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Q9UKL0

- RCOR1_HUMAN

UniProt

Q9UKL0 - RCOR1_HUMAN

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Protein

REST corepressor 1

Gene
RCOR1, KIAA0071, RCOR
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. chromatin binding Source: InterPro
  2. protein binding Source: UniProtKB
  3. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: UniProtKB
  4. transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. histone H4 deacetylation Source: UniProtKB
  3. negative regulation of transcription, DNA-templated Source: UniProtKB
  4. negative regulation of transcription from RNA polymerase II promoter Source: GOC
  5. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.

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
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:17441. RCOR1.

Subcellular locationi

Nucleus
Note: Upon infection by HSV-1, it is partially translocated into the cytoplasm in an HSV-1-dependent manner.2 Publications

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: UniProtKB
  3. transcriptional repressor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34305.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 482482REST corepressor 1PRO_0000226773Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei124 – 1241Phosphoserine3 Publications
Modified residuei257 – 2571Phosphoserine4 Publications
Modified residuei457 – 4571Phosphoserine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UKL0.
PaxDbiQ9UKL0.
PeptideAtlasiQ9UKL0.
PRIDEiQ9UKL0.

PTM databases

PhosphoSiteiQ9UKL0.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

ArrayExpressiQ9UKL0.
BgeeiQ9UKL0.
CleanExiHS_RCOR1.
GenevestigatoriQ9UKL0.

Organism-specific databases

HPAiCAB001956.
HPA049327.
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.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
KDM1AO603415EBI-926563,EBI-710124
SMARCE1Q969G3-12EBI-926563,EBI-455091
SMARCE1Q969G3-24EBI-926563,EBI-455096

Protein-protein interaction databases

BioGridi116796. 46 interactions.
DIPiDIP-35263N.
IntActiQ9UKL0. 15 interactions.
MINTiMINT-3081566.
STRINGi9606.ENSP00000262241.

Structurei

Secondary structure

1
482
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi318 – 3247
Beta strandi326 – 3294
Helixi330 – 36233
Turni364 – 3674
Helixi368 – 3703
Helixi385 – 39814
Helixi402 – 4098
Beta strandi410 – 4123
Helixi414 – 42310
Turni424 – 4296
Helixi430 – 4389

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ9UKL0.
SMRiQ9UKL0. Positions 100-236, 308-440.

Miscellaneous databases

EvolutionaryTraceiQ9UKL0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini100 – 18687ELM2Add
BLAST
Domaini187 – 23852SANT 1Add
BLAST
Domaini378 – 42952SANT 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni75 – 254180Interaction with HDAC1Add
BLAST
Regioni293 – 38189Interaction with KDM1AAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili241 – 27030 Reviewed predictionAdd
BLAST
Coiled coili331 – 36636 Reviewed predictionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi18 – 7457Ala-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the CoREST family.
Contains 1 ELM2 domain.
Contains 2 SANT domains.

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG326181.
HOGENOMiHOG000065784.
HOVERGENiHBG079800.
InParanoidiQ9UKL0.
KOiK11829.
PhylomeDBiQ9UKL0.
TreeFamiTF106450.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR000949. ELM2_dom.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
[Graphical view]
PfamiPF01448. ELM2. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
[Graphical view]
SMARTiSM00717. SANT. 2 hits.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 2 hits.
PROSITEiPS51156. ELM2. 1 hit.
PS51293. SANT. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9UKL0-1 [UniParc]FASTAAdd to Basket

« Hide

MVEKGPEVSG KRRGRNNAAA SASAAAASAA ASAACASPAA TAASGAAASS    50
ASAAAASAAA APNNGQNKSL AAAAPNGNSS SNSWEEGSSG SSSDEEHGGG 100
GMRVGPQYQA VVPDFDPAKL ARRSQERDNL GMLVWSPNQN LSEAKLDEYI 150
AIAKEKHGYN MEQALGMLFW HKHNIEKSLA DLPNFTPFPD EWTVEDKVLF 200
EQAFSFHGKT FHRIQQMLPD KSIASLVKFY YSWKKTRTKT SVMDRHARKQ 250
KREREESEDE LEEANGNNPI DIEVDQNKES KKEVPPTETV PQVKKEKHST 300
QAKNRAKRKP PKGMFLSQED VEAVSANATA ATTVLRQLDM ELVSVKRQIQ 350
NIKQTNSALK EKLDGGIEPY RLPEVIQKCN ARWTTEEQLL AVQAIRKYGR 400
DFQAISDVIG NKSVVQVKNF FVNYRRRFNI DEVLQEWEAE HGKEETNGPS 450
NQKPVKSPDN SIKMPEEEDE APVLDVRYAS AS 482
Length:482
Mass (Da):53,028
Last modified:May 1, 2000 - v1
Checksum:i17541695A56CFFD3
GO

Sequence cautioni

The sequence AAH64495.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF155595 mRNA. Translation: AAF01498.1.
BC051003 mRNA. Translation: AAH51003.1.
BC064495 mRNA. Translation: AAH64495.1. Sequence problems.
D31888 mRNA. Translation: BAA06686.1.
RefSeqiNP_055971.2. NM_015156.3.
UniGeneiHs.510521.

Genome annotation databases

EnsembliENST00000570597; ENSP00000459789; ENSG00000089902.
GeneIDi23186.
KEGGihsa:23186.

Polymorphism databases

DMDMi74762776.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF155595 mRNA. Translation: AAF01498.1 .
BC051003 mRNA. Translation: AAH51003.1 .
BC064495 mRNA. Translation: AAH64495.1 . Sequence problems.
D31888 mRNA. Translation: BAA06686.1 .
RefSeqi NP_055971.2. NM_015156.3.
UniGenei Hs.510521.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
3ZMS X-ray 2.96 B 1-482 [» ]
3ZMT X-ray 3.10 B 1-482 [» ]
3ZMU X-ray 3.20 B 1-482 [» ]
3ZMV X-ray 3.00 B 1-482 [» ]
3ZMZ X-ray 3.00 B 1-482 [» ]
3ZN0 X-ray 2.80 B 1-482 [» ]
3ZN1 X-ray 3.10 B 1-482 [» ]
4BAY X-ray 3.10 B 308-440 [» ]
4KUM X-ray 3.05 B 286-482 [» ]
ProteinModelPortali Q9UKL0.
SMRi Q9UKL0. Positions 100-236, 308-440.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116796. 46 interactions.
DIPi DIP-35263N.
IntActi Q9UKL0. 15 interactions.
MINTi MINT-3081566.
STRINGi 9606.ENSP00000262241.

PTM databases

PhosphoSitei Q9UKL0.

Polymorphism databases

DMDMi 74762776.

Proteomic databases

MaxQBi Q9UKL0.
PaxDbi Q9UKL0.
PeptideAtlasi Q9UKL0.
PRIDEi Q9UKL0.

Protocols and materials databases

DNASUi 23186.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000570597 ; ENSP00000459789 ; ENSG00000089902 .
GeneIDi 23186.
KEGGi hsa:23186.

Organism-specific databases

CTDi 23186.
GeneCardsi GC14P103059.
HGNCi HGNC:17441. RCOR1.
HPAi CAB001956.
HPA049327.
HPA054241.
MIMi 607675. gene.
neXtProti NX_Q9UKL0.
PharmGKBi PA34305.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG326181.
HOGENOMi HOG000065784.
HOVERGENi HBG079800.
InParanoidi Q9UKL0.
KOi K11829.
PhylomeDBi Q9UKL0.
TreeFami TF106450.

Enzyme and pathway databases

Reactomei REACT_24970. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

EvolutionaryTracei Q9UKL0.
GeneWikii RCOR1.
GenomeRNAii 23186.
NextBioi 44655.
PROi Q9UKL0.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UKL0.
Bgeei Q9UKL0.
CleanExi HS_RCOR1.
Genevestigatori Q9UKL0.

Family and domain databases

Gene3Di 1.10.10.60. 1 hit.
InterProi IPR000949. ELM2_dom.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
[Graphical view ]
Pfami PF01448. ELM2. 1 hit.
PF00249. Myb_DNA-binding. 1 hit.
[Graphical view ]
SMARTi SM00717. SANT. 2 hits.
[Graphical view ]
SUPFAMi SSF46689. SSF46689. 2 hits.
PROSITEi PS51156. ELM2. 1 hit.
PS51293. SANT. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: FUNCTION.
  11. "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.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "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.
  18. "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.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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].
  21. 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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 286-482 IN COMPLEX WITH KDM1A.

Entry informationi

Entry nameiRCOR1_HUMAN
AccessioniPrimary (citable) accession number: Q9UKL0
Secondary accession number(s): Q15044, Q6P2I9, Q86VG5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: May 1, 2000
Last modified: September 3, 2014
This is version 128 of the entry and version 1 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 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

External Data

Dasty 3

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