Reviewed, UniProtKB/Swiss-Prot O88712 (CTBP1_MOUSE)

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

Protein attributes

Sequence length	441 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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.
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 FOXP1, FOXP2, HIPK2, NRIP1, HDAC4, HDAC5, HDAC9 and WIZ. Interacts with GLIS2 but not GLIS1 or GLIS3.
Subcellular location	Cytoplasm. Nucleus. Ref.1 Ref.10
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.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	NAD
Molecular function	Oxidoreductase
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
Cellular component	transcription factor complex Inferred from direct assay. Source: MGI
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro 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
Complete GO annotation...

Binary interactions

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

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 441	441	C-terminal-binding protein 1		PRO_0000076042
Regions
	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
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

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2007. Version 2. Checksum: 2105CC8D69D915F4	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
	Isoform 2. Checksum: 0A36DBF66E6A8605	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
	Isoform 3. Checksum: 0E71CBDFDBF2EDA9	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

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. , 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: 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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
HSSP	HSSP built from PDB template 1HKU based on UniProtKB Q9Z2F5.
SMR	O88712. Positions 28-352.
ModBase	Search...
Protein-protein interaction databases
IntAct	O88712. 3 interactions.
PTM databases
PhosphoSite	O88712.
Proteomic databases
PRIDE	O88712.
Genome annotation databases
Ensembl	ENSMUSG00000037373. Mus musculus. [Contig view]
GeneID	13016.
KEGG	mmu:13016.
Organism-specific databases
MGI	MGI:1201685. Ctbp1.
Phylogenomic databases
HOVERGEN	O88712.
OMA	O88712. PIMNGPM.
Gene expression databases
ArrayExpress	O88712.
Bgee	O88712.
CleanEx	MM_CTBP1.
GermOnline	ENSMUSG00000037373. Mus musculus.
Family and domain databases
InterPro	IPR006139. D-isomer_2_OHA_DH. 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...

Entry information

Entry name

CTBP1_MOUSE

Accession

Primary (citable) accession number: O88712
Secondary accession number(s): Q3TAT1 , Q3TDL5, Q3TUM5, Q91WI6, Q91YX3, Q9QYG2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 1, 2007
Last modified:	June 16, 2009
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)