IDS2_YEAST
ID IDS2_YEAST Reviewed; 469 AA.
AC P46958; D6VW39;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=IME2-dependent-signaling protein;
GN Name=IDS2; OrderedLocusNames=YJL146W; ORFNames=J0642;
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=SK1;
RX PubMed=7565676; DOI=10.1128/mcb.15.10.5279;
RA Sia R.A., Mitchell A.P.;
RT "Stimulation of later functions of the yeast meiotic protein kinase Ime2p
RT by the IDS2 gene product.";
RL Mol. Cell. Biol. 15:5279-5287(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8813765;
RX DOI=10.1002/(sici)1097-0061(19960630)12:8<787::aid-yea954>3.0.co;2-4;
RA Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D.;
RT "Sequence analysis of a 40.7 kb segment from the left arm of yeast
RT chromosome X reveals 14 known genes and 13 new open reading frames
RT including homologues of genes clustered on the right arm of chromosome
RT XI.";
RL Yeast 12:787-797(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
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 [5]
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 [6]
RP IDENTIFICATION BY 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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13; SER-130 AND SER-136, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-27; SER-39; SER-122;
RP SER-130; SER-136; SER-147 AND SER-148, AND IDENTIFICATION BY MASS
RP 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 [10]
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).
CC -!- FUNCTION: Seems to act indirectly to modify IME2 activity, thus
CC permitting IME2 to carry out later meiotic functions.
CC -!- MISCELLANEOUS: Present with 1850 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U21326; AAA87184.1; -; Genomic_DNA.
DR EMBL; Z49421; CAA89441.1; -; Genomic_DNA.
DR EMBL; X87371; CAA60809.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08655.1; -; Genomic_DNA.
DR PIR; S55167; S55167.
DR RefSeq; NP_012389.1; NM_001181579.1.
DR AlphaFoldDB; P46958; -.
DR BioGRID; 33612; 108.
DR DIP; DIP-902N; -.
DR IntAct; P46958; 5.
DR MINT; P46958; -.
DR STRING; 4932.YJL146W; -.
DR iPTMnet; P46958; -.
DR MaxQB; P46958; -.
DR PaxDb; P46958; -.
DR PRIDE; P46958; -.
DR EnsemblFungi; YJL146W_mRNA; YJL146W; YJL146W.
DR GeneID; 853295; -.
DR KEGG; sce:YJL146W; -.
DR SGD; S000003682; IDS2.
DR VEuPathDB; FungiDB:YJL146W; -.
DR eggNOG; ENOG502R2Z2; Eukaryota.
DR HOGENOM; CLU_034560_0_0_1; -.
DR InParanoid; P46958; -.
DR OMA; CIREYMT; -.
DR BioCyc; YEAST:G3O-31590-MON; -.
DR Reactome; R-SCE-3322077; Glycogen synthesis.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-70221; Glycogen breakdown (glycogenolysis).
DR PRO; PR:P46958; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P46958; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:SGD.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Acetylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..469
FT /note="IME2-dependent-signaling protein"
FT /id="PRO_0000084152"
FT REGION 22..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 13
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 268
FT /note="G -> GF (in Ref. 1; AAA87184)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="S -> R (in Ref. 1; AAA87184)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="R -> W (in Ref. 1; AAA87184)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 53216 MW; 1E3E22698E6D946F CRC64;
MDNQQESISE DITGDLAAAV RKSWSESQDN PLLLNFNNSP IGTPTDRYSP EPATMMEGNA
MNLSSLARGS TQQQQRLYGS SQTREKSDQQ QQDYQLFKHH YSLGQETRES VSDILNDLTL
GSPEPSERAS PIRQPSVDVP PLTTRRSSIQ DVQWIRHLLN PRSSFSGASS NEPTNSPGDF
LNQSRAWITI LHDSSAESLQ AVIVLAESLK NVNSQYNLWV LHSSEVNAFQ LAQVGIKTLI
IDEYINLFMN FGTGSGFSAS SQSTETKGEL NFKWCKLFLF FSLIDRFELI CYLSPTCLVL
QNIDELLEST EVSDEIDNET CVLLSNKVNY INEDLVSVNQ DQSSAENYDD DPQIIILKPN
RAVAMCIKEY FTIYGNDFEG ESKRSMFHQM NDLQIMKALF GDKWSYIDSV GYCAVPIASV
PANRLNYKII EFKILKPWER QNYIAAGQHR ESIMNKWLDL WRDFLNQAN
