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PIK1_YEAST
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   03-AUG-2022, entry version 183.
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   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   [12]
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). PIK1 is part of a nuclear
CC       phosphoinositide cycle and could control cytokinesis through the actin
CC       cytoskeleton (PubMed:8194527). Involved in the response to mating
CC       pheromone (PubMed:8248783). {ECO:0000269|PubMed:8194527,
CC       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}.
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; 252.
DR   DIP; DIP-6770N; -.
DR   IntAct; P39104; 5.
DR   MINT; P39104; -.
DR   STRING; 4932.YNL267W; -.
DR   iPTMnet; P39104; -.
DR   MaxQB; P39104; -.
DR   PaxDb; P39104; -.
DR   PRIDE; P39104; -.
DR   EnsemblFungi; YNL267W_mRNA; YNL267W; YNL267W.
DR   GeneID; 855454; -.
DR   KEGG; sce:YNL267W; -.
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; QPCFNAG; -.
DR   BioCyc; YEAST:YNL267W-MON; -.
DR   Reactome; R-SCE-1660514; Synthesis of PIPs at the Golgi membrane.
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:0052742; F:phosphatidylinositol kinase activity; IBA:GO_Central.
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   Gene3D; 1.10.1070.11; -; 1.
DR   Gene3D; 1.25.40.70; -; 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; IPR015433; PI_Kinase.
DR   PANTHER; PTHR10048; PTHR10048; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF11522; Pik1; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF56112; SSF56112; 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; Kinase; Nucleotide-binding; Nucleus;
KW   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
 
 
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