EUC1_YEAST
ID EUC1_YEAST Reviewed; 462 AA.
AC Q04461; D6VZT4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Transcription factor-like protein EUC1 {ECO:0000303|PubMed:31015336};
DE AltName: Full=Enriches ubiquitin on chromatin protein 1 {ECO:0000303|PubMed:31015336};
GN Name=EUC1 {ECO:0000303|PubMed:31015336}; OrderedLocusNames=YMR111C;
GN ORFNames=YM9718.10C;
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 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-23; SER-237; SER-249
RP AND THR-254, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, SUBUNIT, INTERACTION WITH
RP SLX5, DISRUPTION PHENOTYPE, SUMOYLATION AT LYS-231, MUTAGENESIS OF LYS-231;
RP TRP-333 AND ARG-334, AND DOMAIN.
RX PubMed=31015336; DOI=10.15252/embj.2018100368;
RA Hoepfler M., Kern M.J., Straub T., Prytuliak R., Habermann B.H.,
RA Pfander B., Jentsch S.;
RT "Slx5/Slx8-dependent ubiquitin hotspots on chromatin contribute to stress
RT tolerance.";
RL EMBO J. 38:0-0(2019).
CC -!- FUNCTION: Transcription factor-like protein that binds to specific DNA
CC motifs called ub-HS-motif associated with several locations where
CC proteins other than histone H2B are ubiquitinated (ub-hotspots)
CC (PubMed:31015336). Ubiquitination at these sites depends on the SUMO-
CC targeted ubiquitin ligase (STUbL) complex SLX5/SLX8 and protein
CC turnover on the CDC48 segregase (PubMed:31015336). UBC9, SIZ1, or SIZ2
CC sumoylate DNA-bound EUC1 to stabilize its DNA-binding
CC (PubMed:31015336). Sumoylated EUC1 acts a cofactor required for the
CC recruitment of the SLX5/SLX8 STUbL complex via specific contacts
CC between EUC1 and SLX5, as well as an additional SUMO-mediated
CC interaction (PubMed:31015336). SLX5/SLX8 then ubiquitinates EUC1 and
CC presumably other targets at ub-hotspots, and the CDC48/UFD1/NPL4
CC complex, together with UBX4 and UBX5, removes Lys-48-linked
CC ubiquitinated proteins from chromatin. Ubiquitinated proteins could be
CC either degraded by the proteasome or recycled by deubiquitination
CC (PubMed:31015336). EUC1 itself does not seem to underlie extensive
CC turnover, as it is a very stable protein (PubMed:31015336). EUC1 is
CC able to act as a transcription factor, but its function at ub-hotspots
CC does not seem to depend on this ability (PubMed:31015336). EUC1-
CC mediated ub-hotspots are crucial during stress responses when gene
CC expression control is impaired (PubMed:31015336).
CC {ECO:0000269|PubMed:31015336}.
CC -!- SUBUNIT: Homodimer (PubMed:31015336). Interacts with SLX5
CC (PubMed:31015336). {ECO:0000269|PubMed:31015336}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:31015336}.
CC Note=Localizes to few distinct genomic hotspots where proteins other
CC than histone H2B are ubiquitinated (ub-hotspots).
CC {ECO:0000269|PubMed:31015336}.
CC -!- DOMAIN: The coiled-coil motif is required for homodimerization.
CC {ECO:0000269|PubMed:31015336}.
CC -!- PTM: Sumoylated at Lys-231 and subsequently ubiquitinated by the SUMO-
CC targeted ubiquitin ligase (STUbL) complex SLX5/SLX8.
CC {ECO:0000269|PubMed:31015336}.
CC -!- DISRUPTION PHENOTYPE: Prevents ub-hotspot formation and exacerbates
CC heat sensitivity of cells deficient in Rpd3L histone deacetylase
CC complex members (PubMed:31015336). Leads to the up-regulation of the
CC expression of the Rpd3S complex subunit RCO1 of the Rpd3S complex and
CC down-regulation of HSP12 and SIR2 (PubMed:31015336).
CC {ECO:0000269|PubMed:31015336}.
CC -!- MISCELLANEOUS: Present with 238 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z49702; CAA89747.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10008.1; -; Genomic_DNA.
DR PIR; S54572; S54572.
DR RefSeq; NP_013829.1; NM_001182611.1.
DR AlphaFoldDB; Q04461; -.
DR SMR; Q04461; -.
DR BioGRID; 35287; 117.
DR DIP; DIP-2716N; -.
DR IntAct; Q04461; 11.
DR MINT; Q04461; -.
DR STRING; 4932.YMR111C; -.
DR iPTMnet; Q04461; -.
DR MaxQB; Q04461; -.
DR PaxDb; Q04461; -.
DR PRIDE; Q04461; -.
DR EnsemblFungi; YMR111C_mRNA; YMR111C; YMR111C.
DR GeneID; 855138; -.
DR KEGG; sce:YMR111C; -.
DR SGD; S000004717; EUC1.
DR VEuPathDB; FungiDB:YMR111C; -.
DR eggNOG; ENOG502R143; Eukaryota.
DR HOGENOM; CLU_044103_0_0_1; -.
DR InParanoid; Q04461; -.
DR OMA; RRYGSTW; -.
DR BioCyc; YEAST:G3O-32807-MON; -.
DR PRO; PR:Q04461; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04461; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0060963; P:positive regulation of ribosomal protein gene transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0031503; P:protein-containing complex localization; IMP:SGD.
DR InterPro; IPR022210; TF_GCR1-like.
DR Pfam; PF12550; GCR1_C; 1.
PE 1: Evidence at protein level;
KW Chromosome; Coiled coil; DNA-binding; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..462
FT /note="Transcription factor-like protein EUC1"
FT /id="PRO_0000203291"
FT REGION 11..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..140
FT /note="Homodimerization region"
FT /evidence="ECO:0000269|PubMed:31015336"
FT REGION 190..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..385
FT /note="GCR1 DNA-binding region"
FT /evidence="ECO:0000269|PubMed:31015336"
FT REGION 441..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 105..135
FT /evidence="ECO:0000255"
FT COMPBIAS 18..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..462
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 254
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 231
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:31015336"
FT MUTAGEN 231
FT /note="K->R: Strongly reduces EUC1 sumoylation and the
FT formation of ub-hotspots."
FT /evidence="ECO:0000269|PubMed:31015336"
FT MUTAGEN 333
FT /note="W->A: Leads to complete loss of association with ub-
FT hotspots; when associated with A-34."
FT /evidence="ECO:0000269|PubMed:31015336"
FT MUTAGEN 334
FT /note="R->A: Leads to complete loss of association with ub-
FT hotspots; when associated with A-33."
FT /evidence="ECO:0000269|PubMed:31015336"
SQ SEQUENCE 462 AA; 52370 MW; F20C91FFBA73CB04 CRC64;
MPAREYNYVE GFGGYGSLDD DDSDRDSERR NHDLGQRTIT TSPTGVSRHA ALNRYMIPGR
INPLFRPTDA AQPPIVSTST SASATEPTNR IGPGRIKETP ETNFNAFLIA QLTRMEEQNA
NLKEEISLMK KEQELFFLEN QKKLEKGFKD INKYVEDVSA MKEVFKEVVG IMTGERIRFI
DHTGENVTPQ EAARVGNPST STQAHQSQSR STNWQEYSMH ASILAGDPRI KPEPGLSDFE
NGEYDGNESD ENATTRNLPL NNPDSVSNAD DSNNQLDGTG NENDIRNRRG CVGTSYKLNR
AIQNVTDAAR EYFEGLPGQP SVLSLERRYG STWRRSAKER TLFTKRMTII KRIIDIKDDP
SKYGLSLPEN KISRNQAIKV VENIRLGNNT FKGHHCRLSM SQLYEYFSKK MDKLEDYSLT
LKRRGKPRRI FLLEEREARL SLQQPHSIPN SSTGTPEHDQ DT
