REST_RAT
ID REST_RAT Reviewed; 1069 AA.
AC O54963; O54964;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=RE1-silencing transcription factor;
DE AltName: Full=Neural-restrictive silencer factor;
GN Name=Rest; Synonyms=Nrsf;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6 AND 7), FUNCTION,
RP TISSUE SPECIFICITY, INDUCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=9454838; DOI=10.1523/jneurosci.18-04-01280.1998;
RA Palm K., Belluardo N., Metsis M., Timmusk T.;
RT "Neuronal expression of zinc finger transcription factor REST/NRSF/XBR
RT gene.";
RL J. Neurosci. 18:1280-1296(1998).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=10490617; DOI=10.1128/mcb.19.10.6788;
RA Shimojo M., Paquette A.J., Anderson D.J., Hersh L.B.;
RT "Protein kinase A regulates cholinergic gene expression in PC12 cells:
RT REST4 silences the silencing activity of neuron-restrictive silencer
RT factor/REST.";
RL Mol. Cell. Biol. 19:6788-6795(1999).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY
RP ISCHEMIA.
RX PubMed=12657670; DOI=10.1523/jneurosci.23-06-02112.2003;
RA Calderone A., Jover T., Noh K.M., Tanaka H., Yokota H., Lin Y.,
RA Grooms S.Y., Regis R., Bennett M.V., Zukin R.S.;
RT "Ischemic insults derepress the gene silencer REST in neurons destined to
RT die.";
RL J. Neurosci. 23:2112-2121(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-948, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND INDUCTION.
RX PubMed=22960932; DOI=10.1038/nn.3214;
RA Rodenas-Ruano A., Chavez A.E., Cossio M.J., Castillo P.E., Zukin R.S.;
RT "REST-dependent epigenetic remodeling promotes the developmental switch in
RT synaptic NMDA receptors.";
RL Nat. Neurosci. 15:1382-1390(2012).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION BY
RP ISCHEMIA.
RX PubMed=22371606; DOI=10.1073/pnas.1121568109;
RA Noh K.M., Hwang J.Y., Follenzi A., Athanasiadou R., Miyawaki T.,
RA Greally J.M., Bennett M.V., Zukin R.S.;
RT "Repressor element-1 silencing transcription factor (REST)-dependent
RT epigenetic remodeling is critical to ischemia-induced neuronal death.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E962-E971(2012).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY ISCHEMIA.
RX PubMed=25108103; DOI=10.1016/j.jmb.2014.07.032;
RA Hwang J.Y., Kaneko N., Noh K.M., Pontarelli F., Zukin R.S.;
RT "The gene silencing transcription factor REST represses miR-132 expression
RT in hippocampal neurons destined to die.";
RL J. Mol. Biol. 426:3454-3466(2014).
CC -!- FUNCTION: Transcriptional repressor which binds neuron-restrictive
CC silencer element (NRSE) and represses neuronal gene transcription in
CC non-neuronal cells (By similarity). Restricts the expression of
CC neuronal genes by associating with two distinct corepressors, SIN3A and
CC RCOR1, which in turn recruit histone deacetylase to the promoters of
CC REST-regulated genes (By similarity). Mediates repression by recruiting
CC the BHC complex at RE1/NRSE sites which acts by deacetylating and
CC demethylating specific sites on histones, thereby acting as a chromatin
CC modifier (PubMed:9454838). Transcriptional repression by REST-CDYL via
CC the recruitment of histone methyltransferase EHMT2 may be important in
CC transformation suppression (By similarity). Represses the expression of
CC SRRM4 in non-neural cells to prevent the activation of neural-specific
CC splicing events and to prevent production of REST isoform 6 (By
CC similarity). Repressor activity may be inhibited by forming
CC heterodimers with isoform 6, thereby preventing binding to NRSE or
CC binding to corepressors and leading to derepression of target genes (By
CC similarity). Also maintains repression of neuronal genes in neural stem
CC cells, and allows transcription and differentiation into neurons by
CC dissociation from RE1/NRSE sites of target genes (By similarity).
CC Thereby is involved in maintaining the quiescent state of adult
CC hippocampal neural stem cells and preventing premature differentiation
CC into mature neurons (By similarity). Plays a role in the developmental
CC switch in synaptic NMDA receptor composition during postnatal
CC development, by repressing GRIN2B expression and thereby altering NMDA
CC receptor properties from containing primarily GRIN2B to primarily
CC GRIN2A subunits (PubMed:22960932). Acts as a regulator of osteoblast
CC differentiation (By similarity). Key repressor of gene expression in
CC hypoxia; represses genes in hypoxia by direct binding to an RE1/NRSE
CC site on their promoter regions (By similarity). May also function in
CC stress resistance in the brain during aging; possibly by regulating
CC expression of genes involved in cell death and in the stress response
CC (By similarity). Repressor of gene expression in the hippocampus after
CC ischemia by directly binding to RE1/NRSE sites and recruiting SIN3A and
CC RCOR1 to promoters of target genes, thereby promoting changes in
CC chromatin modifications and ischemia-induced cell death
CC (PubMed:22371606, PubMed:12657670). After ischemia, might play a role
CC in repression of miR-132 expression in hippocampal neurons, thereby
CC leading to neuronal cell death (PubMed:25108103).
CC {ECO:0000250|UniProtKB:Q13127, ECO:0000250|UniProtKB:Q8VIG1,
CC ECO:0000269|PubMed:12657670, ECO:0000269|PubMed:22371606,
CC ECO:0000269|PubMed:22960932, ECO:0000269|PubMed:25108103,
CC ECO:0000269|PubMed:9454838}.
CC -!- FUNCTION: [Isoform 6]: Binds to the 3' region of the neuron-restrictive
CC silencer element (NRSE), with lower affinity than full-length REST
CC isoform 1 (By similarity). Exhibits weaker repressor activity compared
CC to isoform 1 (By similarity). May negatively regulate the repressor
CC activity of isoform 1 by binding to isoform 1, thereby preventing its
CC binding to NRSE and leading to derepression of target genes (By
CC similarity). However, in another study, does not appear to be
CC implicated in repressor activity of a NRSE motif-containing reporter
CC construct nor in inhibitory activity on the isoform 1 transcriptional
CC repressor activity (By similarity). Post-transcriptional inactivation
CC of REST by SRRM4-dependent alternative splicing into isoform 6 is
CC required in mechanosensory hair cells in the inner ear for derepression
CC of neuronal genes and hearing (By similarity).
CC {ECO:0000250|UniProtKB:Q13127, ECO:0000250|UniProtKB:Q8VIG1}.
CC -!- SUBUNIT: Isoform 1 and isoform 6 form heterodimers (By similarity).
CC Isoform 6: Forms homodimers and homooligomers; binds to the neuron-
CC restrictive silencer element (NRSE) as monomer (By similarity).
CC Interacts with SIN3A, SIN3B and RCOR1 (By similarity). Interacts with
CC CDYL (By similarity). Interacts with EHMT1 and EHMT2 only in the
CC presence of CDYL (By similarity). Part of a complex containing at least
CC CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2 (By similarity). Interacts (via
CC zinc-finger DNA-binding domain) with ZFP90 (via N- and C-termini); the
CC interaction inhibits REST repressor activity (By similarity). Interacts
CC (via C2H2-type zinc finger 5) with PRICKLE1 (By similarity). Interacts
CC with FBXW11 and BTRC (By similarity). Interacts with USP7 (By
CC similarity). {ECO:0000250|UniProtKB:Q13127,
CC ECO:0000250|UniProtKB:Q8VIG1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10490617,
CC ECO:0000269|PubMed:12657670, ECO:0000269|PubMed:22371606,
CC ECO:0000269|PubMed:22960932}. Cytoplasm {ECO:0000250|UniProtKB:Q13127}.
CC Note=Colocalizes with ZFP90 in the nucleus (By similarity). In response
CC to hypoxia, there is a more pronounced increase in levels in the
CC nucleus as compared to the cytoplasm (By similarity). In aging neurons,
CC increased levels in the nucleus as compared to the cytoplasm (By
CC similarity). {ECO:0000250|UniProtKB:Q13127,
CC ECO:0000250|UniProtKB:Q8VIG1}.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Nucleus
CC {ECO:0000250|UniProtKB:Q13127}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=O54963-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O54963-2; Sequence=VSP_022074, VSP_022075;
CC Name=3; Synonyms=REST1;
CC IsoId=O54963-3; Sequence=VSP_022073;
CC Name=4; Synonyms=REST2;
CC IsoId=O54963-4; Sequence=VSP_022079, VSP_022080;
CC Name=5; Synonyms=REST3;
CC IsoId=O54963-5; Sequence=VSP_022078, VSP_022081;
CC Name=6; Synonyms=REST4;
CC IsoId=O54963-6; Sequence=VSP_022077, VSP_022082;
CC Name=7; Synonyms=REST5;
CC IsoId=O54963-7; Sequence=VSP_022076, VSP_022083;
CC -!- TISSUE SPECIFICITY: Expressed in the hippocampus including the granule
CC cell layer of the dentate gyrus, the pyramidal cell layers of CA1 and
CC CA3, the apical and basilar dendrite layers of the stratum radiatum and
CC stratum oriens of CA1, the stratum lucidum and stratum oriens of CA3
CC and in astroglia (at protein level) (PubMed:22960932, PubMed:22371606,
CC PubMed:12657670). Expressed in the brain, with the highest levels in
CC the neurons of hippocampus, pons/medulla and midbrain (PubMed:9454838,
CC PubMed:25108103). {ECO:0000269|PubMed:12657670,
CC ECO:0000269|PubMed:22371606, ECO:0000269|PubMed:22960932,
CC ECO:0000269|PubMed:25108103, ECO:0000269|PubMed:9454838}.
CC -!- DEVELOPMENTAL STAGE: Levels decrease during embryonic brain development
CC (PubMed:9454838). Expressed during postnatal days P3 to P60, with an
CC increase in expression at postnatal day P14-P15 (PubMed:22960932).
CC Increased abundance in the nucleus at P14-P15 relative to P9
CC (PubMed:22960932). {ECO:0000269|PubMed:22960932,
CC ECO:0000269|PubMed:9454838}.
CC -!- INDUCTION: Up-regulated by kainic acid (PubMed:9454838). Up-regulated
CC in the pyramidal cell layer of CA1 in the hippocampus by global
CC ischemia (PubMed:25108103, PubMed:22371606, PubMed:12657670). Down-
CC regulated in the hippocampus by maternal deprivation (PubMed:22960932).
CC {ECO:0000269|PubMed:12657670, ECO:0000269|PubMed:22371606,
CC ECO:0000269|PubMed:22960932, ECO:0000269|PubMed:25108103,
CC ECO:0000269|PubMed:9454838}.
CC -!- DOMAIN: The C2H2-type zinc finger 5 is required for nuclear
CC localization. {ECO:0000250|UniProtKB:Q13127}.
CC -!- PTM: O-glycosylated. {ECO:0000250|UniProtKB:Q8VIG1}.
CC -!- PTM: Phosphorylated; phosphorylation is required for ubiquitination.
CC {ECO:0000250|UniProtKB:Q13127}.
CC -!- PTM: Ubiquitinated; ubiquitination is mediated by BTRC and leads to
CC proteasomal degradation in G2 phase (By similarity). Ubiquitination
CC increases during neuronal differentiation (By similarity).
CC Deubiquitinated by USP7; leading to its stabilization and promoting the
CC maintenance of neural progenitor cells (By similarity).
CC {ECO:0000250|UniProtKB:Q13127}.
CC -!- MISCELLANEOUS: [Isoform 6]: Produced by SRRM4-dependent alternative
CC splicing in neurons and inner ear hair cells (By similarity). Lacks the
CC four C-terminal zinc fingers and the RCOR1 corepressor interaction site
CC found in full length REST isoform 1, which are required for full DNA-
CC binding and repressive activity (By similarity).
CC {ECO:0000250|UniProtKB:Q8VIG1}.
CC -!- CAUTION: Isoform 6: Controversial data exists concerning the repressor
CC activity of isoform 6. In human, a study showed that human isoform 3
CC exhibits weak repressor activity of a NRSE motif-containing reporter
CC construct (By similarity). Another report, however, does not observe
CC any isoform 3 repressor activity of a NRSE motif-containing reporter
CC construct (By similarity). Isoform 6: Controversial data also exists
CC regarding the function of isoform 6 on the negative regulation of
CC isoform 1. In mouse, it was shown that isoform 2 negatively regulates
CC the repressor activity of isoform 1 by binding to isoform 1, thereby
CC preventing its binding to NRSE and leading to derepression of target
CC genes (By similarity). Another study in human, however, did not observe
CC any inhibitory activity of human isoform 3 on the isoform 1
CC transcriptional repressor activity (By similarity).
CC {ECO:0000250|UniProtKB:Q13127, ECO:0000250|UniProtKB:Q8VIG1}.
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DR EMBL; AF037199; AAB94893.1; -; mRNA.
DR EMBL; AF037203; AAB94894.1; -; mRNA.
DR RefSeq; NP_113976.1; NM_031788.1. [O54963-1]
DR AlphaFoldDB; O54963; -.
DR BMRB; O54963; -.
DR SMR; O54963; -.
DR BioGRID; 249783; 2.
DR STRING; 10116.ENSRNOP00000002837; -.
DR CarbonylDB; O54963; -.
DR iPTMnet; O54963; -.
DR PhosphoSitePlus; O54963; -.
DR PaxDb; O54963; -.
DR PRIDE; O54963; -.
DR GeneID; 83618; -.
DR KEGG; rno:83618; -.
DR UCSC; RGD:621069; rat. [O54963-1]
DR CTD; 5978; -.
DR RGD; 621069; Rest.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; O54963; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; O54963; -.
DR PRO; PR:O54963; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0000785; C:chromatin; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0017053; C:transcription repressor complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; ISS:UniProtKB.
DR GO; GO:0060379; P:cardiac muscle cell myoblast differentiation; ISS:UniProtKB.
DR GO; GO:0071257; P:cellular response to electrical stimulus; ISS:UniProtKB.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISS:UniProtKB.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISS:UniProtKB.
DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; ISS:UniProtKB.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:RGD.
DR GO; GO:0070933; P:histone H4 deacetylation; ISS:UniProtKB.
DR GO; GO:0099563; P:modification of synaptic structure; IMP:UniProtKB.
DR GO; GO:0043922; P:negative regulation by host of viral transcription; ISS:UniProtKB.
DR GO; GO:0032348; P:negative regulation of aldosterone biosynthetic process; IMP:UniProtKB.
DR GO; GO:2000798; P:negative regulation of amniotic stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0045955; P:negative regulation of calcium ion-dependent exocytosis; IMP:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:2000065; P:negative regulation of cortisol biosynthetic process; IMP:UniProtKB.
DR GO; GO:2000706; P:negative regulation of dense core granule biogenesis; IMP:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0046676; P:negative regulation of insulin secretion; ISS:UniProtKB.
DR GO; GO:2000740; P:negative regulation of mesenchymal stem cell differentiation; ISO:RGD.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; ISO:RGD.
DR GO; GO:0050768; P:negative regulation of neurogenesis; ISS:UniProtKB.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:RGD.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IEP:RGD.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:1903223; P:positive regulation of oxidative stress-induced neuron death; IMP:UniProtKB.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0045667; P:regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:1903203; P:regulation of oxidative stress-induced neuron death; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR GO; GO:0002931; P:response to ischemia; IDA:UniProtKB.
DR GO; GO:0035019; P:somatic stem cell population maintenance; ISS:UniProtKB.
DR InterPro; IPR027757; REST.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24403:SF64; PTHR24403:SF64; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1069
FT /note="RE1-silencing transcription factor"
FT /id="PRO_0000269549"
FT ZN_FING 158..180
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 215..237
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 247..269
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 275..297
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 303..325
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 331..354
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 360..382
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 388..411
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1032..1054
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 32..121
FT /note="Interaction with SIN3A"
FT /evidence="ECO:0000250|UniProtKB:Q13127"
FT REGION 43..57
FT /note="Interaction with SIN3B"
FT /evidence="ECO:0000250|UniProtKB:Q13127"
FT REGION 85..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..417
FT /note="Interaction with ZFP90"
FT /evidence="ECO:0000250|UniProtKB:Q13127"
FT REGION 200..211
FT /note="Required for binding to the neuron-restrictive
FT silencer element"
FT /evidence="ECO:0000250|UniProtKB:Q8VIG1"
FT REGION 425..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 981..1059
FT /note="Interaction with RCOR1"
FT /evidence="ECO:0000250|UniProtKB:Q13127"
FT COMPBIAS 86..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..582
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 667..737
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..864
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..940
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..993
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 948
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 300..1069
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9454838"
FT /id="VSP_022073"
FT VAR_SEQ 300..302
FT /note="ERP -> KRA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9454838"
FT /id="VSP_022074"
FT VAR_SEQ 303..1069
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9454838"
FT /id="VSP_022075"
FT VAR_SEQ 328..336
FT /note="EKPFKCDQC -> CDLVGYVFR (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:9454838"
FT /id="VSP_022076"
FT VAR_SEQ 328..332
FT /note="EKPFK -> CDLVG (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:9454838"
FT /id="VSP_022077"
FT VAR_SEQ 328..329
FT /note="EK -> AI (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:9454838"
FT /id="VSP_022078"
FT VAR_SEQ 328
FT /note="E -> W (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9454838"
FT /id="VSP_022079"
FT VAR_SEQ 329..1069
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:9454838"
FT /id="VSP_022080"
FT VAR_SEQ 330..1069
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:9454838"
FT /id="VSP_022081"
FT VAR_SEQ 333..1069
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:9454838"
FT /id="VSP_022082"
FT VAR_SEQ 337..1069
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:9454838"
FT /id="VSP_022083"
SQ SEQUENCE 1069 AA; 117126 MW; 0A040248D8526992 CRC64;
MATQVMGQSS GGGSLFNNSG NMGMALPNDM YDLHDLSKAE LAAPQLIMLA NVALTGEVNG
SCCDYLVGEE RQMAELMPVG DNHFSDSEGE GLEESAELKG DPSGLDNMEL RSLELSVVEP
QPVFEASAAP EVYSSNKDPA PEAPVAEDKC KNLKAKPFRC KPCQYEAESE EQFVHHIRVH
SAKKFFVEES AEKQAKARES GASPSEEGEF SKGPIRCDRC GYNTNRYDHY TAHLKHHLRA
GDNERVYKCI ICTYTTVSEY HWRKHLRNHF PRKVYTCSKC NYFSTEKNNY VQHVRTHTGE
RPYKCELCPY SSSQKTHLTR HMRTHSGEKP FKCDQCNYVA SNQHEVTRHA RQVHNGPKPL
NCPHCDYKTA DRSNFKKHVE LHVNPRQFNC PVCDYAASKK CNLQYHFKSK HPTCPSKTMD
VSKVKLKKTK RREADLHRDA AAAATEQTDT EQAKTKGVDA SARRSERPVK GVGKDVPKEK
KPCSNASVVQ VTTRTRKSAV ETKAAEGKHT DGQTGNNAEK SSKAKKSKRK MDAEAHPSVE
PVTEGPVTKK KKTESKPKTS GEVPKGSRVE DRKADKQQSA SIKKGGKKTA LKTKTAKKGS
KLAPKWVGHT EPSSEMAQGG ESPVPALTQA VVTPSGSTQT ELSSPMDIAQ TEPAQMDVSQ
TGPPQVQRPL PVEPAQLEPS PPQEPPQVEP PACVEPPPPV EPPCPMEPAE MEPSPPMEPS
QVEPPPHLEP PLPMELPQVE LPPVEDCQKE LPPVEHAQTK VAQTGPTQVG AVQEEPLFCL
RATSSQANQK VISPKDRAKE KLSVLSEMAR QEQVLIEVGL VPVRDSQLLK ASKSAPDLPA
PPSPLPKGHL RREETPKDQE MFSDGEGNKV SPLEKGGTEE AGESRAELAA PMESTSALSS
EQSSNAPDGE TLHSECQADS TAVCEMEVDT EQKTDRVPLK DSAVEPVSPL NPRVDPEAAA
PAVVASPPIT LAESQEIDED EGIHSHDGSD LSDNMSEGSD DSGLHGARPA PQEATSKSGK
EGLAVKVTEG EFVCIFCDRS FRKEKDYSKH LNRHLVNVYF LEEAAEEQE
