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 15-DEC-2009, entry version 88. DE RecName: Full=cGMP-dependent protein kinase 2; DE Short=CGK 2; DE EC=2.7.11.12; DE AltName: Full=Type II cGMP-dependent protein kinase; DE AltName: Full=cGKII; 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. RC TISSUE=Pituitary; 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). RN [5] RP VARIANTS [LARGE SCALE ANALYSIS] ARG-106 AND ARG-716. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). 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 protein kinase superfamily. AGC Ser/Thr CC protein kinase family. cGMP subfamily. CC -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain. 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 IPI; IPI00012322; -. DR PIR; S68217; S68217. DR RefSeq; NP_006250.1; -. DR UniGene; Hs.570833; -. DR STRING; Q13237; -. DR PhosphoSite; Q13237; -. DR PRIDE; Q13237; -. DR Ensembl; ENST00000264399; ENSP00000264399; ENSG00000138669; Homo sapiens. DR Ensembl; ENST00000395578; ENSP00000378945; ENSG00000138669; Homo sapiens. DR GeneID; 5593; -. DR KEGG; hsa:5593; -. DR UCSC; uc003hmh.1; human. DR CTD; 5593; -. DR GeneCards; GC04M082304; -. DR H-InvDB; HIX0031503; -. DR HGNC; HGNC:9416; PRKG2. DR HPA; CAB018739; -. DR HPA; HPA007386; -. DR MIM; 601591; gene. DR PharmGKB; PA33778; -. DR HOGENOM; HBG755340; -. DR HOVERGEN; Q13237; -. DR InParanoid; Q13237; -. DR OMA; KGVPPDE; -. DR OrthoDB; EOG944P4Z; -. DR BRENDA; 2.7.11.12; 247. DR NextBio; 21704; -. DR ArrayExpress; Q13237; -. DR Bgee; Q13237; -. DR CleanEx; HS_PRKG2; -. DR Genevestigator; Q13237; -. DR GermOnline; ENSG00000138669; Homo sapiens. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW. DR GO; GO:0004692; F:cGMP-dependent protein kinase activity; IEA:EC. DR GO; GO:0006468; P:protein amino acid phosphorylation; TAS:ProtInc. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR016232; cGMP-dependent_protein_kinase. DR InterPro; IPR002374; cGMP_kinase_core. DR InterPro; IPR000595; cNMP_bd. DR InterPro; IPR018490; cNMP_bd-like. DR InterPro; IPR018488; cNMP_bd_CS. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_cat_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR017442; Se/Thr_prot_kinase-like_dom. DR InterPro; IPR008271; Ser/Thr_prot_kinase_AS. DR InterPro; IPR002290; Ser/Thr_prot_kinase_dom. DR Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 2. DR Pfam; PF00027; cNMP_binding; 2. DR Pfam; PF00069; Pkinase; 1. DR PIRSF; PIRSF000559; cGMP-dep_kinase; 1. DR PRINTS; PR00104; CGMPKINASE. DR SMART; SM00100; cNMP; 2. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS51285; AGC_KINASE_CTER; 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. PE 1: Evidence at protein level; KW ATP-binding; cGMP; cGMP-binding; Complete proteome; Kinase; Nitration; KW Nucleotide-binding; Polymorphism; Serine/threonine-protein kinase; KW Transferase. FT CHAIN 1 762 cGMP-dependent protein kinase 2. FT /FTId=PRO_0000086123. FT DOMAIN 453 711 Protein kinase. FT DOMAIN 712 762 AGC-kinase C-terminal. 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 VARIANT 22 22 T -> S (in dbSNP:rs34956759). FT /FTId=VAR_051633. FT VARIANT 106 106 H -> R (in dbSNP:rs34616910). FT /FTId=VAR_040608. FT VARIANT 716 716 W -> R (in a colorectal adenocarcinoma FT sample; somatic mutation). FT /FTId=VAR_040609. FT CONFLICT 57 58 QL -> HG (in Ref. 2; BAA18934). FT CONFLICT 154 154 S -> I (in Ref. 3; CAA76073). FT CONFLICT 460 460 G -> A (in Ref. 2; BAA18934). 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 //