ID BLK_HUMAN STANDARD; PRT; 504 AA. AC P51451; Q16291; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-OCT-2000 (Rel. 40, Last annotation update) DE TYROSINE-PROTEIN KINASE BLK (EC 2.7.1.112) (B LYMPHOCYTE KINASE) (P55- DE BLK). GN BLK. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95123078; PubMed=7822795; RA Islam K.B., Rabbani H., Larsson C., Sanders R., Smith C.I.; RT "Molecular cloning, characterization, and chromosomal localization of RT a human lymphoid tyrosine kinase related to murine Blk."; RL J. Immunol. 154:1265-1272(1995). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95148218; PubMed=7845672; RA Drebin J.A., Hartzell S.W., Griffin C., Campbell M.J., RA Niederhuber J.E.; RT "Molecular cloning and chromosomal localization of the human homologue RT of a B-lymphocyte specific protein tyrosine kinase (blk)."; RL Oncogene 10:477-486(1995). CC -!- FUNCTION: BLK MAY FUNCTION IN A SIGNAL TRANSDUCTION PATHWAY THAT CC IS RESTRICTED TO B LYMPHOID CELLS. CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP + CC PROTEIN TYROSINE PHOSPHATE. CC -!- SIMILARITY: TO OTHER PROTEIN-TYROSINE KINASES IN THE CATALYTIC CC DOMAIN. BELONGS TO THE SRC SUBFAMILY. CC -!- SIMILARITY: CONTAINS 1 SH2 DOMAIN. CC -!- SIMILARITY: CONTAINS 1 SH3 DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z33998; CAA83965.1; -. DR EMBL; S76617; AAB33265.1; -. DR HSSP; P16277; 1BLJ. DR MIM; 191305; -. DR INTERPRO; IPR000719; -. DR INTERPRO; IPR000980; -. DR INTERPRO; IPR001245; -. DR INTERPRO; IPR001452; -. DR PFAM; PF00017; SH2; 1. DR PFAM; PF00018; SH3; 1. DR PFAM; PF00069; pkinase; 1. DR PRINTS; PR00109; TYRKINASE. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00452; SH3DOMAIN. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; FALSE_NEG. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS50001; SH2; 1. DR PROSITE; PS50002; SH3; 1. KW Tyrosine-protein kinase; Phosphorylation; Transferase; ATP-binding; KW Myristate; SH2 domain; SH3 domain. FT INIT_MET 0 0 BY SIMILARITY. FT LIPID 1 1 MYRISTATE (BY SIMILARITY). FT DOMAIN 57 117 SH3. FT DOMAIN 123 219 SH2. FT DOMAIN 240 493 PROTEIN KINASE. FT NP_BIND 246 254 ATP (BY SIMILARITY). FT BINDING 268 268 ATP (BY SIMILARITY). FT ACT_SITE 359 359 BY SIMILARITY. FT MOD_RES 388 388 PHOSPHORYLATION (AUTO-) (BY SIMILARITY). FT CONFLICT 286 286 M -> V (IN REF. 2). FT CONFLICT 406 406 I -> Y (IN REF. 2). SQ SEQUENCE 504 AA; 57607 MW; BDB1DF50EC7370C8 CRC64; GLVSSKKPDK EKPIKEKDKG QWSPLKVSAQ DKDAPPLPPL VVFNHLTPPP PDEHLDEDKH FVVALYDYTA MNDRDLQMLK GEKLQVLKGT GDWWLARSLV TGREGYVPSN FVARVESLEM ERWFFRSQGR KEAERQLLAP INKAGSFLIR ESETNKGAFS LSVKDVTTQG ELIKHYKIRC LDEGGYYISP RITFPSLQAL VQHYSKKGDG LCQRLTLPCV RPAPQNPWAQ DEWEIPRQSL RLVRKLGSGQ FGEVWMGYYK NNMKVAIKTL KEGTMSPEAF LGEANMMKAL QHERLVRLYA VVTKEPIYIV TEYMARGCLL DFLKTDEGSR LSLPRLIDMS AQIAEGMAYI ERMNSIHRDL RAANILVSEA LCCKIADFGL ARIIDSEYTA QEGAKFPIKW TAPEAIHFGV FTIKADVWSF GVLLMEVVTY GRVPYPGMSN PEVIRNLERG YRMPRPDTCP PELYRGVIAE CWRSRPEERP TFEFLQSVLE DFYTATERQY ELQP //