ID PIK1_YEAST Reviewed; 1066 AA.
AC P39104; D6W0S7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 27-MAR-2024, entry version 191.
DE RecName: Full=Phosphatidylinositol 4-kinase PIK1 {ECO:0000303|PubMed:8194527};
DE Short=PI4-kinase {ECO:0000303|PubMed:8194527};
DE Short=PtdIns-4-kinase {ECO:0000303|PubMed:8194527};
DE EC=2.7.1.67 {ECO:0000269|PubMed:8194527};
GN Name=PIK1 {ECO:0000303|PubMed:8194527}; OrderedLocusNames=YNL267W;
GN ORFNames=N0795;
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], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=JK9-3D;
RX PubMed=8194527; DOI=10.1002/j.1460-2075.1994.tb06519.x;
RA Garcia-Bustos J.F., Marini F., Stevenson I., Frei C., Hall M.N.;
RT "PIK1, an essential phosphatidylinositol 4-kinase associated with the yeast
RT nucleus.";
RL EMBO J. 13:2352-2361(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8248783; DOI=10.1126/science.8248783;
RA Flanagan C.A., Schnieders E.A., Emerick A.W., Kunisawa R., Admon A.,
RA Thorner J.;
RT "Phosphatidylinositol 4-kinase: gene structure and requirement for yeast
RT cell viability.";
RL Science 262:1444-1448(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8740425;
RX DOI=10.1002/(sici)1097-0061(199604)12:5<505::aid-yea932>3.0.co;2-f;
RA Sen-Gupta M., Lyck R., Fleig U., Niedenthal R.K., Hegemann J.H.;
RT "The sequence of a 24,152 bp segment from the left arm of chromosome XIV
RT from Saccharomyces cerevisiae between the BNI1 and the POL2 genes.";
RL Yeast 12:505-514(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [5]
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 [6]
RP INTERACTION WITH FRQ1.
RX PubMed=10559922; DOI=10.1038/12058;
RA Hendricks K.B., Wang B.Q., Schnieders E.A., Thorner J.;
RT "Yeast homologue of neuronal frequenin is a regulator of
RT phosphatidylinositol-4-OH kinase.";
RL Nat. Cell Biol. 1:234-241(1999).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; THR-394 AND SER-396, AND
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-384 AND SER-592, AND
RP IDENTIFICATION BY 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 [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19898464; DOI=10.1038/ncb1989;
RA Natarajan P., Liu K., Patil D.V., Sciorra V.A., Jackson C.L., Graham T.R.;
RT "Regulation of a Golgi flippase by phosphoinositides and an ArfGEF.";
RL Nat. Cell Biol. 11:1421-1426(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, 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).
RN [13]
RP STRUCTURE BY NMR OF 121-172.
RX PubMed=17720810; DOI=10.1074/jbc.m705499200;
RA Strahl T., Huttner I.G., Lusin J.D., Osawa M., King D., Thorner J.,
RA Ames J.B.;
RT "Structural insights into activation of phosphatidylinositol 4-kinase
RT (Pik1) by yeast frequenin (Frq1).";
RL J. Biol. Chem. 282:30949-30959(2007).
CC -!- FUNCTION: Acts on phosphatidylinositol (PI) in the first committed step
CC in the production of the second messenger inositol 1,4,5,-trisphosphate
CC (PubMed:8194527, PubMed:8248783, PubMed:19898464). PIK1 is part of a
CC nuclear phosphoinositide cycle and could control cytokinesis through
CC the actin cytoskeleton (PubMed:8194527). Involved in the response to
CC mating pheromone (PubMed:8248783). {ECO:0000269|PubMed:19898464,
CC ECO:0000269|PubMed:8194527, ECO:0000269|PubMed:8248783}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP +
CC H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216;
CC EC=2.7.1.67; Evidence={ECO:0000269|PubMed:8194527,
CC ECO:0000269|PubMed:8248783};
CC -!- SUBUNIT: Interacts with FRQ1. {ECO:0000269|PubMed:10559922}.
CC -!- INTERACTION:
CC P39104; Q06389: FRQ1; NbExp=3; IntAct=EBI-13423, EBI-11946;
CC P39104; P38817: GGA2; NbExp=3; IntAct=EBI-13423, EBI-7569;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8194527}. Golgi
CC apparatus, trans-Golgi network {ECO:0000269|PubMed:19898464}.
CC -!- MISCELLANEOUS: Present with 1600 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type III PI4K
CC subfamily. {ECO:0000305}.
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DR EMBL; X76058; CAA53658.1; -; Genomic_DNA.
DR EMBL; L20220; AAA34873.1; -; Genomic_DNA.
DR EMBL; X92494; CAA63231.1; -; Genomic_DNA.
DR EMBL; Z71543; CAA96174.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10293.1; -; Genomic_DNA.
DR PIR; A49335; A49335.
DR RefSeq; NP_014132.1; NM_001183105.1.
DR PDB; 2JU0; NMR; -; B=121-172.
DR PDBsum; 2JU0; -.
DR AlphaFoldDB; P39104; -.
DR SMR; P39104; -.
DR BioGRID; 35573; 259.
DR DIP; DIP-6770N; -.
DR IntAct; P39104; 5.
DR MINT; P39104; -.
DR STRING; 4932.YNL267W; -.
DR GlyGen; P39104; 10 sites, 1 O-linked glycan (10 sites).
DR iPTMnet; P39104; -.
DR MaxQB; P39104; -.
DR PaxDb; 4932-YNL267W; -.
DR PeptideAtlas; P39104; -.
DR EnsemblFungi; YNL267W_mRNA; YNL267W; YNL267W.
DR GeneID; 855454; -.
DR KEGG; sce:YNL267W; -.
DR AGR; SGD:S000005211; -.
DR SGD; S000005211; PIK1.
DR VEuPathDB; FungiDB:YNL267W; -.
DR eggNOG; KOG0903; Eukaryota.
DR GeneTree; ENSGT00550000074892; -.
DR HOGENOM; CLU_002446_2_0_1; -.
DR InParanoid; P39104; -.
DR OMA; ANYFRCE; -.
DR OrthoDB; 147843at2759; -.
DR BioCyc; YEAST:YNL267W-MONOMER; -.
DR Reactome; R-SCE-1660514; Synthesis of PIPs at the Golgi membrane.
DR BioGRID-ORCS; 855454; 0 hits in 10 CRISPR screens.
DR EvolutionaryTrace; P39104; -.
DR PRO; PR:P39104; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P39104; Protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005802; C:trans-Golgi network; IDA:SGD.
DR GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IMP:CACAO.
DR GO; GO:0140504; P:microlipophagy; IMP:SGD.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IDA:SGD.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IMP:SGD.
DR GO; GO:0042998; P:positive regulation of Golgi to plasma membrane protein transport; IMP:CACAO.
DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:CACAO.
DR CDD; cd05168; PI4Kc_III_beta; 1.
DR Gene3D; 6.10.140.1260; -; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR021601; Phosphatidylino_kinase_fungi.
DR InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR InterPro; IPR018936; PI3/4_kinase_CS.
DR InterPro; IPR001263; PI3K_accessory_dom.
DR InterPro; IPR042236; PI3K_accessory_sf.
DR InterPro; IPR049160; PI4KB-PIK1_PIK.
DR InterPro; IPR015433; PI_Kinase.
DR PANTHER; PTHR10048:SF22; PHOSPHATIDYLINOSITOL 4-KINASE BETA; 1.
DR PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF21245; PI4KB-PIK1_PIK; 1.
DR Pfam; PF11522; Pik1; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR PROSITE; PS51545; PIK_HELICAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Golgi apparatus; Kinase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..1066
FT /note="Phosphatidylinositol 4-kinase PIK1"
FT /id="PRO_0000088834"
FT DOMAIN 1..133
FT /note="PIK helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00878"
FT DOMAIN 770..1049
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 218..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..782
FT /note="G-loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 915..923
FT /note="Catalytic loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT REGION 934..958
FT /note="Activation loop"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00269"
FT COMPBIAS 218..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 394
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 126..135
FT /evidence="ECO:0007829|PDB:2JU0"
FT HELIX 156..168
FT /evidence="ECO:0007829|PDB:2JU0"
SQ SEQUENCE 1066 AA; 119923 MW; 7666979CA14B1CB5 CRC64;
MHKASSSKKS FDDTIELKKN EQLLKLINSS EFTLHNCVEL LCKHSENIGI HYYLCQKLAT
FPHSELQFYI PQLVQVLVTM ETESMALEDL LLRLRAENPH FALLTFWQLQ ALLTDLSTDP
ASYGFQVARR VLNNLQTNLF NTSSGSDKNV KIHENVAPAL VLSSMIMSAI AFPQLSEVTK
PLVESQGRRQ KAFVFKLARS AMKDFTKNMT LKNTLLNKKT SRSKRVSSNR SSTPTSPIDL
IDPIKTKEDA SFRKSRHSEV KLDFDIVDDI GNQVFEERIS SSIKLPKRKP KYLDNSYVHR
TYDGKNINRD GSISNTAKAL DGNKGDYISP KGRNDENNEI GNNEDETGGE TEEDADALNS
DHFTSSMPDL HNIQPRTSSA SSASLEGTPK LNRTNSQPLS RQAFKNSKKA NSSLSQEIDL
SQLSTTSKIK MLKANYFRCE TQFAIALETI SQRLARVPTE ARLSALRAEL FLLNRDLPAE
VDIPTLLPPN KKGKLHKLVT ITANEAQVLN SAEKVPYLLL IEYLRDEFDF DPTSETNERL
LKKISGNQGG LIFDLNYMNR KENNENRNES TLTSNNTRSS VYDSNSFNNG ASRNEGLSST
SRSDSASTAH VRTEVNKEED LGDMSMVKVR NRTDDEAYRN ALVIQSAANV PILPDDSQDR
SPELNFGSNL DEVLIENGIN SKNIHSQTDA LADQMRVSAV MLAQLDKSPQ QLSESTKQIR
AQIISSMKEV QDKFGYHDLE ALHGMAGERK LENDLMTGGI DTSYLGEDWA TKKERIRKTS
EYGHFENWDL CSVIAKTGDD LRQEAFAYQM IQAMANIWVK EKVDVWVKRM KILITSANTG
LVETITNAMS VHSIKKALTK KMIEDAELDD KGGIASLNDH FLRAFGNPNG FKYRRAQDNF
ASSLAAYSVI CYLLQVKDRH NGNIMIDNEG HVSHIDFGFM LSNSPGSVGF EAAPFKLTYE
YIELLGGVEG EAFKKFVELT KSSFKALRKY ADQIVSMCEI MQKDNMQPCF DAGEQTSVQL
RQRFQLDLSE KEVDDFVENF LIGKSLGSIY TRIYDQFQLI TQGIYS
//
