ID MKK2_DROME STANDARD; PRT; 359 AA. AC P49071; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE MAP KINASE-ACTIVATED PROTEIN KINASE 2 (EC 2.7.1.-) (MAPK-ACTIVATED DE PROTEIN KINASE 2) (MAPKAP KINASE 2) (MAPKAPK-2). GN MAPK-AK2. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BIC-D(R26); TISSUE=OVARY; RX MEDLINE; 96011635. RA Larochelle S., Suter B.; RT "The Drosophila melanogaster homolog of the mammalian MAPK-activated RT protein kinase-2 (MAPKAPK-2) lacks a proline-rich N-terminus."; RL Gene 163:209-214(1995). CC -!- FUNCTION: ITS PHYSIOGICAL SUBSTRATE SEEMS TO BE THE SMALL HEAT CC SHOCK PROTEIN (HSP27/HSP25) (BY SIMILARITY). CC -!- PTM: PHOSPHORYLATED AND ACTIVATED BY MAP KINASE (BY SIMILARITY). CC -!- SIMILARITY: WITH THE CONSERVED CATALYTIC DOMAINS OF SER/THR- CC 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 -------------------------------------------------------------------------- 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; U20757; AAA86885.1; -. DR HSSP; Q63450; 1A06. DR FLYBASE; FBgn0013987; MAPk-Ak2. DR INTERPRO; IPR000719; -. DR INTERPRO; IPR002290; -. DR PFAM; PF00069; pkinase; 1. 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; ATP-binding; KW Phosphorylation. FT DOMAIN 20 281 PROTEIN KINASE. FT NP_BIND 26 34 ATP (BY SIMILARITY). FT BINDING 49 49 ATP (BY SIMILARITY). FT ACT_SITE 142 142 BY SIMILARITY. SQ SEQUENCE 359 AA; 41401 MW; 69C5F9A94D1511EC CRC64; MLSLQNQRQP KTTPLTDDYV TSNTVLGYGI NGKVVQCTHR RTQQNYALKV LLDSERARRE VDLHWRVSGC RYIVNIIDVY ENTFKDRKCL LVVMECMEGG ELFQRIQDKA DGAFTEREAA QIMHEICAAV DYLHSRDIAH RDLKPENLLY TTTQPNATLK LTDFGFAKET FTSYTLQTPC YTPYYVAPEV LGPEKYDKSC DIWSLGVVMY IIMCGFPPFY SNHGLAISPG MKNRIRTGQY DFPDPEWTNV SQAAKDLIKG MLNVDPSKRL RIQDVISNKW IAQYNAVPQT PLCTGRMLKE AEETWPEVQE EMTRSLATMR VDYDQMQIKA LDKSNNPLLT KRRKKIEEME LYMANATRN //