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Entry version 145 (29 Sep 2021)
Sequence version 1 (01 Jun 1998)
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Protein

RE1-silencing transcription factor

Gene

Rest

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Transcriptional repressor which binds neuron-restrictive silencer element (NRSE) and represses neuronal gene transcription in non-neuronal cells (By similarity).

Restricts the expression of neuronal genes by associating with two distinct corepressors, SIN3A and RCOR1, which in turn recruit histone deacetylase to the promoters of REST-regulated genes (By similarity).

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 (PubMed:9454838).

Transcriptional repression by REST-CDYL via the recruitment of histone methyltransferase EHMT2 may be important in transformation suppression (By similarity).

Represses the expression of SRRM4 in non-neural cells to prevent the activation of neural-specific splicing events and to prevent production of REST isoform 6 (By similarity).

Repressor activity may be inhibited by forming heterodimers with isoform 6, thereby preventing binding to NRSE or binding to corepressors and leading to derepression of target genes (By similarity).

Also maintains repression of neuronal genes in neural stem cells, and allows transcription and differentiation into neurons by dissociation from RE1/NRSE sites of target genes (By similarity).

Thereby is involved in maintaining the quiescent state of adult hippocampal neural stem cells and preventing premature differentiation into mature neurons (By similarity).

Plays a role in the developmental switch in synaptic NMDA receptor composition during postnatal development, by repressing GRIN2B expression and thereby altering NMDA receptor properties from containing primarily GRIN2B to primarily GRIN2A subunits (PubMed:22960932).

Acts as a regulator of osteoblast differentiation (By similarity).

Key repressor of gene expression in hypoxia; represses genes in hypoxia by direct binding to an RE1/NRSE site on their promoter regions (By similarity).

May also function in stress resistance in the brain during aging; possibly by regulating expression of genes involved in cell death and in the stress response (By similarity).

Repressor of gene expression in the hippocampus after ischemia by directly binding to RE1/NRSE sites and recruiting SIN3A and RCOR1 to promoters of target genes, thereby promoting changes in chromatin modifications and ischemia-induced cell death (PubMed:22371606, PubMed:12657670).

After ischemia, might play a role in repression of miR-132 expression in hippocampal neurons, thereby leading to neuronal cell death (PubMed:25108103).

By similarity5 Publications

Binds to the 3' region of the neuron-restrictive silencer element (NRSE), with lower affinity than full-length REST isoform 1 (By similarity).

Exhibits weaker repressor activity compared to isoform 1 (By similarity).

May negatively regulate the repressor activity of isoform 1 by binding to isoform 1, thereby preventing its binding to NRSE and leading to derepression of target genes (By similarity).

However, in another study, does not appear to be implicated in repressor activity of a NRSE motif-containing reporter construct nor in inhibitory activity on the isoform 1 transcriptional repressor activity (By similarity).

Post-transcriptional inactivation of REST by SRRM4-dependent alternative splicing into isoform 6 is required in mechanosensory hair cells in the inner ear for derepression of neuronal genes and hearing (By similarity).

By similarity

Caution

Isoform 6: Controversial data exists concerning the repressor activity of isoform 6. In human, a study showed that human isoform 3 exhibits weak repressor activity of a NRSE motif-containing reporter construct (By similarity). Another report, however, does not observe any isoform 3 repressor activity of a NRSE motif-containing reporter construct (By similarity). Isoform 6: Controversial data also exists regarding the function of isoform 6 on the negative regulation of isoform 1. In mouse, it was shown that isoform 2 negatively regulates the repressor activity of isoform 1 by binding to isoform 1, thereby preventing its binding to NRSE and leading to derepression of target genes (By similarity). Another study in human, however, did not observe any inhibitory activity of human isoform 3 on the isoform 1 transcriptional repressor activity (By similarity).By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri158 – 180C2H2-type 1PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri215 – 237C2H2-type 2PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri247 – 269C2H2-type 3PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri275 – 297C2H2-type 4PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri303 – 325C2H2-type 5PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri331 – 354C2H2-type 6PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri360 – 382C2H2-type 7PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri388 – 411C2H2-type 8PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri1032 – 1054C2H2-type 9PROSITE-ProRule annotationAdd BLAST23

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionRepressor
Biological processTranscription, Transcription regulation
LigandMetal-binding, Zinc

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
RE1-silencing transcription factor
Alternative name(s):
Neural-restrictive silencer factor
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Rest
Synonyms:Nrsf
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
621069, Rest

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002695491 – 1069RE1-silencing transcription factorAdd BLAST1069

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei948PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

O-glycosylated.By similarity
Phosphorylated; phosphorylation is required for ubiquitination.By similarity
Ubiquitinated; ubiquitination is mediated by BTRC and leads to proteasomal degradation in G2 phase (By similarity). Ubiquitination increases during neuronal differentiation (By similarity). Deubiquitinated by USP7; leading to its stabilization and promoting the maintenance of neural progenitor cells (By similarity).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
O54963

PRoteomics IDEntifications database

More...
PRIDEi
O54963

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
O54963

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O54963

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
O54963

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in the hippocampus including the granule cell layer of the dentate gyrus, the pyramidal cell layers of CA1 and CA3, the apical and basilar dendrite layers of the stratum radiatum and stratum oriens of CA1, the stratum lucidum and stratum oriens of CA3 and in astroglia (at protein level) (PubMed:22960932, PubMed:22371606, PubMed:12657670). Expressed in the brain, with the highest levels in the neurons of hippocampus, pons/medulla and midbrain (PubMed:9454838, PubMed:25108103).5 Publications

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Levels decrease during embryonic brain development (PubMed:9454838). Expressed during postnatal days P3 to P60, with an increase in expression at postnatal day P14-P15 (PubMed:22960932). Increased abundance in the nucleus at P14-P15 relative to P9 (PubMed:22960932).2 Publications

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by kainic acid (PubMed:9454838). Up-regulated in the pyramidal cell layer of CA1 in the hippocampus by global ischemia (PubMed:25108103, PubMed:22371606, PubMed:12657670). Down-regulated in the hippocampus by maternal deprivation (PubMed:22960932).5 Publications

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Isoform 1 and isoform 6 form heterodimers (By similarity). Isoform 6: Forms homodimers and homooligomers; binds to the neuron-restrictive silencer element (NRSE) as monomer (By similarity).

Interacts with SIN3A, SIN3B and RCOR1 (By similarity).

Interacts with CDYL (By similarity).

Interacts with EHMT1 and EHMT2 only in the presence of CDYL (By similarity).

Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2 (By similarity).

Interacts (via zinc-finger DNA-binding domain) with ZFP90 (via N- and C-termini); the interaction inhibits REST repressor activity (By similarity).

Interacts (via C2H2-type zinc finger 5) with PRICKLE1 (By similarity).

Interacts with FBXW11 and BTRC (By similarity).

Interacts with USP7 (By similarity).

By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
249783, 2 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000002837

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Biological Magnetic Resonance Data Bank

More...
BMRBi
O54963

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
O54963

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni32 – 121Interaction with SIN3ABy similarityAdd BLAST90
Regioni43 – 57Interaction with SIN3BBy similarityAdd BLAST15
Regioni85 – 104DisorderedSequence analysisAdd BLAST20
Regioni144 – 417Interaction with ZFP90By similarityAdd BLAST274
Regioni200 – 211Required for binding to the neuron-restrictive silencer elementBy similarityAdd BLAST12
Regioni425 – 737DisorderedSequence analysisAdd BLAST313
Regioni830 – 1022DisorderedSequence analysisAdd BLAST193
Regioni981 – 1059Interaction with RCOR1By similarityAdd BLAST79

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi86 – 100Basic and acidic residuesSequence analysisAdd BLAST15
Compositional biasi425 – 444Basic and acidic residuesSequence analysisAdd BLAST20
Compositional biasi452 – 481Basic and acidic residuesSequence analysisAdd BLAST30
Compositional biasi521 – 537Basic and acidic residuesSequence analysisAdd BLAST17
Compositional biasi545 – 582Basic and acidic residuesSequence analysisAdd BLAST38
Compositional biasi628 – 666Polar residuesSequence analysisAdd BLAST39
Compositional biasi667 – 737Pro residuesSequence analysisAdd BLAST71
Compositional biasi847 – 864Basic and acidic residuesSequence analysisAdd BLAST18
Compositional biasi893 – 918Polar residuesSequence analysisAdd BLAST26
Compositional biasi926 – 940Basic and acidic residuesSequence analysisAdd BLAST15
Compositional biasi977 – 993Basic and acidic residuesSequence analysisAdd BLAST17

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The C2H2-type zinc finger 5 is required for nuclear localization.By similarity

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri158 – 180C2H2-type 1PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri215 – 237C2H2-type 2PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri247 – 269C2H2-type 3PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri275 – 297C2H2-type 4PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri303 – 325C2H2-type 5PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri331 – 354C2H2-type 6PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri360 – 382C2H2-type 7PROSITE-ProRule annotationAdd BLAST23
Zinc fingeri388 – 411C2H2-type 8PROSITE-ProRule annotationAdd BLAST24
Zinc fingeri1032 – 1054C2H2-type 9PROSITE-ProRule annotationAdd BLAST23

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1721, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O54963

Database of Orthologous Groups

More...
OrthoDBi
1318335at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O54963

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR027757, REST
IPR036236, Znf_C2H2_sf
IPR013087, Znf_C2H2_type

The PANTHER Classification System

More...
PANTHERi
PTHR24403:SF64, PTHR24403:SF64, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00355, ZnF_C2H2, 9 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF57667, SSF57667, 3 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00028, ZINC_FINGER_C2H2_1, 1 hit
PS50157, ZINC_FINGER_C2H2_2, 6 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (7+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 7 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 7 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O54963-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MATQVMGQSS GGGSLFNNSG NMGMALPNDM YDLHDLSKAE LAAPQLIMLA
60 70 80 90 100
NVALTGEVNG SCCDYLVGEE RQMAELMPVG DNHFSDSEGE GLEESAELKG
110 120 130 140 150
DPSGLDNMEL RSLELSVVEP QPVFEASAAP EVYSSNKDPA PEAPVAEDKC
160 170 180 190 200
KNLKAKPFRC KPCQYEAESE EQFVHHIRVH SAKKFFVEES AEKQAKARES
210 220 230 240 250
GASPSEEGEF SKGPIRCDRC GYNTNRYDHY TAHLKHHLRA GDNERVYKCI
260 270 280 290 300
ICTYTTVSEY HWRKHLRNHF PRKVYTCSKC NYFSTEKNNY VQHVRTHTGE
310 320 330 340 350
RPYKCELCPY SSSQKTHLTR HMRTHSGEKP FKCDQCNYVA SNQHEVTRHA
360 370 380 390 400
RQVHNGPKPL NCPHCDYKTA DRSNFKKHVE LHVNPRQFNC PVCDYAASKK
410 420 430 440 450
CNLQYHFKSK HPTCPSKTMD VSKVKLKKTK RREADLHRDA AAAATEQTDT
460 470 480 490 500
EQAKTKGVDA SARRSERPVK GVGKDVPKEK KPCSNASVVQ VTTRTRKSAV
510 520 530 540 550
ETKAAEGKHT DGQTGNNAEK SSKAKKSKRK MDAEAHPSVE PVTEGPVTKK
560 570 580 590 600
KKTESKPKTS GEVPKGSRVE DRKADKQQSA SIKKGGKKTA LKTKTAKKGS
610 620 630 640 650
KLAPKWVGHT EPSSEMAQGG ESPVPALTQA VVTPSGSTQT ELSSPMDIAQ
660 670 680 690 700
TEPAQMDVSQ TGPPQVQRPL PVEPAQLEPS PPQEPPQVEP PACVEPPPPV
710 720 730 740 750
EPPCPMEPAE MEPSPPMEPS QVEPPPHLEP PLPMELPQVE LPPVEDCQKE
760 770 780 790 800
LPPVEHAQTK VAQTGPTQVG AVQEEPLFCL RATSSQANQK VISPKDRAKE
810 820 830 840 850
KLSVLSEMAR QEQVLIEVGL VPVRDSQLLK ASKSAPDLPA PPSPLPKGHL
860 870 880 890 900
RREETPKDQE MFSDGEGNKV SPLEKGGTEE AGESRAELAA PMESTSALSS
910 920 930 940 950
EQSSNAPDGE TLHSECQADS TAVCEMEVDT EQKTDRVPLK DSAVEPVSPL
960 970 980 990 1000
NPRVDPEAAA PAVVASPPIT LAESQEIDED EGIHSHDGSD LSDNMSEGSD
1010 1020 1030 1040 1050
DSGLHGARPA PQEATSKSGK EGLAVKVTEG EFVCIFCDRS FRKEKDYSKH
1060
LNRHLVNVYF LEEAAEEQE
Length:1,069
Mass (Da):117,126
Last modified:June 1, 1998 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i0A040248D8526992
GO
Isoform 2 (identifier: O54963-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     300-302: ERP → KRA
     303-1069: Missing.

Show »
Length:302
Mass (Da):33,808
Checksum:i8B2E58D2A3030930
GO
Isoform 3 (identifier: O54963-3) [UniParc]FASTAAdd to basket
Also known as: REST1

The sequence of this isoform differs from the canonical sequence as follows:
     300-1069: Missing.

Show »
Length:299
Mass (Da):33,452
Checksum:iA2A3030930AE9F9E
GO
Isoform 4 (identifier: O54963-4) [UniParc]FASTAAdd to basket
Also known as: REST2

The sequence of this isoform differs from the canonical sequence as follows:
     328-328: E → W
     329-1069: Missing.

Show »
Length:328
Mass (Da):36,954
Checksum:iF756C8D12253B085
GO
Isoform 5 (identifier: O54963-5) [UniParc]FASTAAdd to basket
Also known as: REST3

The sequence of this isoform differs from the canonical sequence as follows:
     328-329: EK → AI
     330-1069: Missing.

Show »
Length:329
Mass (Da):36,952
Checksum:iBFA9F6C8D12253B0
GO
Isoform 6 (identifier: O54963-6) [UniParc]FASTAAdd to basket
Also known as: REST4

The sequence of this isoform differs from the canonical sequence as follows:
     328-332: EKPFK → CDLVG
     333-1069: Missing.

Note: Produced by SRRM4-dependent alternative splicing in neurons and inner ear hair cells (By similarity). Lacks the four C-terminal zinc fingers and the RCOR1 corepressor interaction site found in full length REST isoform 1, which are required for full DNA-binding and repressive activity (By similarity).By similarity
Show »
Length:332
Mass (Da):37,256
Checksum:i5D77E2F55A96C8D1
GO
Isoform 7 (identifier: O54963-7) [UniParc]FASTAAdd to basket
Also known as: REST5

The sequence of this isoform differs from the canonical sequence as follows:
     328-336: EKPFKCDQC → CDLVGYVFR
     337-1069: Missing.

Show »
Length:336
Mass (Da):37,821
Checksum:i0D2FCBF5DD77E2F5
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D4A7T2D4A7T2_RAT
RE1-silencing transcription factor
Rest
1,086Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F1M9A3F1M9A3_RAT
RE1-silencing transcription factor
Rest
1,068Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_022073300 – 1069Missing in isoform 3. 1 PublicationAdd BLAST770
Alternative sequenceiVSP_022074300 – 302ERP → KRA in isoform 2. 1 Publication3
Alternative sequenceiVSP_022075303 – 1069Missing in isoform 2. 1 PublicationAdd BLAST767
Alternative sequenceiVSP_022076328 – 336EKPFKCDQC → CDLVGYVFR in isoform 7. 1 Publication9
Alternative sequenceiVSP_022077328 – 332EKPFK → CDLVG in isoform 6. 1 Publication5
Alternative sequenceiVSP_022078328 – 329EK → AI in isoform 5. 1 Publication2
Alternative sequenceiVSP_022079328E → W in isoform 4. 1 Publication1
Alternative sequenceiVSP_022080329 – 1069Missing in isoform 4. 1 PublicationAdd BLAST741
Alternative sequenceiVSP_022081330 – 1069Missing in isoform 5. 1 PublicationAdd BLAST740
Alternative sequenceiVSP_022082333 – 1069Missing in isoform 6. 1 PublicationAdd BLAST737
Alternative sequenceiVSP_022083337 – 1069Missing in isoform 7. 1 PublicationAdd BLAST733

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF037199 mRNA Translation: AAB94893.1
AF037203 mRNA Translation: AAB94894.1

NCBI Reference Sequences

More...
RefSeqi
NP_113976.1, NM_031788.1 [O54963-1]

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
83618

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:83618

UCSC genome browser

More...
UCSCi
RGD:621069, rat [O54963-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF037199 mRNA Translation: AAB94893.1
AF037203 mRNA Translation: AAB94894.1
RefSeqiNP_113976.1, NM_031788.1 [O54963-1]

3D structure databases

BMRBiO54963
SMRiO54963
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi249783, 2 interactors
STRINGi10116.ENSRNOP00000002837

PTM databases

CarbonylDBiO54963
iPTMnetiO54963
PhosphoSitePlusiO54963

Proteomic databases

PaxDbiO54963
PRIDEiO54963

Genome annotation databases

GeneIDi83618
KEGGirno:83618
UCSCiRGD:621069, rat [O54963-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5978
RGDi621069, Rest

Phylogenomic databases

eggNOGiKOG1721, Eukaryota
InParanoidiO54963
OrthoDBi1318335at2759
PhylomeDBiO54963

Miscellaneous databases

Protein Ontology

More...
PROi
PR:O54963

Family and domain databases

InterProiView protein in InterPro
IPR027757, REST
IPR036236, Znf_C2H2_sf
IPR013087, Znf_C2H2_type
PANTHERiPTHR24403:SF64, PTHR24403:SF64, 1 hit
SMARTiView protein in SMART
SM00355, ZnF_C2H2, 9 hits
SUPFAMiSSF57667, SSF57667, 3 hits
PROSITEiView protein in PROSITE
PS00028, ZINC_FINGER_C2H2_1, 1 hit
PS50157, ZINC_FINGER_C2H2_2, 6 hits

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiREST_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O54963
Secondary accession number(s): O54964
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: June 1, 1998
Last modified: September 29, 2021
This is version 145 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome
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