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Q13363

- CTBP1_HUMAN

UniProt

Q13363 - CTBP1_HUMAN

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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

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

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
Complete GO annotation...

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 – 3001Phosphoserine1 Publication
Modified residuei422 – 4221Phosphoserine; by HIPK21 Publication
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

BgeeiQ13363.
CleanExiHS_CTBP1.
ExpressionAtlasiQ13363. baseline and differential.
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. 127 interactions.
DIPiDIP-24245N.
IntActiQ13363. 25 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.
GeneTreeiENSGT00530000063021.
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.
IPR029753. D-isomer_DH_CS.
IPR029752. D-isomer_DH_CS1.
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) [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

        10         20         30         40         50
MGSSHLLNKG LPLGVRPPIM NGPLHPRPLV ALLDGRDCTV EMPILKDVAT
60 70 80 90 100
VAFCDAQSTQ EIHEKVLNEA VGALMYHTIT LTREDLEKFK ALRIIVRIGS
110 120 130 140 150
GFDNIDIKSA GDLGIAVCNV PAASVEETAD STLCHILNLY RRATWLHQAL
160 170 180 190 200
REGTRVQSVE QIREVASGAA RIRGETLGII GLGRVGQAVA LRAKAFGFNV
210 220 230 240 250
LFYDPYLSDG VERALGLQRV STLQDLLFHS DCVTLHCGLN EHNHHLINDF
260 270 280 290 300
TVKQMRQGAF LVNTARGGLV DEKALAQALK EGRIRGAALD VHESEPFSFS
310 320 330 340 350
QGPLKDAPNL ICTPHAAWYS EQASIEMREE AAREIRRAIT GRIPDSLKNC
360 370 380 390 400
VNKDHLTAAT HWASMDPAVV HPELNGAAYR YPPGVVGVAP TGIPAAVEGI
410 420 430 440
VPSAMSLSHG LPPVAHPPHA PSPGQTVKPE ADRDHASDQL
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. 127 interactions.
DIPi DIP-24245N.
IntActi Q13363. 25 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.
GeneTreei ENSGT00530000063021.
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

Bgeei Q13363.
CleanExi HS_CTBP1.
ExpressionAtlasi Q13363. baseline and differential.
Genevestigatori Q13363.

Family and domain databases

Gene3Di 3.40.50.720. 2 hits.
InterProi IPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR029752. D-isomer_DH_CS1.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 161 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

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