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Q13127

- REST_HUMAN

UniProt

Q13127 - REST_HUMAN

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Protein

RE1-silencing transcription factor

Gene

REST

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.5 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri159 – 18123C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri216 – 23823C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri248 – 27023C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri276 – 29823C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri304 – 32623C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri332 – 35524C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri361 – 38323C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri389 – 41224C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1060 – 108223C2H2-type 9PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: UniProtKB
  2. core promoter binding Source: UniProtKB
  3. core promoter sequence-specific DNA binding Source: UniProtKB
  4. metal ion binding Source: UniProtKB-KW
  5. outward rectifier potassium channel activity Source: UniProtKB
  6. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: UniProtKB
  7. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  8. transcription factor binding Source: UniProtKB
  9. transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  1. cardiac muscle cell myoblast differentiation Source: UniProtKB
  2. cellular response to drug Source: UniProtKB
  3. cellular response to electrical stimulus Source: UniProtKB
  4. cellular response to glucocorticoid stimulus Source: UniProtKB
  5. hematopoietic progenitor cell differentiation Source: Ensembl
  6. histone H4 deacetylation Source: UniProtKB
  7. negative regulation by host of viral transcription Source: UniProtKB
  8. negative regulation of aldosterone biosynthetic process Source: UniProtKB
  9. negative regulation of amniotic stem cell differentiation Source: UniProtKB
  10. negative regulation of calcium ion-dependent exocytosis Source: UniProtKB
  11. negative regulation of cell proliferation Source: UniProtKB
  12. negative regulation of cortisol biosynthetic process Source: UniProtKB
  13. negative regulation of dense core granule biogenesis Source: UniProtKB
  14. negative regulation of gene expression Source: UniProtKB
  15. negative regulation of insulin secretion Source: UniProtKB
  16. negative regulation of mesenchymal stem cell differentiation Source: UniProtKB
  17. negative regulation of neurogenesis Source: UniProtKB
  18. negative regulation of neuron differentiation Source: UniProtKB
  19. negative regulation of transcription, DNA-templated Source: UniProtKB
  20. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  21. positive regulation of apoptotic process Source: UniProtKB
  22. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  23. positive regulation of transcription, DNA-templated Source: UniProtKB
  24. potassium ion transmembrane transport Source: GOC
  25. regulation of transcription, DNA-templated Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ13127.

Names & Taxonomyi

Protein namesi
Recommended name:
RE1-silencing transcription factor
Alternative name(s):
Neural-restrictive silencer factor
X2 box repressor
Gene namesi
Name:REST
Synonyms:NRSF, XBR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:9966. REST.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. nucleus Source: UniProtKB
  3. transcriptional repressor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34334.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10971097RE1-silencing transcription factorPRO_0000269547Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei864 – 8641Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ13127.
PaxDbiQ13127.
PRIDEiQ13127.

PTM databases

PhosphoSiteiQ13127.

Expressioni

Tissue specificityi

Ubiquitous. Expressed at higher levels in the tissues of the lymphocytic compartment, including spleen, thymus, peripheral blood lymphocytes and ovary.1 Publication

Gene expression databases

BgeeiQ13127.
CleanExiHS_REST.
ExpressionAtlasiQ13127. baseline and differential.
GenevestigatoriQ13127.

Organism-specific databases

HPAiHPA006079.

Interactioni

Subunit structurei

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 EHMT2.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SMARCA4P515322EBI-926706,EBI-302489

Protein-protein interaction databases

BioGridi111910. 37 interactions.
DIPiDIP-35264N.
IntActiQ13127. 4 interactions.
STRINGi9606.ENSP00000311816.

Structurei

Secondary structure

1
1097
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi44 – 5512

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CZYNMR-B43-57[»]
ProteinModelPortaliQ13127.
SMRiQ13127. Positions 149-410.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13127.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 12291Interaction with SIN3AAdd
BLAST
Regioni43 – 5715Interaction with SIN3BAdd
BLAST
Regioni1009 – 108779Interaction with RCOR1Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi11 – 144Poly-Gly
Compositional biasi400 – 603204Lys-richAdd
BLAST
Compositional biasi595 – 815221Pro-richAdd
BLAST

Sequence similaritiesi

Contains 9 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri159 – 18123C2H2-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri216 – 23823C2H2-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri248 – 27023C2H2-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri276 – 29823C2H2-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri304 – 32623C2H2-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri332 – 35524C2H2-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri361 – 38323C2H2-type 7PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri389 – 41224C2H2-type 8PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1060 – 108223C2H2-type 9PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG271556.
GeneTreeiENSGT00530000063458.
HOVERGENiHBG093893.
InParanoidiQ13127.
KOiK09222.
OMAiVQKEPVQ.
OrthoDBiEOG73FQM4.
PhylomeDBiQ13127.
TreeFamiTF332861.

Family and domain databases

Gene3Di3.30.160.60. 4 hits.
InterProiIPR027775. C2H2_Znf_fam.
IPR027757. REST.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PANTHERiPTHR10032. PTHR10032. 1 hit.
PTHR10032:SF71. PTHR10032:SF71. 1 hit.
SMARTiSM00355. ZnF_C2H2. 9 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 6 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q13127-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MATQVMGQSS GGGGLFTSSG NIGMALPNDM YDLHDLSKAE LAAPQLIMLA
60 70 80 90 100
NVALTGEVNG SCCDYLVGEE RQMAELMPVG DNNFSDSEEG EGLEESADIK
110 120 130 140 150
GEPHGLENME LRSLELSVVE PQPVFEASGA PDIYSSNKDL PPETPGAEDK
160 170 180 190 200
GKSSKTKPFR CKPCQYEAES EEQFVHHIRV HSAKKFFVEE SAEKQAKARE
210 220 230 240 250
SGSSTAEEGD FSKGPIRCDR CGYNTNRYDH YTAHLKHHTR AGDNERVYKC
260 270 280 290 300
IICTYTTVSE YHWRKHLRNH FPRKVYTCGK CNYFSDRKNN YVQHVRTHTG
310 320 330 340 350
ERPYKCELCP YSSSQKTHLT RHMRTHSGEK PFKCDQCSYV ASNQHEVTRH
360 370 380 390 400
ARQVHNGPKP LNCPHCDYKT ADRSNFKKHV ELHVNPRQFN CPVCDYAASK
410 420 430 440 450
KCNLQYHFKS KHPTCPNKTM DVSKVKLKKT KKREADLPDN ITNEKTEIEQ
460 470 480 490 500
TKIKGDVAGK KNEKSVKAEK RDVSKEKKPS NNVSVIQVTT RTRKSVTEVK
510 520 530 540 550
EMDVHTGSNS EKFSKTKKSK RKLEVDSHSL HGPVNDEESS TKKKKKVESK
560 570 580 590 600
SKNNSQEVPK GDSKVEENKK QNTCMKKSTK KKTLKNKSSK KSSKPPQKEP
610 620 630 640 650
VEKGSAQMDP PQMGPAPTEA VQKGPVQVEP PPPMEHAQME GAQIRPAPDE
660 670 680 690 700
PVQMEVVQEG PAQKELLPPV EPAQMVGAQI VLAHMELPPP METAQTEVAQ
710 720 730 740 750
MGPAPMEPAQ MEVAQVESAP MQVVQKEPVQ MELSPPMEVV QKEPVQIELS
760 770 780 790 800
PPMEVVQKEP VKIELSPPIE VVQKEPVQME LSPPMGVVQK EPAQREPPPP
810 820 830 840 850
REPPLHMEPI SKKPPLRKDK KEKSNMQSER ARKEQVLIEV GLVPVKDSWL
860 870 880 890 900
LKESVSTEDL SPPSPPLPKE NLREEASGDQ KLLNTGEGNK EAPLQKVGAE
910 920 930 940 950
EADESLPGLA ANINESTHIS SSGQNLNTPE GETLNGKHQT DSIVCEMKMD
960 970 980 990 1000
TDQNTRENLT GINSTVEEPV SPMLPPSAVE EREAVSKTAL ASPPATMAAN
1010 1020 1030 1040 1050
ESQEIDEDEG IHSHEGSDLS DNMSEGSDDS GLHGARPVPQ ESSRKNAKEA
1060 1070 1080 1090
LAVKAAKGDF VCIFCDRSFR KGKDYSKHLN RHLVNVYYLE EAAQGQE
Length:1,097
Mass (Da):121,872
Last modified:May 18, 2010 - v3
Checksum:iEBC652EED19CA161
GO
Isoform 2 (identifier: Q13127-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     301-313: ERPYKCELCPYSS → KRSFLVHKFSSLF
     314-1097: Missing.

Show »
Length:313
Mass (Da):35,048
Checksum:i3B0F550EBD70F79D
GO
Isoform 3 (identifier: Q13127-3) [UniParc]FASTAAdd to Basket

Also known as: N4

The sequence of this isoform differs from the canonical sequence as follows:
     329-329: E → W
     330-1097: Missing.

Show »
Length:329
Mass (Da):36,972
Checksum:iAD25D9BAC94FCAF7
GO
Isoform 4 (identifier: Q13127-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,074
Mass (Da):119,083
Checksum:i7D5F7CBD2C74EC0A
GO

Sequence cautioni

The sequence AAH38985.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
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 BAD92987.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti295 – 2951V → L in AAC50114. (PubMed:7871435)Curated
Sequence conflicti596 – 5994PQKE → SRNS in AAC50115. (PubMed:7871435)Curated
Sequence conflicti630 – 6301P → L in AAB17211. (PubMed:7697725)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti626 – 6261V → I.1 Publication
Corresponds to variant rs2228991 [ dbSNP | Ensembl ].
VAR_029795
Natural varianti692 – 6921E → D.
Corresponds to variant rs2227902 [ dbSNP | Ensembl ].
VAR_029796
Natural varianti762 – 7621K → Q.
Corresponds to variant rs2227903 [ dbSNP | Ensembl ].
VAR_029797
Natural varianti797 – 7971P → L.1 Publication
Corresponds to variant rs3796529 [ dbSNP | Ensembl ].
VAR_029798

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei301 – 31313ERPYK…CPYSS → KRSFLVHKFSSLF in isoform 2. 1 PublicationVSP_022064Add
BLAST
Alternative sequencei304 – 32623Missing in isoform 4. CuratedVSP_022067Add
BLAST
Alternative sequencei314 – 1097784Missing in isoform 2. 1 PublicationVSP_022065Add
BLAST
Alternative sequencei329 – 3291E → W in isoform 3. CuratedVSP_022066
Alternative sequencei330 – 1097768Missing in isoform 3. CuratedVSP_022068Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS3509.1. [Q13127-1]
PIRiA56138.
I38754.
I38755.
RefSeqiNP_001180437.1. NM_001193508.1. [Q13127-1]
NP_005603.3. NM_005612.4. [Q13127-1]
UniGeneiHs.307836.

Genome annotation databases

EnsembliENST00000309042; ENSP00000311816; ENSG00000084093. [Q13127-1]
ENST00000619101; ENSP00000484836; ENSG00000084093. [Q13127-1]
GeneIDi5978.
KEGGihsa:5978.
UCSCiuc003hch.3. human. [Q13127-1]
uc031ser.1. human. [Q13127-2]
uc031ses.1. human. [Q13127-3]
uc031sex.1. human. [Q13127-4]

Polymorphism databases

DMDMi296452989.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS3509.1. [Q13127-1 ]
PIRi A56138.
I38754.
I38755.
RefSeqi NP_001180437.1. NM_001193508.1. [Q13127-1 ]
NP_005603.3. NM_005612.4. [Q13127-1 ]
UniGenei Hs.307836.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CZY NMR - B 43-57 [» ]
ProteinModelPortali Q13127.
SMRi Q13127. Positions 149-410.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111910. 37 interactions.
DIPi DIP-35264N.
IntActi Q13127. 4 interactions.
STRINGi 9606.ENSP00000311816.

PTM databases

PhosphoSitei Q13127.

Polymorphism databases

DMDMi 296452989.

Proteomic databases

MaxQBi Q13127.
PaxDbi Q13127.
PRIDEi Q13127.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000309042 ; ENSP00000311816 ; ENSG00000084093 . [Q13127-1 ]
ENST00000619101 ; ENSP00000484836 ; ENSG00000084093 . [Q13127-1 ]
GeneIDi 5978.
KEGGi hsa:5978.
UCSCi uc003hch.3. human. [Q13127-1 ]
uc031ser.1. human. [Q13127-2 ]
uc031ses.1. human. [Q13127-3 ]
uc031sex.1. human. [Q13127-4 ]

Organism-specific databases

CTDi 5978.
GeneCardsi GC04P057774.
H-InvDB HIX0031381.
HGNCi HGNC:9966. REST.
HPAi HPA006079.
MIMi 600571. gene.
neXtProti NX_Q13127.
PharmGKBi PA34334.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG271556.
GeneTreei ENSGT00530000063458.
HOVERGENi HBG093893.
InParanoidi Q13127.
KOi K09222.
OMAi VQKEPVQ.
OrthoDBi EOG73FQM4.
PhylomeDBi Q13127.
TreeFami TF332861.

Enzyme and pathway databases

SignaLinki Q13127.

Miscellaneous databases

ChiTaRSi REST. human.
EvolutionaryTracei Q13127.
GeneWikii RE1-silencing_transcription_factor.
GenomeRNAii 5978.
NextBioi 23267.
PROi Q13127.
SOURCEi Search...

Gene expression databases

Bgeei Q13127.
CleanExi HS_REST.
ExpressionAtlasi Q13127. baseline and differential.
Genevestigatori Q13127.

Family and domain databases

Gene3Di 3.30.160.60. 4 hits.
InterProi IPR027775. C2H2_Znf_fam.
IPR027757. REST.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view ]
PANTHERi PTHR10032. PTHR10032. 1 hit.
PTHR10032:SF71. PTHR10032:SF71. 1 hit.
SMARTi SM00355. ZnF_C2H2. 9 hits.
[Graphical view ]
PROSITEi PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. 6 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: FUNCTION.
  12. "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.
  13. "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].
  14. "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.
  15. "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.

Entry informationi

Entry nameiREST_HUMAN
AccessioniPrimary (citable) accession number: Q13127
Secondary accession number(s): A2RUE0
, B9EGJ0, Q12956, Q12957, Q13134, Q59ER1, Q8IWI3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: May 18, 2010
Last modified: October 29, 2014
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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