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General transcriptional corepressor TUP1 (Flocculation suppressor protein) (Glucose repression regulatory protein TUP1) (Repressor AER2)

 TUP1_YEAST              Reviewed;         713 AA.
P16649; D6VR85; P17995; P18323;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 2.
25-OCT-2017, entry version 189.
RecName: Full=General transcriptional corepressor TUP1;
AltName: Full=Flocculation suppressor protein;
AltName: Full=Glucose repression regulatory protein TUP1;
AltName: Full=Repressor AER2;
Name=TUP1; Synonyms=AAR1, AER2, AMM1, CYC9, FLK1, SFL2, UMR7;
OrderedLocusNames=YCR084C; ORFNames=YCR84C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
PubMed=2247069; DOI=10.1128/MCB.10.12.6500;
Williams F.E., Trumbly R.J.;
"Characterization of TUP1, a mediator of glucose repression in
Saccharomyces cerevisiae.";
Mol. Cell. Biol. 10:6500-6511(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1900249; DOI=10.1016/0378-1119(91)90047-F;
Zhang M., Rosenblum-Vos L.S., Lowry C.V., Boakye K., Zitomer R.S.;
"A yeast protein with homology to the beta-subunit of G proteins is
involved in control of heme-regulated and catabolite-repressed
genes.";
Gene 97:153-161(1991).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 44774 / DBY747;
PubMed=2197185; DOI=10.1016/0378-1119(90)90210-I;
Fujita A., Matsumoto S., Kuhara S., Misumi Y., Kobayashi H.;
"Cloning of the yeast SFL2 gene: its disruption results in pleiotropic
phenotypes characteristic for tup1 mutants.";
Gene 89:93-99(1990).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=1574125; DOI=10.1038/357038a0;
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M.,
Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W.,
Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H.,
Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V.,
Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A.,
de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H.,
Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K.,
Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B.,
Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A.,
Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y.,
Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R.,
Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G.,
Tzermia M., Urrestarazu L.A., Valle G., Vetter I.,
van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H.,
Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C.,
Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.;
"The complete DNA sequence of yeast chromosome III.";
Nature 357:38-46(1992).
[5]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[6]
SIMILARITY TO BETA SUBUNIT OF G-PROTEINS.
PubMed=1901558; DOI=10.1016/0378-1119(91)90118-U;
Kearsley S.;
"The SFL2 (TUP1?) protein of Saccharomyces cerevisiae contains a
repeating motif homologous to beta subunits of G proteins.";
Gene 98:147-148(1991).
[7]
INTERACTION WITH MATALPHA2.
PubMed=7995523; DOI=10.1101/gad.8.23.2857;
Komachi K., Redd M.J., Johnson A.D.;
"The WD repeats of Tup1 interact with the homeo domain protein alpha
2.";
Genes Dev. 8:2857-2867(1994).
[8]
INTERACTION WITH HISTONE H3 AND HISTONE H4.
PubMed=8675011; DOI=10.1101/gad.10.10.1247;
Edmondson D.G., Smith M.M., Roth S.Y.;
"Repression domain of the yeast global repressor Tup1 interacts
directly with histones H3 and H4.";
Genes Dev. 10:1247-1259(1996).
[9]
SUBUNIT.
PubMed=8943325; DOI=10.1128/MCB.16.12.6707;
Varanasi U.S., Klis M., Mikesell P.B., Trumbly R.J.;
"The Cyc8 (Ssn6)-Tup1 corepressor complex is composed of one Cyc8 and
four Tup1 subunits.";
Mol. Cell. Biol. 16:6707-6714(1996).
[10]
INTERACTION WITH RFX1.
PubMed=9741624; DOI=10.1016/S0092-8674(00)81601-3;
Huang M., Zhou Z., Elledge S.J.;
"The DNA replication and damage checkpoint pathways induce
transcription by inhibition of the Crt1 repressor.";
Cell 94:595-605(1998).
[11]
INTERACTION WITH CYC8 AND RPD3, AND FUNCTION OF THE CYC8-TUP1 COMPLEX.
PubMed=11069890; DOI=10.1101/gad.829100;
Watson A.D., Edmondson D.G., Bone J.R., Mukai Y., Yu Y., Du W.,
Stillman D.J., Roth S.Y.;
"Ssn6-Tup1 interacts with class I histone deacetylases required for
repression.";
Genes Dev. 14:2737-2744(2000).
[12]
INTERACTION WITH PGD1, AND FUNCTION OF THE CYC8-TUP1 COMPLEX.
PubMed=10722672; DOI=10.1074/jbc.275.12.8397;
Papamichos-Chronakis M., Conlan R.S., Gounalaki N., Copf T.,
Tzamarias D.;
"Hrs1/Med3 is a Cyc8-Tup1 corepressor target in the RNA polymerase II
holoenzyme.";
J. Biol. Chem. 275:8397-8403(2000).
[13]
FUNCTION OF THE CYC8-TUP1 COMPLEX.
PubMed=11230135; DOI=10.1093/emboj/20.5.1123;
Proft M., Pascual-Ahuir A., de Nadal E., Arino J., Serrano R.,
Posas F.;
"Regulation of the Sko1 transcriptional repressor by the Hog1 MAP
kinase in response to osmotic stress.";
EMBO J. 20:1123-1133(2001).
[14]
INTERACTION WITH SKO1.
PubMed=11500510; DOI=10.1074/jbc.M105755200;
Pascual-Ahuir A., Posas F., Serrano R., Proft M.;
"Multiple levels of control regulate the yeast cAMP-response element-
binding protein repressor Sko1p in response to stress.";
J. Biol. Chem. 276:37373-37378(2001).
[15]
INTERACTION WITH HDA1 AND HDA2, AND FUNCTION OF THE CYC8-TUP1 COMPLEX.
PubMed=11172717; DOI=10.1016/S1097-2765(01)00160-5;
Wu J., Suka N., Carlson M., Grunstein M.;
"TUP1 utilizes histone H3/H2B-specific HDA1 deacetylase to repress
gene activity in yeast.";
Mol. Cell 7:117-126(2001).
[16]
FUNCTION OF THE CYC8-TUP1 COMPLEX.
PubMed=11784848; DOI=10.1128/MCB.22.3.693-703.2002;
Davie J.K., Trumbly R.J., Dent S.Y.;
"Histone-dependent association of Tup1-Ssn6 with repressed genes in
vivo.";
Mol. Cell. Biol. 22:693-703(2002).
[17]
FUNCTION OF THE CYC8-TUP1 COMPLEX.
PubMed=14665463; DOI=10.1128/EC.2.6.1288-1303.2003;
Mennella T.A., Klinkenberg L.G., Zitomer R.S.;
"Recruitment of Tup1-Ssn6 by yeast hypoxic genes and chromatin-
independent exclusion of TATA binding protein.";
Eukaryot. Cell 2:1288-1303(2003).
[18]
INTERACTION WITH HOS1; HOS2 AND RPD3.
PubMed=14525981; DOI=10.1074/jbc.M309753200;
Davie J.K., Edmondson D.G., Coco C.B., Dent S.Y.;
"Tup1-Ssn6 interacts with multiple class I histone deacetylases in
vivo.";
J. Biol. Chem. 278:50158-50162(2003).
[19]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[20]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[25]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 282-713.
PubMed=10856245; DOI=10.1093/emboj/19.12.3016;
Sprague E.R., Redd M.J., Johnson A.D., Wolberger C.;
"Structure of the C-terminal domain of Tup1, a corepressor of
transcription in yeast.";
EMBO J. 19:3016-3027(2000).
-!- FUNCTION: Acts as component of the CYC8-TUP1 corepressor complex
which is involved in the repression of many genes in a wide
variety of physiological processes including heme-regulated and
catabolite repressed genes. May also be involved in the
derepression of at least some target genes. The complex is
recruited to target genes by interaction with DNA-bound
transcriptional repressors, like MATALPHA2, MIG1, RFX1 and SKO1.
The complex recruits histone deacetylases to produce a repressive
chromatin structure, interacts with hypoacetylated N-terminal
tails of histones H3 and H4 that have been programmed for
repression by the action of histone deacetylases and interferes
directly with the transcriptional machinery by associating with
the RNA polymerase II mediator complex.
{ECO:0000269|PubMed:10722672, ECO:0000269|PubMed:11069890,
ECO:0000269|PubMed:11172717, ECO:0000269|PubMed:11230135,
ECO:0000269|PubMed:11784848, ECO:0000269|PubMed:14665463,
ECO:0000269|PubMed:2247069}.
-!- SUBUNIT: Associates with CYC8/SSN6 to form the CYC8-TUP1 (or TUP1-
SSN6) corepressor complex that is composed of 4 copies of TUP1 and
one copy of CYC8. Interacts with histone H3, histone H4,
MATALPHA2, RFX1, SKO1, PGD1, HDA1, HDA2, HOS1, HOS2 AND RPD3.
{ECO:0000269|PubMed:10722672, ECO:0000269|PubMed:11069890,
ECO:0000269|PubMed:11172717, ECO:0000269|PubMed:11500510,
ECO:0000269|PubMed:14525981, ECO:0000269|PubMed:7995523,
ECO:0000269|PubMed:8675011, ECO:0000269|PubMed:8943325,
ECO:0000269|PubMed:9741624}.
-!- INTERACTION:
P14922:CYC8; NbExp=6; IntAct=EBI-19654, EBI-18215;
P40356:PGD1; NbExp=3; IntAct=EBI-19654, EBI-13268;
P48743:RFX1; NbExp=2; IntAct=EBI-19654, EBI-15036;
P32561:RPD3; NbExp=2; IntAct=EBI-19654, EBI-15864;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
-!- MISCELLANEOUS: Present with 5840 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the WD repeat TUP1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA34411.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; M31733; AAA35182.1; -; Genomic_DNA.
EMBL; M35861; AAA34413.1; -; Genomic_DNA.
EMBL; X16365; CAA34411.1; ALT_INIT; Genomic_DNA.
EMBL; X59720; CAA42259.1; -; Genomic_DNA.
EMBL; BK006937; DAA07554.1; -; Genomic_DNA.
PIR; JN0133; JN0133.
RefSeq; NP_010007.1; NM_001178790.1.
PDB; 1ERJ; X-ray; 2.30 A; A/B/C=282-388, A/B/C=432-713.
PDB; 3VP8; X-ray; 1.91 A; A/B/C/D=1-92.
PDB; 3VP9; X-ray; 1.80 A; A/B=1-92.
PDBsum; 1ERJ; -.
PDBsum; 3VP8; -.
PDBsum; 3VP9; -.
ProteinModelPortal; P16649; -.
SMR; P16649; -.
BioGrid; 31057; 102.
DIP; DIP-512N; -.
IntAct; P16649; 27.
MINT; MINT-648551; -.
STRING; 4932.YCR084C; -.
iPTMnet; P16649; -.
MaxQB; P16649; -.
PRIDE; P16649; -.
EnsemblFungi; CAA42259; CAA42259; CAA42259.
EnsemblFungi; YCR084C; YCR084C; YCR084C.
GeneID; 850445; -.
KEGG; sce:YCR084C; -.
EuPathDB; FungiDB:YCR084C; -.
SGD; S000000680; TUP1.
GeneTree; ENSGT00890000139543; -.
HOGENOM; HOG000200558; -.
InParanoid; P16649; -.
KO; K06666; -.
OMA; WFMNEKS; -.
OrthoDB; EOG092C21A7; -.
BioCyc; YEAST:G3O-29380-MONOMER; -.
EvolutionaryTrace; P16649; -.
PRO; PR:P16649; -.
Proteomes; UP000002311; Chromosome III.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0017053; C:transcriptional repressor complex; IPI:SGD.
GO; GO:0042393; F:histone binding; IDA:SGD.
GO; GO:0042826; F:histone deacetylase binding; IDA:SGD.
GO; GO:0036033; F:mediator complex binding; IDA:SGD.
GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:SGD.
GO; GO:0001191; F:transcriptional repressor activity, RNA polymerase II transcription factor binding; IDA:SGD.
GO; GO:0043486; P:histone exchange; IMP:SGD.
GO; GO:0035955; P:negative regulation of dipeptide transport by negative regulation of transcription from RNA polymerase II promoter; IMP:SGD.
GO; GO:0001198; P:negative regulation of mating-type specific transcription from RNA polymerase II promoter; IMP:SGD.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:SGD.
GO; GO:0000433; P:negative regulation of transcription from RNA polymerase II promoter by glucose; IMP:SGD.
GO; GO:0007070; P:negative regulation of transcription from RNA polymerase II promoter during mitotic cell cycle; IMP:SGD.
GO; GO:0016584; P:nucleosome positioning; IDA:SGD.
GO; GO:2000531; P:regulation of fatty acid biosynthetic process by regulation of transcription from RNA polymerase II promoter; IMP:SGD.
GO; GO:2000217; P:regulation of invasive growth in response to glucose limitation; IMP:SGD.
GO; GO:2001020; P:regulation of response to DNA damage stimulus; IMP:SGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR013890; Tscrpt_rep_Tup1_N.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF08581; Tup_N; 1.
Pfam; PF00400; WD40; 7.
PRINTS; PR00320; GPROTEINBRPT.
ProDom; PD010558; Transcrip_repressor_Tup1_N; 1.
SMART; SM00320; WD40; 7.
SUPFAM; SSF50978; SSF50978; 2.
PROSITE; PS00678; WD_REPEATS_1; 4.
PROSITE; PS50082; WD_REPEATS_2; 5.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; WD repeat.
CHAIN 1 713 General transcriptional corepressor TUP1.
/FTId=PRO_0000051312.
REPEAT 342 371 WD 1.
REPEAT 441 471 WD 2.
REPEAT 483 513 WD 3.
REPEAT 524 555 WD 4.
REPEAT 574 604 WD 5.
REPEAT 628 658 WD 6.
REPEAT 670 706 WD 7.
COMPBIAS 97 118 Gln-rich.
COMPBIAS 181 198 Poly-Gln.
COMPBIAS 399 409 Thr-rich.
MOD_RES 439 439 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
CONFLICT 75 75 E -> A (in Ref. 1; AAA35182).
{ECO:0000305}.
CONFLICT 100 100 R -> Q (in Ref. 1; AAA35182).
{ECO:0000305}.
CONFLICT 685 685 P -> S (in Ref. 1; AAA35182 and 2;
AAA34413). {ECO:0000305}.
TURN 19 26 {ECO:0000244|PDB:3VP9}.
HELIX 27 84 {ECO:0000244|PDB:3VP9}.
STRAND 290 292 {ECO:0000244|PDB:1ERJ}.
HELIX 300 303 {ECO:0000244|PDB:1ERJ}.
STRAND 307 310 {ECO:0000244|PDB:1ERJ}.
STRAND 314 317 {ECO:0000244|PDB:1ERJ}.
STRAND 322 325 {ECO:0000244|PDB:1ERJ}.
STRAND 333 342 {ECO:0000244|PDB:1ERJ}.
STRAND 349 352 {ECO:0000244|PDB:1ERJ}.
STRAND 356 362 {ECO:0000244|PDB:1ERJ}.
STRAND 367 371 {ECO:0000244|PDB:1ERJ}.
TURN 372 374 {ECO:0000244|PDB:1ERJ}.
STRAND 377 381 {ECO:0000244|PDB:1ERJ}.
STRAND 445 451 {ECO:0000244|PDB:1ERJ}.
STRAND 455 462 {ECO:0000244|PDB:1ERJ}.
STRAND 467 471 {ECO:0000244|PDB:1ERJ}.
TURN 472 475 {ECO:0000244|PDB:1ERJ}.
STRAND 476 481 {ECO:0000244|PDB:1ERJ}.
STRAND 488 493 {ECO:0000244|PDB:1ERJ}.
STRAND 497 504 {ECO:0000244|PDB:1ERJ}.
STRAND 507 513 {ECO:0000244|PDB:1ERJ}.
TURN 514 517 {ECO:0000244|PDB:1ERJ}.
STRAND 518 524 {ECO:0000244|PDB:1ERJ}.
STRAND 529 534 {ECO:0000244|PDB:1ERJ}.
STRAND 541 546 {ECO:0000244|PDB:1ERJ}.
STRAND 551 555 {ECO:0000244|PDB:1ERJ}.
TURN 556 558 {ECO:0000244|PDB:1ERJ}.
STRAND 561 565 {ECO:0000244|PDB:1ERJ}.
STRAND 579 584 {ECO:0000244|PDB:1ERJ}.
STRAND 588 595 {ECO:0000244|PDB:1ERJ}.
STRAND 598 604 {ECO:0000244|PDB:1ERJ}.
STRAND 622 627 {ECO:0000244|PDB:1ERJ}.
STRAND 633 638 {ECO:0000244|PDB:1ERJ}.
HELIX 640 642 {ECO:0000244|PDB:1ERJ}.
STRAND 644 649 {ECO:0000244|PDB:1ERJ}.
STRAND 652 658 {ECO:0000244|PDB:1ERJ}.
TURN 659 661 {ECO:0000244|PDB:1ERJ}.
STRAND 664 669 {ECO:0000244|PDB:1ERJ}.
STRAND 675 680 {ECO:0000244|PDB:1ERJ}.
STRAND 691 697 {ECO:0000244|PDB:1ERJ}.
STRAND 700 709 {ECO:0000244|PDB:1ERJ}.
SEQUENCE 713 AA; 78308 MW; 444104AAD63CB944 CRC64;
MTASVSNTQN KLNELLDAIR QEFLQVSQEA NTYRLQNQKD YDFKMNQQLA EMQQIRNTVY
ELELTHRKMK DAYEEEIKHL KLGLEQRDHQ IASLTVQQQR QQQQQQQVQQ HLQQQQQQLA
AASASVPVAQ QPPATTSATA TPAANTTTGS PSAFPVQASR PNLVGSQLPT TTLPVVSSNA
QQQLPQQQLQ QQQLQQQQPP PQVSVAPLSN TAINGSPTSK ETTTLPSVKA PESTLKETEP
ENNNTSKIND TGSATTATTT TATETEIKPK EEDATPASLH QDHYLVPYNQ RANHSKPIPP
FLLDLDSQSV PDALKKQTND YYILYNPALP REIDVELHKS LDHTSVVCCV KFSNDGEYLA
TGCNKTTQVY RVSDGSLVAR LSDDSAANNH RNSITENNTT TSTDNNTMTT TTTTTITTTA
MTSAAELAKD VENLNTSSSP SSDLYIRSVC FSPDGKFLAT GAEDRLIRIW DIENRKIVMI
LQGHEQDIYS LDYFPSGDKL VSGSGDRTVR IWDLRTGQCS LTLSIEDGVT TVAVSPGDGK
YIAAGSLDRA VRVWDSETGF LVERLDSENE SGTGHKDSVY SVVFTRDGQS VVSGSLDRSV
KLWNLQNANN KSDSKTPNSG TCEVTYIGHK DFVLSVATTQ NDEYILSGSK DRGVLFWDKK
SGNPLLMLQG HRNSVISVAV ANGSPLGPEY NVFATGSGDC KARIWKYKKI APN


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29-041 HIF1AN is a co-repressor that interacts with hypoxia-inducible factor 1 (HIF-1) alpha and the von Hippel-Lindau tumor suppressor protein to mediate repression of HIF-1 transcriptional activity. 0.05 mg
27-739 HIF1AN is a co-repressor that interacts with hypoxia-inducible factor 1 (HIF-1) alpha and the von Hippel-Lindau tumor suppressor protein to mediate repression of HIF-1 transcriptional activity. 0.05 mg
25-495 HIF1AN is a co-repressor that interacts with hypoxia-inducible factor 1 (HIF-1) alpha and the von Hippel-Lindau tumor suppressor protein to mediate repression of HIF-1 transcriptional activity. 0.05 mg
27-738 HIF1AN is a co-repressor that interacts with hypoxia-inducible factor 1 (HIF-1) alpha and the von Hippel-Lindau tumor suppressor protein to mediate repression of HIF-1 transcriptional activity. 0.1 mg
26-995 IRF2BP1 acts as a transcriptional repressor. IRF2BP1 also acts as a transcriptional corepressor in a IRF2-dependent manner. This repression is not mediated at least in part by histone deacetylase acti 0.05 mg
EIAAB38582 Corl2,Fussel-18 homolog,Ladybird homeobox corepressor 1-like protein,LBX1 corepressor 1-like protein,Mouse,Mus musculus,SKI family transcriptional corepressor 2,Skor2,Transcriptional corepressor Corl2
25-070 SIN3A is a transcriptional regulatory protein. It contains paired amphipathic helix (PAH) domains, which are important for protein-protein interactions and may mediate repression by the Mad-Max comple 0.05 mg
EIAAB04804 AKI1,Akt kinase-interacting protein 1,CC2D1A,Coiled-coil and C2 domain-containing protein 1A,Five repressor element under dual repression-binding protein 1,FRE under dual repression-binding protein 1,
27-683 The tumor suppressor WT1 represses and activates transcription. Anti-Prostate Apoptosis Response Protein Par-4 (PAWR) is a WT1-interacting protein that itself functions as a transcriptional repressor. 0.1 mg
27-492 The tumor suppressor WT1 represses and activates transcription. Anti-Prostate Apoptosis Response Protein Par-4 (PAWR) is a WT1-interacting protein that itself functions as a transcriptional repressor. 0.05 mg
orb108869 TUP1 antibody 100 ug
EIAAB04803 Cc2d1a,Coiled-coil and C2 domain-containing protein 1A,Five repressor element under dual repression-binding protein 1,FRE under dual repression-binding protein 1,Freud-1,Mouse,Mus musculus
EIAAB04805 Cc2d1a,Coiled-coil and C2 domain-containing protein 1A,Five repressor element under dual repression-binding protein 1,FRE under dual repression-binding protein 1,Freud-1,Rat,Rattus norvegicus
MAB1790 TUP1 monoclonal antibody, clone 10 100 ug
EIAAB38578 Corl1,Fussel-15 homolog,Ladybird homeobox corepressor 1,Lbx1 corepressor 1,Lbxcor1,Mouse,Mus musculus,SKI family transcriptional corepressor 1,Skor1,Transcriptional corepressor Corl1
X1538M Yeast (Saccharomyces cerevisiae) TUP1 Monoclonal Antibody 100
27-757 RBAK is a nuclear protein which interacts with the tumor suppressor retinoblastoma 1. The two interacting proteins are thought to act as a transcriptional repressor for promoters which are activated b 0.1 mg
27-756 RBAK encodes a nuclear protein which interacts with the tumor suppressor retinoblastoma 1. The two interacting proteins are thought to act as a transcriptional repressor for promoters which are activa 0.05 mg
EIAAB13397 ETS domain transcriptional repressor PE1,ETS translocation variant 3,Etv3,Mets,Mitogenic Ets transcriptional suppressor,Mouse,Mus musculus,Pe1,PE-1
X1538M TUP1 type: Monoclonal Antibody host: Mouse clone: 10 Isotype: IgG 100
EIAAB13396 ETS domain transcriptional repressor PE1,ETS translocation variant 3,ETV3,Homo sapiens,Human,METS,Mitogenic Ets transcriptional suppressor,PE1,PE-1
EIAAB38581 CORL2,Functional Smad-suppressing element on chromosome 18,FUSSEL18,Fussel-18,Homo sapiens,Human,Ladybird homeobox corepressor 1-like protein,LBX1 corepressor 1-like protein,SKI family transcriptional
27-373 The adipocyte enhancer binding protein 1 (AEBP1) is a transcriptional repressor with carboxypeptidase (CP) activity. This protein binds to a regulatory sequence, adipocyte enhancer 1 (AE-1), located i 0.05 mg
20-372-60075 ets variant gene 3 - Mouse monoclonal anti-human ETV3 antibody; ETS domain transcriptional repressor PE1; PE-1; Mitogenic Ets transcriptional suppressor Monoclonal 0.1 mg
EIAAB47329 58 kDa repressor protein,Rat,Rattus norvegicus,Rp58,rRP58,Transcriptional repressor RP58,Zfp238,Zinc finger protein 238,Znf238


 

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