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Q9UKL0

- RCOR1_HUMAN

UniProt

Q9UKL0 - RCOR1_HUMAN

Protein

REST corepressor 1

Gene

RCOR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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

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

    GO - Cellular componenti

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

    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 – 1241Phosphoserine4 Publications
    Modified residuei257 – 2571Phosphoserine5 Publications
    Modified residuei457 – 4571Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated by HSV-1 protein kinases in case of infection.6 Publications

    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.By similarity12 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UKL0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini100 – 18687ELM2PROSITE-ProRule annotationAdd
    BLAST
    Domaini187 – 23852SANT 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini378 – 42952SANT 2PROSITE-ProRule annotationAdd
    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 – 27030Sequence AnalysisAdd
    BLAST
    Coiled coili331 – 36636Sequence AnalysisAdd
    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.Curated
    Contains 1 ELM2 domain.PROSITE-ProRule annotation
    Contains 2 SANT domains.PROSITE-ProRule annotation

    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

    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: October 1, 2014
    This is version 129 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

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