IPMK_YEAST
ID IPMK_YEAST Reviewed; 355 AA.
AC P07250; D6VSF5; E9P8S7;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Inositol polyphosphate multikinase {ECO:0000305};
DE Short=IPMK;
DE EC=2.7.1.127;
DE EC=2.7.1.151;
DE AltName: Full=Arginine metabolism regulation protein III;
DE AltName: Full=GLE1 synthetic lethal protein 3 {ECO:0000303|PubMed:10390371};
DE AltName: Full=Inositol polyphosphate kinase 2 {ECO:0000303|PubMed:10720331};
GN Name=ARG82;
GN Synonyms=ARGR3, GSL3 {ECO:0000303|PubMed:10390371},
GN IPK2 {ECO:0000303|PubMed:10720331}; OrderedLocusNames=YDR173C;
GN ORFNames=YD9395.06C;
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], AND FUNCTION.
RX PubMed=3298999; DOI=10.1007/bf00331501;
RA Dubois E., Bercy J., Messenguy F.;
RT "Characterization of two genes, ARGRI and ARGRIII required for specific
RT regulation of arginine metabolism in yeast.";
RL Mol. Gen. Genet. 207:142-148(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=3311884; DOI=10.1016/0378-1119(87)90287-3;
RA Bercy J., Dubois E., Messenguy F.;
RT "Regulation of arginine metabolism in Saccharomyces cerevisiae: expression
RT of the three ARGR regulatory genes and cellular localization of their
RT products.";
RL Gene 55:277-285(1987).
RN [6]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7945194; DOI=10.1042/bj3020709;
RA Estevez F., Pulford D., Stark M.J., Carter A.N., Downes C.P.;
RT "Inositol trisphosphate metabolism in Saccharomyces cerevisiae:
RT identification, purification and properties of inositol 1,4,5-trisphosphate
RT 6-kinase.";
RL Biochem. J. 302:709-716(1994).
RN [7]
RP FUNCTION.
RX PubMed=8043104; DOI=10.1007/bf00301067;
RA Dubois E., Messenguy F.;
RT "Pleiotropic function of ArgRIIIp (Arg82p), one of the regulators of
RT arginine metabolism in Saccharomyces cerevisiae. Role in expression of
RT cell-type-specific genes.";
RL Mol. Gen. Genet. 243:315-324(1994).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=10574768; DOI=10.1016/s0960-9822(00)80055-x;
RA Saiardi A., Erdjument-Bromage H., Snowman A.M., Tempst P., Snyder S.H.;
RT "Synthesis of diphosphoinositol pentakisphosphate by a newly identified
RT family of higher inositol polyphosphate kinases.";
RL Curr. Biol. 9:1323-1326(1999).
RN [9]
RP FUNCTION.
RX PubMed=10390371; DOI=10.1126/science.285.5424.96;
RA York J.D., Odom A.R., Murphy R., Ives E.B., Wente S.R.;
RT "A phospholipase C-dependent inositol polyphosphate kinase pathway required
RT for efficient messenger RNA export.";
RL Science 285:96-100(1999).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=10683435; DOI=10.1016/s0014-5793(00)01194-7;
RA Saiardi A., Caffrey J.J., Snyder S.H., Shears S.B.;
RT "Inositol polyphosphate multikinase (ArgRIII) determines nuclear mRNA
RT export in Saccharomyces cerevisiae.";
RL FEBS Lett. 468:28-32(2000).
RN [11]
RP FUNCTION.
RX PubMed=11119723; DOI=10.1016/s0014-5793(00)02318-8;
RA Dubois E., Dewaste V., Erneux C., Messenguy F.;
RT "Inositol polyphosphate kinase activity of Arg82/ArgRIII is not required
RT for the regulation of the arginine metabolism in yeast.";
RL FEBS Lett. 486:300-304(2000).
RN [12]
RP INTERACTION WITH ARG80 AND MCM1, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10632874; DOI=10.1046/j.1365-2958.2000.01665.x;
RA El Bakkoury M., Dubois E., Messenguy F.;
RT "Recruitment of the yeast MADS-box proteins, ArgRI and Mcm1 by the
RT pleiotropic factor ArgRIII is required for their stability.";
RL Mol. Microbiol. 35:15-31(2000).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=10720331; DOI=10.1126/science.287.5460.2026;
RA Odom A.R., Stahlberg A., Wente S.R., York J.D.;
RT "A role for nuclear inositol 1,4,5-trisphosphate kinase in transcriptional
RT control.";
RL Science 287:2026-2029(2000).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11311242; DOI=10.1016/s0014-5793(01)02351-1;
RA Zhang T., Caffrey J.J., Shears S.B.;
RT "The transcriptional regulator, Arg82, is a hybrid kinase with both
RT monophosphoinositol and diphosphoinositol polyphosphate synthase
RT activity.";
RL FEBS Lett. 494:208-212(2001).
RN [15]
RP FUNCTION, AND MUTAGENESIS OF ASP-131 AND 257-SER--LEU-260.
RX PubMed=12828642; DOI=10.1046/j.1365-2958.2003.03562.x;
RA El Alami M., Messenguy F., Scherens B., Dubois E.;
RT "Arg82p is a bifunctional protein whose inositol polyphosphate kinase
RT activity is essential for nitrogen and PHO gene expression but not for
RT Mcm1p chaperoning in yeast.";
RL Mol. Microbiol. 49:457-468(2003).
RN [16]
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 [17]
RP FUNCTION.
RX PubMed=12434012; DOI=10.1126/science.1078062;
RA Steger D.J., Haswell E.S., Miller A.L., Wente S.R., O'Shea E.K.;
RT "Regulation of chromatin remodeling by inositol polyphosphates.";
RL Science 299:114-116(2003).
RN [18]
RP FUNCTION.
RX PubMed=15944147; DOI=10.1074/jbc.m505089200;
RA Seeds A.M., Bastidas R.J., York J.D.;
RT "Molecular definition of a novel inositol polyphosphate metabolic pathway
RT initiated by inositol 1,4,5-trisphosphate 3-kinase activity in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 280:27654-27661(2005).
RN [19]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF LYS-133.
RX PubMed=16123124; DOI=10.1073/pnas.0506184102;
RA Resnick A.C., Snowman A.M., Kang B.N., Hurt K.J., Snyder S.H., Saiardi A.;
RT "Inositol polyphosphate multikinase is a nuclear PI3-kinase with
RT transcriptional regulatory activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12783-12788(2005).
RN [20]
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, 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 [22]
RP FUNCTION.
RX PubMed=22992733; DOI=10.1074/jbc.m112.384255;
RA Bosch D., Saiardi A.;
RT "Arginine transcriptional response does not require inositol phosphate
RT synthesis.";
RL J. Biol. Chem. 287:38347-38355(2012).
RN [23]
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).
RN [24]
RP FUNCTION, AND MUTAGENESIS OF ASP-131 AND LYS-133.
RX PubMed=28923943; DOI=10.1073/pnas.1714361114;
RA Wickner R.B., Kelly A.C., Bezsonov E.E., Edskes H.K.;
RT "[PSI+] prion propagation is controlled by inositol polyphosphates.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E8402-E8410(2017).
RN [25] {ECO:0007744|PDB:2IEW, ECO:0007744|PDB:2IF8}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CALCIUM AND ADP.
RX PubMed=17050532; DOI=10.1074/jbc.m606883200;
RA Holmes W., Jogl G.;
RT "Crystal structure of inositol phosphate multikinase 2 and implications for
RT substrate specificity.";
RL J. Biol. Chem. 281:38109-38116(2006).
CC -!- FUNCTION: Inositol phosphate kinase with both monophosphoinositol and
CC diphosphoinositol polyphosphate synthase activities. Able to
CC phosphorylate inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) on both the
CC carbon-3 and carbon-6 positions to synthesize inositol 1,3,4,5-
CC tetrakisphosphate (Ins(1,3,4,5)P4) and inositol 1,4,5,6-
CC tetrakisphosphate (Ins(1,4,5,6)P4), and then to subsequently
CC phosphorylate and convert either isomer of InsP4 to inositol 1,3,4,5,6-
CC pentakisphosphate (Ins(1,3,4,5,6)P5) (PubMed:10574768, PubMed:10683435,
CC PubMed:11311242). Its predominant in vivo catalytic function is to
CC convert Ins(1,4,5)P3 to Ins(1,4,5,6)P4 to Ins(1,3,4,5,6)P5 via 6- and
CC 3-kinase activities (PubMed:15944147). It can also use Ins(1,3,4,5,6)P5
CC as a substrate and act as a diphosphoinositol polyphosphate synthase to
CC generate two different isomers of PP-InsP4 (PubMed:11311242). Has also
CC a role in transcription regulation. Forms a complex with ARG80, ARG81
CC and MCM1 (ArgR-MCM1), which coordinates the expression of arginine
CC anabolic and catabolic genes in response to arginine. Recruits ARG80
CC and MCM21 to stabilize them (PubMed:3298999, PubMed:8043104,
CC PubMed:10632874). Neither the kinase activity nor inositol phosphates
CC are required for the formation of ArgR-MCM1 transciptional complexes on
CC DNA promoter elements and the control of arginine metabolism
CC (PubMed:11119723, PubMed:10720331, PubMed:12828642, PubMed:22992733).
CC In contrast, only the catalytic activity is required for PHO gene
CC repression by phosphate and for NCR gene activation in response to
CC nitrogen availability, indicating a role for inositol pyrophosphates in
CC these controls (PubMed:12828642). Inositol polyphosphates may be
CC involved in the regulation of chromatin remodeling of transcription
CC (PubMed:12434012). Regulates nuclear mRNA export via inositol phosphate
CC metabolism (PubMed:10390371, PubMed:10683435). Also has lipid kinase
CC activity, transforming the lipid inositol phosphatidylinositol 4,5-
CC bisphosphate (PI(4,5)P2) into phosphatidylinositol 3,4,5-trisphosphate
CC (PI(3,4,5)P3) in the nucleus (PubMed:16123124). Its kinase activity is
CC necessary for the propagation of most [PSI+] prion variants
CC (PubMed:28923943). {ECO:0000269|PubMed:10390371,
CC ECO:0000269|PubMed:10574768, ECO:0000269|PubMed:10632874,
CC ECO:0000269|PubMed:10683435, ECO:0000269|PubMed:10720331,
CC ECO:0000269|PubMed:11119723, ECO:0000269|PubMed:11311242,
CC ECO:0000269|PubMed:12434012, ECO:0000269|PubMed:12828642,
CC ECO:0000269|PubMed:15944147, ECO:0000269|PubMed:16123124,
CC ECO:0000269|PubMed:22992733, ECO:0000269|PubMed:28923943,
CC ECO:0000269|PubMed:3298999, ECO:0000269|PubMed:8043104}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,4,5-trisphosphate + 2 ATP = 1D-myo-inositol
CC 1,3,4,5,6-pentakisphosphate + 2 ADP + 2 H(+); Xref=Rhea:RHEA:32359,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57733,
CC ChEBI:CHEBI:203600, ChEBI:CHEBI:456216; EC=2.7.1.151;
CC Evidence={ECO:0000269|PubMed:10574768};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,4,5-trisphosphate + ATP = 1D-myo-inositol
CC 1,4,5,6-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:17717,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57627,
CC ChEBI:CHEBI:203600, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:10683435, ECO:0000269|PubMed:10720331,
CC ECO:0000269|PubMed:7945194};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17718;
CC Evidence={ECO:0000305|PubMed:10683435, ECO:0000305|PubMed:10720331,
CC ECO:0000305|PubMed:7945194};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,4,5-trisphosphate + ATP = 1D-myo-inositol
CC 1,3,4,5-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:11020,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57895,
CC ChEBI:CHEBI:203600, ChEBI:CHEBI:456216; EC=2.7.1.127;
CC Evidence={ECO:0000269|PubMed:10683435};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11021;
CC Evidence={ECO:0000305|PubMed:10683435};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,4,5,6-tetrakisphosphate + ATP = 1D-myo-
CC inositol 1,3,4,5,6-pentakisphosphate + ADP + H(+);
CC Xref=Rhea:RHEA:11856, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57627, ChEBI:CHEBI:57733, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:10683435, ECO:0000269|PubMed:10720331};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11857;
CC Evidence={ECO:0000305|PubMed:10683435, ECO:0000305|PubMed:10720331};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-
CC bisphosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-3,4,5-trisphosphate) + ADP + H(+); Xref=Rhea:RHEA:21292,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57836,
CC ChEBI:CHEBI:58456, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:16123124};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21293;
CC Evidence={ECO:0000269|PubMed:16123124};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:17050532};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15.3 uM for 1D-myo-inositol 1,4,5-trisphosphate
CC {ECO:0000269|PubMed:11311242};
CC KM=7.1 uM for 1D-myo-inositol 1,4,5-trisphosphate
CC {ECO:0000269|PubMed:7945194};
CC KM=62 uM for 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
CC {ECO:0000269|PubMed:11311242};
CC KM=30 uM for phosphatidylinositol 4,5-bisphosphate
CC {ECO:0000269|PubMed:11311242};
CC KM=2.1 mM for ATP {ECO:0000269|PubMed:7945194};
CC Vmax=6272 nmol/min/mg enzyme for 1D-myo-inositol 1,4,5-trisphosphate
CC {ECO:0000269|PubMed:11311242};
CC Vmax=4.9 nmol/min/mg enzyme for 1D-myo-inositol 1,3,4,5,6-
CC pentakisphosphate {ECO:0000269|PubMed:11311242};
CC -!- SUBUNIT: Interacts with ARG80 and MCM1. {ECO:0000269|PubMed:10632874,
CC ECO:0000269|PubMed:17050532}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10632874,
CC ECO:0000269|PubMed:16123124, ECO:0000269|PubMed:3311884}.
CC -!- DISRUPTION PHENOTYPE: Impairs nuclear mRNA export, slows cell growth,
CC increases cellular InsP3 170-fold and decreases InsP6 100-fold.
CC {ECO:0000269|PubMed:10683435, ECO:0000269|PubMed:10720331}.
CC -!- MISCELLANEOUS: The expression of this protein is not effected by the
CC presence of arginine. {ECO:0000269|PubMed:3311884}.
CC -!- MISCELLANEOUS: Present with 2720 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the inositol phosphokinase (IPK) family.
CC {ECO:0000305}.
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DR EMBL; X05328; CAA28945.1; -; Genomic_DNA.
DR EMBL; Z46727; CAA86678.1; -; Genomic_DNA.
DR EMBL; AY557696; AAS56022.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12015.1; -; Genomic_DNA.
DR PIR; S05823; RGBYR3.
DR RefSeq; NP_010458.3; NM_001180480.3.
DR PDB; 2IEW; X-ray; 2.00 A; A/B=1-355.
DR PDB; 2IF8; X-ray; 2.40 A; A/B=1-355.
DR PDBsum; 2IEW; -.
DR PDBsum; 2IF8; -.
DR AlphaFoldDB; P07250; -.
DR SMR; P07250; -.
DR BioGRID; 32226; 45.
DR ComplexPortal; CPX-1152; ARGR-MCM1 transcription regulation complex.
DR DIP; DIP-1242N; -.
DR IntAct; P07250; 3.
DR MINT; P07250; -.
DR STRING; 4932.YDR173C; -.
DR SwissLipids; SLP:000000958; -.
DR MoonProt; P07250; -.
DR iPTMnet; P07250; -.
DR MaxQB; P07250; -.
DR PaxDb; P07250; -.
DR PRIDE; P07250; -.
DR EnsemblFungi; YDR173C_mRNA; YDR173C; YDR173C.
DR GeneID; 851753; -.
DR KEGG; sce:YDR173C; -.
DR SGD; S000002580; ARG82.
DR VEuPathDB; FungiDB:YDR173C; -.
DR eggNOG; KOG1620; Eukaryota.
DR GeneTree; ENSGT00940000167316; -.
DR HOGENOM; CLU_042569_3_0_1; -.
DR InParanoid; P07250; -.
DR OMA; RMYSASI; -.
DR BioCyc; MetaCyc:MON3O-64; -.
DR BioCyc; YEAST:MON3O-64; -.
DR Reactome; R-SCE-1855167; Synthesis of pyrophosphates in the cytosol.
DR Reactome; R-SCE-1855191; Synthesis of IPs in the nucleus.
DR SABIO-RK; P07250; -.
DR EvolutionaryTrace; P07250; -.
DR PRO; PR:P07250; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P07250; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IC:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000824; F:inositol tetrakisphosphate 3-kinase activity; IDA:SGD.
DR GO; GO:0000825; F:inositol tetrakisphosphate 6-kinase activity; IDA:SGD.
DR GO; GO:0051765; F:inositol tetrakisphosphate kinase activity; IBA:GO_Central.
DR GO; GO:0000827; F:inositol-1,3,4,5,6-pentakisphosphate kinase activity; IDA:SGD.
DR GO; GO:0008440; F:inositol-1,4,5-trisphosphate 3-kinase activity; IMP:SGD.
DR GO; GO:0000823; F:inositol-1,4,5-trisphosphate 6-kinase activity; IDA:SGD.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035004; F:phosphatidylinositol 3-kinase activity; IDA:SGD.
DR GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; IEA:RHEA.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IMP:SGD.
DR GO; GO:0006525; P:arginine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0032958; P:inositol phosphate biosynthetic process; IDA:SGD.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IDA:SGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0050821; P:protein stabilization; IMP:SGD.
DR GO; GO:0000821; P:regulation of arginine metabolic process; IMP:SGD.
DR Gene3D; 3.30.470.160; -; 1.
DR InterPro; IPR005522; IPK.
DR InterPro; IPR038286; IPK_sf.
DR PANTHER; PTHR12400; PTHR12400; 1.
DR Pfam; PF03770; IPK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Arginine metabolism; ATP-binding; Calcium;
KW Kinase; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Transferase.
FT CHAIN 1..355
FT /note="Inositol polyphosphate multikinase"
FT /id="PRO_0000066873"
FT REGION 284..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..304
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 31
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17050532,
FT ECO:0007744|PDB:2IF8"
FT BINDING 118..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17050532,
FT ECO:0007744|PDB:2IF8"
FT BINDING 127..135
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17050532,
FT ECO:0007744|PDB:2IF8"
FT BINDING 271
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17050532,
FT ECO:0007744|PDB:2IEW, ECO:0007744|PDB:2IF8"
FT BINDING 274
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17050532,
FT ECO:0007744|PDB:2IEW"
FT BINDING 325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17050532,
FT ECO:0007744|PDB:2IF8"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:17050532,
FT ECO:0007744|PDB:2IEW, ECO:0007744|PDB:2IF8"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 131
FT /note="D->A: Abolishes catalytic activity, but preserves
FT its nonkinase transcription regulation functions."
FT /evidence="ECO:0000269|PubMed:12828642,
FT ECO:0000269|PubMed:28923943"
FT MUTAGEN 133
FT /note="K->A: Abolishes catalytic activity, but preserves
FT its nonkinase transcription regulation functions."
FT /evidence="ECO:0000269|PubMed:16123124,
FT ECO:0000269|PubMed:28923943"
FT MUTAGEN 257..260
FT /note="SSLL->AAAA: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:12828642"
FT CONFLICT 109
FT /note="E -> K (in Ref. 4; AAS56022)"
FT /evidence="ECO:0000305"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:2IEW"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:2IEW"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:2IEW"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:2IEW"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:2IEW"
FT TURN 120..123
FT /evidence="ECO:0007829|PDB:2IEW"
FT STRAND 125..134
FT /evidence="ECO:0007829|PDB:2IEW"
FT HELIX 145..157
FT /evidence="ECO:0007829|PDB:2IEW"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:2IEW"
FT STRAND 164..173
FT /evidence="ECO:0007829|PDB:2IEW"
FT HELIX 176..181
FT /evidence="ECO:0007829|PDB:2IEW"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:2IEW"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:2IEW"
FT HELIX 200..205
FT /evidence="ECO:0007829|PDB:2IEW"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:2IEW"
FT HELIX 211..219
FT /evidence="ECO:0007829|PDB:2IEW"
FT HELIX 226..249
FT /evidence="ECO:0007829|PDB:2IEW"
FT STRAND 252..264
FT /evidence="ECO:0007829|PDB:2IEW"
FT HELIX 267..272
FT /evidence="ECO:0007829|PDB:2IEW"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:2IEW"
FT STRAND 319..324
FT /evidence="ECO:0007829|PDB:2IEW"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:2IEW"
FT HELIX 339..355
FT /evidence="ECO:0007829|PDB:2IEW"
SQ SEQUENCE 355 AA; 40353 MW; F858B39E3C54E6BF CRC64;
MDTVNNYRVL EHKAAGHDGT LTDGDGLLIF KPAFPQELEF YKAIQVRDVS RRKSSADGDA
PLCSWMPTYL GVLNEGAKIE QSGDAALLKI DERLSDSTDN LDSIPVKSEK SKQYLVLENL
LYGFSKPNIL DIKLGKTLYD SKASLEKRER MKRVSETTTS GSLGFRICGM KIQKNPSVLN
QLSLEYYEEE ADSDYIFINK LYGRSRTDQN VSDAIELYFN NPHLSDARKH QLKKTFLKRL
QLFYNTMLEE EVRMISSSLL FIYEGDPERW ELLNDVDKLM RDDFIDDDDD DDDNDDDDDD
DAEGSSEGPK DKKTTGSLSS MSLIDFAHSE ITPGKGYDEN VIEGVETLLD IFMKF
