C-terminal-binding protein 1 - Mus musculus (Mouse)

Hide | Top

Names and origin

Protein names

Recommended name:
    C-terminal-binding protein 1
      Short name=CtBP1
    EC=1.1.1.-

Gene names

Name:

Ctbp1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Hide | Top

Protein attributes

Sequence length	441 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

Hide | Top

General annotation (Comments)

Function	Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex By similarity. Co-repressor targeting diverse transcription regulators such as GLIS2. Has dehydrogenase activity. Functions in brown adipose tissue (BAT) differentiation. Ref.1 Ref.2 Ref.10 Ref.12 Ref.13
Cofactor	NAD. Required for efficient interaction with E1A. Cofactor binding induces a conformation change By similarity.
Subunit structure	Can form homodimers or heterodimers of CTBP1 and CTBP2. Interacts with PNN. Interacts with ZFHX1B By similarity. Interacts with MECOM By similarity. Interacts with FOXP1, FOXP2, HIPK2, NRIP1, HDAC4, HDAC5, HDAC9 and WIZ. Interacts with GLIS2 but not GLIS1 or GLIS3. Interaction with non acetylated SATB1 stabilizes its attachment to DNA and promotes transcription repression. Interacts with PRDM16; represses white adipose tissue (WAT)-specific genes expression. Ref.10 Ref.12 Ref.13 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11
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 (BFA) By similarity. The level of phosphorylation appears to be regulated during the cell cycle. Phosphorylated upon DNA damage, probably by ATM or ATR. 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.

Hide | Top

Ontologies

Keywords
Biological process	Differentiation Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	NAD
Molecular function	Oxidoreductase Repressor
PTM	ADP-ribosylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: MGI oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW white fat cell differentiation Ref.12 Inferred from direct assay. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell transcription factor complex Inferred from direct assay. Source: MGI transcriptional repressor complex Ref.12 Inferred from direct assay. Source: UniProtKB
Molecular function	NAD or NADH binding Inferred from sequence or structural similarity. Source: UniProtKB oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Inferred from electronic annotation. Source: InterPro transcription factor activity Inferred from direct assay. Source: MGI transcription factor binding Ref.9 Inferred from physical interaction. Source: UniProtKB transcription repressor activity Ref.12 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Hide | Top

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Lbxcor1	Q8BX46	1	EBI-604547,EBI-604451

Hide | Top

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.

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 441

441

C-terminal-binding protein 1

PRO_0000076042

Regions

Nucleotide binding

180 – 185

6

NAD By similarity

Nucleotide binding

237 – 243

7

NAD By similarity

Nucleotide binding

264 – 266

3

NAD By similarity

Nucleotide binding

315 – 318

4

NAD By similarity

Region

1 – 70

70

Interaction with GLIS2 1

Region

288 – 360

73

Interaction with GLIS2 2

Sites

Active site

266

1

By similarity

Active site

295

1

By similarity

Active site

315

1

Proton donor By similarity

Binding site

100

1

NAD By similarity

Binding site

204

1

NAD By similarity

Binding site

290

1

NAD By similarity

Amino acid modifications

Modified residue

300

1

Phosphoserine By similarity

Modified residue

423

1

Phosphoserine By similarity

Cross-link

429

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence

1 – 74

74

Missing in isoform 3.

VSP_024737

Alternative sequence

1 – 13

13

MGSSH…KGLPL → MS in isoform 2.

VSP_024738

Experimental info

Sequence conflict

55

1

D → G in BAE41586. Ref.3

Sequence conflict

55

1

D → G in BAE42587. Ref.3

Sequence conflict

108

1

K → R in BAE35946. Ref.3

Sequence conflict

380

1

Missing in CAA09219. Ref.1

Sequence conflict

380

1

Missing in BAE35946. Ref.3

Hide | Top

Sequences

Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified May 1, 2007. Version 2. Checksum: 2105CC8D69D915F4 Show »	FASTA	441	47,745
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. Checksum: 0A36DBF66E6A8605 Show »	FASTA	430	46,614
10 20 30 40 50 60 MSGVRPPIMN GPMHPRPLVA LLDGRDCTVE MPILKDVATV AFCDAQSTQE IHEKVLNEAV 70 80 90 100 110 120 GALMYHTITL TREDLEKFKA LRIIVRIGSG FDNIDIKSAG DLGIAVCNVP AASVEETADS 130 140 150 160 170 180 TLCHILNLYR RTTWLHQALR EGTRVQSVEQ IREVASGAAR IRGETLGIIG LGRVGQAVAL 190 200 210 220 230 240 RAKAFGFNVL FYDPYLSDGI ERALGLQRVS TLQDLLFHSD CVTLHCGLNE HNHHLINDFT 250 260 270 280 290 300 VKQMRQGAFL VNTARGGLVD EKALAQALKE GRIRGAALDV HESEPFSFSQ GPLKDAPNLI 310 320 330 340 350 360 CTPHAAWYSE QASIEMREEA AREIRRAITG RIPDSLKNCV NKDHLTAATH WASMDPAVVH 370 380 390 400 410 420 PELNGAAYSR YPPGVVSVAP TGIPAAVEGI VPSAMSLSHG LPPVAHPPHA PSPGQTVKPE 430 ADRDHTSDQL « Hide
Isoform 3. Checksum: 0E71CBDFDBF2EDA9 Show »	FASTA	367	39,848
10 20 30 40 50 60 MYHTITLTRE DLEKFKALRI IVRIGSGFDN IDIKSAGDLG IAVCNVPAAS VEETADSTLC 70 80 90 100 110 120 HILNLYRRTT WLHQALREGT RVQSVEQIRE VASGAARIRG ETLGIIGLGR VGQAVALRAK 130 140 150 160 170 180 AFGFNVLFYD PYLSDGIERA LGLQRVSTLQ DLLFHSDCVT LHCGLNEHNH HLINDFTVKQ 190 200 210 220 230 240 MRQGAFLVNT ARGGLVDEKA LAQALKEGRI RGAALDVHES EPFSFSQGPL KDAPNLICTP 250 260 270 280 290 300 HAAWYSEQAS IEMREEAARE IRRAITGRIP DSLKNCVNKD HLTAATHWAS MDPAVVHPEL 310 320 330 340 350 360 NGAAYSRYPP GVVSVAPTGI PAAVEGIVPS AMSLSHGLPP VAHPPHAPSP GQTVKPEADR DHTSDQL « Hide

Hide | Top

References

	« Hide 'large scale' referencesShow '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: 10369679] [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: 10567582] [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. Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [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: 15489334] [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, 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: 11022042] [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: 14567915] [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: 14736873] [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: 14701752] [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: 16326862] [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: 16702210] [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: 18483224] [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: 19103759] [Abstract] Cited for: FUNCTION, INTERACTION WITH SATB1.
+	Additional computationally mapped references.

Hide | Top

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.
IPI	IPI00128155. IPI00845557. IPI00845775.
RefSeq	NP_038530.1.
UniGene	Mm.7286
3D structure databases
SMR	O88712. Positions 26-356.
ModBase	Search...
Protein-protein interaction databases
IntAct	O88712. 4 interactions.
STRING	O88712.
PTM databases
PhosphoSite	O88712.
Proteomic databases
PRIDE	O88712.
Genome annotation databases
Ensembl	ENSMUST00000079746; ENSMUSP00000078682; ENSMUSG00000037373; Mus musculus. [Genome view]
GeneID	13016.
KEGG	mmu:13016.
UCSC	uc008xan.1. mouse.
Organism-specific databases
CTD	13016.
MGI	MGI:1201685. Ctbp1.
Phylogenomic databases
eggNOG	roNOG10005.
HOVERGEN	O88712.
InParanoid	O88712.
OMA	PIMNGPM.
OrthoDB	EOG9X3KKH.
PhylomeDB	O88712.
Gene expression databases
ArrayExpress	O88712.
Bgee	O88712.
CleanEx	MM_CTBP1.
Genevestigator	O88712.
GermOnline	ENSMUSG00000037373. Mus musculus.
Family and domain databases
InterPro	IPR006139. D-isomer_2_OHA_DH_cat_dom. IPR006140. D-isomer_2_OHA_DH_NAD-bd. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
Pfam	PF00389. 2-Hacid_dh. 1 hit. PF02826. 2-Hacid_dh_C. 1 hit. [Graphical view]
PROSITE	PS00065. D_2_HYDROXYACID_DH_1. 1 hit. PS00670. D_2_HYDROXYACID_DH_2. False negative. PS00671. D_2_HYDROXYACID_DH_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	282870.
SOURCE	Search...

Hide | Top

Entry information

Entry name

CTBP1_MOUSE

Accession

Primary (citable) accession number: O88712
Secondary accession number(s): Q3TAT1

Q9QYG2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 2007
Last modified:	February 9, 2010
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents