SRL2_YEAST
ID SRL2_YEAST Reviewed; 392 AA.
AC Q12020; D6VY82;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein SRL2;
DE AltName: Full=Suppressor of RAD53 null lethality protein 2;
GN Name=SRL2; OrderedLocusNames=YLR082C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
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 [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-139, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, 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).
CC -!- INTERACTION:
CC Q12020; P39014: MET30; NbExp=3; IntAct=EBI-38714, EBI-11507;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 538 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z73254; CAA97641.1; -; Genomic_DNA.
DR EMBL; U53880; AAB67586.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09398.1; -; Genomic_DNA.
DR PIR; S64914; S64914.
DR RefSeq; NP_013183.1; NM_001181969.1.
DR AlphaFoldDB; Q12020; -.
DR BioGRID; 31355; 108.
DR DIP; DIP-1442N; -.
DR IntAct; Q12020; 9.
DR MINT; Q12020; -.
DR STRING; 4932.YLR082C; -.
DR iPTMnet; Q12020; -.
DR MaxQB; Q12020; -.
DR PaxDb; Q12020; -.
DR PRIDE; Q12020; -.
DR EnsemblFungi; YLR082C_mRNA; YLR082C; YLR082C.
DR GeneID; 850771; -.
DR KEGG; sce:YLR082C; -.
DR SGD; S000004072; SRL2.
DR VEuPathDB; FungiDB:YLR082C; -.
DR HOGENOM; CLU_071668_0_0_1; -.
DR OMA; STHTICF; -.
DR BioCyc; YEAST:G3O-32233-MON; -.
DR PRO; PR:Q12020; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12020; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IMP:SGD.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..392
FT /note="Protein SRL2"
FT /id="PRO_0000270577"
FT REGION 18..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 392 AA; 45140 MW; A39CD3D2E0F9BBF3 CRC64;
MSNFKNFTLN SFEDYYGKPS ETPKMEEEKL EVTNVNASSS KKVHKSKKST SKYDQKNVFR
NSMTGIAQIL PTKPVKIIEQ NIDFANPKSF DLLQSTHTIC FNKRINTTNT KLNVETHTSS
DIDNDILHVG APTDLGGNSN DEAETRQLRK FRWSNNKEKS LCEKLTVIYW ALLLHTTKRA
SKRRPILCHQ MIAEFFNRVY KEKSRVPITS RYIRDNLVAW VTQGKELHEK GWVGDAKTGD
LQEQFNIATV KLYESAEDGR LSIGKDKPFR EENTGSDSLV RAEEDSTAVT NENGHISSEK
NLKKDRRESI RNQILTLDLN DEDFFQNVMK VLSAIDEPEL RQYVIVISEL VSMEMDDGKT
VREKLRDVEL NINRLQVDIK EIKEMLVTLI NK