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Protein

REST corepressor 1

Gene

RCOR1

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

Functioni

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.7 Publications

GO - Molecular functioni

GO - Biological processi

  • blood coagulation Source: Reactome
  • histone H4 deacetylation Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
  • viral process Source: UniProtKB-KW

Keywordsi

Molecular functionChromatin regulator, Repressor
Biological processHost-virus interaction, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-HSA-3214815. HDACs deacetylate histones.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SIGNORiQ9UKL0.

Names & Taxonomyi

Protein namesi
Recommended name:
REST corepressor 1
Alternative name(s):
Protein CoREST
Gene namesi
Name:RCOR1
Synonyms:KIAA0071, RCOR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:17441. RCOR1.

Subcellular locationi

GO - Cellular componenti

  • DNA repair complex Source: MGI
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • transcriptional repressor complex Source: UniProtKB
  • transcription factor complex Source: GO_Central

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi23186.
OpenTargetsiENSG00000089902.
PharmGKBiPA34305.

Chemistry databases

ChEMBLiCHEMBL3137262.

Polymorphism and mutation databases

BioMutaiRCOR1.
DMDMi74762776.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002267731 – 485REST corepressor 1Add BLAST485

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei127PhosphoserineCombined sources1
Modified residuei260PhosphoserineCombined sources1
Modified residuei460PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated by HSV-1 protein kinases in case of infection.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9UKL0.
MaxQBiQ9UKL0.
PaxDbiQ9UKL0.
PeptideAtlasiQ9UKL0.
PRIDEiQ9UKL0.

PTM databases

iPTMnetiQ9UKL0.
PhosphoSitePlusiQ9UKL0.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiENSG00000089902.
CleanExiHS_RCOR1.

Organism-specific databases

HPAiHPA049327.
HPA054241.

Interactioni

Subunit structurei

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.By similarity12 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi116796. 59 interactors.
DIPiDIP-35263N.
IntActiQ9UKL0. 23 interactors.
MINTiMINT-3081566.
STRINGi9606.ENSP00000459789.

Chemistry databases

BindingDBiQ9UKL0.

Structurei

Secondary structure

1485
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi318 – 324Combined sources7
Beta strandi325 – 329Combined sources5
Helixi330 – 362Combined sources33
Turni364 – 367Combined sources4
Helixi368 – 370Combined sources3
Helixi385 – 398Combined sources14
Helixi402 – 409Combined sources8
Beta strandi410 – 412Combined sources3
Helixi414 – 423Combined sources10
Turni424 – 429Combined sources6
Helixi430 – 438Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IW5X-ray2.57B289-485[»]
2UXNX-ray2.72B289-485[»]
2UXXX-ray2.74B289-485[»]
2V1DX-ray3.10B308-485[»]
2X0LX-ray3.00B311-443[»]
2XAFX-ray3.25B4-485[»]
2XAGX-ray3.10B4-485[»]
2XAHX-ray3.10B4-485[»]
2XAJX-ray3.30B4-485[»]
2XAQX-ray3.20B4-485[»]
2XASX-ray3.20B4-485[»]
2Y48X-ray3.00B308-485[»]
3ZMSX-ray2.96B4-485[»]
3ZMTX-ray3.10B4-485[»]
3ZMUX-ray3.20B4-485[»]
3ZMVX-ray3.00B4-485[»]
3ZMZX-ray3.00B4-485[»]
3ZN0X-ray2.80B4-485[»]
3ZN1X-ray3.10B4-485[»]
4BAYX-ray3.10B311-443[»]
4KUMX-ray3.05B289-485[»]
4UV8X-ray2.80B4-485[»]
4UV9X-ray3.00B4-485[»]
4UVAX-ray2.90B4-485[»]
4UVBX-ray2.80B4-485[»]
4UVCX-ray3.10B4-485[»]
4UXNX-ray2.85B4-485[»]
4XBFX-ray2.80B311-443[»]
5L3BX-ray3.30B4-485[»]
5L3CX-ray3.31B4-485[»]
5L3DX-ray2.60B4-485[»]
5L3EX-ray2.80B308-485[»]
5L3FX-ray3.50B308-485[»]
5L3GX-ray3.10B308-485[»]
5LBQX-ray3.30B308-485[»]
ProteinModelPortaliQ9UKL0.
SMRiQ9UKL0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UKL0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini103 – 189ELM2PROSITE-ProRule annotationAdd BLAST87
Domaini190 – 241SANT 1PROSITE-ProRule annotationAdd BLAST52
Domaini381 – 432SANT 2PROSITE-ProRule annotationAdd BLAST52

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni78 – 257Interaction with HDAC11 PublicationAdd BLAST180
Regioni296 – 384Interaction with KDM1A1 PublicationAdd BLAST89

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili244 – 273Sequence analysisAdd BLAST30
Coiled coili334 – 369Sequence analysisAdd BLAST36

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi21 – 77Ala-richAdd BLAST57

Domaini

The SANT domains may bridge the nucleosomal substrates and the demethylase KDM1A.1 Publication

Sequence similaritiesi

Belongs to the CoREST family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG1194. Eukaryota.
ENOG410XSIS. LUCA.
GeneTreeiENSGT00840000129748.
HOGENOMiHOG000065784.
HOVERGENiHBG079800.
InParanoidiQ9UKL0.
KOiK11829.
OrthoDBiEOG091G096Y.
PhylomeDBiQ9UKL0.
TreeFamiTF106450.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiView protein in InterPro
IPR000949. ELM2_dom.
IPR009057. Homeobox-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
PfamiView protein in Pfam
PF01448. ELM2. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
SMARTiView protein in SMART
SM01189. ELM2. 1 hit.
SM00717. SANT. 2 hits.
SUPFAMiSSF46689. SSF46689. 2 hits.
PROSITEiView protein in PROSITE
PS51156. ELM2. 1 hit.
PS51293. SANT. 2 hits.

Sequencei

Sequence statusi: Complete.

Q9UKL0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAMVEKGPE VSGKRRGRNN AAASASAAAA SAAASAACAS PAATAASGAA
60 70 80 90 100
ASSASAAAAS AAAAPNNGQN KSLAAAAPNG NSSSNSWEEG SSGSSSDEEH
110 120 130 140 150
GGGGMRVGPQ YQAVVPDFDP AKLARRSQER DNLGMLVWSP NQNLSEAKLD
160 170 180 190 200
EYIAIAKEKH GYNMEQALGM LFWHKHNIEK SLADLPNFTP FPDEWTVEDK
210 220 230 240 250
VLFEQAFSFH GKTFHRIQQM LPDKSIASLV KFYYSWKKTR TKTSVMDRHA
260 270 280 290 300
RKQKREREES EDELEEANGN NPIDIEVDQN KESKKEVPPT ETVPQVKKEK
310 320 330 340 350
HSTQAKNRAK RKPPKGMFLS QEDVEAVSAN ATAATTVLRQ LDMELVSVKR
360 370 380 390 400
QIQNIKQTNS ALKEKLDGGI EPYRLPEVIQ KCNARWTTEE QLLAVQAIRK
410 420 430 440 450
YGRDFQAISD VIGNKSVVQV KNFFVNYRRR FNIDEVLQEW EAEHGKEETN
460 470 480
GPSNQKPVKS PDNSIKMPEE EDEAPVLDVR YASAS
Length:485
Mass (Da):53,327
Last modified:February 15, 2017 - v2
Checksum:i77E90FB0EFD514B2
GO

Sequence cautioni

The sequence AAH51003 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH64495 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH64495 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL132801 Genomic DNA. No translation available.
AL136293 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81793.1.
BC051003 mRNA. Translation: AAH51003.1. Different initiation.
BC064495 mRNA. Translation: AAH64495.1. Sequence problems.
AF155595 mRNA. Translation: AAF01498.1.
D31888 mRNA. Translation: BAA06686.1.
RefSeqiNP_055971.2. NM_015156.3.
UniGeneiHs.510521.

Genome annotation databases

EnsembliENST00000262241; ENSP00000262241; ENSG00000089902.
GeneIDi23186.
KEGGihsa:23186.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL132801 Genomic DNA. No translation available.
AL136293 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81793.1.
BC051003 mRNA. Translation: AAH51003.1. Different initiation.
BC064495 mRNA. Translation: AAH64495.1. Sequence problems.
AF155595 mRNA. Translation: AAF01498.1.
D31888 mRNA. Translation: BAA06686.1.
RefSeqiNP_055971.2. NM_015156.3.
UniGeneiHs.510521.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2IW5X-ray2.57B289-485[»]
2UXNX-ray2.72B289-485[»]
2UXXX-ray2.74B289-485[»]
2V1DX-ray3.10B308-485[»]
2X0LX-ray3.00B311-443[»]
2XAFX-ray3.25B4-485[»]
2XAGX-ray3.10B4-485[»]
2XAHX-ray3.10B4-485[»]
2XAJX-ray3.30B4-485[»]
2XAQX-ray3.20B4-485[»]
2XASX-ray3.20B4-485[»]
2Y48X-ray3.00B308-485[»]
3ZMSX-ray2.96B4-485[»]
3ZMTX-ray3.10B4-485[»]
3ZMUX-ray3.20B4-485[»]
3ZMVX-ray3.00B4-485[»]
3ZMZX-ray3.00B4-485[»]
3ZN0X-ray2.80B4-485[»]
3ZN1X-ray3.10B4-485[»]
4BAYX-ray3.10B311-443[»]
4KUMX-ray3.05B289-485[»]
4UV8X-ray2.80B4-485[»]
4UV9X-ray3.00B4-485[»]
4UVAX-ray2.90B4-485[»]
4UVBX-ray2.80B4-485[»]
4UVCX-ray3.10B4-485[»]
4UXNX-ray2.85B4-485[»]
4XBFX-ray2.80B311-443[»]
5L3BX-ray3.30B4-485[»]
5L3CX-ray3.31B4-485[»]
5L3DX-ray2.60B4-485[»]
5L3EX-ray2.80B308-485[»]
5L3FX-ray3.50B308-485[»]
5L3GX-ray3.10B308-485[»]
5LBQX-ray3.30B308-485[»]
ProteinModelPortaliQ9UKL0.
SMRiQ9UKL0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116796. 59 interactors.
DIPiDIP-35263N.
IntActiQ9UKL0. 23 interactors.
MINTiMINT-3081566.
STRINGi9606.ENSP00000459789.

Chemistry databases

BindingDBiQ9UKL0.
ChEMBLiCHEMBL3137262.

PTM databases

iPTMnetiQ9UKL0.
PhosphoSitePlusiQ9UKL0.

Polymorphism and mutation databases

BioMutaiRCOR1.
DMDMi74762776.

Proteomic databases

EPDiQ9UKL0.
MaxQBiQ9UKL0.
PaxDbiQ9UKL0.
PeptideAtlasiQ9UKL0.
PRIDEiQ9UKL0.

Protocols and materials databases

DNASUi23186.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262241; ENSP00000262241; ENSG00000089902.
GeneIDi23186.
KEGGihsa:23186.

Organism-specific databases

CTDi23186.
DisGeNETi23186.
GeneCardsiRCOR1.
HGNCiHGNC:17441. RCOR1.
HPAiHPA049327.
HPA054241.
MIMi607675. gene.
neXtProtiNX_Q9UKL0.
OpenTargetsiENSG00000089902.
PharmGKBiPA34305.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1194. Eukaryota.
ENOG410XSIS. LUCA.
GeneTreeiENSGT00840000129748.
HOGENOMiHOG000065784.
HOVERGENiHBG079800.
InParanoidiQ9UKL0.
KOiK11829.
OrthoDBiEOG091G096Y.
PhylomeDBiQ9UKL0.
TreeFamiTF106450.

Enzyme and pathway databases

ReactomeiR-HSA-3214815. HDACs deacetylate histones.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SIGNORiQ9UKL0.

Miscellaneous databases

ChiTaRSiRCOR1. human.
EvolutionaryTraceiQ9UKL0.
GeneWikiiRCOR1.
GenomeRNAii23186.
PROiQ9UKL0.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000089902.
CleanExiHS_RCOR1.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiView protein in InterPro
IPR000949. ELM2_dom.
IPR009057. Homeobox-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
PfamiView protein in Pfam
PF01448. ELM2. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
SMARTiView protein in SMART
SM01189. ELM2. 1 hit.
SM00717. SANT. 2 hits.
SUPFAMiSSF46689. SSF46689. 2 hits.
PROSITEiView protein in PROSITE
PS51156. ELM2. 1 hit.
PS51293. SANT. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiRCOR1_HUMAN
AccessioniPrimary (citable) accession number: Q9UKL0
Secondary accession number(s): J3KN32
, Q15044, Q6P2I9, Q86VG5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: February 15, 2017
Last modified: March 15, 2017
This is version 156 of the entry and version 2 of the sequence. See 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 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.