ID KGP2_HUMAN Reviewed; 762 AA. AC Q13237; O00125; O60916; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 28-NOV-2006, entry version 57. DE cGMP-dependent protein kinase 2 (EC 2.7.11.12) (CGK 2) (cGKII) (Type DE II cGMP-dependent protein kinase). GN Name=PRKG2; Synonyms=PRKGR2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=96183022; PubMed=8607838; DOI=10.1006/bbrc.1996.0477; 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 NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=96085221; PubMed=7498513; DOI=10.1016/0014-5793(95)01223-2; 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 lost RT upon introduction of SV40 T antigen or immortalization in human RT cells."; RL FEBS Lett. 375:263-267(1995). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-734. RX MEDLINE=98204768; PubMed=9535793; DOI=10.1006/bbrc.1998.8399; 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). RN [4] RP NITRATION [LARGE SCALE ANALYSIS] AT TYR-354, AND MASS SPECTROMETRY. RX PubMed=15555551; DOI=10.1016/j.bbrc.2004.10.169; RA Zhan X., Desiderio D.M.; RT "The human pituitary nitroproteome: detection of nitrotyrosyl-proteins RT with two-dimensional Western blotting, and amino acid sequence RT determination with mass spectrometry."; RL Biochem. Biophys. Res. Commun. 325:1180-1186(2004). CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- ENZYME REGULATION: Binding of cGMP results in enzyme activation. CC -!- TISSUE SPECIFICITY: Highly concentrated in brain, lung and CC intestinal mucosa. CC -!- SIMILARITY: Belongs to the Ser/Thr protein kinase family. cGMP CC subfamily. CC -!- SIMILARITY: Contains 2 cyclic nucleotide-binding domains. CC -!- SIMILARITY: Contains 1 protein kinase domain. 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; -; mRNA. DR EMBL; D70899; BAA18934.1; -; mRNA. DR EMBL; Y16106; CAA76073.1; -; Genomic_DNA. DR EMBL; Y16107; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16108; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16109; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16110; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16111; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16112; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16113; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16114; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16115; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16116; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16117; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16118; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16119; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16120; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16121; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16122; CAA76073.1; JOINED; Genomic_DNA. DR EMBL; Y16123; CAA76073.1; JOINED; Genomic_DNA. DR PIR; S68217; S68217. DR UniGene; Hs.570833; -. DR HSSP; P36887; 1CTP. DR Ensembl; ENSG00000138669; Homo sapiens. DR KEGG; hsa:5593; -. DR HGNC; HGNC:9416; PRKG2. DR MIM; 601591; gene. DR ArrayExpress; Q13237; -. DR GO; GO:0004672; F:protein kinase activity; TAS:ProtInc. DR GO; GO:0006468; P:protein amino acid phosphorylation; TAS:ProtInc. DR GO; GO:0000074; P:regulation of progression through cell cycle; TAS:ProtInc. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR InterPro; IPR002374; cGMP_kin. DR InterPro; IPR000595; cNMP_bd. DR InterPro; IPR011009; Kinase_like. DR InterPro; IPR000961; Pkinase_C. DR InterPro; IPR000719; Prot_kinase. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF00027; cNMP_binding; 2. DR Pfam; PF00069; Pkinase; 1. DR PRINTS; PR00104; CGMPKINASE. DR ProDom; PD000001; Prot_kinase; 2. DR SMART; SM00100; cNMP; 2. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS00888; CNMP_BINDING_1; 2. DR PROSITE; PS00889; CNMP_BINDING_2; 2. DR PROSITE; PS50042; CNMP_BINDING_3; 2. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. KW ATP-binding; cGMP; cGMP-binding; Kinase; Nitration; KW Nucleotide-binding; Serine/threonine-protein kinase; Transferase. FT CHAIN 1 762 cGMP-dependent protein kinase 2. FT /FTId=PRO_0000086123. FT DOMAIN 453 711 Protein kinase. FT NP_BIND 168 285 cGMP 1. FT NP_BIND 286 417 cGMP 2. FT NP_BIND 459 467 ATP (By similarity). FT ACT_SITE 576 576 Proton acceptor (By similarity). FT BINDING 482 482 ATP (By similarity). FT MOD_RES 354 354 Nitrated tyrosine. 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 //