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; INSECTA; DIPTERA. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BIC-D(R26); TISSUE=OVARY; RX MEDLINE; 96011635. RA LAROCHELLE S., SUTER B.; 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 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; G755491; -. DR FLYBASE; FBGN0013987; MAPK-AK2. 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; 34E3AA17 CRC32; 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 //