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O88712

- CTBP1_MOUSE

UniProt

O88712 - CTBP1_MOUSE

Protein

C-terminal-binding protein 1

Gene

Ctbp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (01 May 2007)
      Previous versions | rss
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    Functioni

    Corepressor targeting diverse transcription regulators such as GLIS2 or BCL6. Has dehydrogenase activity. Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Functions in brown adipose tissue (BAT) differentiation.5 Publications

    Cofactori

    NAD. Cofactor binding induces a conformation change By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei100 – 1001NADBy similarity
    Binding sitei204 – 2041NADBy similarity
    Active sitei266 – 2661By similarity
    Binding sitei290 – 2901NADBy similarity
    Active sitei295 – 2951By similarity
    Active sitei315 – 3151Proton donorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi180 – 1856NADBy similarity
    Nucleotide bindingi237 – 2437NADBy similarity
    Nucleotide bindingi264 – 2663NADBy similarity
    Nucleotide bindingi315 – 3184NADBy similarity

    GO - Molecular functioni

    1. NAD binding Source: UniProtKB
    2. oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: InterPro
    3. protein binding Source: UniProtKB
    4. RNA polymerase II transcription corepressor activity Source: Ensembl
    5. sequence-specific DNA binding transcription factor activity Source: MGI
    6. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. Golgi organization Source: Ensembl
    2. negative regulation of histone H4 acetylation Source: Ensembl
    3. negative regulation of transcription, DNA-templated Source: UniProtKB
    4. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    5. positive regulation of histone deacetylation Source: Ensembl
    6. regulation of cell cycle Source: Ensembl
    7. regulation of transcription by chromatin organization Source: Ensembl
    8. white fat cell differentiation Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase, Repressor

    Keywords - Biological processi

    Differentiation, Transcription, Transcription regulation

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    ReactomeiREACT_219771. deactivation of the beta-catenin transactivating complex.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    C-terminal-binding protein 1 (EC:1.1.1.-)
    Short name:
    CtBP1
    Gene namesi
    Name:Ctbp1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:1201685. Ctbp1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. nucleus Source: UniProtKB
    3. transcriptional repressor complex Source: UniProtKB
    4. transcription factor complex Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 441441C-terminal-binding protein 1PRO_0000076042Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei300 – 3001PhosphoserineBy similarity
    Modified residuei423 – 4231PhosphoserineBy similarity
    Cross-linki429 – 429Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

    Post-translational modificationi

    ADP-ribosylated; when cells are exposed to brefeldin A.By similarity
    The level of phosphorylation appears to be regulated during the cell cycle. Phosphorylation by HIPK2 on Ser-423 induces proteasomal degradation By similarity.By similarity
    Sumoylation on Lys-429 is promoted by the E3 SUMO-protein ligase CBX4.By similarity

    Keywords - PTMi

    ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO88712.
    PaxDbiO88712.
    PRIDEiO88712.

    PTM databases

    PhosphoSiteiO88712.

    Expressioni

    Tissue specificityi

    Expressed in a wide range of adult tissues.1 Publication

    Developmental stagei

    Expressed throughout the developmental stages.1 Publication

    Gene expression databases

    BgeeiO88712.
    CleanExiMM_CTBP1.
    GenevestigatoriO88712.

    Interactioni

    Subunit structurei

    Homo- or heterodimer. Heterodimer with CTBP2. Interacts with ELK3 (via its PXDLS motif). Interacts with RBBP8 (via its PXDLS motif). Interacts with PNN, MECOM, ZNF366 and ZFHX1B. Interaction with SATB1 (non-acetylated form); the interaction stabilizes its attachment to DNA and promotes transcription repression. Interacts with PRDM16; the interaction represses white adipose tissue (WAT)-specific genes expression. Interacts with GLIS2, HIPK2, FOXP1, FOXP2, HDAC4, HDAC5, HDAC9, NRIP1, WIZ and ZNF217. Interacts with BCL6; the interaction is required for BCL6 transcriptional autoinhibition and inhibition of some BCL6 target genes.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HIC1Q1452610EBI-604547,EBI-2507362From a different organism.
    Zeb1Q643184EBI-604547,EBI-8560245

    Protein-protein interaction databases

    BioGridi198961. 13 interactions.
    DIPiDIP-33907N.
    IntActiO88712. 10 interactions.
    MINTiMINT-146962.

    Structurei

    3D structure databases

    ProteinModelPortaliO88712.
    SMRiO88712. Positions 26-356.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 7070Interaction with GLIS2 1Add
    BLAST
    Regioni288 – 36073Interaction with GLIS2 2Add
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0111.
    GeneTreeiENSGT00530000063021.
    HOVERGENiHBG001898.
    InParanoidiO88712.
    KOiK04496.
    OMAiDRDHPSD.
    OrthoDBiEOG761BT9.
    PhylomeDBiO88712.
    TreeFamiTF313593.

    Family and domain databases

    Gene3Di3.40.50.720. 2 hits.
    InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
    IPR006140. D-isomer_DH_NAD-bd.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00389. 2-Hacid_dh. 1 hit.
    PF02826. 2-Hacid_dh_C. 1 hit.
    [Graphical view]
    PROSITEiPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
    PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O88712-1) [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

    MGSSHLLNKG LPLGVRPPIM NGPMHPRPLV ALLDGRDCTV EMPILKDVAT    50
    VAFCDAQSTQ EIHEKVLNEA VGALMYHTIT LTREDLEKFK ALRIIVRIGS 100
    GFDNIDIKSA GDLGIAVCNV PAASVEETAD STLCHILNLY RRTTWLHQAL 150
    REGTRVQSVE QIREVASGAA RIRGETLGII GLGRVGQAVA LRAKAFGFNV 200
    LFYDPYLSDG IERALGLQRV STLQDLLFHS DCVTLHCGLN EHNHHLINDF 250
    TVKQMRQGAF LVNTARGGLV DEKALAQALK EGRIRGAALD VHESEPFSFS 300
    QGPLKDAPNL ICTPHAAWYS EQASIEMREE AAREIRRAIT GRIPDSLKNC 350
    VNKDHLTAAT HWASMDPAVV HPELNGAAYS RYPPGVVSVA PTGIPAAVEG 400
    IVPSAMSLSH GLPPVAHPPH APSPGQTVKP EADRDHTSDQ L 441
    Length:441
    Mass (Da):47,745
    Last modified:May 1, 2007 - v2
    Checksum:i2105CC8D69D915F4
    GO
    Isoform 2 (identifier: O88712-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-13: MGSSHLLNKGLPL → MS

    Show »
    Length:430
    Mass (Da):46,614
    Checksum:i0A36DBF66E6A8605
    GO
    Isoform 3 (identifier: O88712-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-74: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:367
    Mass (Da):39,848
    Checksum:i0E71CBDFDBF2EDA9
    GO

    Sequence cautioni

    The sequence BAE41586.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti55 – 551D → G in BAE41586. (PubMed:16141072)Curated
    Sequence conflicti55 – 551D → G in BAE42587. (PubMed:16141072)Curated
    Sequence conflicti108 – 1081K → R in BAE35946. (PubMed:16141072)Curated
    Sequence conflicti380 – 3801Missing in CAA09219. (PubMed:10369679)Curated
    Sequence conflicti380 – 3801Missing in BAE35946. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7474Missing in isoform 3. 1 PublicationVSP_024737Add
    BLAST
    Alternative sequencei1 – 1313MGSSH…KGLPL → MS in isoform 2. 2 PublicationsVSP_024738Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ010483 mRNA. Translation: CAA09219.1.
    AB033122 mRNA. Translation: BAA85180.1.
    AK133816 mRNA. Translation: BAE21859.1.
    AK160658 mRNA. Translation: BAE35946.1.
    AK165276 mRNA. Translation: BAE38115.1.
    AK170133 mRNA. Translation: BAE41586.1. Different initiation.
    AK171650 mRNA. Translation: BAE42587.1.
    BC013702 mRNA. Translation: AAH13702.1.
    BC015071 mRNA. Translation: AAH15071.1.
    BC042425 mRNA. Translation: AAH42425.1.
    CCDSiCCDS19201.1. [O88712-1]
    RefSeqiNP_001185788.1. NM_001198859.1.
    NP_001185789.1. NM_001198860.1.
    NP_001185790.1. NM_001198861.1. [O88712-2]
    NP_038530.1. NM_013502.3. [O88712-1]
    XP_006503773.1. XM_006503710.1. [O88712-3]
    UniGeneiMm.7286.

    Genome annotation databases

    EnsembliENSMUST00000079746; ENSMUSP00000078682; ENSMUSG00000037373. [O88712-1]
    GeneIDi13016.
    KEGGimmu:13016.
    UCSCiuc008xaj.2. mouse. [O88712-1]
    uc008xak.2. mouse. [O88712-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ010483 mRNA. Translation: CAA09219.1 .
    AB033122 mRNA. Translation: BAA85180.1 .
    AK133816 mRNA. Translation: BAE21859.1 .
    AK160658 mRNA. Translation: BAE35946.1 .
    AK165276 mRNA. Translation: BAE38115.1 .
    AK170133 mRNA. Translation: BAE41586.1 . Different initiation.
    AK171650 mRNA. Translation: BAE42587.1 .
    BC013702 mRNA. Translation: AAH13702.1 .
    BC015071 mRNA. Translation: AAH15071.1 .
    BC042425 mRNA. Translation: AAH42425.1 .
    CCDSi CCDS19201.1. [O88712-1 ]
    RefSeqi NP_001185788.1. NM_001198859.1.
    NP_001185789.1. NM_001198860.1.
    NP_001185790.1. NM_001198861.1. [O88712-2 ]
    NP_038530.1. NM_013502.3. [O88712-1 ]
    XP_006503773.1. XM_006503710.1. [O88712-3 ]
    UniGenei Mm.7286.

    3D structure databases

    ProteinModelPortali O88712.
    SMRi O88712. Positions 26-356.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198961. 13 interactions.
    DIPi DIP-33907N.
    IntActi O88712. 10 interactions.
    MINTi MINT-146962.

    PTM databases

    PhosphoSitei O88712.

    Proteomic databases

    MaxQBi O88712.
    PaxDbi O88712.
    PRIDEi O88712.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000079746 ; ENSMUSP00000078682 ; ENSMUSG00000037373 . [O88712-1 ]
    GeneIDi 13016.
    KEGGi mmu:13016.
    UCSCi uc008xaj.2. mouse. [O88712-1 ]
    uc008xak.2. mouse. [O88712-2 ]

    Organism-specific databases

    CTDi 1487.
    MGIi MGI:1201685. Ctbp1.

    Phylogenomic databases

    eggNOGi COG0111.
    GeneTreei ENSGT00530000063021.
    HOVERGENi HBG001898.
    InParanoidi O88712.
    KOi K04496.
    OMAi DRDHPSD.
    OrthoDBi EOG761BT9.
    PhylomeDBi O88712.
    TreeFami TF313593.

    Enzyme and pathway databases

    Reactomei REACT_219771. deactivation of the beta-catenin transactivating complex.

    Miscellaneous databases

    ChiTaRSi CTBP1. mouse.
    NextBioi 282870.
    PROi O88712.
    SOURCEi Search...

    Gene expression databases

    Bgeei O88712.
    CleanExi MM_CTBP1.
    Genevestigatori O88712.

    Family and domain databases

    Gene3Di 3.40.50.720. 2 hits.
    InterProi IPR006139. D-isomer_2_OHA_DH_cat_dom.
    IPR006140. D-isomer_DH_NAD-bd.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF00389. 2-Hacid_dh. 1 hit.
    PF02826. 2-Hacid_dh_C. 1 hit.
    [Graphical view ]
    PROSITEi PS00065. D_2_HYDROXYACID_DH_1. 1 hit.
    PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Net, a negative Ras-switchable TCF, contains a second inhibition domain, the CID, that mediates repression through interactions with CtBP and de-acetylation."
      Criqui-Filipe P., Ducret C., Maira S.-M., Wasylyk B.
      EMBO J. 18:3392-3403(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
    2. "Identification of CtBP1 and CtBP2 as corepressors of zinc finger-homeodomain factor deltaEF1."
      Furusawa T., Moribe H., Kondoh H., Higashi Y.
      Mol. Cell. Biol. 19:8581-8590(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Strain: ICR.
    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] (ISOFORMS 2 AND 3).
      Strain: C57BL/6J and NOD.
      Tissue: Spleen.
    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] (ISOFORMS 1 AND 2).
      Strain: 129, FVB/N and FVB/N-3.
      Tissue: Mammary tumor and Salivary gland.
    5. Lubec G., Klug S., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 98-108 AND 286-305, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain and Hippocampus.
    6. "Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting transcription repressor (MITR) contributes to transcriptional repression of the MEF2 transcription factor."
      Zhang C.L., McKinsey T.A., Lu J.R., Olson E.N.
      J. Biol. Chem. 276:35-39(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HDAC4; HDAC5 AND HDAC9.
    7. "Homeodomain interacting protein kinase 2 promotes apoptosis by downregulating the transcriptional corepressor CtBP."
      Zhang Q., Yoshimatsu Y., Hildebrand J., Frisch S.M., Goodman R.H.
      Cell 115:177-186(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIPK2.
    8. "Characterization of four autonomous repression domains in the corepressor receptor interacting protein 140."
      Christian M., Tullet J.M.A., Parker M.G.
      J. Biol. Chem. 279:15645-15651(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NRIP1.
    9. "Transcriptional and DNA binding activity of the Foxp1/2/4 family is modulated by heterotypic and homotypic protein interactions."
      Li S., Weidenfeld J., Morrisey E.E.
      Mol. Cell. Biol. 24:809-822(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FOXP1 AND FOXP2.
    10. "Kruppel-like zinc finger protein Gli-similar 2 (Glis2) represses transcription through interaction with C-terminal binding protein 1 (CtBP1)."
      Kim S.-C., Kim Y.-S., Jetten A.M.
      Nucleic Acids Res. 33:6805-6815(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GLIS2, FUNCTION, SUBCELLULAR LOCATION.
    11. "Zinc finger protein Wiz links G9a/GLP histone methyltransferases to the co-repressor molecule CtBP."
      Ueda J., Tachibana M., Ikura T., Shinkai Y.
      J. Biol. Chem. 281:20120-20128(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WIZ.
    12. "Regulation of the brown and white fat gene programs through a PRDM16/CtBP transcriptional complex."
      Kajimura S., Seale P., Tomaru T., Erdjument-Bromage H., Cooper M.P., Ruas J.L., Chin S., Tempst P., Lazar M.A., Spiegelman B.M.
      Genes Dev. 22:1397-1409(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PRDM16, SUBCELLULAR LOCATION.
    13. "Acetylation-dependent interaction of SATB1 and CtBP1 mediates transcriptional repression by SATB1."
      Purbey P.K., Singh S., Notani D., Kumar P.P., Limaye A.S., Galande S.
      Mol. Cell. Biol. 29:1321-1337(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SATB1.

    Entry informationi

    Entry nameiCTBP1_MOUSE
    AccessioniPrimary (citable) accession number: O88712
    Secondary accession number(s): Q3TAT1
    , Q3TDL5, Q3TUM5, Q91WI6, Q91YX3, Q9QYG2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 134 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, Direct protein sequencing, 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