Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q6ZPI3

- LCOR_MOUSE

UniProt

Q6ZPI3 - LCOR_MOUSE

Protein

Ligand-dependent corepressor

Gene

Lcor

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 2 (30 May 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Repressor of ligand-dependent transcription activation by various nuclear repressors. Repressor of ligand-dependent transcription activation by ESR1, ESR2, NR3C1, PGR, RARA, RARB, RARG, RXRA and VDR By similarity. May act as transcription activator that binds DNA elements with the sequence 5'-CCCTATCGATCGATCTCTACCT-3'.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: MGI
    3. transcription factor binding Source: MGI

    GO - Biological processi

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

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:2443930. Lcor.

    Subcellular locationi

    Nucleus PROSITE-ProRule annotation

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 433433Ligand-dependent corepressorPRO_0000236808Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei63 – 631PhosphoserineBy similarity
    Modified residuei249 – 2491PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ6ZPI3.

    PTM databases

    PhosphoSiteiQ6ZPI3.

    Expressioni

    Tissue specificityi

    Detected in heart and kidney.1 Publication

    Gene expression databases

    ArrayExpressiQ6ZPI3.
    BgeeiQ6ZPI3.
    CleanExiMM_LCOR.
    GenevestigatoriQ6ZPI3.

    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 By similarity.By similarity

    Protein-protein interaction databases

    DIPiDIP-60279N.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6ZPI3.
    SMRiQ6ZPI3. Positions 346-405.
    ModBaseiSearch...
    MobiDBiSearch...

    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 receptorsBy similarity
    Motifi339 – 3457Nuclear localization signalSequence Analysis

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG309364.
    GeneTreeiENSGT00520000055615.
    HOGENOMiHOG000253915.
    HOVERGENiHBG079596.
    InParanoidiQ6ZPI3.
    OMAiFQDCEPE.
    OrthoDBiEOG73RBBB.
    PhylomeDBiQ6ZPI3.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q6ZPI3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQRMIQQFAA EYTSKTSSTQ DPSQPNSTKN QSLPKASPVT TSPTAATTQN    50
    PVLSKLLMAD QDSPLDLTVR KSQSEPSEQD GVLDLSTKKS PCASSTSLSH 100
    SPGCSSTQGN GRPGRPSQYR PDGLRSGDGV PPRSLQDGTR EGFGHSTSLK 150
    VPLARSLQIS EELLSRNQLS TAASLGPSGL QNHGQHLILS REASWAKPHY 200
    EFSLSRMKFR GNGALSNISD LPFLAENSAF PKMAHQTKQD GKRDMSHSSP 250
    VDLKIPQVRG MDLSWESRTG DQYSYSSLVM GSQTESALSK KLRAILPKQN 300
    RKSMLDAGPD SWGSDAEQST SGQPYPTSDQ EGDPGSKQPR KKRGRYRQYN 350
    SEILEEAISV VMSGKMSVSK AQSIYGIPHS TLEYKVKERL GTLKNPPKKK 400
    MKLMRSEGPD VSVKIELDPQ GEAAQSANES KTE 433
    Length:433
    Mass (Da):47,125
    Last modified:May 30, 2006 - v2
    Checksum:i736656D1F7E9A041
    GO

    Sequence cautioni

    The sequence BAE32988.1 differs from that shown. Reason: Frameshift at position 421.
    The sequence BAC98252.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti311 – 3111S → F in BAE32988. (PubMed:16141072)Curated
    Sequence conflicti382 – 3821L → P in AAH90652. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB076079 mRNA. Translation: BAC20955.1.
    AK129442 mRNA. Translation: BAC98252.1. Different initiation.
    AK041090 mRNA. Translation: BAC30816.1.
    AK041621 mRNA. Translation: BAC31007.2.
    AK155007 mRNA. Translation: BAE32988.1. Frameshift.
    BC050068 mRNA. Translation: AAH50068.1.
    BC090652 mRNA. Translation: AAH90652.1.
    CCDSiCCDS29810.1.
    RefSeqiNP_742166.1. NM_172154.4.
    XP_006526912.1. XM_006526849.1.
    XP_006526913.1. XM_006526850.1.
    UniGeneiMm.422910.
    Mm.459119.

    Genome annotation databases

    EnsembliENSMUST00000067795; ENSMUSP00000067603; ENSMUSG00000025019.
    ENSMUST00000163929; ENSMUSP00000126441; ENSMUSG00000025019.
    GeneIDi212391.
    KEGGimmu:212391.
    UCSCiuc008hly.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB076079 mRNA. Translation: BAC20955.1 .
    AK129442 mRNA. Translation: BAC98252.1 . Different initiation.
    AK041090 mRNA. Translation: BAC30816.1 .
    AK041621 mRNA. Translation: BAC31007.2 .
    AK155007 mRNA. Translation: BAE32988.1 . Frameshift.
    BC050068 mRNA. Translation: AAH50068.1 .
    BC090652 mRNA. Translation: AAH90652.1 .
    CCDSi CCDS29810.1.
    RefSeqi NP_742166.1. NM_172154.4.
    XP_006526912.1. XM_006526849.1.
    XP_006526913.1. XM_006526850.1.
    UniGenei Mm.422910.
    Mm.459119.

    3D structure databases

    ProteinModelPortali Q6ZPI3.
    SMRi Q6ZPI3. Positions 346-405.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-60279N.

    PTM databases

    PhosphoSitei Q6ZPI3.

    Proteomic databases

    PRIDEi Q6ZPI3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000067795 ; ENSMUSP00000067603 ; ENSMUSG00000025019 .
    ENSMUST00000163929 ; ENSMUSP00000126441 ; ENSMUSG00000025019 .
    GeneIDi 212391.
    KEGGi mmu:212391.
    UCSCi uc008hly.1. mouse.

    Organism-specific databases

    CTDi 84458.
    MGIi MGI:2443930. Lcor.
    Rougei Search...

    Phylogenomic databases

    eggNOGi NOG309364.
    GeneTreei ENSGT00520000055615.
    HOGENOMi HOG000253915.
    HOVERGENi HBG079596.
    InParanoidi Q6ZPI3.
    OMAi FQDCEPE.
    OrthoDBi EOG73RBBB.
    PhylomeDBi Q6ZPI3.
    TreeFami TF319589.

    Miscellaneous databases

    NextBioi 373549.
    PROi Q6ZPI3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6ZPI3.
    Bgeei Q6ZPI3.
    CleanExi MM_LCOR.
    Genevestigatori Q6ZPI3.

    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. "Identification and characterization of Mlr1,2: two mouse homologues of Mblk-1, a transcription factor from the honeybee brain."
      Kunieda T., Park J.-M., Takeuchi H., Kubo T.
      FEBS Lett. 535:61-65(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: Brain.
    2. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
      DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Embryonic tail.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Aorta, Dendritic cell, Thymus and Vein.
    4. "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].
      Strain: C57BL/6.
      Tissue: Head and Mammary gland.

    Entry informationi

    Entry nameiLCOR_MOUSE
    AccessioniPrimary (citable) accession number: Q6ZPI3
    Secondary accession number(s): Q3U302
    , Q5CZW7, Q80VA8, Q8BGT2, Q8C9Q0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2006
    Last sequence update: May 30, 2006
    Last modified: October 1, 2014
    This is version 73 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3