2. ^ Uniprot database entry for CD2 (accession number P06729)
  3. ^ Wilkins AL, Yang W, Yang JJ (2003). "Structural biology of the cell adhesion protein CD2: from molecular recognition to protein folding and design". Curr Protein Pept Sci 4 (5): 367–73. PMID 14529530. doi:10.2174/1389203033487063. 
  4. ^ a b Yang JJ, Ye Y, Carroll A, Yang W, Lee HW (2001). "Structural biology of the cell adhesion protein CD2: alternatively folded states and structure-function relation". Curr Protein Pept Sci 2 (1): 1–17. PMID 12369898. doi:10.2174/1389203013381251. 
  5. ^ Leong, Anthony S-Y; Cooper, Kumarason; Leong, F Joel W-M (2003). Manual of Diagnostic Cytology (2 ed.). Greenwich Medical Media, Ltd. p. 61. ISBN 1-84110-100-1. 
  6. ^ Nishizawa K, Freund C, Li J, Wagner G, Reinherz EL (December 1998). "Identification of a proline-binding motif regulating CD2-triggered T lymphocyte activation". Proc. Natl. Acad. Sci. U.S.A. 95 (25): 14897–902. PMC 24547. PMID 9843987. doi:10.1073/pnas.95.25.14897. 
  7. ^ Bell GM, Fargnoli J, Bolen JB, Kish L, Imboden JB (January 1996). "The SH3 domain of p56lck binds to proline-rich sequences in the cytoplasmic domain of CD2". J. Exp. Med. 183 (1): 169–78. PMC 2192399. PMID 8551220. doi:10.1084/jem.183.1.169. 
  8. ^ Li J, Nishizawa K, An W, Hussey RE, Lialios FE, Salgia R et al. (December 1998). "A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion". EMBO J. 17 (24): 7320–36. PMC 1171078. PMID 9857189. doi:10.1093/emboj/17.24.7320. 

Further reading


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