REST corepressor 1 - Homo sapiens (Human)

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Q9UKL0 (RCOR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 101. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
REST corepressor 1

Alternative name(s):
Protein CoREST

Gene names

Name:	RCOR1
Synonyms:	KIAA0071, RCOR

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	482 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential component of the BHC complex, a corepressor complex that represses transcription of neuron-specific genes in non-neuronal cells. The BHC complex is recruited at RE1/NRSE sites by REST and acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier. In the BHC complex, it serves as a molecular beacon for the recruitment of molecular machinery, including MeCP2 and SUV39H1, that imposes silencing across a chromosomal interval. Plays a central role in demethylation of Lys-4 of histone H3 by promoting demethylase activity of KDM1A on core histones and nucleosomal substrates. It also protects KDM1A from the proteasome. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development and controls hematopoietic differentiation. Ref.5 Ref.7 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14
Subunit structure	Interacts directly with GFI1 and GFI1B in a RCOR/GFI/KDM1A/HDAC complex By similarity. Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and PHF21A/BHC80. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Interacts with REST. Interacts with the SMARCE1/BAF57, suggesting that the BHC complex may recruit the ATP-dependent chromatin-remodeling SWI-SNF complex. Interacts with herpes virus HSV-1 ICP0 protein; the interaction leads to the disruption of the BHC complex, thereby preventing the BHC complex from repressing transcription of viral genes. Ref.1 Ref.4 Ref.5 Ref.8 Ref.13 Ref.14 Ref.15
Subcellular location	Nucleus. Note: Upon infection by HSV-1, it is partially translocated into the cytoplasm in an HSV-1-dependent manner. Ref.4 Ref.15
Tissue specificity	Ubiquitously expressed. Ref.1
Domain	The SANT domains may bridge the nucleosomal substrates and the demethylase KDM1A. Ref.13
Post-translational modification	Phosphorylated by HSV-1 protein kinases in case of infection. Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20
Sequence similarities	Belongs to the CoREST family. Contains 1 ELM2 domain. Contains 2 SANT domains.
Sequence caution	The sequence AAH64495.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation
Cellular component	Nucleus
Domain	Coiled coil Repeat
Molecular function	Chromatin regulator Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	blood coagulation Traceable author statement. Source: Reactome histone H4 deacetylation Inferred from direct assay. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	transcriptional repressor complex Inferred from direct assay Ref.4. 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.1. Source: UniProtKB protein binding Inferred from physical interaction Ref.1 Ref.8. Source: UniProtKB transcription regulatory region DNA binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
KDM1A	O60341	2	EBI-926563,EBI-710124
SMARCE1	Q969G3-1	2	EBI-926563,EBI-455091
SMARCE1	Q969G3-2	4	EBI-926563,EBI-455096

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 482

482

REST corepressor 1

PRO_0000226773

Regions

Domain

100 – 186

ELM2

Domain

187 – 238

SANT 1

Domain

378 – 429

SANT 2

Region

75 – 254

180

Interaction with HDAC1

Region

293 – 381

Interaction with KDM1A

Coiled coil

241 – 270

Potential

Coiled coil

331 – 366

Potential

Compositional bias

18 – 74

Ala-rich

Amino acid modifications

Modified residue

124

Phosphoserine Ref.19 Ref.20

Modified residue

257

Phosphoserine Ref.16 Ref.17 Ref.18 Ref.19

Modified residue

457

Phosphoserine Ref.16

Secondary structure

482

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q9UKL0 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 17541695A56CFFD3
Show »

FASTA

482

53,028

        10         20         30         40         50         60 
MVEKGPEVSG KRRGRNNAAA SASAAAASAA ASAACASPAA TAASGAAASS ASAAAASAAA 

        70         80         90        100        110        120 
APNNGQNKSL AAAAPNGNSS SNSWEEGSSG SSSDEEHGGG GMRVGPQYQA VVPDFDPAKL 

       130        140        150        160        170        180 
ARRSQERDNL GMLVWSPNQN LSEAKLDEYI AIAKEKHGYN MEQALGMLFW HKHNIEKSLA 

       190        200        210        220        230        240 
DLPNFTPFPD EWTVEDKVLF EQAFSFHGKT FHRIQQMLPD KSIASLVKFY YSWKKTRTKT 

       250        260        270        280        290        300 
SVMDRHARKQ KREREESEDE LEEANGNNPI DIEVDQNKES KKEVPPTETV PQVKKEKHST 

       310        320        330        340        350        360 
QAKNRAKRKP PKGMFLSQED VEAVSANATA ATTVLRQLDM ELVSVKRQIQ NIKQTNSALK 

       370        380        390        400        410        420 
EKLDGGIEPY RLPEVIQKCN ARWTTEEQLL AVQAIRKYGR DFQAISDVIG NKSVVQVKNF 

       430        440        450        460        470        480 
FVNYRRRFNI DEVLQEWEAE HGKEETNGPS NQKPVKSPDN SIKMPEEEDE APVLDVRYAS 


AS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 10449787] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH REST, TISSUE SPECIFICITY. Tissue: Cervix carcinoma.
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-295. Tissue: Lymph.
[3]	"Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1." Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S. DNA Res. 1:223-229(1994) [PubMed: 7584044] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 87-482. Tissue: Bone marrow.
[4]	"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: 10734093] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH REST.
[5]	"Regulation of neuronal traits by a novel transcriptional complex." Ballas N., Battaglioli E., Atouf F., Andres M.E., Chenoweth J., Anderson M.E., Burger C., Moniwa M., Davie J.R., Bowers W.J., Federoff H.J., Rose D.W., Rosenfeld M.G., Brehm P., Mandel G. Neuron 31:353-365(2001) [PubMed: 11516394] [Abstract] Cited for: FUNCTION, INTERACTION WITH HDAC1 AND HDAC2.
[6]	"Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1." Humphrey G.W., Wang Y., Russanova V.R., Hirai T., Qin J., Nakatani Y., Howard B.H. J. Biol. Chem. 276:6817-6824(2001) [PubMed: 11102443] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BHC COMPLEX WITH HDAC1 AND KDM1A.
[7]	"CoREST is an integral component of the CoREST-human histone deacetylase complex." You A., Tong J.K., Grozinger C.M., Schreiber S.L. Proc. Natl. Acad. Sci. U.S.A. 98:1454-1458(2001) [PubMed: 11171972] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BHC COMPLEX WITH HDAC1; HDAC2 AND KDM1A.
[8]	"REST repression of neuronal genes requires components of the hSWI.SNF complex." Battaglioli E., Andres M.E., Rose D.W., Chenoweth J.G., Rosenfeld M.G., Anderson M.E., Mandel G. J. Biol. Chem. 277:41038-41045(2002) [PubMed: 12192000] [Abstract] Cited for: INTERACTION WITH SMARCE1.
[9]	"A core-BRAF35 complex containing histone deacetylase mediates repression of neuronal-specific genes." Hakimi M.-A., Bochar D.A., Chenoweth J., Lane W.S., Mandel G., Shiekhattar R. Proc. Natl. Acad. Sci. U.S.A. 99:7420-7425(2002) [PubMed: 12032298] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BHC COMPLEX WITH HDAC1; HDAC2; HMG20B; KDM1A AND PHF21A.
[10]	"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: 12399542] [Abstract] Cited for: FUNCTION.
[11]	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)
[12]	"A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes." Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R. J. Biol. Chem. 278:7234-7239(2003) [PubMed: 12493763] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE BHC COMPLEX WITH HDAC1; HDAC2; HMG20B; KDM1A; PHF21A; ZMYM2; ZNF217; ZMYM3; KIAA0182 AND GTF2I.
[13]	"Regulation of LSD1 histone demethylase activity by its associated factors." Shi Y.-J., Matson C., Lan F., Iwase S., Baba T., Shi Y. Mol. Cell 19:857-864(2005) [PubMed: 16140033] [Abstract] Cited for: FUNCTION, DOMAIN, INTERACTION WITH KDM1A.
[14]	"An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation." Lee M.G., Wynder C., Cooch N., Shiekhattar R. Nature 437:432-435(2005) [PubMed: 16079794] [Abstract] Cited for: FUNCTION, INTERACTION WITH KDM1A.
[15]	"Components of the REST/CoREST/histone deacetylase repressor complex are disrupted, modified, and translocated in HSV-1-infected cells." Gu H., Liang Y., Mandel G., Roizman B. Proc. Natl. Acad. Sci. U.S.A. 102:7571-7576(2005) [PubMed: 15897453] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH HSV-1 ICP0.
[16]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257 AND SER-457, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma.
[18]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[19]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-257, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[21]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]	"Structural basis for CoREST-dependent demethylation of nucleosomes by the human LSD1 histone demethylase." Yang M., Gocke C.B., Luo X., Borek D., Tomchick D.R., Machius M., Otwinowski Z., Yu H. Mol. Cell 23:377-387(2006) [PubMed: 16885027] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 286-482 IN COMPLEX WITH KDM1A.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF155595 mRNA. Translation: AAF01498.1.
BC051003 mRNA. Translation: AAH51003.1.
BC064495 mRNA. Translation: AAH64495.1. Sequence problems.
D31888 mRNA. Translation: BAA06686.1.

IPI

IPI00008531.

RefSeq

NP_055971.2. NM_015156.3.

UniGene

Hs.510521.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IW5	X-ray	2.57	B	286-482	[»]
2UXN	X-ray	2.72	B	286-482	[»]
2UXX	X-ray	2.74	B	286-482	[»]
2V1D	X-ray	3.10	B	305-482	[»]
2X0L	X-ray	3.00	B	308-440	[»]
2XAF	X-ray	3.25	B	1-482	[»]
2XAG	X-ray	3.10	B	1-482	[»]
2XAH	X-ray	3.10	B	1-482	[»]
2XAJ	X-ray	3.30	B	1-482	[»]
2XAQ	X-ray	3.20	B	1-482	[»]
2XAS	X-ray	3.20	B	1-482	[»]
2Y48	X-ray	3.00	B	305-482	[»]

ProteinModelPortal

Q9UKL0.

SMR

Q9UKL0. Positions 188-240, 308-440.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35263N.

IntAct

Q9UKL0. 12 interactions.

MINT

MINT-3081566.

STRING

Q9UKL0.

PTM databases

PhosphoSite

Q9UKL0.

Polymorphism databases

DMDM

74762776.

Proteomic databases

PeptideAtlas

Q9UKL0.

PRIDE

Q9UKL0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000262241; ENSP00000262241; ENSG00000089902.

GeneID

23186.

KEGG

hsa:23186.

UCSC

uc001ymb.1. human.

Organism-specific databases

CTD

23186.

GeneCards

GC14P103059.

H-InvDB

HIX0011991.

HGNC

HGNC:17441. RCOR1.

HPA

CAB001956.

MIM

607675. gene.

neXtProt

NX_Q9UKL0.

PharmGKB

PA34305.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG15529.

GeneTree

ENSGT00550000074554.

HOGENOM

HBG444636.

HOVERGEN

HBG079800.

InParanoid

Q9UKL0.

OMA

TVPQIKK.

OrthoDB

EOG49ZXPF.

PhylomeDB

Q9UKL0.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

Q9UKL0.

Bgee

Q9UKL0.

CleanEx

HS_RCOR1.

Genevestigator

Q9UKL0.

Family and domain databases

InterPro

IPR000949. ELM2_dom.
IPR009057. Homeodomain-like.
IPR012287. Homeodomain-rel.
IPR014778. Myb_DNA-bd.
IPR001005. SANT_DNA-bd.
IPR017884. SANT_eukarya.
[Graphical view]

Gene3D

G3DSA:1.10.10.60. Homeodomain-rel. 1 hit.

K11829.

Pfam

PF01448. ELM2. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
[Graphical view]

SMART

SM00717. SANT. 2 hits.
[Graphical view]

SUPFAM

SSF46689. Homeodomain_like. 2 hits.

PROSITE

PS51156. ELM2. 1 hit.
PS51293. SANT. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

44655.

SOURCE

Search...

Entry information

Entry name

RCOR1_HUMAN

Accession

Primary (citable) accession number: Q9UKL0
Secondary accession number(s): Q15044, Q6P2I9, Q86VG5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 101 of the entry and version 1 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.

Relevant documents

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents