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Q13363

- CTBP1_HUMAN

UniProt

Q13363 - CTBP1_HUMAN

Protein

C-terminal-binding protein 1

Gene

CTBP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 2 (15 Jul 1999)
      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. Required for efficient interaction with E1A. Cofactor binding induces a conformation change.1 Publication

    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. protein C-terminus binding Source: ProtInc
    5. protein domain specific binding Source: UniProtKB
    6. repressing transcription factor binding Source: BHF-UCL
    7. RNA polymerase II transcription corepressor activity Source: BHF-UCL
    8. sequence-specific DNA binding transcription factor activity Source: Ensembl
    9. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. Golgi organization Source: Ensembl
    2. negative regulation of cell proliferation Source: ProtInc
    3. negative regulation of histone acetylation Source: BHF-UCL
    4. negative regulation of histone H4 acetylation Source: BHF-UCL
    5. negative regulation of transcription, DNA-templated Source: UniProtKB
    6. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    7. positive regulation of histone deacetylation Source: BHF-UCL
    8. protein phosphorylation Source: ProtInc
    9. regulation of cell cycle Source: BHF-UCL
    10. regulation of transcription by chromatin organization Source: BHF-UCL
    11. viral genome replication Source: ProtInc
    12. white fat cell differentiation Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase, Repressor

    Keywords - Biological processi

    Differentiation, Host-virus interaction, Transcription, Transcription regulation

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    ReactomeiREACT_200731. deactivation of the beta-catenin transactivating complex.
    SignaLinkiQ13363.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    C-terminal-binding protein 1 (EC:1.1.1.-)
    Short name:
    CtBP1
    Gene namesi
    Name:CTBP1
    Synonyms:CTBP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:2494. CTBP1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi134 – 1341C → A: Strongly reduces E1A binding; when associated with A-138; A-141 and A-150. 1 Publication
    Mutagenesisi138 – 1381N → A: Strongly reduces E1A binding; when associated with A-134; A-141 and A-150. 1 Publication
    Mutagenesisi141 – 1422RR → AA: Strongly reduces E1A binding; when associated with A-163 and A-171. 1 Publication
    Mutagenesisi141 – 1411R → A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-150. 1 Publication
    Mutagenesisi150 – 1501L → A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-141. 1 Publication
    Mutagenesisi163 – 1631R → A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-171. 1 Publication
    Mutagenesisi171 – 1711R → A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-163. 1 Publication
    Mutagenesisi181 – 1811G → V: Strongly reduces E1A binding; when associated with V-183 and A-204. 1 Publication
    Mutagenesisi183 – 1831G → V: Strongly reduces E1A binding; when associated with V-181 and A-204. 1 Publication
    Mutagenesisi204 – 2041D → A: Strongly reduces E1A binding; when associated with V-181 and V-183. 1 Publication
    Mutagenesisi266 – 2661R → A: Strongly reduces E1A binding; when associated with A-290; A-295 and A-315. 1 Publication
    Mutagenesisi290 – 2901D → A: Strongly reduces E1A binding; when associated with A-266; A-295 and A-315. 1 Publication
    Mutagenesisi295 – 2951E → A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-315. 1 Publication
    Mutagenesisi315 – 3151H → A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-295. 1 Publication
    Mutagenesisi422 – 4221S → A: Abolishes phosphorylation by HIPK2 and prevents UV-induced clearance. 1 Publication

    Organism-specific databases

    PharmGKBiPA26995.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 440440C-terminal-binding protein 1PRO_0000076041Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei300 – 3001Phosphoserine2 Publications
    Modified residuei422 – 4221Phosphoserine; by HIPK22 Publications
    Cross-linki428 – 428Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

    Post-translational modificationi

    The level of phosphorylation appears to be regulated during the cell cycle. Phosphorylation by HIPK2 on Ser-422 induces proteasomal degradation.3 Publications
    ADP-ribosylated; when cells are exposed to brefeldin A.By similarity
    Sumoylation on Lys-428 is promoted by the E3 SUMO-protein ligase CBX4.1 Publication

    Keywords - PTMi

    ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ13363.
    PaxDbiQ13363.
    PRIDEiQ13363.

    PTM databases

    PhosphoSiteiQ13363.

    Expressioni

    Tissue specificityi

    Expressed in germinal center B-cells.1 Publication

    Gene expression databases

    ArrayExpressiQ13363.
    BgeeiQ13363.
    CleanExiHS_CTBP1.
    GenevestigatoriQ13363.

    Organism-specific databases

    HPAiCAB004217.
    HPA018987.
    HPA044971.

    Interactioni

    Subunit structurei

    Homo- or heterodimer. Heterodimer with CTBP2. Interacts with PRDM16; the interaction represses white adipose tissue (WAT)-specific genes expression. Interacts with GLIS2, FOXP2, HDAC4, HDAC5, HDAC9 and ZNF217. Interacts with adenovirus E1A protein (via its C-terminus); the interaction disrupts the interaction of CTBP1 with RBBP8. Interacts with Epstein-Barr virus EBNA3 and EBNA6. Interacts with ELK3 (via its PXDLS motif). Interacts with RBBP8 (via its PXDLS motif); the interaction is disrupted by binding to adenovirus E1A. Interacts with FOXP1, HIPK2, PNN, NRIP1, MECOM, ZNF366, ZFHX1B and WIZ. Interaction with SATB1 (non-acetylated form); the interaction stabilizes its attachment to DNA and promotes transcription repression. Interacts with BCL6; the interaction is required for BCL6 transcriptional autoinhibition and inhibition of some BCL6 target genes.17 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HEMGNQ9BXL52EBI-908846,EBI-3916399
    HIC1Q145264EBI-908846,EBI-2507362
    KLF4O434744EBI-908846,EBI-7232405
    THAP11Q96EK42EBI-908846,EBI-1790529
    Zbp1A2APF72EBI-908846,EBI-6115394From a different organism.
    ZNF366Q8N8955EBI-908846,EBI-2813661

    Protein-protein interaction databases

    BioGridi107869. 90 interactions.
    DIPiDIP-24245N.
    IntActiQ13363. 24 interactions.
    MINTiMINT-94454.
    STRINGi9606.ENSP00000290921.

    Structurei

    Secondary structure

    1
    440
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi29 – 346
    Turni39 – 413
    Helixi42 – 454
    Turni46 – 483
    Beta strandi50 – 534
    Helixi59 – 613
    Helixi64 – 696
    Beta strandi70 – 756
    Beta strandi77 – 793
    Helixi83 – 864
    Beta strandi94 – 1007
    Helixi107 – 1126
    Beta strandi116 – 1183
    Helixi125 – 14117
    Helixi143 – 1519
    Helixi159 – 1657
    Turni166 – 1683
    Beta strandi176 – 1805
    Helixi184 – 19411
    Turni195 – 1973
    Beta strandi199 – 2035
    Helixi211 – 2155
    Helixi223 – 2297
    Beta strandi231 – 2355
    Beta strandi246 – 2483
    Helixi249 – 2524
    Beta strandi259 – 2635
    Helixi267 – 2693
    Helixi272 – 2809
    Beta strandi283 – 2908
    Beta strandi293 – 2964
    Turni303 – 3064
    Beta strandi308 – 3125
    Helixi321 – 34020
    Turni343 – 3464
    Beta strandi348 – 3503

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1MX3X-ray1.95A28-353[»]
    4LCEX-ray2.38A28-353[»]
    ProteinModelPortaliQ13363.
    SMRiQ13363. Positions 28-352.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13363.

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0111.
    HOGENOMiHOG000136701.
    HOVERGENiHBG001898.
    InParanoidiQ13363.
    KOiK04496.
    OMAiDRDHPSD.
    OrthoDBiEOG761BT9.
    PhylomeDBiQ13363.
    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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13363-1) [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 NGPLHPRPLV ALLDGRDCTV EMPILKDVAT    50
    VAFCDAQSTQ EIHEKVLNEA VGALMYHTIT LTREDLEKFK ALRIIVRIGS 100
    GFDNIDIKSA GDLGIAVCNV PAASVEETAD STLCHILNLY RRATWLHQAL 150
    REGTRVQSVE QIREVASGAA RIRGETLGII GLGRVGQAVA LRAKAFGFNV 200
    LFYDPYLSDG VERALGLQRV STLQDLLFHS DCVTLHCGLN EHNHHLINDF 250
    TVKQMRQGAF LVNTARGGLV DEKALAQALK EGRIRGAALD VHESEPFSFS 300
    QGPLKDAPNL ICTPHAAWYS EQASIEMREE AAREIRRAIT GRIPDSLKNC 350
    VNKDHLTAAT HWASMDPAVV HPELNGAAYR YPPGVVGVAP TGIPAAVEGI 400
    VPSAMSLSHG LPPVAHPPHA PSPGQTVKPE ADRDHASDQL 440
    Length:440
    Mass (Da):47,535
    Last modified:July 15, 1999 - v2
    Checksum:iF071DD30B385603F
    GO
    Isoform 2 (identifier: Q13363-2) [UniParc]FASTAAdd to Basket

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

    Note: No experimental confirmation available.

    Show »
    Length:429
    Mass (Da):46,405
    Checksum:i0366A6370016910B
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1313MGSSH…KGLPL → MS in isoform 2. 1 PublicationVSP_043305Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U37408 mRNA. Translation: AAC62822.1.
    AF091555 mRNA. Translation: AAD14597.1.
    AC092535 Genomic DNA. Translation: AAY40989.1.
    CH471131 Genomic DNA. Translation: EAW82599.1.
    CH471131 Genomic DNA. Translation: EAW82600.1.
    CH471131 Genomic DNA. Translation: EAW82601.1.
    BC011655 mRNA. Translation: AAH11655.1.
    BC053320 mRNA. Translation: AAH53320.1.
    CCDSiCCDS3348.1. [Q13363-1]
    CCDS43203.1. [Q13363-2]
    RefSeqiNP_001012632.1. NM_001012614.1. [Q13363-2]
    NP_001319.1. NM_001328.2. [Q13363-1]
    UniGeneiHs.208597.

    Genome annotation databases

    EnsembliENST00000290921; ENSP00000290921; ENSG00000159692. [Q13363-1]
    ENST00000382952; ENSP00000372411; ENSG00000159692. [Q13363-2]
    GeneIDi1487.
    KEGGihsa:1487.
    UCSCiuc003gcu.1. human. [Q13363-2]
    uc003gcv.1. human. [Q13363-1]

    Polymorphism databases

    DMDMi6014741.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U37408 mRNA. Translation: AAC62822.1 .
    AF091555 mRNA. Translation: AAD14597.1 .
    AC092535 Genomic DNA. Translation: AAY40989.1 .
    CH471131 Genomic DNA. Translation: EAW82599.1 .
    CH471131 Genomic DNA. Translation: EAW82600.1 .
    CH471131 Genomic DNA. Translation: EAW82601.1 .
    BC011655 mRNA. Translation: AAH11655.1 .
    BC053320 mRNA. Translation: AAH53320.1 .
    CCDSi CCDS3348.1. [Q13363-1 ]
    CCDS43203.1. [Q13363-2 ]
    RefSeqi NP_001012632.1. NM_001012614.1. [Q13363-2 ]
    NP_001319.1. NM_001328.2. [Q13363-1 ]
    UniGenei Hs.208597.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MX3 X-ray 1.95 A 28-353 [» ]
    4LCE X-ray 2.38 A 28-353 [» ]
    ProteinModelPortali Q13363.
    SMRi Q13363. Positions 28-352.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107869. 90 interactions.
    DIPi DIP-24245N.
    IntActi Q13363. 24 interactions.
    MINTi MINT-94454.
    STRINGi 9606.ENSP00000290921.

    PTM databases

    PhosphoSitei Q13363.

    Polymorphism databases

    DMDMi 6014741.

    Proteomic databases

    MaxQBi Q13363.
    PaxDbi Q13363.
    PRIDEi Q13363.

    Protocols and materials databases

    DNASUi 1487.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000290921 ; ENSP00000290921 ; ENSG00000159692 . [Q13363-1 ]
    ENST00000382952 ; ENSP00000372411 ; ENSG00000159692 . [Q13363-2 ]
    GeneIDi 1487.
    KEGGi hsa:1487.
    UCSCi uc003gcu.1. human. [Q13363-2 ]
    uc003gcv.1. human. [Q13363-1 ]

    Organism-specific databases

    CTDi 1487.
    GeneCardsi GC04M001205.
    HGNCi HGNC:2494. CTBP1.
    HPAi CAB004217.
    HPA018987.
    HPA044971.
    MIMi 602618. gene.
    neXtProti NX_Q13363.
    PharmGKBi PA26995.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0111.
    HOGENOMi HOG000136701.
    HOVERGENi HBG001898.
    InParanoidi Q13363.
    KOi K04496.
    OMAi DRDHPSD.
    OrthoDBi EOG761BT9.
    PhylomeDBi Q13363.
    TreeFami TF313593.

    Enzyme and pathway databases

    Reactomei REACT_200731. deactivation of the beta-catenin transactivating complex.
    SignaLinki Q13363.

    Miscellaneous databases

    ChiTaRSi CTBP1. human.
    EvolutionaryTracei Q13363.
    GeneWikii CTBP1.
    GenomeRNAii 1487.
    NextBioi 6105.
    PROi Q13363.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13363.
    Bgeei Q13363.
    CleanExi HS_CTBP1.
    Genevestigatori Q13363.

    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. "Molecular cloning and characterization of a cellular phosphoprotein that interacts with a conserved C-terminal domain of adenovirus E1A involved in negative modulation of oncogenic transformation."
      Schaeper U., Boyd J.M., Verma S., Uhlmann E., Subramanian T., Chinnadurai G.
      Proc. Natl. Acad. Sci. U.S.A. 92:10467-10471(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 98-108, INTERACTION WITH RBBP8 AND ADENOVIRUS E1A.
      Tissue: B-cell and Cervix carcinoma.
    2. "C-terminal binding protein is a transcriptional repressor that interacts with a specific class of vertebrate polycomb proteins."
      Sewalt R.G.A.B., Gunster M.J., van der Vlag J., Satijn D.P.E., Otte A.P.
      Mol. Cell. Biol. 19:777-787(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SEQUENCE REVISION, FUNCTION.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [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] (ISOFORMS 1 AND 2).
      Tissue: Brain and Lung.
    6. "A region in the C-terminus of adenovirus 2/5 E1a protein is required for association with a cellular phosphoprotein and important for the negative modulation of T24-ras mediated transformation, tumorigenesis and metastasis."
      Boyd J.M., Subramanian T., Schaeper U., la Regina M., Bayley S., Chinnadurai G.
      EMBO J. 12:469-478(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ADENOVIRUS E1A, PHOSPHORYLATION.
    7. "Interaction of EVI1 with cAMP-responsive element-binding protein-binding protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible acetylation of EVI1 and in co-localization in nuclear speckles."
      Chakraborty S., Senyuk V., Sitailo S., Chi Y., Nucifora G.
      J. Biol. Chem. 276:44936-44943(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MECOM.
    8. "Physical and functional interactions between the corepressor CtBP and the Epstein-Barr virus nuclear antigen EBNA3C."
      Touitou R., Hickabottom M., Parker G., Crook T., Allday M.J.
      J. Virol. 75:7749-7755(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EBV EBNA6.
    9. "Acetylation of nuclear hormone receptor-interacting protein RIP140 regulates binding of the transcriptional corepressor CtBP."
      Vo N., Fjeld C., Goodman R.H.
      Mol. Cell. Biol. 21:6181-6188(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NRIP1.
    10. "Two nonconsensus sites in the Epstein-Barr virus oncoprotein EBNA3A cooperate to bind the co-repressor carboxyl-terminal-binding protein (CtBP)."
      Hickabottom M., Parker G.A., Freemont P., Crook T., Allday M.J.
      J. Biol. Chem. 277:47197-47204(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EBV EBNA3.
    11. "The polycomb protein Pc2 is a SUMO E3."
      Kagey M.H., Melhuish T.A., Wotton D.
      Cell 113:127-137(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-428, SUBCELLULAR LOCATION.
    12. "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, PHOSPHORYLATION AT SER-422, MUTAGENESIS OF SER-422.
    13. "Nuclear speckle-associated protein Pnn/DRS binds to the transcriptional corepressor CtBP and relieves CtBP-mediated repression of the E-cadherin gene."
      Alpatov R., Munguba G.C., Caton P., Joo J.H., Shi Y., Shi Y., Hunt M.E., Sugrue S.P.
      Mol. Cell. Biol. 24:10223-10235(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRANSCRIPTIONAL REPRESSION, INTERACTION WITH PNN.
    14. "Multiple domains of the receptor-interacting protein 140 contribute to transcription inhibition."
      Castet A., Boulahtouf A., Versini G., Bonnet S., Augereau P., Vignon F., Khochbin S., Jalaguier S., Cavailles V.
      Nucleic Acids Res. 32:1957-1966(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NRIP1.
    15. "Pc2-mediated sumoylation of Smad-interacting protein 1 attenuates transcriptional repression of E-cadherin."
      Long J., Zuo D., Park M.
      J. Biol. Chem. 280:35477-35489(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZFHX1B.
    16. "Oligomerization of Evi-1 regulated by the PR domain contributes to recruitment of corepressor CtBP."
      Nitta E., Izutsu K., Yamaguchi Y., Imai Y., Ogawa S., Chiba S., Kurokawa M., Hirai H.
      Oncogene 24:6165-6173(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MECOM.
    17. Cited for: INTERACTION WITH FOXP1.
    18. "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.
    19. "ZNF366 is an estrogen receptor corepressor that acts through CtBP and histone deacetylases."
      Lopez-Garcia J., Periyasamy M., Thomas R.S., Christian M., Leao M., Jat P., Kindle K.B., Heery D.M., Parker M.G., Buluwela L., Kamalati T., Ali S.
      Nucleic Acids Res. 34:6126-6136(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZNF366.
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    21. Cited for: FUNCTION AS COREPRESSOR, INTERACTION WITH BCL6, TISSUE SPECIFICITY.
    22. "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.
    23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 28-353 IN COMPLEX WITH NAD, FUNCTION, COFACTOR, MUTAGENESIS OF CYS-134; ASN-138; ARG-141; 141-ARG-ARG-142; LEU-150; ARG-163; ARG-171; GLY-181; GLY-183; ASP-204; ARG-266; ASP-290; GLU-295 AND HIS-315, DIMERIZATION.

    Entry informationi

    Entry nameiCTBP1_HUMAN
    AccessioniPrimary (citable) accession number: Q13363
    Secondary accession number(s): Q4W5N3, Q7Z2Q5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 15, 1999
    Last modified: October 1, 2014
    This is version 160 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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