KAPB_YEAST
ID KAPB_YEAST Reviewed; 380 AA.
AC P06245; D6W3G6;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=cAMP-dependent protein kinase type 2;
DE Short=PKA 2;
DE EC=2.7.11.11;
GN Name=TPK2; Synonyms=PKA2, YKR1; OrderedLocusNames=YPL203W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3036373; DOI=10.1016/0092-8674(87)90223-6;
RA Toda T., Cameron S., Sass P., Zoller M., Wigler M.;
RT "Three different genes in S. cerevisiae encode the catalytic subunits of
RT the cAMP-dependent protein kinase.";
RL Cell 50:277-287(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26786 / X2180-1A;
RX PubMed=3308514; DOI=10.1016/0014-5793(87)80386-1;
RA Ohno S., Aoshima M., Matsumoto S., Yahara I., Suzuki K.;
RT "A yeast gene coding for a putative protein kinase homologous to cdc25
RT suppressing protein kinase.";
RL FEBS Lett. 222:279-285(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-224, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.11;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.11;
CC -!- ACTIVITY REGULATION: Activated by cAMP.
CC -!- INTERACTION:
CC P06245; P07278: BCY1; NbExp=6; IntAct=EBI-9465, EBI-9475;
CC -!- MISCELLANEOUS: Present with 2220 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. cAMP subfamily. {ECO:0000305}.
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DR EMBL; M17073; AAA35165.1; -; Genomic_DNA.
DR EMBL; Y00694; CAA68689.1; -; Genomic_DNA.
DR EMBL; Z73559; CAA97917.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11232.1; -; Genomic_DNA.
DR PIR; S65222; OKBYC2.
DR RefSeq; NP_015121.1; NM_001184017.1.
DR AlphaFoldDB; P06245; -.
DR SMR; P06245; -.
DR BioGRID; 35981; 217.
DR ComplexPortal; CPX-537; cAMP-dependent protein kinase complex variant 2.
DR ComplexPortal; CPX-572; cAMP-dependent protein kinase complex variant 4.
DR ComplexPortal; CPX-574; cAMP-dependent protein kinase complex variant 6.
DR DIP; DIP-549N; -.
DR IntAct; P06245; 46.
DR MINT; P06245; -.
DR STRING; 4932.YPL203W; -.
DR iPTMnet; P06245; -.
DR MaxQB; P06245; -.
DR PaxDb; P06245; -.
DR PRIDE; P06245; -.
DR EnsemblFungi; YPL203W_mRNA; YPL203W; YPL203W.
DR GeneID; 855898; -.
DR KEGG; sce:YPL203W; -.
DR SGD; S000006124; TPK2.
DR VEuPathDB; FungiDB:YPL203W; -.
DR eggNOG; KOG0616; Eukaryota.
DR GeneTree; ENSGT00940000176357; -.
DR HOGENOM; CLU_000288_63_5_1; -.
DR InParanoid; P06245; -.
DR OMA; WQDSRNL; -.
DR BioCyc; YEAST:G3O-34095-MON; -.
DR BRENDA; 2.7.11.11; 984.
DR Reactome; R-SCE-163615; PKA activation.
DR Reactome; R-SCE-164378; PKA activation in glucagon signalling.
DR Reactome; R-SCE-180024; DARPP-32 events.
DR Reactome; R-SCE-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-SCE-442720; CREB1 phosphorylation through the activation of Adenylate Cyclase.
DR Reactome; R-SCE-5610787; Hedgehog 'off' state.
DR Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-SCE-9634597; GPER1 signaling.
DR Reactome; R-SCE-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:P06245; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P06245; protein.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IDA:SGD.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0000932; C:P-body; IDA:SGD.
DR GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IDA:SGD.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0031369; F:translation initiation factor binding; IPI:SGD.
DR GO; GO:0001403; P:invasive growth in response to glucose limitation; IMP:SGD.
DR GO; GO:0010607; P:negative regulation of cytoplasmic mRNA processing body assembly; IGI:SGD.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; IMP:SGD.
DR GO; GO:0010737; P:protein kinase A signaling; IGI:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0007265; P:Ras protein signal transduction; IGI:SGD.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
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 Acetylation; ATP-binding; cAMP; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..380
FT /note="cAMP-dependent protein kinase type 2"
FT /id="PRO_0000086048"
FT DOMAIN 70..324
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 325..380
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ACT_SITE 193
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 76..84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 224
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 214..220
FT /note="FAKEVQT -> LRQRGTN (in Ref. 2; CAA68689)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="A -> V (in Ref. 2; CAA68689)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="H -> Q (in Ref. 1; AAA35165)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 44220 MW; 1BC255C6D0F33137 CRC64;
MEFVAERAQP VGQTIQQQNV NTYGQGVLQP HHDLQQRQQQ QQQRQHQQLL TSQLPQKSLV
SKGKYTLHDF QIMRTLGTGS FGRVHLVRSV HNGRYYAIKV LKKQQVVKMK QVEHTNDERR
MLKLVEHPFL IRMWGTFQDA RNIFMVMDYI EGGELFSLLR KSQRFPNPVA KFYAAEVILA
LEYLHAHNII YRDLKPENIL LDRNGHIKIT DFGFAKEVQT VTWTLCGTPD YIAPEVITTK
PYNKSVDWWS LGVLIYEMLA GYTPFYDTTP MKTYEKILQG KVVYPPYFHP DVVDLLSKLI
TADLTRRIGN LQSGSRDIKA HPWFSEVVWE RLLAKDIETP YEPPITSGIG DTSLFDQYPE
EQLDYGIQGD DPYAEYFQDF
