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RE1-silencing transcription factor (Neural-restrictive silencer factor) (X2 box repressor)

 REST_HUMAN              Reviewed;        1097 AA.
Q13127; A2RUE0; B9EGJ0; Q12956; Q12957; Q13134; Q59ER1; Q8IWI3;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
25-OCT-2017, entry version 159.
RecName: Full=RE1-silencing transcription factor;
AltName: Full=Neural-restrictive silencer factor;
AltName: Full=X2 box repressor;
Name=REST; Synonyms=NRSF, XBR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
PubMed=7697725; DOI=10.1016/0092-8674(95)90298-8;
Chong J.A., Tapia-Ramirez J., Kim S., Toledo-Aral J.J., Zheng Y.,
Boutros M.C., Altshuller Y.M., Frohman M.A., Kraner S.D., Mandel G.;
"REST: a mammalian silencer protein that restricts sodium channel gene
expression to neurons.";
Cell 80:949-957(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF
1-599 (ISOFORM 1), AND FUNCTION.
PubMed=7871435; DOI=10.1126/science.7871435;
Schoenherr C.J., Anderson D.J.;
"The neuron-restrictive silencer factor (NRSF): a coordinate repressor
of multiple neuron-specific genes.";
Science 267:1360-1363(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
AND VARIANT LEU-797.
PubMed=8568247;
Scholl T., Stevens M.B., Mahanta S., Strominger J.L.;
"A zinc finger protein that represses transcription of the human MHC
class II gene, DPA.";
J. Immunol. 156:1448-1457(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ILE-626.
TISSUE=Testis, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
ALTERNATIVE SPLICING (ISOFORMS 3 AND 4).
PubMed=10521596; DOI=10.1016/S0169-328X(99)00196-5;
Palm K., Metsis M., Timmusk T.;
"Neuron-specific splicing of zinc finger transcription factor
REST/NRSF/XBR is frequent in neuroblastomas and conserved in human,
mouse and rat.";
Brain Res. Mol. Brain Res. 72:30-39(1999).
[9]
INTERACTION WITH RCOR1.
PubMed=10449787; DOI=10.1073/pnas.96.17.9873;
Andres M.E., Burger C., Peral-Rubio M.J., Battaglioli E.,
Anderson M.E., Grimes J., Dallman J., Ballas N., Mandel G.;
"CoREST: a functional corepressor required for regulation of neural-
specific gene expression.";
Proc. Natl. Acad. Sci. U.S.A. 96:9873-9878(1999).
[10]
INTERACTION WITH RCOR1 AND SIN3A.
PubMed=10734093; DOI=10.1074/jbc.275.13.9461;
Grimes J.A., Nielsen S.J., Battaglioli E., Miska E.A., Speh J.C.,
Berry D.L., Atouf F., Holdener B.C., Mandel G., Kouzarides T.;
"The co-repressor mSin3A is a functional component of the REST-CoREST
repressor complex.";
J. Biol. Chem. 275:9461-9467(2000).
[11]
FUNCTION.
PubMed=12399542; DOI=10.1126/science.1076469;
Lunyak V.V., Burgess R., Prefontaine G.G., Nelson C., Sze S.-H.,
Chenoweth J., Schwartz P., Pevzner P.A., Glass C., Mandel G.,
Rosenfeld M.G.;
"Corepressor-dependent silencing of chromosomal regions encoding
neuronal genes.";
Science 298:1747-1752(2002).
[12]
ERRATUM.
Lunyak V.V., Burgess R., Prefontaine G.G., Nelson C., Sze S.-H.,
Chenoweth J., Schwartz P., Pevzner P.A., Glass C., Mandel G.,
Rosenfeld M.G.;
Science 299:1663-1663(2003).
[13]
FUNCTION, INTERACTION WITH CDYL; EHMT1 AND EHMT2, AND IDENTIFICATION
IN A COMPLEX WITH CDYL; SETB1; EHMT1; EHMT2 AND WIZ.
PubMed=19061646; DOI=10.1016/j.molcel.2008.10.025;
Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B.,
Macia E., Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J.,
Shi Y.;
"CDYL bridges REST and histone methyltransferases for gene repression
and suppression of cellular transformation.";
Mol. Cell 32:718-726(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-864, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
INTERACTION WITH ZFP90.
PubMed=21284946; DOI=10.1016/j.yjmcc.2011.01.017;
Hata L., Murakami M., Kuwahara K., Nakagawa Y., Kinoshita H.,
Usami S., Yasuno S., Fujiwara M., Kuwabara Y., Minami T., Yamada Y.,
Yamada C., Nakao K., Ueshima K., Nishikimi T., Nakao K.;
"Zinc-finger protein 90 negatively regulates neuron-restrictive
silencer factor-mediated transcriptional repression of fetal cardiac
genes.";
J. Mol. Cell. Cardiol. 50:972-981(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-864, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[18]
STRUCTURE BY NMR OF 43-57 IN COMPLEX WITH SIN3B, AND INTERACTION WITH
SIN3B.
PubMed=16288918; DOI=10.1016/j.jmb.2005.10.008;
Nomura M., Uda-Tochio H., Murai K., Mori N., Nishimura Y.;
"The neural repressor NRSF/REST binds the PAH1 domain of the Sin3
corepressor by using its distinct short hydrophobic helix.";
J. Mol. Biol. 354:903-915(2005).
[19]
INVOLVEMENT IN WT6, VARIANTS WT6 PRO-160; TYR-290; ARG-322 AND
GLN-412, CHARACTERIZATION OF VARIANT PRO-160; TYR-290 AND ARG-322,
FUNCTION, AND MUTAGENESIS OF GLU-91; MET-420; SER-593; ALA-642 AND
HIS-918.
PubMed=26551668; DOI=10.1038/ng.3440;
Mahamdallie S.S., Hanks S., Karlin K.L., Zachariou A., Perdeaux E.R.,
Ruark E., Shaw C.A., Renwick A., Ramsay E., Yost S., Elliott A.,
Birch J., Capra M., Gray J., Hale J., Kingston J., Levitt G.,
McLean T., Sheridan E., Renwick A., Seal S., Stiller C., Sebire N.,
Westbrook T.F., Rahman N.;
"Mutations in the transcriptional repressor REST predispose to Wilms
tumor.";
Nat. Genet. 47:1471-1474(2015).
-!- FUNCTION: Transcriptional repressor which binds neuron-restrictive
silencer element (NRSE) and represses neuronal gene transcription
in non-neuronal cells. Restricts the expression of neuronal genes
by associating with two distinct corepressors, mSin3 and CoREST,
which in turn recruit histone deacetylase to the promoters of
REST-regulated genes. Mediates repression by recruiting the BHC
complex at RE1/NRSE sites which acts by deacetylating and
demethylating specific sites on histones, thereby acting as a
chromatin modifier. Transcriptional repression by REST-CDYL via
the recruitment of histone methyltransferase EHMT2 may be
important in transformation suppression.
{ECO:0000269|PubMed:12399542, ECO:0000269|PubMed:19061646,
ECO:0000269|PubMed:26551668, ECO:0000269|PubMed:7697725,
ECO:0000269|PubMed:7871435, ECO:0000269|PubMed:8568247}.
-!- SUBUNIT: Interacts with SIN3A, SIN3B and RCOR1. Interacts with
CDYL. Interacts with EHMT1 and EHMT2 only in the presence of CDYL.
Part of a complex containing at least CDYL, REST, WIZ, SETB1,
EHMT1 and EHMT2. Interacts (via zinc-finger DNA-binding domain)
with ZFP90 (via N- and C-termini); the interaction inhibits REST
repressor activity (PubMed:21284946).
{ECO:0000269|PubMed:10449787, ECO:0000269|PubMed:10734093,
ECO:0000269|PubMed:16288918, ECO:0000269|PubMed:19061646,
ECO:0000269|PubMed:21284946}.
-!- INTERACTION:
Q9Y297:BTRC; NbExp=10; IntAct=EBI-926706, EBI-307461;
Q9UKB1:FBXW11; NbExp=3; IntAct=EBI-926706, EBI-355189;
P41229:KDM5C; NbExp=3; IntAct=EBI-926706, EBI-1246541;
P51532:SMARCA4; NbExp=2; IntAct=EBI-926706, EBI-302489;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8VIG1}.
Note=Colocalizes with ZFP90 in the nucleus.
{ECO:0000250|UniProtKB:Q8VIG1}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=Q13127-1; Sequence=Displayed;
Name=2;
IsoId=Q13127-2; Sequence=VSP_022064, VSP_022065;
Name=3; Synonyms=N4;
IsoId=Q13127-3; Sequence=VSP_022066, VSP_022068;
Name=4;
IsoId=Q13127-4; Sequence=VSP_022067;
-!- TISSUE SPECIFICITY: Ubiquitous. Expressed at higher levels in the
tissues of the lymphocytic compartment, including spleen, thymus,
peripheral blood lymphocytes and ovary.
{ECO:0000269|PubMed:8568247}.
-!- DISEASE: Wilms tumor 6 (WT6) [MIM:616806]: A pediatric malignancy
of kidney, and the most common childhood abdominal malignancy. It
is caused by the uncontrolled multiplication of renal stem,
stromal, and epithelial cells. {ECO:0000269|PubMed:26551668}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAA98503.1; Type=Frameshift; Positions=188, 198, 202, 212, 1087; Evidence={ECO:0000305};
Sequence=AAC50114.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAC50115.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAH38985.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAD92987.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RESTID44266ch4q12.html";
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EMBL; U22314; AAB17211.1; -; mRNA.
EMBL; U13877; AAC50114.1; ALT_INIT; mRNA.
EMBL; U13879; AAC50115.1; ALT_INIT; mRNA.
EMBL; U22680; AAA98503.1; ALT_FRAME; mRNA.
EMBL; AB209750; BAD92987.1; ALT_INIT; mRNA.
EMBL; AC069307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471057; EAX05517.1; -; Genomic_DNA.
EMBL; BC038985; AAH38985.1; ALT_SEQ; mRNA.
EMBL; BC132859; AAI32860.1; -; mRNA.
EMBL; BC136491; AAI36492.1; -; mRNA.
CCDS; CCDS3509.1; -. [Q13127-1]
PIR; A56138; A56138.
PIR; I38754; I38754.
PIR; I38755; I38755.
RefSeq; NP_001180437.1; NM_001193508.1. [Q13127-1]
RefSeq; NP_005603.3; NM_005612.4. [Q13127-1]
RefSeq; XP_011532703.1; XM_011534401.2. [Q13127-1]
UniGene; Hs.307836; -.
PDB; 2CZY; NMR; -; B=43-57.
PDBsum; 2CZY; -.
ProteinModelPortal; Q13127; -.
SMR; Q13127; -.
BioGrid; 111910; 44.
CORUM; Q13127; -.
DIP; DIP-35264N; -.
IntAct; Q13127; 14.
STRING; 9606.ENSP00000311816; -.
iPTMnet; Q13127; -.
PhosphoSitePlus; Q13127; -.
BioMuta; REST; -.
DMDM; 296452989; -.
MaxQB; Q13127; -.
PaxDb; Q13127; -.
PeptideAtlas; Q13127; -.
PRIDE; Q13127; -.
Ensembl; ENST00000309042; ENSP00000311816; ENSG00000084093. [Q13127-1]
Ensembl; ENST00000619101; ENSP00000484836; ENSG00000084093. [Q13127-1]
GeneID; 5978; -.
KEGG; hsa:5978; -.
UCSC; uc003hch.4; human. [Q13127-1]
CTD; 5978; -.
DisGeNET; 5978; -.
EuPathDB; HostDB:ENSG00000084093.15; -.
GeneCards; REST; -.
H-InvDB; HIX0031381; -.
HGNC; HGNC:9966; REST.
HPA; CAB068222; -.
HPA; HPA006079; -.
MalaCards; REST; -.
MIM; 600571; gene.
MIM; 616806; phenotype.
neXtProt; NX_Q13127; -.
OpenTargets; ENSG00000084093; -.
PharmGKB; PA34334; -.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00890000139371; -.
HOVERGEN; HBG093893; -.
InParanoid; Q13127; -.
KO; K09222; -.
OMA; VQKEPVQ; -.
OrthoDB; EOG091G01NI; -.
PhylomeDB; Q13127; -.
TreeFam; TF332861; -.
Reactome; R-HSA-3214815; HDACs deacetylate histones.
Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
SignaLink; Q13127; -.
SIGNOR; Q13127; -.
ChiTaRS; REST; human.
EvolutionaryTrace; Q13127; -.
GeneWiki; RE1-silencing_transcription_factor; -.
GenomeRNAi; 5978; -.
PRO; PR:Q13127; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000084093; -.
CleanEx; HS_REST; -.
ExpressionAtlas; Q13127; baseline and differential.
Genevisible; Q13127; HS.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0017053; C:transcriptional repressor complex; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0004407; F:histone deacetylase activity; TAS:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0015271; F:outward rectifier potassium channel activity; IMP:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IEA:Ensembl.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:UniProtKB.
GO; GO:0060379; P:cardiac muscle cell myoblast differentiation; ISS:UniProtKB.
GO; GO:0035690; P:cellular response to drug; IMP:UniProtKB.
GO; GO:0071257; P:cellular response to electrical stimulus; IMP:UniProtKB.
GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IDA:UniProtKB.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
GO; GO:0070933; P:histone H4 deacetylation; IDA:UniProtKB.
GO; GO:0043922; P:negative regulation by host of viral transcription; IDA:UniProtKB.
GO; GO:0032348; P:negative regulation of aldosterone biosynthetic process; IMP:UniProtKB.
GO; GO:2000798; P:negative regulation of amniotic stem cell differentiation; IMP:UniProtKB.
GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:2000065; P:negative regulation of cortisol biosynthetic process; IMP:UniProtKB.
GO; GO:2000706; P:negative regulation of dense core granule biogenesis; ISS:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:0046676; P:negative regulation of insulin secretion; IMP:UniProtKB.
GO; GO:2000740; P:negative regulation of mesenchymal stem cell differentiation; IMP:UniProtKB.
GO; GO:0050768; P:negative regulation of neurogenesis; ISS:UniProtKB.
GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
Gene3D; 2.40.155.10; -; 1.
InterPro; IPR009017; GFP.
InterPro; IPR027757; REST.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
PANTHER; PTHR45014; PTHR45014; 2.
SMART; SM00355; ZnF_C2H2; 9.
SUPFAM; SSF57667; SSF57667; 3.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Disease mutation; Metal-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 1097 RE1-silencing transcription factor.
/FTId=PRO_0000269547.
ZN_FING 159 181 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 216 238 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 248 270 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 276 298 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 304 326 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 332 355 C2H2-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 361 383 C2H2-type 7. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 389 412 C2H2-type 8. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 1060 1082 C2H2-type 9. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 32 122 Interaction with SIN3A.
{ECO:0000269|PubMed:10734093}.
REGION 43 57 Interaction with SIN3B.
{ECO:0000269|PubMed:16288918}.
REGION 145 418 Interaction with ZFP90.
{ECO:0000269|PubMed:21284946}.
REGION 1009 1087 Interaction with RCOR1.
COMPBIAS 11 14 Poly-Gly.
COMPBIAS 400 603 Lys-rich.
COMPBIAS 595 815 Pro-rich.
MOD_RES 864 864 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 971 971 Phosphoserine.
{ECO:0000250|UniProtKB:O54963}.
VAR_SEQ 301 313 ERPYKCELCPYSS -> KRSFLVHKFSSLF (in
isoform 2). {ECO:0000303|PubMed:7871435}.
/FTId=VSP_022064.
VAR_SEQ 304 326 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_022067.
VAR_SEQ 314 1097 Missing (in isoform 2).
{ECO:0000303|PubMed:7871435}.
/FTId=VSP_022065.
VAR_SEQ 329 329 E -> W (in isoform 3). {ECO:0000305}.
/FTId=VSP_022066.
VAR_SEQ 330 1097 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_022068.
VARIANT 160 160 R -> P (in WT6; inhibits transcriptional
repression activity).
{ECO:0000269|PubMed:26551668}.
/FTId=VAR_076333.
VARIANT 290 290 N -> Y (in WT6; inhibits transcriptional
repression activity).
{ECO:0000269|PubMed:26551668}.
/FTId=VAR_076334.
VARIANT 322 322 H -> R (in WT6; inhibits transcriptional
repression activity; dbSNP:rs869025312).
{ECO:0000269|PubMed:26551668}.
/FTId=VAR_076335.
VARIANT 412 412 H -> Q (in WT6).
{ECO:0000269|PubMed:26551668}.
/FTId=VAR_076336.
VARIANT 626 626 V -> I (in dbSNP:rs2228991).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_029795.
VARIANT 692 692 E -> D (in dbSNP:rs2227902).
/FTId=VAR_029796.
VARIANT 762 762 K -> Q (in dbSNP:rs2227903).
/FTId=VAR_029797.
VARIANT 797 797 P -> L (in dbSNP:rs3796529).
{ECO:0000269|PubMed:8568247}.
/FTId=VAR_029798.
MUTAGEN 91 91 E->G: Does not change transcriptional
repression activity.
{ECO:0000269|PubMed:26551668}.
MUTAGEN 420 420 M->T: Inhibits transcriptional repression
activity. {ECO:0000269|PubMed:26551668}.
MUTAGEN 593 593 S->N: Does not change transcriptional
repression activity.
{ECO:0000269|PubMed:26551668}.
MUTAGEN 642 642 A->T: Does not change transcriptional
repression activity.
{ECO:0000269|PubMed:26551668}.
MUTAGEN 918 918 H->Y: Does not change transcriptional
repression activity.
{ECO:0000269|PubMed:26551668}.
CONFLICT 295 295 V -> L (in Ref. 2; AAC50114).
{ECO:0000305}.
CONFLICT 596 599 PQKE -> SRNS (in Ref. 2; AAC50115).
{ECO:0000305}.
CONFLICT 630 630 P -> L (in Ref. 1; AAB17211).
{ECO:0000305}.
HELIX 44 55 {ECO:0000244|PDB:2CZY}.
SEQUENCE 1097 AA; 121872 MW; EBC652EED19CA161 CRC64;
MATQVMGQSS GGGGLFTSSG NIGMALPNDM YDLHDLSKAE LAAPQLIMLA NVALTGEVNG
SCCDYLVGEE RQMAELMPVG DNNFSDSEEG EGLEESADIK GEPHGLENME LRSLELSVVE
PQPVFEASGA PDIYSSNKDL PPETPGAEDK GKSSKTKPFR CKPCQYEAES EEQFVHHIRV
HSAKKFFVEE SAEKQAKARE SGSSTAEEGD FSKGPIRCDR CGYNTNRYDH YTAHLKHHTR
AGDNERVYKC IICTYTTVSE YHWRKHLRNH FPRKVYTCGK CNYFSDRKNN YVQHVRTHTG
ERPYKCELCP YSSSQKTHLT RHMRTHSGEK PFKCDQCSYV ASNQHEVTRH ARQVHNGPKP
LNCPHCDYKT ADRSNFKKHV ELHVNPRQFN CPVCDYAASK KCNLQYHFKS KHPTCPNKTM
DVSKVKLKKT KKREADLPDN ITNEKTEIEQ TKIKGDVAGK KNEKSVKAEK RDVSKEKKPS
NNVSVIQVTT RTRKSVTEVK EMDVHTGSNS EKFSKTKKSK RKLEVDSHSL HGPVNDEESS
TKKKKKVESK SKNNSQEVPK GDSKVEENKK QNTCMKKSTK KKTLKNKSSK KSSKPPQKEP
VEKGSAQMDP PQMGPAPTEA VQKGPVQVEP PPPMEHAQME GAQIRPAPDE PVQMEVVQEG
PAQKELLPPV EPAQMVGAQI VLAHMELPPP METAQTEVAQ MGPAPMEPAQ MEVAQVESAP
MQVVQKEPVQ MELSPPMEVV QKEPVQIELS PPMEVVQKEP VKIELSPPIE VVQKEPVQME
LSPPMGVVQK EPAQREPPPP REPPLHMEPI SKKPPLRKDK KEKSNMQSER ARKEQVLIEV
GLVPVKDSWL LKESVSTEDL SPPSPPLPKE NLREEASGDQ KLLNTGEGNK EAPLQKVGAE
EADESLPGLA ANINESTHIS SSGQNLNTPE GETLNGKHQT DSIVCEMKMD TDQNTRENLT
GINSTVEEPV SPMLPPSAVE EREAVSKTAL ASPPATMAAN ESQEIDEDEG IHSHEGSDLS
DNMSEGSDDS GLHGARPVPQ ESSRKNAKEA LAVKAAKGDF VCIFCDRSFR KGKDYSKHLN
RHLVNVYYLE EAAQGQE


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