B-cell receptor CD22
Details
- Name
- B-cell receptor CD22
- Synonyms
- B-lymphocyte cell adhesion molecule
- BL-CAM
- Sialic acid-binding Ig-like lectin 2
- Siglec-2
- SIGLEC2
- T-cell surface antigen Leu-14
- Gene Name
- CD22
- Organism
- Humans
- Amino acid sequence
>lcl|BSEQ0000365|B-cell receptor CD22 MHLLGPWLLLLVLEYLAFSDSSKWVFEHPETLYAWEGACVWIPCTYRALDGDLESFILFH NPEYNKNTSKFDGTRLYESTKDGKVPSEQKRVQFLGDKNKNCTLSIHPVHLNDSGQLGLR MESKTEKWMERIHLNVSERPFPPHIQLPPEIQESQEVTLTCLLNFSCYGYPIQLQWLLEG VPMRQAAVTSTSLTIKSVFTRSELKFSPQWSHHGKIVTCQLQDADGKFLSNDTVQLNVKH TPKLEIKVTPSDAIVREGDSVTMTCEVSSSNPEYTTVSWLKDGTSLKKQNTFTLNLREVT KDQSGKYCCQVSNDVGPGRSEEVFLQVQYAPEPSTVQILHSPAVEGSQVEFLCMSLANPL PTNYTWYHNGKEMQGRTEEKVHIPKILPWHAGTYSCVAENILGTGQRGPGAELDVQYPPK KVTTVIQNPMPIREGDTVTLSCNYNSSNPSVTRYEWKPHGAWEEPSLGVLKIQNVGWDNT TIACAACNSWCSWASPVALNVQYAPRDVRVRKIKPLSEIHSGNSVSLQCDFSSSHPKEVQ FFWEKNGRLLGKESQLNFDSISPEDAGSYSCWVNNSIGQTASKAWTLEVLYAPRRLRVSM SPGDQVMEGKSATLTCESDANPPVSHYTWFDWNNQSLPYHSQKLRLEPVKVQHSGAYWCQ GTNSVGKGRSPLSTLTVYYSPETIGRRVAVGLGSCLAILILAICGLKLQRRWKRTQSQQG LQENSSGQSFFVRNKKVRRAPLSEGPHSLGCYNPMMEDGISYTTLRFPEMNIPRTGDAES SEMQRPPPDCDDTVTYSALHKRQVGDYENVIPDFPEDEGIHYSELIQFGVGERPQAQENV DYVILKH
- Number of residues
- 847
- Molecular Weight
- 95347.07
- Theoretical pI
- 6.64
- GO Classification
- Functionscarbohydrate bindingProcessescell adhesionComponentsexternal side of plasma membrane / extracellular exosome / integral component of plasma membrane
- General Function
- Carbohydrate binding
- Specific Function
- Mediates B-cell B-cell interactions. May be involved in the localization of B-cells in lymphoid tissues. Binds sialylated glycoproteins; one of which is CD45. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site can be masked by cis interactions with sialic acids on the same cell surface. Upon ligand induced tyrosine phosphorylation in the immune response seems to be involved in regulation of B-cell antigen receptor signaling. Plays a role in positive regulation through interaction with Src family tyrosine kinases and may also act as an inhibitory receptor by recruiting cytoplasmic phosphatases via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules.
- Pfam Domain Function
- Transmembrane Regions
- 688-706
- Cellular Location
- Cell membrane
- Gene sequence
>lcl|BSEQ0018925|B-cell receptor CD22 (CD22) ATGCATCTCCTCGGCCCCTGGCTCCTGCTCCTGGTTCTAGAATACTTGGCTTTCTCTGAC TCAAGTAAATGGGTTTTTGAGCACCCTGAAACCCTCTACGCCTGGGAGGGGGCCTGCGTC TGGATCCCCTGCACCTACAGAGCCCTAGATGGTGACCTGGAAAGCTTCATCCTGTTCCAC AATCCTGAGTATAACAAGAACACCTCGAAGTTTGATGGGACAAGACTCTATGAAAGCACA AAGGATGGGAAGGTTCCTTCTGAGCAGAAAAGGGTGCAATTCCTGGGAGACAAGAATAAG AACTGCACACTGAGTATCCACCCGGTGCACCTCAATGACAGTGGTCAGCTGGGGCTGAGG ATGGAGTCCAAGACTGAGAAATGGATGGAACGAATACACCTCAATGTCTCTGAAAGGCCT TTTCCACCTCATATCCAGCTCCCTCCAGAAATTCAAGAGTCCCAGGAAGTCACTCTGACC TGCTTGCTGAATTTCTCCTGCTATGGGTATCCGATCCAATTGCAGTGGCTCCTAGAGGGG GTTCCAATGAGGCAGGCTGCTGTCACCTCGACCTCCTTGACCATCAAGTCTGTCTTCACC CGGAGCGAGCTCAAGTTCTCCCCACAGTGGAGTCACCATGGGAAGATTGTGACCTGCCAG CTTCAGGATGCAGATGGGAAGTTCCTCTCCAATGACACGGTGCAGCTGAACGTGAAGCAC ACCCCGAAGTTGGAGATCAAGGTCACTCCCAGTGATGCCATAGTGAGGGAGGGGGACTCT GTGACCATGACCTGCGAGGTCAGCAGCAGCAACCCGGAGTACACGACGGTATCCTGGCTC AAGGATGGGACCTCGCTGAAGAAGCAGAATACATTCACGCTAAACCTGCGCGAAGTGACC AAGGACCAGAGTGGGAAGTACTGCTGTCAGGTCTCCAATGACGTGGGCCCGGGAAGGTCG GAAGAAGTGTTCCTGCAAGTGCAGTATCCTCCCAAGAAGGTGACCACAGTGATTCAAAAC CCCATGCCGATTCGAGAAGGAGACACAGTGACCCTTTCCTGTAACTACAATTCCAGTAAC CCCAGTGTTACCCGGTATGAATGGAAACCCCATGGCGCCTGGGAGGAGCCATCGCTTGGG GTGCTGAAGATCCAAAACGTTGGCTGGGACAACACAACCATCGCCTGCGCAGCTTGTAAT AGTTGGTGCTCGTGGGCCTCCCCTGTCGCCCTGAATGTCCAGTATGCCCCCCGAGACGTG AGGGTCCGGAAAATCAAGCCCCTTTCCGAGATTCACTCTGGAAACTCGGTCAGCCTCCAA TGTGACTTCTCAAGCAGCCACCCCAAAGAAGTCCAGTTCTTCTGGGAGAAAAATGGCAGG CTTCTGGGGAAAGAAAGCCAGCTGAATTTTGACTCCATCTCCCCAGAAGATGCTGGGAGT TACAGCTGCTGGGTGAACAACTCCATAGGACAGACAGCGTCCAAGGCCTGGACACTTGAA GTGCTGTATGCACCCAGGAGGCTGCGTGTGTCCATGAGCCCGGGGGACCAAGTGATGGAG GGGAAGAGTGCAACCCTGACCTGTGAGAGCGACGCCAACCCTCCCGTCTCCCACTACACC TGGTTTGACTGGAATAACCAAAGCCTCCCCTACCACAGCCAGAAGCTGAGATTGGAGCCG GTGAAGGTCCAGCACTCGGGTGCCTACTGGTGCCAGGGGACCAACAGTGTGGGCAAGGGC CGTTCGCCTCTCAGCACCCTCACCGTCTACTATAGCCCGGAGACCATCGGCAGGCGAGTG GCTGTGGGACTCGGGTCCTGCCTCGCCATCCTCATCCTGGCAATCTGTGGGCTCAAGCTC CAGCGACGTTGGAAGAGGACACAGAGCCAGCAGGGGCTTCAGGAGAATTCCAGCGGCCAG AGCTTCTTTGTGAGGAATAAAAAGGTTAGAAGGGCCCCCCTCTCTGAAGGCCCCCACTCC CTGGGATGCTACAATCCAATGATGGAAGATGGCATTAGCTACACCACCCTGCGCTTTCCC GAGATGAACATACCACGAACTGGAGATGCAGAGTCCTCAGAGATGCAGAGACCTCCCCCG GACTGCGATGACACGGTCACTTATTCAGCATTGCACAAGCGCCAAGTGGGCGACTATGAG AACGTCATTCCAGATTTTCCAGAAGATGAGGGGATTCATTACTCAGAGCTGATCCAGTTT GGGGTCGGGGAGCGGCCTCAGGCACAAGAAAATGTGGACTATGTGATCCTCAAACATTGA
- Chromosome Location
- 19
- Locus
- 19q13.1
- External Identifiers
Resource Link UniProtKB ID P20273 UniProtKB Entry Name CD22_HUMAN GenBank Protein ID 36091 GenBank Gene ID X59350 GenAtlas ID CD22 HGNC ID HGNC:1643 - General References
- Stamenkovic I, Seed B: The B-cell antigen CD22 mediates monocyte and erythrocyte adhesion. Nature. 1990 May 3;345(6270):74-7. [Article]
- Wilson GL, Fox CH, Fauci AS, Kehrl JH: cDNA cloning of the B cell membrane protein CD22: a mediator of B-B cell interactions. J Exp Med. 1991 Jan 1;173(1):137-46. [Article]
- Wilson GL, Najfeld V, Kozlow E, Menniger J, Ward D, Kehrl JH: Genomic structure and chromosomal mapping of the human CD22 gene. J Immunol. 1993 Jun 1;150(11):5013-24. [Article]
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- Hatta Y, Tsuchiya N, Matsushita M, Shiota M, Hagiwara K, Tokunaga K: Identification of the gene variations in human CD22. Immunogenetics. 1999 Apr;49(4):280-6. [Article]
- Powell LD, Sgroi D, Sjoberg ER, Stamenkovic I, Varki A: Natural ligands of the B cell adhesion molecule CD22 beta carry N-linked oligosaccharides with alpha-2,6-linked sialic acids that are required for recognition. J Biol Chem. 1993 Apr 5;268(10):7019-27. [Article]
- Doody GM, Justement LB, Delibrias CC, Matthews RJ, Lin J, Thomas ML, Fearon DT: A role in B cell activation for CD22 and the protein tyrosine phosphatase SHP. Science. 1995 Jul 14;269(5221):242-4. [Article]
- Tuscano JM, Engel P, Tedder TF, Agarwal A, Kehrl JH: Involvement of p72syk kinase, p53/56lyn kinase and phosphatidyl inositol-3 kinase in signal transduction via the human B lymphocyte antigen CD22. Eur J Immunol. 1996 Jun;26(6):1246-52. [Article]
- Law CL, Sidorenko SP, Chandran KA, Zhao Z, Shen SH, Fischer EH, Clark EA: CD22 associates with protein tyrosine phosphatase 1C, Syk, and phospholipase C-gamma(1) upon B cell activation. J Exp Med. 1996 Feb 1;183(2):547-60. [Article]
- Tedder TF, Tuscano J, Sato S, Kehrl JH: CD22, a B lymphocyte-specific adhesion molecule that regulates antigen receptor signaling. Annu Rev Immunol. 1997;15:481-504. [Article]
- Hendriks IA, D'Souza RC, Yang B, Verlaan-de Vries M, Mann M, Vertegaal AC: Uncovering global SUMOylation signaling networks in a site-specific manner. Nat Struct Mol Biol. 2014 Oct;21(10):927-36. doi: 10.1038/nsmb.2890. Epub 2014 Sep 14. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB04958 Epratuzumab investigational yes antibodyregulator Details DB05889 Inotuzumab ozogamicin approved, investigational yes antibodyregulator Details DB12688 Moxetumomab pasudotox approved, investigational yes binderantibodyregulator Details