SUB1_YEAST
ID SUB1_YEAST Reviewed; 292 AA.
AC P54000; D6VZL4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=RNA polymerase II transcriptional coactivator SUB1;
GN Name=SUB1; Synonyms=TSP1; OrderedLocusNames=YMR039C; ORFNames=YM9532.04C;
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].
RX PubMed=8617240; DOI=10.1002/j.1460-2075.1996.tb00544.x;
RA Knaus R., Pollock R., Guarente L.;
RT "Yeast SUB1 is a suppressor of TFIIB mutations and has homology to the
RT human co-activator PC4.";
RL EMBO J. 15:1933-1940(1996).
RN [2]
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 [3]
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 [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-119; SER-268 AND SER-269, AND
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-289, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; SER-268; SER-269 AND
RP SER-289, AND 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).
CC -!- FUNCTION: Plays a role in the release of TFIIB from the transcription
CC complex during transcription initiation. Binds to TFIIB and
CC specifically inhibits the formation of the TBP-TFIIB-promoter
CC complexes.
CC -!- INTERACTION:
CC P54000; P25299: RNA15; NbExp=2; IntAct=EBI-18492, EBI-15640;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 7820 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the transcriptional coactivator PC4 family.
CC {ECO:0000305}.
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DR EMBL; Z48502; CAA88405.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09938.1; -; Genomic_DNA.
DR PIR; S52888; S52888.
DR RefSeq; NP_013753.1; NM_001182536.1.
DR AlphaFoldDB; P54000; -.
DR SMR; P54000; -.
DR BioGRID; 35211; 462.
DR DIP; DIP-4696N; -.
DR IntAct; P54000; 4.
DR MINT; P54000; -.
DR STRING; 4932.YMR039C; -.
DR iPTMnet; P54000; -.
DR MaxQB; P54000; -.
DR PaxDb; P54000; -.
DR PRIDE; P54000; -.
DR EnsemblFungi; YMR039C_mRNA; YMR039C; YMR039C.
DR GeneID; 855055; -.
DR KEGG; sce:YMR039C; -.
DR SGD; S000004642; SUB1.
DR VEuPathDB; FungiDB:YMR039C; -.
DR eggNOG; KOG2712; Eukaryota.
DR GeneTree; ENSGT00390000008802; -.
DR HOGENOM; CLU_065855_0_0_1; -.
DR InParanoid; P54000; -.
DR OMA; EMNRADD; -.
DR BioCyc; YEAST:G3O-32744-MON; -.
DR PRO; PR:P54000; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P54000; protein.
DR GO; GO:0005730; C:nucleolus; IDA:CACAO.
DR GO; GO:0005654; C:nucleoplasm; IDA:CACAO.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:SGD.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:SGD.
DR GO; GO:0006972; P:hyperosmotic response; IGI:SGD.
DR GO; GO:0075297; P:negative regulation of ascospore formation; IMP:SGD.
DR GO; GO:0051053; P:negative regulation of DNA metabolic process; IMP:CACAO.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IDA:SGD.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:SGD.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0070898; P:RNA polymerase III preinitiation complex assembly; IDA:SGD.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IGI:SGD.
DR Gene3D; 2.30.31.10; -; 1.
DR InterPro; IPR003173; PC4_C.
DR InterPro; IPR009044; ssDNA-bd_transcriptional_reg.
DR InterPro; IPR045125; Sub1/Tcp4-like.
DR PANTHER; PTHR13215; PTHR13215; 1.
DR Pfam; PF02229; PC4; 1.
DR SUPFAM; SSF54447; SSF54447; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..292
FT /note="RNA polymerase II transcriptional coactivator SUB1"
FT /id="PRO_0000215951"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 292 AA; 33102 MW; 1E278C3EF2D569C8 CRC64;
MSYYNRYRNK RRSDNGGGNL SNSNNNNGGM PSGLSASDAI FDLGKNKRVT VRQFRNINLI
DIREYYLDSS TGEMKPGKKG ISLTEDLYDE LLKHRLNIDE ALRRLGSKRP KTKMVRLLSD
DEYEDDNNND STNNDKDKNG KDKNSPKKRR EDKSKASNES HDLEPRSKKK KPAPPTLLPH
EENIQNAERE ANATLIIPGQ AGRKQQEERK QKEKEEAEEA KAKAVAEQEK EAKAKEKIAE
PEPEPVPTLQ AKKEDIVSNI NESKDANSSD EEFAQSLEAE MNKAEDDISE EE
