Q13127 (REST_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RE1-silencing transcription factor

Alternative name(s):
Neural-restrictive silencer factor
X2 box repressor

Gene names

Name:	REST
Synonyms:	NRSF, XBR

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1097 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.1 Ref.2 Ref.3 Ref.11
Subunit structure	Interacts with SIN3A, SIN3B and RCOR1. Ref.9 Ref.10 Ref.14
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 process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cardiac 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 insulin secretion Inferred from mutant phenotype PubMed 20942606. 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 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-dependent Inferred from direct assay PubMed 17984088. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA cytosol Inferred from electronic annotation. Source: Compara transcriptional repressor complex Inferred from direct assay Ref.10. Source: UniProtKB
Molecular_function	RNA 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 sequence-specific DNA binding Inferred from direct assay Ref.3. Source: UniProtKB outward rectifier potassium channel activity Inferred from mutant phenotype PubMed 18570921. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SMARCA4	P51532	2	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1097

1097

RE1-silencing transcription factor

PRO_0000269547

Regions

Zinc finger

159 – 181

23

C2H2-type 1

Zinc finger

216 – 238

23

C2H2-type 2

Zinc finger

248 – 270

23

C2H2-type 3

Zinc finger

276 – 298

23

C2H2-type 4

Zinc finger

304 – 326

23

C2H2-type 5

Zinc finger

332 – 355

24

C2H2-type 6

Zinc finger

361 – 383

23

C2H2-type 7

Zinc finger

389 – 412

24

C2H2-type 8

Zinc finger

1060 – 1082

23

C2H2-type 9

Region

32 – 122

91

Interaction with SIN3A

Region

43 – 57

15

Interaction with SIN3B

Region

1009 – 1087

79

Interaction with RCOR1

Compositional bias

11 – 14

4

Poly-Gly

Compositional bias

400 – 603

204

Lys-rich

Compositional bias

595 – 815

221

Pro-rich

Amino acid modifications

Modified residue

864

1

Phosphoserine Ref.13

Natural variations

Alternative sequence

301 – 313

13

ERPYK…CPYSS → KRSFLVHKFSSLF in isoform 2.

VSP_022064

Alternative sequence

304 – 326

23

Missing in isoform 4.

VSP_022067

Alternative sequence

314 – 1097

784

Missing in isoform 2.

VSP_022065

Alternative sequence

329

1

E → W in isoform 3.

VSP_022066

Alternative sequence

330 – 1097

768

Missing in isoform 3.

VSP_022068

Natural variant

626

1

V → I. Ref.7
Corresponds to variant rs2228991 [ dbSNP | Ensembl ].

VAR_029795

Natural variant

692

1

E → D.
Corresponds to variant rs2227902 [ dbSNP | Ensembl ].

VAR_029796

Natural variant

762

1

K → Q.
Corresponds to variant rs2227903 [ dbSNP | Ensembl ].

VAR_029797

Natural variant

797

1

P → L. Ref.3
Corresponds to variant rs3796529 [ dbSNP | Ensembl ].

VAR_029798

Experimental info

Sequence conflict

295

1

V → L in AAC50114. Ref.2

Sequence conflict

596 – 599

4

PQKE → SRNS in AAC50115. Ref.2

Sequence conflict

630

1

P → L in AAB17211. Ref.1

Secondary structure

1

.

.

.

1097

Helix Strand Turn

Details...

Helix

44 – 55

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 18, 2010. Version 3. Checksum: EBC652EED19CA161	FASTA	1,097	121,872
	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
	Isoform 2 [UniParc]. Checksum: 3B0F550EBD70F79D	FASTA	313	35,048
	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 KRSFLVHKFS SLF
	Isoform 3 (N4) [UniParc]. Checksum: AD25D9BAC94FCAF7	FASTA	329	36,972
	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 ERPYKCELCP YSSSQKTHLT RHMRTHSGW
	Isoform 4 [UniParc]. Checksum: 7D5F7CBD2C74EC0A	FASTA	1,074	119,083
	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 ERPSGEKPFK CDQCSYVASN QHEVTRHARQ VHNGPKPLNC PHCDYKTADR SNFKKHVELH 370 380 390 400 410 420 VNPRQFNCPV CDYAASKKCN LQYHFKSKHP TCPNKTMDVS KVKLKKTKKR EADLPDNITN 430 440 450 460 470 480 EKTEIEQTKI KGDVAGKKNE KSVKAEKRDV SKEKKPSNNV SVIQVTTRTR KSVTEVKEMD 490 500 510 520 530 540 VHTGSNSEKF SKTKKSKRKL EVDSHSLHGP VNDEESSTKK KKKVESKSKN NSQEVPKGDS 550 560 570 580 590 600 KVEENKKQNT CMKKSTKKKT LKNKSSKKSS KPPQKEPVEK GSAQMDPPQM GPAPTEAVQK 610 620 630 640 650 660 GPVQVEPPPP MEHAQMEGAQ IRPAPDEPVQ MEVVQEGPAQ KELLPPVEPA QMVGAQIVLA 670 680 690 700 710 720 HMELPPPMET AQTEVAQMGP APMEPAQMEV AQVESAPMQV VQKEPVQMEL SPPMEVVQKE 730 740 750 760 770 780 PVQIELSPPM EVVQKEPVKI ELSPPIEVVQ KEPVQMELSP PMGVVQKEPA QREPPPPREP 790 800 810 820 830 840 PLHMEPISKK PPLRKDKKEK SNMQSERARK EQVLIEVGLV PVKDSWLLKE SVSTEDLSPP 850 860 870 880 890 900 SPPLPKENLR EEASGDQKLL NTGEGNKEAP LQKVGAEEAD ESLPGLAANI NESTHISSSG 910 920 930 940 950 960 QNLNTPEGET LNGKHQTDSI VCEMKMDTDQ NTRENLTGIN STVEEPVSPM LPPSAVEERE 970 980 990 1000 1010 1020 AVSKTALASP PATMAANESQ EIDEDEGIHS HEGSDLSDNM SEGSDDSGLH GARPVPQESS 1030 1040 1050 1060 1070 RKNAKEALAV KAAKGDFVCI FCDRSFRKGK DYSKHLNRHL VNVYYLEEAA QGQE

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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.

IPI

IPI00159969.
IPI00816294.
IPI00816510.
IPI00816561.

PIR

A56138.
I38754.
I38755.

RefSeq

NP_001180437.1. NM_001193508.1.
NP_005603.3. NM_005612.4.

UniGene

Hs.307836.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CZY	NMR	-	B	43-57	[»]

ProteinModelPortal

Q13127.

SMR

Q13127. Positions 149-410.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35264N.

IntAct

Q13127. 3 interactions.

STRING

9606.ENSP00000311816.

PTM databases

PhosphoSite

Q13127.

Polymorphism databases

DMDM

296452989.

Proteomic databases

PaxDb

Q13127.

PRIDE

Q13127.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000309042; ENSP00000311816; ENSG00000084093.

GeneID

5978.

KEGG

hsa:5978.

UCSC

uc003hch.3. human.
uc003hcj.1. human.

Organism-specific databases

CTD

5978.

GeneCards

GC04P057689.

H-InvDB

HIX0031381.

HGNC

HGNC:9966. REST.

HPA

HPA006079.

MIM

600571. gene.

neXtProt

NX_Q13127.

PharmGKB

PA34334.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG271556.

HOVERGEN

HBG093893.

InParanoid

Q13127.

KO

K09222.

OMA

VQKEPVQ.

OrthoDB

EOG4NP73G.

PhylomeDB

Q13127.

Gene expression databases

Bgee

Q13127.

CleanEx

HS_REST.

Genevestigator

Q13127.

Family and domain databases

Gene3D

3.30.160.60. 4 hits.

InterPro

IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]

SMART

SM00355. ZnF_C2H2. 9 hits.
[Graphical view]

PROSITE

PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 6 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

REST. human.

EvolutionaryTrace

Q13127.

GenomeRNAi

5978.

NextBio

23267.

SOURCE

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Entry information

Entry name

REST_HUMAN

Accession

Primary (citable) accession number: Q13127
Secondary accession number(s): A2RUE0 , B9EGJ0, Q12956, Q12957, Q13134, Q59ER1, Q8IWI3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 115 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.