ID KGP2_HUMAN STANDARD; PRT; 762 AA. AC Q13237; O00125; O60916; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE cGMP-dependent protein kinase 2 (EC 2.7.1.37) (CGK 2) (cGKII) (Type II DE cGMP-dependent protein kinase). GN PRKG2 OR PRKGR2. 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=96183022; PubMed=8607838; RA Orstavik S., Solberg R., Taskn K., Nordahl M., Altherr M.R., RA Hansson V., Jahnsen T., Sandberg M.; RT "Molecular cloning, cDNA structure, and chromosomal localization of RT the human type II cGMP-dependent protein kinase."; RL Biochem. Biophys. Res. Commun. 220:759-765(1996). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=96085221; PubMed=7498513; RA Fujii M., Ogata T., Takahashi E., Yamada K., Nakabayashi K., Oishi M., RA Ayusawa D.; RT "Expression of the human cGMP-dependent protein kinase II gene is RT lost upon introduction of SV40 T antigen or immortalization in human RT cells."; RL FEBS Lett. 375:263-267(1995). RN [3] RP SEQUENCE OF 1-734 FROM N.A. RX MEDLINE=98204768; PubMed=9535793; RA Witczak O., Orstavik S., Natarajan V., Frengen E., Jahnsen T., RA Sandberg M.; RT "Characterization of the gene encoding the human type II cGMP- RT dependent protein kinase."; RL Biochem. Biophys. Res. Commun. 245:113-119(1998). CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- ENZYME REGULATION: BINDING OF CGMP TO CGK RESULTS IN ENZYME CC ACTIVATION. CC -!- TISSUE SPECIFICITY: HIGHLY CONCENTRATED IN BRAIN, LUNG, AND CC INTESTINAL MUCOSA. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC CGMP SUBFAMILY. CC -!- SIMILARITY: CONTAINS 2 CYCLIC NUCLEOTIDE-BINDING DOMAINS. 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; X94612; CAA64318.1; -. DR EMBL; D70899; BAA18934.1; -. DR EMBL; Y16106; CAA76073.1; -. DR EMBL; Y16107; CAA76073.1; JOINED. DR EMBL; Y16108; CAA76073.1; JOINED. DR EMBL; Y16109; CAA76073.1; JOINED. DR EMBL; Y16110; CAA76073.1; JOINED. DR EMBL; Y16111; CAA76073.1; JOINED. DR EMBL; Y16112; CAA76073.1; JOINED. DR EMBL; Y16113; CAA76073.1; JOINED. DR EMBL; Y16114; CAA76073.1; JOINED. DR EMBL; Y16115; CAA76073.1; JOINED. DR EMBL; Y16116; CAA76073.1; JOINED. DR EMBL; Y16117; CAA76073.1; JOINED. DR EMBL; Y16118; CAA76073.1; JOINED. DR EMBL; Y16119; CAA76073.1; JOINED. DR EMBL; Y16120; CAA76073.1; JOINED. DR EMBL; Y16121; CAA76073.1; JOINED. DR EMBL; Y16122; CAA76073.1; JOINED. DR EMBL; Y16123; CAA76073.1; JOINED. DR HSSP; P05132; 1BKX. DR MIM; 601591; -. DR InterPro; IPR000719; Euk_pkinase. DR InterPro; IPR000961; Pkinase_C. DR InterPro; IPR002290; Ser_thr_pkinase. DR InterPro; IPR002374; cGMP_kin. DR InterPro; IPR000595; cNMP_binding. DR Pfam; PF00027; cNMP_binding; 2. DR Pfam; PF00069; pkinase; 1. DR PRINTS; PR00104; CGMPKINASE. DR ProDom; PD000001; Euk_pkinase; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SMART; SM00100; cNMP; 2. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00888; CNMP_BINDING_1; 2. DR PROSITE; PS00889; CNMP_BINDING_2; 2. DR PROSITE; PS50042; CNMP_BINDING_3; 2. KW Transferase; Serine/threonine-protein kinase; ATP-binding; KW cGMP-binding. FT NP_BIND 168 285 CGMP 1. FT NP_BIND 286 417 CGMP 2. FT DOMAIN 453 711 PROTEIN KINASE. FT NP_BIND 459 467 ATP (BY SIMILARITY). FT BINDING 482 482 ATP (BY SIMILARITY). FT ACT_SITE 576 576 BY SIMILARITY. FT CONFLICT 57 58 QL -> HG (IN REF. 2). FT CONFLICT 154 154 S -> I (IN REF. 3). FT CONFLICT 460 460 G -> A (IN REF. 2). SQ SEQUENCE 762 AA; 87432 MW; FA7BA149906B5996 CRC64; MGNGSVKPKH SKHPDGHSGN LTTDALRNKV TELERELRRK DAEIQEREYH LKELREQLSK QTVAIAELTE ELQNKCIQLN KLQDVVHMQG GSPLQASPDK VPLEVHRKTS GLVSLHSRRG AKAGVSAEPT TRTYDLNKPP EFSFEKARVR KDSSEKKLIT DALNKNQFLK RLDPQQIKDM VECMYGRNYQ QGSYIIKQGE PGNHIFVLAE GRLEVFQGEK LLSSIPMWTT FGELAILYNC TRTASVKAIT NVKTWALDRE VFQNIMRRTA QARDEQYRNF LRSVSLLKNL PEDKLTKIID CLEVEYYDKG DYIIREGEEG STFFILAKGK VKVTQSTEGH DQPQLIKTLQ KGEYFGEKAL ISDDVRSANI IAEENDVACL VIDRETFNQT VGTFEELQKY LEGYVANLNR DDEKRHAKRS MSNWKLSKAL SLEMIQLKEK VARFSSSSPF QNLEIIATLG VGGFGRVELV KVKNENVAFA MKCIRKKHIV DTKQQEHVYS EKRILEELCS PFIVKLYRTF KDNKYVYMLL EACLGGELWS ILRDRGSFDE PTSKFCVACV TEAFDYLHRL GIIYRDLKPE NLILDAEGYL KLVDFGFAKK IGSGQKTWTF CGTPEYVAPE VILNKGHDFS VDFWSLGILV YELLTGNPPF SGVDQMMTYN LILKGIEKMD FPRKITRRPE DLIRRLCRQN PTERLGNLKN GINDIKKHRW LNGFNWEGLK ARSLPSPLQR ELKGPIDHSY FDKYPPEKGM PPDELSGWDK DF //