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Q96JN0

- LCOR_HUMAN

UniProt

Q96JN0 - LCOR_HUMAN

Protein

Ligand-dependent corepressor

Gene

LCOR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 2 (30 May 2006)
      Previous versions | rss
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    Functioni

    May act as transcription activator that binds DNA elements with the sequence 5'-CCCTATCGATCGATCTCTACCT-3' By similarity. Repressor of ligand-dependent transcription activation by target nuclear receptors. Repressor of ligand-dependent transcription activation by ESR1, ESR2, NR3C1, PGR, RARA, RARB, RARG, RXRA and VDR.By similarity1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi368 – 38821H-T-H motifPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. sequence-specific DNA binding transcription factor activity Source: Ensembl

    GO - Biological processi

    1. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    2. transcription from RNA polymerase II promoter Source: Ensembl

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ligand-dependent corepressor
    Short name:
    LCoR
    Alternative name(s):
    Mblk1-related protein 2
    Gene namesi
    Name:LCOR
    Synonyms:KIAA1795, MLR2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:29503. LCOR.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi56 – 572LL → AA: Loss of estradiol-dependent interaction with ESR1 and ESR2. 1 Publication

    Organism-specific databases

    PharmGKBiPA145148487.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 433433Ligand-dependent corepressorPRO_0000236807Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei63 – 631Phosphoserine1 Publication
    Modified residuei249 – 2491Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ96JN0.
    PaxDbiQ96JN0.
    PRIDEiQ96JN0.

    PTM databases

    PhosphoSiteiQ96JN0.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    BgeeiQ96JN0.
    CleanExiHS_LCOR.
    GenevestigatoriQ96JN0.

    Organism-specific databases

    HPAiHPA031428.

    Interactioni

    Subunit structurei

    Interacts with ESR1 and ESR2 in the presence of estradiol. Interacts with CTBP1, HDAC3 and HDAC6. Component of a large corepressor complex that contains about 20 proteins, including CTBP1, CTBP2, HDAC1 and HDAC2.2 Publications

    Protein-protein interaction databases

    BioGridi124093. 10 interactions.
    STRINGi9606.ENSP00000348298.

    Structurei

    Secondary structure

    1
    433
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi351 – 36212
    Helixi368 – 3758
    Helixi379 – 38911
    Turni390 – 3934

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2COBNMR-A343-405[»]
    ProteinModelPortaliQ96JN0.
    SMRiQ96JN0. Positions 346-405.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96JN0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini340 – 39253HTH psq-typePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi53 – 575Interaction with nuclear receptors
    Motifi339 – 3457Nuclear localization signalSequence Analysis

    Sequence similaritiesi

    Contains 1 HTH psq-type DNA-binding domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG309364.
    HOVERGENiHBG079596.
    InParanoidiQ96JN0.
    OMAiFQDCEPE.
    OrthoDBiEOG73RBBB.
    PhylomeDBiQ96JN0.
    TreeFamiTF319589.

    Family and domain databases

    InterProiIPR009057. Homeodomain-like.
    IPR007889. HTH_Psq.
    [Graphical view]
    PfamiPF05225. HTH_psq. 1 hit.
    [Graphical view]
    SUPFAMiSSF46689. SSF46689. 1 hit.
    PROSITEiPS50960. HTH_PSQ. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96JN0-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MQRMIQQFAA EYTSKNSSTQ DPSQPNSTKN QSLPKASPVT TSPTAATTQN    50
    PVLSKLLMAD QDSPLDLTVR KSQSEPSEQD GVLDLSTKKS PCAGSTSLSH 100
    SPGCSSTQGN GRPGRPSQYR PDGLRSGDGV PPRSLQDGTR EGFGHSTSLK 150
    VPLARSLQIS EELLSRNQLS TAASLGPSGL QNHGQHLILS REASWAKPHY 200
    EFNLSRMKFR GNGALSNISD LPFLAENSAF PKMALQAKQD GKKDVSHSSP 250
    VDLKIPQVRG MDLSWESRTG DQYSYSSLVM GSQTESALSK KLRAILPKQS 300
    RKSMLDAGPD SWGSDAEQST SGQPYPTSDQ EGDPGSKQPR KKRGRYRQYN 350
    SEILEEAISV VMSGKMSVSK AQSIYGIPHS TLEYKVKERL GTLKNPPKKK 400
    MKLMRSEGPD VSVKIELDPQ GEAAQSANES KNE 433
    Length:433
    Mass (Da):47,007
    Last modified:May 30, 2006 - v2
    Checksum:i5F934FE687417740
    GO
    Isoform 2 (identifier: Q96JN0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         405-406: RS → SG
         407-433: Missing.

    Show »
    Length:406
    Mass (Da):44,083
    Checksum:iACE760CF3CB1F2EF
    GO

    Sequence cautioni

    The sequence BAB47424.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61Q → P in CAD91159. (PubMed:17974005)Curated
    Sequence conflicti321 – 3211S → P in CAD38921. (PubMed:17974005)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei405 – 4062RS → SG in isoform 2. 1 PublicationVSP_018585
    Alternative sequencei407 – 43327Missing in isoform 2. 1 PublicationVSP_018586Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB058698 mRNA. Translation: BAB47424.1. Different initiation.
    AL834245 mRNA. Translation: CAD38921.2.
    AL832106 mRNA. Translation: CAD91159.1.
    AL832044 mRNA. Translation: CAD91160.1.
    AL442123 Genomic DNA. Translation: CAH70915.1.
    CH471066 Genomic DNA. Translation: EAW49963.1.
    CH471066 Genomic DNA. Translation: EAW49965.1.
    CH471066 Genomic DNA. Translation: EAW49966.1.
    BC053359 mRNA. Translation: AAH53359.1.
    CCDSiCCDS53561.1. [Q96JN0-2]
    CCDS7451.1. [Q96JN0-1]
    RefSeqiNP_001164236.1. NM_001170765.1. [Q96JN0-1]
    NP_001164237.1. NM_001170766.1. [Q96JN0-2]
    NP_115816.2. NM_032440.3. [Q96JN0-1]
    XP_006718097.1. XM_006718034.1. [Q96JN0-1]
    UniGeneiHs.745068.

    Genome annotation databases

    EnsembliENST00000356016; ENSP00000348298; ENSG00000196233. [Q96JN0-1]
    ENST00000371097; ENSP00000360138; ENSG00000196233. [Q96JN0-1]
    ENST00000371103; ENSP00000360144; ENSG00000196233. [Q96JN0-1]
    ENST00000540664; ENSP00000443431; ENSG00000196233. [Q96JN0-2]
    GeneIDi84458.
    KEGGihsa:84458.
    UCSCiuc001kmr.3. human. [Q96JN0-2]
    uc001kms.2. human. [Q96JN0-1]

    Polymorphism databases

    DMDMi108936028.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB058698 mRNA. Translation: BAB47424.1 . Different initiation.
    AL834245 mRNA. Translation: CAD38921.2 .
    AL832106 mRNA. Translation: CAD91159.1 .
    AL832044 mRNA. Translation: CAD91160.1 .
    AL442123 Genomic DNA. Translation: CAH70915.1 .
    CH471066 Genomic DNA. Translation: EAW49963.1 .
    CH471066 Genomic DNA. Translation: EAW49965.1 .
    CH471066 Genomic DNA. Translation: EAW49966.1 .
    BC053359 mRNA. Translation: AAH53359.1 .
    CCDSi CCDS53561.1. [Q96JN0-2 ]
    CCDS7451.1. [Q96JN0-1 ]
    RefSeqi NP_001164236.1. NM_001170765.1. [Q96JN0-1 ]
    NP_001164237.1. NM_001170766.1. [Q96JN0-2 ]
    NP_115816.2. NM_032440.3. [Q96JN0-1 ]
    XP_006718097.1. XM_006718034.1. [Q96JN0-1 ]
    UniGenei Hs.745068.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2COB NMR - A 343-405 [» ]
    ProteinModelPortali Q96JN0.
    SMRi Q96JN0. Positions 346-405.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124093. 10 interactions.
    STRINGi 9606.ENSP00000348298.

    PTM databases

    PhosphoSitei Q96JN0.

    Polymorphism databases

    DMDMi 108936028.

    Proteomic databases

    MaxQBi Q96JN0.
    PaxDbi Q96JN0.
    PRIDEi Q96JN0.

    Protocols and materials databases

    DNASUi 84458.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356016 ; ENSP00000348298 ; ENSG00000196233 . [Q96JN0-1 ]
    ENST00000371097 ; ENSP00000360138 ; ENSG00000196233 . [Q96JN0-1 ]
    ENST00000371103 ; ENSP00000360144 ; ENSG00000196233 . [Q96JN0-1 ]
    ENST00000540664 ; ENSP00000443431 ; ENSG00000196233 . [Q96JN0-2 ]
    GeneIDi 84458.
    KEGGi hsa:84458.
    UCSCi uc001kmr.3. human. [Q96JN0-2 ]
    uc001kms.2. human. [Q96JN0-1 ]

    Organism-specific databases

    CTDi 84458.
    GeneCardsi GC10P098583.
    HGNCi HGNC:29503. LCOR.
    HPAi HPA031428.
    MIMi 607698. gene.
    neXtProti NX_Q96JN0.
    PharmGKBi PA145148487.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG309364.
    HOVERGENi HBG079596.
    InParanoidi Q96JN0.
    OMAi FQDCEPE.
    OrthoDBi EOG73RBBB.
    PhylomeDBi Q96JN0.
    TreeFami TF319589.

    Miscellaneous databases

    EvolutionaryTracei Q96JN0.
    GeneWikii LCOR.
    GenomeRNAii 84458.
    NextBioi 74251.
    PROi Q96JN0.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q96JN0.
    CleanExi HS_LCOR.
    Genevestigatori Q96JN0.

    Family and domain databases

    InterProi IPR009057. Homeodomain-like.
    IPR007889. HTH_Psq.
    [Graphical view ]
    Pfami PF05225. HTH_psq. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46689. SSF46689. 1 hit.
    PROSITEi PS50960. HTH_PSQ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
      DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Bone marrow and Skeletal muscle.
    3. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 2).
      Tissue: Lung.
    6. "Ligand-dependent nuclear receptor corepressor LCoR functions by histone deacetylase-dependent and -independent mechanisms."
      Fernandes I., Bastien Y., Wai T., Nygard K., Lin R., Cormier O., Lee H.S., Eng F., Bertos N.R., Pelletier N., Mader S., Han V.K.M., Yang X.-J., White J.H.
      Mol. Cell 11:139-150(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CTBP1; ESR1; ESR2; HDAC3 AND HDAC6, SUBCELLULAR LOCATION, MUTAGENESIS OF 56-LEU-LEU-57, TISSUE SPECIFICITY.
    7. "Coordinated histone modifications mediated by a CtBP co-repressor complex."
      Shi Y., Sawada J., Sui G., Affar E.B., Whetstine J.R., Lan F., Ogawa H., Luke M.P.-S., Nakatani Y., Shi Y.
      Nature 422:735-738(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COREPRESSOR COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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-63 AND SER-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Solution structures of the HTH domain of human LCOR protein."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 343-405.

    Entry informationi

    Entry nameiLCOR_HUMAN
    AccessioniPrimary (citable) accession number: Q96JN0
    Secondary accession number(s): D3DR47
    , Q5VW16, Q7Z723, Q86T32, Q86T33, Q8N3L6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2006
    Last sequence update: May 30, 2006
    Last modified: October 1, 2014
    This is version 92 of the entry and version 2 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 10
      Human chromosome 10: 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