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SRP40_YEAST
ID   SRP40_YEAST             Reviewed;         406 AA.
AC   P32583; D6VXF2;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Suppressor protein SRP40;
GN   Name=SRP40; OrderedLocusNames=YKR092C; ORFNames=YKR412A;
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 28383 / FL100 / VTT C-80102;
RX   PubMed=8516295; DOI=10.1073/pnas.90.12.5524;
RA   Lalo D., Carles C., Sentenac A., Thuriaux P.;
RT   "Interactions between three common subunits of yeast RNA polymerases I and
RT   III.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:5524-5528(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8154186; DOI=10.1002/yea.320091209;
RA   Bou G., Esteban P.F., Baladron V., Gonzalez G.A., Cantalejo J.G.,
RA   Remacha M.A., Jimenez A., del Rey F., Ballesta J.P.G., Revuelta J.L.;
RT   "The complete sequence of a 15,820 bp segment of Saccharomyces cerevisiae
RT   chromosome XI contains the UBI2 and MPL1 genes and three new open reading
RT   frames.";
RL   Yeast 9:1349-1354(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-289, 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-394, 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND IDENTIFICATION BY
RP   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 THR-289; SER-293 AND SER-394, AND
RP   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).
RN   [10]
RP   PYROPHOSPHORYLATION.
RX   PubMed=15604408; DOI=10.1126/science.1103344;
RA   Saiardi A., Bhandari R., Resnick A.C., Snowman A.M., Snyder S.H.;
RT   "Phosphorylation of proteins by inositol pyrophosphates.";
RL   Science 306:2101-2105(2004).
RN   [11]
RP   PYROPHOSPHORYLATION.
RX   PubMed=17873058; DOI=10.1073/pnas.0707338104;
RA   Bhandari R., Saiardi A., Ahmadibeni Y., Snowman A.M., Resnick A.C.,
RA   Kristiansen T.Z., Molina H., Pandey A., Werner J.K. Jr., Juluri K.R.,
RA   Xu Y., Prestwich G.D., Parang K., Snyder S.H.;
RT   "Protein pyrophosphorylation by inositol pyrophosphates is a
RT   posttranslational event.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:15305-15310(2007).
CC   -!- FUNCTION: Not known; weak suppressor of a mutant of the subunit AC40 of
CC       DNA dependent RNA polymerase I and III.
CC   -!- PTM: Pyrophosphorylated by 5-diphosphoinositol pentakisphosphate (5-
CC       IP7) (PubMed:15604408). Serine pyrophosphorylation is achieved by
CC       Mg(2+)-dependent, but enzyme independent transfer of a beta-phosphate
CC       from a inositol pyrophosphate to a pre-phosphorylated serine residue
CC       (PubMed:15604408, PubMed:17873058). {ECO:0000269|PubMed:15604408,
CC       ECO:0000269|PubMed:17873058}.
CC   -!- MISCELLANEOUS: Present with 12900 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
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DR   EMBL; L11275; AAA35091.1; -; Genomic_DNA.
DR   EMBL; X73541; CAA51946.1; -; Genomic_DNA.
DR   EMBL; Z28317; CAA82171.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA09242.1; -; Genomic_DNA.
DR   PIR; S38170; S38170.
DR   RefSeq; NP_013018.3; NM_001179882.3.
DR   AlphaFoldDB; P32583; -.
DR   BioGRID; 34223; 254.
DR   DIP; DIP-2115N; -.
DR   IntAct; P32583; 11.
DR   MINT; P32583; -.
DR   STRING; 4932.YKR092C; -.
DR   iPTMnet; P32583; -.
DR   MaxQB; P32583; -.
DR   PaxDb; P32583; -.
DR   PRIDE; P32583; -.
DR   EnsemblFungi; YKR092C_mRNA; YKR092C; YKR092C.
DR   GeneID; 853967; -.
DR   KEGG; sce:YKR092C; -.
DR   SGD; S000001800; SRP40.
DR   VEuPathDB; FungiDB:YKR092C; -.
DR   eggNOG; KOG2992; Eukaryota.
DR   HOGENOM; CLU_781095_0_0_1; -.
DR   InParanoid; P32583; -.
DR   OMA; ENNSGME; -.
DR   BioCyc; YEAST:G3O-32055-MON; -.
DR   PRO; PR:P32583; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P32583; protein.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0006913; P:nucleocytoplasmic transport; ISS:SGD.
DR   InterPro; IPR007718; Srp40_C.
DR   Pfam; PF05022; SRP40_C; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..406
FT                   /note="Suppressor protein SRP40"
FT                   /id="PRO_0000072192"
FT   REGION          1..335
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..278
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        279..298
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        299..320
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         133
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         289
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         293
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         394
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   CONFLICT        400
FT                   /note="G -> N (in Ref. 1; AAA35091)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   406 AA;  41015 MW;  8EA007695AF4BA1D CRC64;
     MASKKIKVDE VPKLSVKEKE IEEKSSSSSS SSSSSSSSSS SSSSSSSSSG ESSSSSSSSS
     SSSSSDSSDS SDSESSSSSS SSSSSSSSSS DSESSSESDS SSSGSSSSSS SSSDESSSES
     ESEDETKKRA RESDNEDAKE TKKAKTEPES SSSSESSSSG SSSSSESESG SESDSDSSSS
     SSSSSDSESD SESDSQSSSS SSSSDSSSDS DSSSSDSSSD SDSSSSSSSS SSDSDSDSDS
     SSDSDSSGSS DSSSSSDSSS DESTSSDSSD SDSDSDSGSS SELETKEATA DESKAEETPA
     SSNESTPSAS SSSSANKLNI PAGTDEIKEG QRKHFSRVDR SKINFEAWEL TDNTYKGAAG
     TWGEKANEKL GRVRGKDFTK NKNKMKRGSY RGGSITLESG SYKFQD
 
 
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