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Q9UKL0 (RCOR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
REST corepressor 1
Alternative name(s):
Protein CoREST
Gene names
Name:RCOR1
Synonyms:KIAA0071, RCOR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Interacts with INMS1 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.6 Ref.7 Ref.8 Ref.9 Ref.12 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

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 processHost-virus interaction
Transcription
Transcription regulation
   Cellular componentNucleus
   DomainCoiled coil
Repeat
   Molecular functionChromatin regulator
Repressor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

histone H4 deacetylation

Inferred from direct assay PubMed 17555596. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.1. Source: GOC

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.1. Source: UniProtKB

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.4. Source: UniProtKB

transcriptional repressor complex

Inferred from direct assay Ref.4. 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.1. Source: UniProtKB

chromatin binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.1Ref.8PubMed 23592795. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from direct assay PubMed 17555596. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 482482REST corepressor 1
PRO_0000226773

Regions

Domain100 – 18687ELM2
Domain187 – 23852SANT 1
Domain378 – 42952SANT 2
Region75 – 254180Interaction with HDAC1
Region293 – 38189Interaction with KDM1A
Coiled coil241 – 27030 Potential
Coiled coil331 – 36636 Potential
Compositional bias18 – 7457Ala-rich

Amino acid modifications

Modified residue1241Phosphoserine Ref.17 Ref.18 Ref.19
Modified residue2571Phosphoserine Ref.16 Ref.18 Ref.19 Ref.21
Modified residue4571Phosphoserine Ref.21

Secondary structure

.................. 482
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UKL0 [UniParc].

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

FASTA48253,028
        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' 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND SER-257, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"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-124 AND SER-257, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257 AND SER-457, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"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] [Europe PMC] [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.
RefSeqNP_055971.2. NM_015156.3.
UniGeneHs.510521.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IW5X-ray2.57B286-482[»]
2UXNX-ray2.72B286-482[»]
2UXXX-ray2.74B286-482[»]
2V1DX-ray3.10B305-482[»]
2X0LX-ray3.00B308-440[»]
2XAFX-ray3.25B1-482[»]
2XAGX-ray3.10B1-482[»]
2XAHX-ray3.10B1-482[»]
2XAJX-ray3.30B1-482[»]
2XAQX-ray3.20B1-482[»]
2XASX-ray3.20B1-482[»]
2Y48X-ray3.00B305-482[»]
3ZMSX-ray2.96B1-482[»]
3ZMTX-ray3.10B1-482[»]
3ZMUX-ray3.20B1-482[»]
3ZMVX-ray3.00B1-482[»]
3ZMZX-ray3.00B1-482[»]
3ZN0X-ray2.80B1-482[»]
3ZN1X-ray3.10B1-482[»]
4BAYX-ray3.10B308-440[»]
4KUMX-ray3.05B286-482[»]
ProteinModelPortalQ9UKL0.
SMRQ9UKL0. Positions 100-236, 308-440.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116796. 46 interactions.
DIPDIP-35263N.
IntActQ9UKL0. 15 interactions.
MINTMINT-3081566.
STRING9606.ENSP00000262241.

PTM databases

PhosphoSiteQ9UKL0.

Polymorphism databases

DMDM74762776.

Proteomic databases

MaxQBQ9UKL0.
PaxDbQ9UKL0.
PeptideAtlasQ9UKL0.
PRIDEQ9UKL0.

Protocols and materials databases

DNASU23186.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000570597; ENSP00000459789; ENSG00000089902.
GeneID23186.
KEGGhsa:23186.

Organism-specific databases

CTD23186.
GeneCardsGC14P103059.
HGNCHGNC:17441. RCOR1.
HPACAB001956.
HPA049327.
HPA054241.
MIM607675. gene.
neXtProtNX_Q9UKL0.
PharmGKBPA34305.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG326181.
HOGENOMHOG000065784.
HOVERGENHBG079800.
InParanoidQ9UKL0.
KOK11829.
PhylomeDBQ9UKL0.
TreeFamTF106450.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressQ9UKL0.
BgeeQ9UKL0.
CleanExHS_RCOR1.
GenevestigatorQ9UKL0.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
InterProIPR000949. ELM2_dom.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
[Graphical view]
PfamPF01448. ELM2. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
[Graphical view]
SMARTSM00717. SANT. 2 hits.
[Graphical view]
SUPFAMSSF46689. SSF46689. 2 hits.
PROSITEPS51156. ELM2. 1 hit.
PS51293. SANT. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9UKL0.
GeneWikiRCOR1.
GenomeRNAi23186.
NextBio44655.
PROQ9UKL0.
SOURCESearch...

Entry information

Entry nameRCOR1_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 127 of the entry and version 1 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 chromosome 14

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