PSK1_YEAST
ID PSK1_YEAST Reviewed; 1356 AA.
AC P31374; D6VPK1;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Serine/threonine-protein kinase PSK1;
DE EC=2.7.11.1;
DE AltName: Full=PAS kinase 1;
GN Name=PSK1; OrderedLocusNames=YAL017W; ORFNames=FUN31, YAL002;
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].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8458570; DOI=10.1139/g93-005;
RA Ouellette B.F.F., Clark M.W., Keng T., Storms R.K., Zhong W.-W., Zeng B.,
RA Fortin N., Delaney S., Barton A.B., Kaback D.B., Bussey H.;
RT "Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of a 32
RT kb region between the LTE1 and SPO7 genes.";
RL Genome 36:32-42(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=1561836; DOI=10.1002/yea.320080208;
RA Clark M.W., Zhong W.-W., Keng T., Storms R.K., Barton A.B., Kaback D.B.,
RA Bussey H.;
RT "Identification of a Saccharomyces cerevisiae homolog of the SNF2
RT transcriptional regulator in the DNA sequence of an 8.6 kb region in the
RT LTE1-CYS1 interval on the left arm of chromosome I.";
RL Yeast 8:133-145(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8322517; DOI=10.1002/yea.320090511;
RA Clark M.W., Zhong W.W., Keng T., Storms R.K., Ouellette B.F.F., Barton A.,
RA Kaback D.B., Bussey H.;
RT "The YAL017 gene on the left arm of chromosome I of Saccharomyces
RT cerevisiae encodes a putative serine/threonine protein kinase.";
RL Yeast 9:543-549(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [5]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 73.
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1018, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286 AND SER-1035, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1079, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-192; SER-327;
RP SER-926; SER-1035 AND SER-1055, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-255; SER-1023 AND
RP SER-1055, AND IDENTIFICATION BY 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.
CC {ECO:0000269|PubMed:12372297, ECO:0000269|PubMed:17531808,
CC ECO:0000269|PubMed:8322517}.
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 P31374; P32861: UGP1; NbExp=3; IntAct=EBI-9442, EBI-19987;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 967 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}.
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; L05146; AAC04940.1; -; Genomic_DNA.
DR EMBL; BK006935; DAA06971.2; -; Genomic_DNA.
DR PIR; S33653; S33653.
DR RefSeq; NP_009385.2; NM_001178162.2.
DR AlphaFoldDB; P31374; -.
DR SMR; P31374; -.
DR BioGRID; 31749; 124.
DR DIP; DIP-6267N; -.
DR IntAct; P31374; 20.
DR MINT; P31374; -.
DR STRING; 4932.YAL017W; -.
DR CarbonylDB; P31374; -.
DR iPTMnet; P31374; -.
DR MaxQB; P31374; -.
DR PaxDb; P31374; -.
DR PRIDE; P31374; -.
DR EnsemblFungi; YAL017W_mRNA; YAL017W; YAL017W.
DR GeneID; 851216; -.
DR KEGG; sce:YAL017W; -.
DR SGD; S000000015; PSK1.
DR VEuPathDB; FungiDB:YAL017W; -.
DR eggNOG; KOG1152; Eukaryota.
DR GeneTree; ENSGT00940000159035; -.
DR HOGENOM; CLU_004134_1_0_1; -.
DR InParanoid; P31374; -.
DR OMA; NMDESEC; -.
DR BioCyc; YEAST:G3O-28829-MON; -.
DR PRO; PR:P31374; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P31374; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IMP:SGD.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0045719; P:negative regulation of glycogen biosynthetic process; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IMP:SGD.
DR GO; GO:0060917; P:regulation of (1->6)-beta-D-glucan biosynthetic process; IGI:SGD.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55785; SSF55785; 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; Repeat; Serine/threonine-protein kinase; Transferase;
KW Translation regulation.
FT CHAIN 1..1356
FT /note="Serine/threonine-protein kinase PSK1"
FT /id="PRO_0000086042"
FT DOMAIN 450..518
FT /note="PAS 1"
FT DOMAIN 738..807
FT /note="PAS 2"
FT DOMAIN 1096..1354
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 20..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..972
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1230
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 1102..1110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 926
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1018
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 1023
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1035
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 1055
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1079
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CONFLICT 73
FT /note="E -> Q (in Ref. 1; no nucleotide entry, 2; no
FT nucleotide entry, 3; no nucleotide entry and 4; AAC04940)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1356 AA; 152332 MW; 9A2AF4A9C1785586 CRC64;
MPYIGASNLS EHSFVNLKEK HAITHKGTSS SVASLQTPPS PDQENHIDNE LENYDTSLSD
VSTPNKKEGD EFEQSLRDTF ASFRKTKPPP PLDFEQPRLP STASSSVDST VSSPLTDEDI
KELEFLPNES THSYSYNPLS PNSLAVRLRI LKRSLEIIIQ NPSMLLEPTP DDLPPLKEFA
GRRSSLPRTS ASANHLMNRN KSQIWNTTSA TLNAFVNNTS SSSAASSALS NKKPGTPVFP
NLDPTHSQTF HRANSLAYLP SILPEQDPLL KHNNSLFRGD YGNNISPERP SFRQPFKDQT
SNLRNSSLLN ERAYQEDETF LPHHGPSMDL LNEQRANLKS LLNLLNETLE KNTSERASDL
HMISLFNLNK LMLGDPKKNN SERDKRTEKL KKILLDSLAE PFFEHYNFIG DNPIADTDEL
KEEIDEFTGS GDTTAITDIR PQQDYGRILR TFTSTKNSAP QAIFTCSQED PWQFRAANDL
ACLVFGISQN AIRALTLMDL IHTDSRNFVL HKLLSTEGQE MVFTGEIIGI VQPETLSSSK
VVWASFWAKR KNGLLVCVFE KVPCDYVDVL LNLDDFGAEN IVDKCELLSD GPTLSSSSTL
SLPKMASSPT GSKLEYSLER KILEKSYTKP TSTENRNGDE NQLDGDSHSE PSLSSSPVRS
KKSVKFANDI KDVKSISQSL AKLMDDVRNG VVFDPDDDLL PMPIKVCNHI NETRYFTLNH
LSYNIPCAVS STVLEDELKL KIHSLPYQAG LFIVDSHTLD IVSSNKSILK NMFGYHFAEL
VGKSITEIIP SFPKFLQFIN DKYPALDITL HKNKGLVLTE HFFRKIQAEI MGDRKSFYTS
VGIDGLHRDG CEIKIDFQLR VMNSKVILLW VTHSRDVVFE EYNTNPSQLK MLKESELSLM
SSASSSASSS KKSSSRISTG TLKDMSNLST YEDLAHRTNK LKYEIGDDSR AHSQSTLSEQ
EQVPLENDKD SGEMMLADPE MKHKLELARI YSRDKSQFVK EGNFKVDENL IISKISLSPS
TESLADSKSS GKGLSPLEEE KLIDENATEN GLAGSPKDED GIIMTNKRGN QPVSTFLRTP
EKNIGAQKHV KKFSDFVSLQ KMGEGAYGKV NLCIHKKNRY IVVIKMIFKE RILVDTWVRD
RKLGTIPSEI QIMATLNKKP HENILRLLDF FEDDDYYYIE TPVHGETGCI DLFDLIEFKT
NMTEFEAKLI FKQVVAGIKH LHDQGIVHRD IKDENVIVDS KGFVKIIDFG SAAYVKSGPF
DVFVGTIDYA APEVLGGNPY EGQPQDIWAI GILLYTVVFK ENPFYNIDEI LEGDLKFNNA
EEVSEDCIEL IKSILNRCVP KRPTIDDINN DKWLVI
