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Showing Protein B-cell receptor CD22 (HMDBP14330)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 0 metabolites
Identification
HMDB Protein ID HMDBP14330
Secondary Accession Numbers None
Name B-cell receptor CD22
Synonyms
  1. B-lymphocyte cell adhesion molecule
  2. Sialic acid-binding Ig-like lectin 2
  3. T-cell surface antigen Leu-14
  4. BL-CAM
  5. Siglec-2
Gene Name CD22
Protein Type Unknown
Biological Properties
General Function Not Available
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.
Pathways
  • B cell receptor signaling pathway
  • Cell adhesion molecules
  • Hematopoietic cell lineage
Reactions Not Available
GO Classification
Biological Process
cell adhesion
negative regulation of calcium-mediated signaling
negative regulation of immunoglobulin production
regulation of B cell proliferation
negative regulation of B cell receptor signaling pathway
regulation of endocytosis
B cell activation
regulation of immune response
Cellular Component
cell surface
cytoplasm
extracellular vesicular exosome
plasma membrane
early endosome
recycling endosome
neuronal cell body membrane
external side of plasma membrane
integral to membrane
integral to plasma membrane
Molecular Function
carbohydrate binding
IgM binding
CD4 receptor binding
receptor binding
sialic acid binding
protein phosphatase binding
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 847
Molecular Weight 95347.07
Theoretical pI 6.654
Pfam Domain Function
Signals
  • 1-19;
Transmembrane Regions
  • 688-706;
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P20273
UniProtKB/Swiss-Prot Entry Name CD22_HUMAN
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed:15057824 ]
  3. 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. [PubMed:1985119 ]
  4. 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. [PubMed:8496602 ]
  5. Stamenkovic I, Seed B: The B-cell antigen CD22 mediates monocyte and erythrocyte adhesion. Nature. 1990 May 3;345(6270):74-7. [PubMed:1691828 ]
  6. 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. [PubMed:10079291 ]
  7. 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. [PubMed:8463235 ]
  8. 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. [PubMed:7618087 ]
  9. 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. [PubMed:8647200 ]
  10. 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. [PubMed:8627166 ]
  11. 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. [PubMed:9143697 ]
  12. 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. [PubMed:25218447 ]