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Reviewed, UniProtKB/Swiss-Prot Q9Z2F5 (CTBP1_RAT)

Last modified November 3, 2009. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended 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
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Corepressor targeting diverse transcription regulators such as GLIS2. Has dehydrogenase activity. Functions in brown adipose tissue (BAT) differentiation. Ref.1 Ref.5 Ref.6

Cofactor

NAD. Required for efficient interaction with E1A By similarity. Cofactor binding induces a conformation change.

Subunit structure

Homodimer, or heterodimer of CTBP1 and CTBP2. Interacts with FOXP1, FOXP2, HIPK2, PNN and NRIP1. Interacts with ZFHX1B, HDAC4, HDAC5, HDAC9 and WIZ. Interacts with GLIS2 but not GLIS1 or GLIS3. Interacts with PRDM16; represses white adipose tissue (WAT)-specific genes expression. Interaction with non acetylated SATB1 stabalizes its attachment to DNA and promotes transcription repression By similarity. Interacts with ZNF217.

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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 430430C-terminal-binding protein 1
PRO_0000076043

Regions

Nucleotide binding169 – 1746NAD
Nucleotide binding226 – 2327NAD
Nucleotide binding253 – 2553NAD
Region1 – 5959Interaction with GLIS2 1 By similarity
Region277 – 34973Interaction with GLIS2 2 By similarity

Sites

Active site2551 By similarity
Active site2841 By similarity
Active site3041Proton donor By similarity
Binding site891NAD
Binding site1931NAD
Binding site2791NAD

Amino acid modifications

Modified residue2891Phosphoserine By similarity
Modified residue4121Phosphoserine By similarity
Cross-link418Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Experimental info

Mutagenesis411A → E: Strongly reduces interaction with E1A. Ref.6
Mutagenesis551V → R: Strongly reduces interaction with E1A. Ref.6
Mutagenesis1721G → E: Loss dimerization and of NAD binding. Ref.8
Sequence conflict1751G → S AA sequence Ref.1

Secondary structure

1 ....................................................................... 430
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q9Z2F5-1 [UniParc].

Last modified June 1, 2001. Version 3.
Checksum: 0A36DBF27E6A8605

FASTA43046,628
        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

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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.
[7]"Specific recognition of ZNF217 and other zinc finger proteins at a surface groove of C-terminal binding proteins."
Quinlan K.G.R., Nardini M., Verger A., Francescato P., Yaswen P., Corda D., Bolognesi M., Crossley M.
Mol. Cell. Biol. 26:8159-8172(2006) [PubMed: 16940172] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-350 IN COMPLEX WITH NAD AND ZNF217, INTERACTION WITH ZNF217.
[8]"CtBP1/BARS Gly172-->Glu mutant structure: impairing NAD(H)-binding and dimerization."
Nardini M., Valente C., Ricagno S., Luini A., Corda D., Bolognesi M.
Biochem. Biophys. Res. Commun. 381:70-74(2009) [PubMed: 19351597] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-350 OF MUTANT GLU-172, NAD BINDING, SUBUNIT, MUTAGENESIS OF GLY-172.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AF067795 mRNA. Translation: AAC79427.2.
IPIIPI00392657.
RefSeqNP_062074.2.
UniGeneRn.3946

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1HKUX-ray2.30A1-350[»]
1HL3X-ray3.10A1-350[»]
2HU2X-ray2.85A1-350[»]
3GA0X-ray3.40A1-350[»]
DisProtDP00499.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9Z2F5.

Genome annotation databases

EnsemblENSRNOT00000037871; ENSRNOP00000035064; ENSRNOG00000005428; Rattus norvegicus. [Genome view]
GeneID29382.
KEGGrno:29382.
UCSCNM_019201. rat.

Organism-specific databases

CTD29382.
RGD2441. Ctbp1.

Phylogenomic databases

HOVERGENQ9Z2F5.

Gene expression databases

ArrayExpressQ9Z2F5.
GenevestigatorQ9Z2F5.
GermOnlineENSRNOG00000005428. Rattus norvegicus.

Family and domain databases

InterProIPR006139. D-isomer_2_OHA_DH.
IPR006140. D-isomer_2_OHA_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
PROSITEPS00065. 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]
ProtoNetSearch...

Other Resources

NextBio608965.

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Entry information

Entry nameCTBP1_RAT
AccessionPrimary (citable) accession number: Q9Z2F5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: June 1, 2001
Last modified: November 3, 2009
This is version 87 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents