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O88712 (CTBP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
C-terminal-binding protein 1

Short name=CtBP1
EC=1.1.1.-
Gene names
Name:Ctbp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length441 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.10 Ref.12 Ref.13

Cofactor

NAD. Cofactor binding induces a conformation change By similarity.

Subunit structure

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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Subcellular location

Cytoplasm. Nucleus Ref.1 Ref.10 Ref.12.

Tissue specificity

Expressed in a wide range of adult tissues. Ref.2

Developmental stage

Expressed throughout the developmental stages. Ref.2

Post-translational modification

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.

Sumoylation on Lys-429 is promoted by the E3 SUMO-protein ligase CBX4 By similarity.

Sequence similarities

Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.

Sequence caution

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

Ontologies

Keywords
   Biological processDifferentiation
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandNAD
   Molecular functionOxidoreductase
Repressor
   PTMADP-ribosylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi organization

Inferred from electronic annotation. Source: Ensembl

negative regulation of histone H4 acetylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 17392792. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.12. Source: UniProtKB

positive regulation of histone deacetylation

Inferred from electronic annotation. Source: Ensembl

regulation of cell cycle

Inferred from electronic annotation. Source: Ensembl

regulation of transcription by chromatin organization

Inferred from electronic annotation. Source: Ensembl

white fat cell differentiation

Inferred from direct assay Ref.12. Source: UniProtKB

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay Ref.12. Source: UniProtKB

transcription factor complex

Inferred from direct assay PubMed 17392792. Source: MGI

transcriptional repressor complex

Inferred from direct assay Ref.12. Source: UniProtKB

   Molecular_functionNAD binding

Inferred from sequence or structural similarity. Source: UniProtKB

RNA polymerase II transcription corepressor activity

Inferred from electronic annotation. Source: Ensembl

oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 17392792. Source: MGI

transcription factor binding

Inferred from physical interaction Ref.9. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HIC1Q1452610EBI-604547,EBI-2507362From a different organism.
Zeb1Q643184EBI-604547,EBI-8560245

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O88712-1)

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.
Isoform 2 (identifier: O88712-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: MGSSHLLNKGLPL → MS
Isoform 3 (identifier: O88712-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-74: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 441441C-terminal-binding protein 1
PRO_0000076042

Regions

Nucleotide binding180 – 1856NAD By similarity
Nucleotide binding237 – 2437NAD By similarity
Nucleotide binding264 – 2663NAD By similarity
Nucleotide binding315 – 3184NAD By similarity
Region1 – 7070Interaction with GLIS2 1
Region288 – 36073Interaction with GLIS2 2

Sites

Active site2661 By similarity
Active site2951 By similarity
Active site3151Proton donor By similarity
Binding site1001NAD By similarity
Binding site2041NAD By similarity
Binding site2901NAD By similarity

Amino acid modifications

Modified residue3001Phosphoserine By similarity
Modified residue4231Phosphoserine By similarity
Cross-link429Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence1 – 7474Missing in isoform 3.
VSP_024737
Alternative sequence1 – 1313MGSSH…KGLPL → MS in isoform 2.
VSP_024738

Experimental info

Sequence conflict551D → G in BAE41586. Ref.3
Sequence conflict551D → G in BAE42587. Ref.3
Sequence conflict1081K → R in BAE35946. Ref.3
Sequence conflict3801Missing in CAA09219. Ref.1
Sequence conflict3801Missing in BAE35946. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: 2105CC8D69D915F4

FASTA44147,745
        10         20         30         40         50         60 
MGSSHLLNKG LPLGVRPPIM NGPMHPRPLV ALLDGRDCTV EMPILKDVAT VAFCDAQSTQ 

        70         80         90        100        110        120 
EIHEKVLNEA VGALMYHTIT LTREDLEKFK ALRIIVRIGS GFDNIDIKSA GDLGIAVCNV 

       130        140        150        160        170        180 
PAASVEETAD STLCHILNLY RRTTWLHQAL REGTRVQSVE QIREVASGAA RIRGETLGII 

       190        200        210        220        230        240 
GLGRVGQAVA LRAKAFGFNV LFYDPYLSDG IERALGLQRV STLQDLLFHS DCVTLHCGLN 

       250        260        270        280        290        300 
EHNHHLINDF TVKQMRQGAF LVNTARGGLV DEKALAQALK EGRIRGAALD VHESEPFSFS 

       310        320        330        340        350        360 
QGPLKDAPNL ICTPHAAWYS EQASIEMREE AAREIRRAIT GRIPDSLKNC VNKDHLTAAT 

       370        380        390        400        410        420 
HWASMDPAVV HPELNGAAYS RYPPGVVSVA PTGIPAAVEG IVPSAMSLSH GLPPVAHPPH 

       430        440 
APSPGQTVKP EADRDHTSDQ L 

« Hide

Isoform 2 [UniParc].

Checksum: 0A36DBF66E6A8605
Show »

FASTA43046,614
Isoform 3 [UniParc].

Checksum: 0E71CBDFDBF2EDA9
Show »

FASTA36739,848

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001185788.1. NM_001198859.1.
NP_001185789.1. NM_001198860.1.
NP_001185790.1. NM_001198861.1.
NP_038530.1. NM_013502.3.
XP_006503773.1. XM_006503710.1.
UniGeneMm.7286.

3D structure databases

ProteinModelPortalO88712.
SMRO88712. Positions 26-356.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198961. 13 interactions.
DIPDIP-33907N.
IntActO88712. 10 interactions.
MINTMINT-146962.

PTM databases

PhosphoSiteO88712.

Proteomic databases

PaxDbO88712.
PRIDEO88712.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000079746; ENSMUSP00000078682; ENSMUSG00000037373. [O88712-1]
GeneID13016.
KEGGmmu:13016.
UCSCuc008xaj.2. mouse. [O88712-1]
uc008xak.2. mouse. [O88712-2]

Organism-specific databases

CTD1487.
MGIMGI:1201685. Ctbp1.

Phylogenomic databases

eggNOGCOG0111.
GeneTreeENSGT00530000063021.
HOVERGENHBG001898.
InParanoidO88712.
KOK04496.
OMADRDHPSD.
OrthoDBEOG761BT9.
PhylomeDBO88712.
TreeFamTF313593.

Gene expression databases

BgeeO88712.
CleanExMM_CTBP1.
GenevestigatorO88712.

Family and domain databases

Gene3D3.40.50.720. 2 hits.
InterProIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR006140. D-isomer_2_OHA_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
PROSITEPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCTBP1. mouse.
NextBio282870.
PROO88712.
SOURCESearch...

Entry information

Entry nameCTBP1_MOUSE
AccessionPrimary (citable) accession number: O88712
Secondary accession number(s): Q3TAT1 expand/collapse secondary AC list , Q3TDL5, Q3TUM5, Q91WI6, Q91YX3, Q9QYG2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 2007
Last modified: April 16, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot