PSK2_YEAST
ID PSK2_YEAST Reviewed; 1101 AA.
AC Q08217; D6W221;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Serine/threonine-protein kinase PSK2;
DE EC=2.7.11.1;
DE AltName: Full=PAS kinase 2;
GN Name=PSK2; OrderedLocusNames=YOL045W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [2]
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 [3]
RP DOMAIN.
RX PubMed=11459942; DOI=10.1073/pnas.161284798;
RA Rutter J., Michnoff C.H., Harper S.M., Gardner K.H., McKnight S.L.;
RT "PAS kinase: an evolutionarily conserved PAS domain-regulated
RT serine/threonine kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8991-8996(2001).
RN [4]
RP FUNCTION.
RX PubMed=12372297; DOI=10.1016/s0092-8674(02)00974-1;
RA Rutter J., Probst B.L., McKnight S.L.;
RT "Coordinate regulation of sugar flux and translation by PAS kinase.";
RL Cell 111:17-28(2002).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
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 [7]
RP FUNCTION.
RX PubMed=17531808; DOI=10.1016/j.molcel.2007.03.025;
RA Smith T.L., Rutter J.;
RT "Regulation of glucose partitioning by PAS kinase and Ugp1
RT phosphorylation.";
RL Mol. Cell 26:491-499(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-118, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-118, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in the control of
CC sugar metabolism and translation. Phosphorylates UGP1, which is
CC required for normal glycogen and beta-(1,6)-glucan synthesis. This
CC phosphorylation shifts glucose partitioning toward cell wall glucan
CC synthesis at the expense of glycogen synthesis. Phosphorylates also the
CC glycogen synthase GSY2 and the translation factors CAF20, TIF11 and
CC SRO9. {ECO:0000269|PubMed:12372297, ECO:0000269|PubMed:17531808}.
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=2.7.11.1;
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=2.7.11.1;
CC -!- INTERACTION:
CC Q08217; P32861: UGP1; NbExp=3; IntAct=EBI-9839, EBI-19987;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
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. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; Z74788; CAA99051.1; -; Genomic_DNA.
DR EMBL; Z74786; CAA99047.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10737.1; -; Genomic_DNA.
DR PIR; S66730; S66730.
DR RefSeq; NP_014597.1; NM_001183299.1.
DR AlphaFoldDB; Q08217; -.
DR SMR; Q08217; -.
DR BioGRID; 34357; 187.
DR DIP; DIP-6430N; -.
DR IntAct; Q08217; 9.
DR MINT; Q08217; -.
DR STRING; 4932.YOL045W; -.
DR iPTMnet; Q08217; -.
DR MaxQB; Q08217; -.
DR PaxDb; Q08217; -.
DR PRIDE; Q08217; -.
DR TopDownProteomics; Q08217; -.
DR EnsemblFungi; YOL045W_mRNA; YOL045W; YOL045W.
DR GeneID; 854111; -.
DR KEGG; sce:YOL045W; -.
DR SGD; S000005405; PSK2.
DR VEuPathDB; FungiDB:YOL045W; -.
DR eggNOG; KOG1152; Eukaryota.
DR GeneTree; ENSGT00940000159035; -.
DR HOGENOM; CLU_004134_1_0_1; -.
DR InParanoid; Q08217; -.
DR OMA; ERVPCDY; -.
DR BioCyc; YEAST:G3O-33459-MON; -.
DR PRO; PR:Q08217; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08217; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; IMP:SGD.
DR GO; GO:0045719; P:negative regulation of glycogen biosynthetic process; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:SGD.
DR GO; GO:0060917; P:regulation of (1->6)-beta-D-glucan biosynthetic process; IGI:SGD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Translation regulation.
FT CHAIN 1..1101
FT /note="Serine/threonine-protein kinase PSK2"
FT /id="PRO_0000086156"
FT DOMAIN 841..1099
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 975
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 847..855
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 870
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 118
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 1101 AA; 124373 MW; 3FC9CF3EF99B7937 CRC64;
MTYPVSAAAP ADISYSKNTP LVGLSKPPCL YQHASSSVDS FSSTFSDDDR SDLVAVPNES
PHAFSYNPIS PNSLGVRLTI LRRSLEIMVN SPDILHELKK KAPVIAYPPS LRHTRNLTET
ATLSASRDPL NGSLISPLVS NMPSPASRPV IQRATSLMVL PDNDTASKLN PAKSELENLL
FLLNLALENN SFERASDLHM LSLLNIKKIN FDSDIQKSET LKKVLLDSLA EPFFENYKKF
PHKDLGSKSQ YNEYEEKHDD IVSLADIKPQ QDYSRILHPF TSAKNSGPEA IFTCSQQYPW
NFKAANDLAC LTFGISKNVI KALTLLDLIH TDSRNFVLEK IMNAEDDNQE IVFTGETIPI
VQPNSTSNNN VPNLIWASLW AKRKNGLLVC VFEKTPCDYI DVMLNLRDFS VDSIIDTTHF
LENFDKKKQQ ESTSPMTEKK TVKFANEIHD IGSVSHSLSK LIDDVRFGKV FSADDDLLPL
SIRVANHVNE ERYFTLNCLS ENIPCAVTTS VLENEIKLKI HSLPYQAGLF IVDSHTLSLL
SFNKSVAKNM FGLRLHELAG SSVTKLVPSL ADMISYINKT YPMLNITLPE NKGLVLTEHF
FRKIEAEMHH DKDSFYTSIG LDGCHKDGNL IKVDVQLRVL NTNAVLLWIT HSRDVVIENY
TTVPSQLPML KENEIDVVGS RGSSSASSKK SSEKIPVNTL KAMADLSISS AETISNSDDE
VDLNQVNEKL RETSCGKVRG IESNDNNNYD DDMTMVDDPE LKHKIELTKM YTQDKSKFVK
DDNFKVDEKF IMRIIEPING EEIKKETNEL DKRNSTLKAT YLTTPEANIG SQKRIKKFSD
FTILQVMGEG AYGKVNLCIH NREHYIVVIK MIFKERILVD TWVRDRKLGT IPSEIQIMAT
LNKNSQENIL KLLDFFEDDD YYYIETPVHG ETGSIDLFDV IEFKKDMVEH EAKLVFKQVV
ASIKHLHDQG IVHRDIKDEN VIVDSHGFVK LIDFGSAAYI KSGPFDVFVG TMDYAAPEVL
GGSSYKGKPQ DIWALGVLLY TIIYKENPYY NIDEILEGEL RFDKSEHVSE ECISLIKRIL
TREVDKRPTI DEIYEDKWLK I
