Reviewed, UniProtKB/Swiss-Prot Q9Z2F5 (CTBP1_RAT)

Names and origin

Protein names

Recommended name:
    C-terminal-binding protein 1
      Short name=CtBP1
    EC=1.1.1.-
Alternative name(s):
    C-terminal-binding protein 3
      Short name=CtBP3
    50 kDa BFA-dependent ADP-ribosylation substrate
    BARS-50

Gene names

Name:	Ctbp1
Synonyms:	Bars, Ctbp3

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	430 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Corepressor targeting diverse transcription regulators such as GLIS2. Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Has dehydrogenase activity. Ref.1 Ref.5 Ref.6
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 FOXP1, FOXP2, HIPK2, PNN and NRIP1. Interacts with ZFHX1B, HDAC4, HDAC5, HDAC9 and WIZ By similarity. Interacts with GLIS2 but not GLIS1 or GLIS3 By similarity.
Subcellular location	Cytoplasm. Nucleus. Ref.1 Ref.5
Post-translational modification	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-412 induces proteasomal degradation By similarity. ADP-ribosylated; when cells are exposed to brefeldin-A (BFA). Sumoylation on Lys-418 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
Ligand	NAD
Molecular function	Oxidoreductase
PTM	ADP-ribosylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	Golgi organization Inferred from mutant phenotype. Source: RGD membrane fusion Ref.6 Traceable author statement. Source: RGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: RGD nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAD or NADH binding Inferred from electronic annotation. Source: InterPro acyltransferase activity Ref.6 Traceable author statement. Source: RGD oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Inferred from electronic annotation. Source: InterPro transcription corepressor activity Traceable author statement. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 430

430

C-terminal-binding protein 1

PRO_0000076043

Regions

Region

1 – 59

59

Interaction with GLIS2 1 By similarity

Region

277 – 349

73

Interaction with GLIS2 2 By similarity

Sites

Active site

255

1

By similarity

Active site

284

1

By similarity

Active site

304

1

Proton donor By similarity

Amino acid modifications

Modified residue

289

1

Phosphoserine By similarity

Modified residue

412

1

Phosphoserine By similarity

Cross-link

418

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

Experimental info

Mutagenesis

41

1

A → E: Strongly reduces interaction with E1A. Ref.6

Mutagenesis

55

1

V → R: Strongly reduces interaction with E1A. Ref.6

Sequence conflict

175

1

G → S AA sequence Ref.1

Secondary structure

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430

Helix Strand Turn

Details...

Beta strand

18 – 23

6

Turn

28 – 30

3

Helix

31 – 34

4

Turn

35 – 37

3

Beta strand

39 – 42

4

Helix

53 – 57

5

Beta strand

60 – 64

5

Beta strand

66 – 68

3

Helix

72 – 75

4

Beta strand

83 – 89

7

Beta strand

92 – 94

3

Helix

96 – 101

6

Beta strand

105 – 108

4

Beta strand

110 – 113

4

Helix

114 – 129

16

Helix

132 – 139

8

Turn

140 – 142

3

Helix

148 – 154

7

Turn

155 – 157

3

Beta strand

166 – 169

4

Helix

173 – 184

12

Beta strand

190 – 192

3

Helix

200 – 204

5

Helix

212 – 218

7

Beta strand

220 – 224

5

Beta strand

230 – 232

3

Helix

238 – 242

5

Beta strand

249 – 252

4

Helix

256 – 258

3

Helix

261 – 270

10

Beta strand

272 – 280

9

Beta strand

282 – 285

4

Beta strand

288 – 291

4

Helix

292 – 295

4

Beta strand

297 – 301

5

Helix

310 – 329

20

Turn

332 – 335

4

Beta strand

337 – 340

4

Sequences

	Sequence		Length	Mass (Da)
	Q9Z2F5-1 [UniParc]. Last modified June 1, 2001. Version 3. Checksum: 0A36DBF27E6A8605	FASTA	430	46,628
	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 ADRDHTTDQL

References

[1]	"Molecular cloning and functional characterization of brefeldin A-ADP-ribosylated substrate. A novel protein involved in the maintenance of the Golgi structure." Spano S., Silletta M.G., Colanzi A., Alberti S., Fiucci G., Valente C., Fusella A., Salmona M., Mironov A., Luini A., Corda D. J. Biol. Chem. 274:17705-17710(1999) [PubMed: 10364211] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION. Strain: Sprague-Dawley. Tissue: Brain.
[2]	Erratum Spano S., Silletta M.G., Colanzi A., Alberti S., Fiucci G., Valente C., Fusella A., Salmona M., Mironov A., Luini A., Corda D. J. Biol. Chem. 274:25188-25188(1999)
[3]	Spano S., Silletta M.G., Colanzi A., Alberti S., Fiucci G., Valente C., Fusella A., Salmona M., Mironov A., Luini A., Corda D. Submitted (MAY-2001) to UniProtKB Cited for: SEQUENCE REVISION TO 259.
[4]	Lubec G., Diao W. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 275-294, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus.
[5]	"Evidence that the 50-kDa substrate of brefeldin A-dependent ADP-ribosylation binds GTP and is modulated by the G-protein beta gamma subunit complex." Di Girolamo M., Silletta M.G., De Matteis M.A., Braca A., Colanzi A., Pawlak D., Rasenick M.M., Luini A., Corda D. Proc. Natl. Acad. Sci. U.S.A. 92:7065-7069(1995) [PubMed: 7624370] [Abstract] Cited for: FUNCTION, RIBOSYLATION, SUBCELLULAR LOCATION.
[6]	"CtBP/BARS: a dual-function protein involved in transcription co-repression and Golgi membrane fission." Nardini M., Spano S., Cericola C., Pesce A., Massaro A., Millo E., Luini A., Corda D., Bolognesi M. EMBO J. 22:3122-3130(2003) [PubMed: 12805226] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-349 IN COMPLEX WITH NADH, FUNCTION, MUTAGENESIS OF ALA-41 AND VAL-55.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF067795 mRNA. Translation: AAC79427.2.

IPI

IPI00392657.

RefSeq

NP_062074.2.

UniGene

Rn.3946

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HKU	X-ray	2.30	A	1-350	[»]
1HL3	X-ray	3.10	A	1-350	[»]
2HU2	X-ray	2.85	A	1-350	[»]
3GA0	X-ray	3.40	A	1-350	[»]

DisProt

DP00499.

ModBase

Search...

Genome annotation databases

Ensembl

ENSRNOG00000005428. Rattus norvegicus. [Contig view]

GeneID

29382.

KEGG

rno:29382.

Organism-specific databases

RGD

2441. Ctbp1.

Phylogenomic databases

HOVERGEN

Q9Z2F5.

Gene expression databases

ArrayExpress

Q9Z2F5.

GermOnline

ENSRNOG00000005428. Rattus norvegicus.

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

608965.

Entry information

Entry name

CTBP1_RAT

Accession

Primary (citable) accession number: Q9Z2F5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	June 1, 2001
Last modified:	June 16, 2009
This is version 82 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)