ID APKB_ARATH STANDARD; PRT; 412 AA. AC P46573; Q9SLH5; DT 01-NOV-1995 (Rel. 32, Created) DT 01-OCT-2000 (Rel. 40, Last sequence update) DT 01-OCT-2000 (Rel. 40, Last annotation update) DE PROTEIN KINASE APK1B (EC 2.7.1.-). GN APK1B OR AT2G28930 OR T9I4.1. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Embryophyta; Tracheophyta; Spermatophyta; OC Magnoliophyta; eudicotyledons; core eudicots; Rosidae; eurosids II; OC Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=20083487; PubMed=10617197; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H., Moffat K.S., RA Cronin L.A., Shen M., VanAken S.E., Umayam L., Tallon L.J., Gill J.E., RA Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., RA Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., RA Salzberg S.L., Fraser C.M., Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis RT thaliana."; RL Nature 402:761-768(1999). RN [2] RP SEQUENCE OF 143-346 FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=93081726; PubMed=1450380; RA Hirayama T., Oka A.; RT "Novel protein kinase of Arabidopsis thaliana (APK1) that RT phosphorylates tyrosine, serine and threonine."; RL Plant Mol. Biol. 20:653-662(1992). CC -!- FUNCTION: POSSIBLE BI-FUNCTIONAL KINASE. IN VITRO, IT EXHIBITS CC SERINE/THREONINE ACTIVITY. IN VIVO, CAN PHOSPHORYLATE TYROSINE CC RESIDUES OF LIMITED SUBSTRATES (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. 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; AC005315; AAC33221.1; -. DR EMBL; D10152; BAA20968.1; -. DR HSSP; P08631; 2HCK. DR INTERPRO; IPR000719; -. DR INTERPRO; IPR001245; -. DR INTERPRO; IPR002290; -. DR PFAM; PF00069; pkinase; 1. DR PRINTS; PR00109; TYRKINASE. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Serine/threonine-protein kinase; Tyrosine-protein kinase; KW ATP-binding; Multigene family; Myristate. FT LIPID 2 2 MYRISTATE (BY SIMILARITY). FT DOMAIN 69 356 PROTEIN KINASE. FT NP_BIND 75 83 ATP (BY SIMILARITY). FT BINDING 107 107 ATP (BY SIMILARITY). FT ACT_SITE 204 204 BY SIMILARITY. SQ SEQUENCE 412 AA; 45746 MW; EB1CA0B1A626A5DA CRC64; MGICLSAQIK AVSPGASPKY MSSEANDSLG SKSSSVSIRT NPRTEGEILQ SPNLKSFTFA ELKAATRNFR PDSVLGEGGF GSVFKGWIDE QTLTASKPGT GVVIAVKKLN QDGWQGHQEW LAEVNYLGQF SHPNLVKLIG YCLEDEHRLL VYEFMPRGSL ENHLFRRGSY FQPLSWTLRL KVALGAAKGL AFLHNAETSV IYRDFKTSNI LLDSEYNAKL SDFGLAKDGP TGDKSHVSTR IMGTYGYAAP EYLATGHLTT KSDVYSYGVV LLEVLSGRRA VDKNRPPGEQ KLVEWARPLL ANKRKLFRVI DNRLQDQYSM EEACKVATLA LRCLTFEIKL RPNMNEVVSH LEHIQTLNEA GGRNIDMVQR RMRRRSDSVA INQKPNAGFA RQTAVGVIAT AYPRPSDSPL FV //