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Q13127 (REST_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RE1-silencing transcription factor
Alternative name(s):
Neural-restrictive silencer factor
X2 box repressor
Gene names
Name:REST
Synonyms:NRSF, XBR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1097 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.2 Ref.3 Ref.11 Ref.13

Subunit structure

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. Ref.9 Ref.10 Ref.13 Ref.16

Subcellular location

Nucleus Probable.

Tissue specificity

Ubiquitous. Expressed at higher levels in the tissues of the lymphocytic compartment, including spleen, thymus, peripheral blood lymphocytes and ovary. Ref.3

Sequence similarities

Contains 9 C2H2-type zinc fingers.

Sequence caution

The sequence AAA98503.1 differs from that shown. Reason: Frameshift at positions 188, 198, 202, 212 and 1087.

The sequence AAC50114.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAC50115.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAH38985.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence BAD92987.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionRepressor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle cell myoblast differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to drug

Inferred from mutant phenotype PubMed 20564196. Source: UniProtKB

cellular response to electrical stimulus

Inferred from mutant phenotype PubMed 18570921. Source: UniProtKB

cellular response to glucocorticoid stimulus

Inferred from direct assay PubMed 17984088. Source: UniProtKB

histone H4 deacetylation

Inferred from direct assay PubMed 17555596. Source: UniProtKB

negative regulation by host of viral transcription

Inferred from direct assay PubMed 17555596. Source: UniProtKB

negative regulation of aldosterone biosynthetic process

Inferred from mutant phenotype PubMed 19342457. Source: UniProtKB

negative regulation of amniotic stem cell differentiation

Inferred from mutant phenotype PubMed 20942606. Source: UniProtKB

negative regulation of calcium ion-dependent exocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 20564196. Source: UniProtKB

negative regulation of cortisol biosynthetic process

Inferred from mutant phenotype PubMed 19342457. Source: UniProtKB

negative regulation of dense core granule biogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of gene expression

Inferred from mutant phenotype PubMed 20564196. Source: UniProtKB

negative regulation of insulin secretion

Inferred from mutant phenotype PubMed 20942606. Source: UniProtKB

negative regulation of mesenchymal stem cell differentiation

Inferred from mutant phenotype PubMed 18570921. Source: UniProtKB

negative regulation of neurogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of neuron differentiation

Inferred from mutant phenotype PubMed 18570921. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 21284946Ref.3. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.9Ref.10PubMed 17984088PubMed 19342457Ref.1. Source: UniProtKB

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 20564196. Source: UniProtKB

positive regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype PubMed 20564196. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 17984088. Source: UniProtKB

potassium ion transmembrane transport

Inferred from mutant phenotype PubMed 18570921. Source: GOC

regulation of transcription, DNA-templated

Non-traceable author statement Ref.2. Source: UniProtKB

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay Ref.10PubMed 16417580PubMed 17984088PubMed 19342457PubMed 21284946Ref.1. Source: UniProtKB

transcriptional repressor complex

Inferred from direct assay Ref.10. Source: UniProtKB

   Molecular_functionRNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription

Inferred from direct assay Ref.9Ref.10PubMed 21284946. Source: UniProtKB

chromatin binding

Inferred from sequence or structural similarity. Source: UniProtKB

core promoter binding

Inferred from direct assay PubMed 17984088. Source: UniProtKB

core promoter sequence-specific DNA binding

Inferred from direct assay Ref.3. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

outward rectifier potassium channel activity

Inferred from mutant phenotype PubMed 18570921. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 19342457. Source: UniProtKB

transcription factor binding

Inferred from physical interaction PubMed 17130167. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from direct assay PubMed 17555596. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SMARCA4P515322EBI-926706,EBI-302489

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q13127-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q13127-2)

The sequence of this isoform differs from the canonical sequence as follows:
     301-313: ERPYKCELCPYSS → KRSFLVHKFSSLF
     314-1097: Missing.
Isoform 3 (identifier: Q13127-3)

Also known as: N4;

The sequence of this isoform differs from the canonical sequence as follows:
     329-329: E → W
     330-1097: Missing.
Isoform 4 (identifier: Q13127-4)

The sequence of this isoform differs from the canonical sequence as follows:
     304-326: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10971097RE1-silencing transcription factor
PRO_0000269547

Regions

Zinc finger159 – 18123C2H2-type 1
Zinc finger216 – 23823C2H2-type 2
Zinc finger248 – 27023C2H2-type 3
Zinc finger276 – 29823C2H2-type 4
Zinc finger304 – 32623C2H2-type 5
Zinc finger332 – 35524C2H2-type 6
Zinc finger361 – 38323C2H2-type 7
Zinc finger389 – 41224C2H2-type 8
Zinc finger1060 – 108223C2H2-type 9
Region32 – 12291Interaction with SIN3A
Region43 – 5715Interaction with SIN3B
Region1009 – 108779Interaction with RCOR1
Compositional bias11 – 144Poly-Gly
Compositional bias400 – 603204Lys-rich
Compositional bias595 – 815221Pro-rich

Amino acid modifications

Modified residue8641Phosphoserine Ref.15

Natural variations

Alternative sequence301 – 31313ERPYK…CPYSS → KRSFLVHKFSSLF in isoform 2.
VSP_022064
Alternative sequence304 – 32623Missing in isoform 4.
VSP_022067
Alternative sequence314 – 1097784Missing in isoform 2.
VSP_022065
Alternative sequence3291E → W in isoform 3.
VSP_022066
Alternative sequence330 – 1097768Missing in isoform 3.
VSP_022068
Natural variant6261V → I. Ref.7
Corresponds to variant rs2228991 [ dbSNP | Ensembl ].
VAR_029795
Natural variant6921E → D.
Corresponds to variant rs2227902 [ dbSNP | Ensembl ].
VAR_029796
Natural variant7621K → Q.
Corresponds to variant rs2227903 [ dbSNP | Ensembl ].
VAR_029797
Natural variant7971P → L. Ref.3
Corresponds to variant rs3796529 [ dbSNP | Ensembl ].
VAR_029798

Experimental info

Sequence conflict2951V → L in AAC50114. Ref.2
Sequence conflict596 – 5994PQKE → SRNS in AAC50115. Ref.2
Sequence conflict6301P → L in AAB17211. Ref.1

Secondary structure

... 1097
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: EBC652EED19CA161

FASTA1,097121,872
        10         20         30         40         50         60 
MATQVMGQSS GGGGLFTSSG NIGMALPNDM YDLHDLSKAE LAAPQLIMLA NVALTGEVNG 

        70         80         90        100        110        120 
SCCDYLVGEE RQMAELMPVG DNNFSDSEEG EGLEESADIK GEPHGLENME LRSLELSVVE 

       130        140        150        160        170        180 
PQPVFEASGA PDIYSSNKDL PPETPGAEDK GKSSKTKPFR CKPCQYEAES EEQFVHHIRV 

       190        200        210        220        230        240 
HSAKKFFVEE SAEKQAKARE SGSSTAEEGD FSKGPIRCDR CGYNTNRYDH YTAHLKHHTR 

       250        260        270        280        290        300 
AGDNERVYKC IICTYTTVSE YHWRKHLRNH FPRKVYTCGK CNYFSDRKNN YVQHVRTHTG 

       310        320        330        340        350        360 
ERPYKCELCP YSSSQKTHLT RHMRTHSGEK PFKCDQCSYV ASNQHEVTRH ARQVHNGPKP 

       370        380        390        400        410        420 
LNCPHCDYKT ADRSNFKKHV ELHVNPRQFN CPVCDYAASK KCNLQYHFKS KHPTCPNKTM 

       430        440        450        460        470        480 
DVSKVKLKKT KKREADLPDN ITNEKTEIEQ TKIKGDVAGK KNEKSVKAEK RDVSKEKKPS 

       490        500        510        520        530        540 
NNVSVIQVTT RTRKSVTEVK EMDVHTGSNS EKFSKTKKSK RKLEVDSHSL HGPVNDEESS 

       550        560        570        580        590        600 
TKKKKKVESK SKNNSQEVPK GDSKVEENKK QNTCMKKSTK KKTLKNKSSK KSSKPPQKEP 

       610        620        630        640        650        660 
VEKGSAQMDP PQMGPAPTEA VQKGPVQVEP PPPMEHAQME GAQIRPAPDE PVQMEVVQEG 

       670        680        690        700        710        720 
PAQKELLPPV EPAQMVGAQI VLAHMELPPP METAQTEVAQ MGPAPMEPAQ MEVAQVESAP 

       730        740        750        760        770        780 
MQVVQKEPVQ MELSPPMEVV QKEPVQIELS PPMEVVQKEP VKIELSPPIE VVQKEPVQME 

       790        800        810        820        830        840 
LSPPMGVVQK EPAQREPPPP REPPLHMEPI SKKPPLRKDK KEKSNMQSER ARKEQVLIEV 

       850        860        870        880        890        900 
GLVPVKDSWL LKESVSTEDL SPPSPPLPKE NLREEASGDQ KLLNTGEGNK EAPLQKVGAE 

       910        920        930        940        950        960 
EADESLPGLA ANINESTHIS SSGQNLNTPE GETLNGKHQT DSIVCEMKMD TDQNTRENLT 

       970        980        990       1000       1010       1020 
GINSTVEEPV SPMLPPSAVE EREAVSKTAL ASPPATMAAN ESQEIDEDEG IHSHEGSDLS 

      1030       1040       1050       1060       1070       1080 
DNMSEGSDDS GLHGARPVPQ ESSRKNAKEA LAVKAAKGDF VCIFCDRSFR KGKDYSKHLN 

      1090 
RHLVNVYYLE EAAQGQE 

« Hide

Isoform 2 [UniParc].

Checksum: 3B0F550EBD70F79D
Show »

FASTA31335,048
Isoform 3 (N4) [UniParc].

Checksum: AD25D9BAC94FCAF7
Show »

FASTA32936,972
Isoform 4 [UniParc].

Checksum: 7D5F7CBD2C74EC0A
Show »

FASTA1,074119,083

References

« Hide 'large scale' references
[1]"REST: a mammalian silencer protein that restricts sodium channel gene expression to neurons."
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.
Cell 80:949-957(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
[2]"The neuron-restrictive silencer factor (NRSF): a coordinate repressor of multiple neuron-specific genes."
Schoenherr C.J., Anderson D.J.
Science 267:1360-1363(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 1-599 (ISOFORM 1), FUNCTION.
[3]"A zinc finger protein that represses transcription of the human MHC class II gene, DPA."
Scholl T., Stevens M.B., Mahanta S., Strominger J.L.
J. Immunol. 156:1448-1457(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, VARIANT LEU-797.
[4]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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
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. expand/collapse author list , 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.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ILE-626.
Tissue: Testis and Uterus.
[8]"Neuron-specific splicing of zinc finger transcription factor REST/NRSF/XBR is frequent in neuroblastomas and conserved in human, mouse and rat."
Palm K., Metsis M., Timmusk T.
Brain Res. Mol. Brain Res. 72:30-39(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS 3 AND 4).
[9]"CoREST: a functional corepressor required for regulation of neural-specific gene expression."
Andres M.E., Burger C., Peral-Rubio M.J., Battaglioli E., Anderson M.E., Grimes J., Dallman J., Ballas N., Mandel G.
Proc. Natl. Acad. Sci. U.S.A. 96:9873-9878(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RCOR1.
[10]"The co-repressor mSin3A is a functional component of the REST-CoREST repressor complex."
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.
J. Biol. Chem. 275:9461-9467(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RCOR1 AND SIN3A.
[11]"Corepressor-dependent silencing of chromosomal regions encoding neuronal genes."
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 298:1747-1752(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[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]"CDYL bridges REST and histone methyltransferases for gene repression and suppression of cellular transformation."
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.
Mol. Cell 32:718-726(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CDYL; EHMT1 AND EHMT2, IDENTIFICATION IN A COMPLEX WITH CDYL; SETB1; EHMT1; EHMT2 AND WIZ.
[14]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-864, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"The neural repressor NRSF/REST binds the PAH1 domain of the Sin3 corepressor by using its distinct short hydrophobic helix."
Nomura M., Uda-Tochio H., Murai K., Mori N., Nishimura Y.
J. Mol. Biol. 354:903-915(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 43-57 IN COMPLEX WITH SIN3B, INTERACTION WITH SIN3B.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U22314 mRNA. Translation: AAB17211.1.
U13877 mRNA. Translation: AAC50114.1. Different initiation.
U13879 mRNA. Translation: AAC50115.1. Different initiation.
U22680 mRNA. Translation: AAA98503.1. Frameshift.
AB209750 mRNA. Translation: BAD92987.1. Different initiation.
AC069307 Genomic DNA. No translation available.
CH471057 Genomic DNA. Translation: EAX05517.1.
BC038985 mRNA. Translation: AAH38985.1. Sequence problems.
BC132859 mRNA. Translation: AAI32860.1.
BC136491 mRNA. Translation: AAI36492.1.
PIRA56138.
I38754.
I38755.
RefSeqNP_001180437.1. NM_001193508.1.
NP_005603.3. NM_005612.4.
UniGeneHs.307836.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CZYNMR-B43-57[»]
ProteinModelPortalQ13127.
SMRQ13127. Positions 157-410.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111910. 35 interactions.
DIPDIP-35264N.
IntActQ13127. 3 interactions.
STRING9606.ENSP00000311816.

PTM databases

PhosphoSiteQ13127.

Polymorphism databases

DMDM296452989.

Proteomic databases

PaxDbQ13127.
PRIDEQ13127.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309042; ENSP00000311816; ENSG00000084093. [Q13127-1]
GeneID5978.
KEGGhsa:5978.
UCSCuc003hch.3. human. [Q13127-1]
uc031ser.1. human. [Q13127-2]
uc031ses.1. human. [Q13127-3]
uc031sex.1. human. [Q13127-4]

Organism-specific databases

CTD5978.
GeneCardsGC04P057689.
H-InvDBHIX0031381.
HGNCHGNC:9966. REST.
HPAHPA006079.
MIM600571. gene.
neXtProtNX_Q13127.
PharmGKBPA34334.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG271556.
HOVERGENHBG093893.
InParanoidQ13127.
KOK09222.
OMAVQKEPVQ.
OrthoDBEOG73FQM4.
PhylomeDBQ13127.
TreeFamTF332861.

Enzyme and pathway databases

SignaLinkQ13127.

Gene expression databases

BgeeQ13127.
CleanExHS_REST.
GenevestigatorQ13127.

Family and domain databases

Gene3D3.30.160.60. 4 hits.
InterProIPR027775. C2H2_Znf_fam.
IPR027757. REST.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PANTHERPTHR10032. PTHR10032. 1 hit.
PTHR10032:SF71. PTHR10032:SF71. 1 hit.
SMARTSM00355. ZnF_C2H2. 9 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSREST. human.
EvolutionaryTraceQ13127.
GeneWikiRE1-silencing_transcription_factor.
GenomeRNAi5978.
NextBio23267.
PROQ13127.
SOURCESearch...

Entry information

Entry nameREST_HUMAN
AccessionPrimary (citable) accession number: Q13127
Secondary accession number(s): A2RUE0 expand/collapse secondary AC list , B9EGJ0, Q12956, Q12957, Q13134, Q59ER1, Q8IWI3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM