ID MPK6_ARATH STANDARD; PRT; 395 AA. AC Q39026; DT 01-NOV-1997 (REL. 35, CREATED) DT 01-NOV-1997 (REL. 35, LAST SEQUENCE UPDATE) DT 15-JUL-1998 (REL. 36, LAST ANNOTATION UPDATE) DE MITOGEN-ACTIVATED PROTEIN KINASE HOMOLOG 6 (EC 2.7.1.-) (MAP KINASE 6) DE (ATMPK6). GN MPK6 OR F18O19.10. OS ARABIDOPSIS THALIANA (MOUSE-EAR CRESS). OC EUKARYOTA; VIRIDIPLANTAE; STREPTOPHYTA; EMBRYOPHYTA; TRACHEOPHYTA; OC EUPHYLLOPHYTES; SPERMATOPHYTA; MAGNOLIOPHYTA; EUDICOTYLEDONS; ROSIDAE; OC CAPPARALES; BRASSICACEAE; ARABIDOPSIS. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE; 94109583. RA MIZOGUCHI T., HAYASHIDA N., YAMAGUCHI-SHINOZAKI K., KAMADA H., RA SHINOZAKI K.; RT "ATMPKs: a gene family of plant MAP kinases in Arabidopsis thaliana."; RL FEBS LETT. 336:440-444(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RA ROUNSLEY S.D., LIN X., KETCHUM K.A., CROSBY M.L., BRANDON R.C., RA SPRIGGS T.A., MASON T.M., KERLAVAGE A.R., ADAMS M.D., SOMERVILLE C.R., RA VENTER J.C.; RL SUBMITTED (JUL-1997) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- ENZYME REGULATION: ACTIVATED BY TYROSINE AND THREONINE CC PHOSPHORYLATION (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE CDC2/CDC28 SUBFAMILY OF SER/THR CC PROTEIN KINASES. STRONGEST SIMILARITY WITH OTHER MAP 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 -------------------------------------------------------------------------- CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D21842; G457404; -. DR EMBL; AC002333; G2281091; -. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PFAM; PF00069; pkinase; 1. DR HSSP; P27703; 1GOL. KW TRANSFERASE; SERINE/THREONINE-PROTEIN KINASE; ATP-BINDING; KW PHOSPHORYLATION; MULTIGENE FAMILY. FT DOMAIN 63 348 PROTEIN KINASE. FT NP_BIND 69 77 ATP (BY SIMILARITY). FT BINDING 92 92 ATP (BY SIMILARITY). FT ACT_SITE 189 189 BY SIMILARITY. FT MOD_RES 221 221 PHOSPHORYLATION (ACTIVATES THE KINASE) FT (BY SIMILARITY). FT MOD_RES 223 223 PHOSPHORYLATION (ACTIVATES THE KINASE) FT (BY SIMILARITY). SQ SEQUENCE 395 AA; 45057 MW; D3A94289 CRC32; MDGGSGQPAA DTEMTEAPGG FPAAAPSPQM PGIENIPATL SHGGRFIQYN IFGNIFEVTA KYKPPIMPIG KGAYGIVCSA MNSETNESVA IKKIANAFDN KIDAKRTLRE IKLLRHMDHE NIVAIRDIIP PPLRNAFNDV YIAYELMDTD LHQIIRSNQA LSEEHCQYFL YQILRGLKYI HSANVLHRDL KPSNLLLNAN CDLKICDFGL ARVTSESDFM TEYVVTRWYR APELLLNSSD YTAAIDVWSV GCIFMELMDR KPLFPGRDHV HQLRLLMELI GTPSEEELEF LNENAKRYIR QLPPYPRQSI TDKFPTVHPL AIDLIEKMLT FDPRRRITVL DALAHPYLNS LHDISDEPEC TIPFNFDFEN HALSEEQMKE LIYREALAFN PEYQQ //