TRI1_YEAST
ID TRI1_YEAST Reviewed; 226 AA.
AC Q05024; D6W059;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Protein TRI1;
GN Name=TRI1; OrderedLocusNames=YMR233W; ORFNames=YM9959.15;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 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 [4]
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 [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 SUMOYLATION AT LYS-201 AND LYS-215, AND MUTAGENESIS OF LYS-201 AND LYS-215.
RX PubMed=17603101; DOI=10.1534/genetics.107.074708;
RA Chen X.L., Silver H.R., Xiong L., Belichenko I., Adegite C., Johnson E.S.;
RT "Topoisomerase I-dependent viability loss in saccharomyces cerevisiae
RT mutants defective in both SUMO conjugation and DNA repair.";
RL Genetics 177:17-30(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, 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 -!- FUNCTION: May be involved in transcription regulation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2360 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z49939; CAA90204.1; -; Genomic_DNA.
DR EMBL; AY557975; AAS56301.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10133.1; -; Genomic_DNA.
DR PIR; S57600; S57600.
DR RefSeq; NP_013960.1; NM_001182740.1.
DR AlphaFoldDB; Q05024; -.
DR SMR; Q05024; -.
DR BioGRID; 35411; 114.
DR DIP; DIP-1551N; -.
DR IntAct; Q05024; 11.
DR MINT; Q05024; -.
DR STRING; 4932.YMR233W; -.
DR iPTMnet; Q05024; -.
DR MaxQB; Q05024; -.
DR PaxDb; Q05024; -.
DR PRIDE; Q05024; -.
DR EnsemblFungi; YMR233W_mRNA; YMR233W; YMR233W.
DR GeneID; 855273; -.
DR KEGG; sce:YMR233W; -.
DR SGD; S000004846; TRI1.
DR VEuPathDB; FungiDB:YMR233W; -.
DR eggNOG; KOG1946; Eukaryota.
DR GeneTree; ENSGT00940000176588; -.
DR HOGENOM; CLU_046065_1_0_1; -.
DR InParanoid; Q05024; -.
DR OMA; KVWQYIR; -.
DR BioCyc; YEAST:G3O-32914-MON; -.
DR Reactome; R-SCE-198323; AKT phosphorylates targets in the cytosol.
DR Reactome; R-SCE-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-SCE-5689880; Ub-specific processing proteases.
DR Reactome; R-SCE-6804757; Regulation of TP53 Degradation.
DR Reactome; R-SCE-69541; Stabilization of p53.
DR PRO; PR:Q05024; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q05024; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000500; C:RNA polymerase I upstream activating factor complex; IBA:GO_Central.
DR GO; GO:0001165; F:RNA polymerase I cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IBA:GO_Central.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; IBA:GO_Central.
DR Gene3D; 1.10.245.10; -; 1.
DR InterPro; IPR014876; DEK_C.
DR InterPro; IPR019835; SWIB_domain.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR Pfam; PF08766; DEK_C; 1.
DR Pfam; PF02201; SWIB; 1.
DR SMART; SM00151; SWIB; 1.
DR SUPFAM; SSF47592; SSF47592; 1.
DR PROSITE; PS51998; DEK_C; 1.
DR PROSITE; PS51925; SWIB_MDM2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..226
FT /note="Protein TRI1"
FT /id="PRO_0000203334"
FT DOMAIN 1..56
FT /note="DEK-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01342"
FT DOMAIN 119..195
FT /note="SWIB/MDM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01273"
FT REGION 83..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT CROSSLNK 215
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT MUTAGEN 201
FT /note="K->R: Impairs sumoylation; when associated with R-
FT 215."
FT /evidence="ECO:0000269|PubMed:17603101"
FT MUTAGEN 215
FT /note="K->R: Impairs sumoylation; when associated with R-
FT 201."
FT /evidence="ECO:0000269|PubMed:17603101"
SQ SEQUENCE 226 AA; 26471 MW; BFE31F963D6B05EC CRC64;
MADINKYIPM VDAILSVSNP DEISPKRVRK ALQILYSVNL DSQRKLINEL ILERFGDIQE
NPRVLIPKND LISRDQELSL RLQKEEERPL RSTRKRKGKS ESKSKRKKKK NDSPDSNSIS
VRKVLLSAPL QKFLGSEELP RTQVVKMIWQ YIKEHDLQNP KDRREILCDE KMEPIFGKKM
TMFSMNKLLT KHLFNPDEIV KHEEEQKQTP EKEIKLENES LPNLSG
