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Protein

C-terminal-binding protein 1

Gene

Ctbp1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Cofactori

NAD+Note: Cofactor binding induces a conformational change.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei89 – 891NAD2 Publications
Binding sitei193 – 1931NAD2 Publications
Active sitei255 – 2551By similarity
Binding sitei279 – 2791NAD2 Publications
Active sitei284 – 2841By similarity
Active sitei304 – 3041Proton donorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi169 – 1746NAD2 Publications
Nucleotide bindingi226 – 2327NAD2 Publications
Nucleotide bindingi253 – 2553NAD2 Publications

GO - Molecular functioni

  • NAD binding Source: UniProtKB
  • oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: InterPro
  • protein homodimerization activity Source: UniProtKB
  • transcription corepressor activity Source: RGD
  • transferase activity, transferring acyl groups Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Repressor

Keywords - Biological processi

Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

NAD

Names & Taxonomyi

Protein namesi
Recommended name:
C-terminal-binding protein 1 (EC:1.1.1.-)
Short name:
CtBP1
Alternative name(s):
50 kDa BFA-dependent ADP-ribosylation substrate
BARS-50
C-terminal-binding protein 3
Short name:
CtBP3
Gene namesi
Name:Ctbp1
Synonyms:Bars, Ctbp3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2441. Ctbp1.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi41 – 411A → E: Strongly reduces interaction with E1A. 1 Publication
Mutagenesisi55 – 551V → R: Strongly reduces interaction with E1A. 1 Publication
Mutagenesisi172 – 1721G → E: Loss dimerization and of NAD binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 430430C-terminal-binding protein 1PRO_0000076043Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei289 – 2891PhosphoserineBy similarity
Modified residuei412 – 4121PhosphoserineBy similarity
Cross-linki418 – 418Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Post-translational modificationi

The level of phosphorylation appears to be regulated during the cell cycle. Phosphorylation by HIPK2 on Ser-412 induces proteasomal degradation (By similarity).By similarity
ADP-ribosylated; when cells are exposed to brefeldin A.
Sumoylation on Lys-418 is promoted by the E3 SUMO-protein ligase CBX4.By similarity

Keywords - PTMi

ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9Z2F5.
PRIDEiQ9Z2F5.

PTM databases

iPTMnetiQ9Z2F5.
PhosphoSiteiQ9Z2F5.

Expressioni

Gene expression databases

GenevisibleiQ9Z2F5. RN.

Interactioni

Subunit structurei

Homo- or heterodimer. Heterodimer with CTBP2. Interacts with ELK3 (via its PXDLS motif). Interacts with RBBP8 (via its PXDLS motif); the interaction is disrupted by binding to adenovirus E1A. 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 and WIZ. Interacts with ZNF217. Interacts with BCL6; the interaction is required for BCL6 transcriptional autoinhibition and inhibition of some BCL6 target genes. Interacts with IKZF4 (By similarity). Interacts with FAM195B (unphosphorylated form, via the PXDLS motif); competitively inhibiting CTBP-ZEB1 interaction (By similarity).By similarity3 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi248034. 4 interactions.
IntActiQ9Z2F5. 2 interactions.
MINTiMINT-216829.
STRINGi10116.ENSRNOP00000062945.

Structurei

Secondary structure

1
430
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 236Combined sources
Turni28 – 303Combined sources
Helixi31 – 344Combined sources
Turni35 – 373Combined sources
Beta strandi39 – 424Combined sources
Helixi48 – 503Combined sources
Helixi53 – 586Combined sources
Beta strandi59 – 646Combined sources
Beta strandi66 – 683Combined sources
Helixi72 – 765Combined sources
Beta strandi83 – 897Combined sources
Beta strandi92 – 943Combined sources
Helixi96 – 1016Combined sources
Beta strandi105 – 1073Combined sources
Beta strandi111 – 1133Combined sources
Helixi114 – 13017Combined sources
Helixi132 – 1409Combined sources
Helixi148 – 1547Combined sources
Turni155 – 1573Combined sources
Beta strandi165 – 1695Combined sources
Helixi173 – 18311Combined sources
Turni184 – 1863Combined sources
Beta strandi188 – 1925Combined sources
Beta strandi194 – 1963Combined sources
Helixi200 – 2034Combined sources
Helixi212 – 2187Combined sources
Beta strandi220 – 2245Combined sources
Beta strandi230 – 2323Combined sources
Helixi238 – 2436Combined sources
Beta strandi248 – 2525Combined sources
Helixi256 – 2583Combined sources
Helixi261 – 2699Combined sources
Beta strandi272 – 2798Combined sources
Beta strandi282 – 2854Combined sources
Beta strandi288 – 2914Combined sources
Turni292 – 2954Combined sources
Beta strandi297 – 3015Combined sources
Helixi310 – 32920Combined sources
Turni332 – 3343Combined sources
Beta strandi337 – 3404Combined sources
Helixi342 – 3443Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HKUX-ray2.30A1-350[»]
1HL3X-ray3.10A1-350[»]
2HU2X-ray2.85A1-350[»]
3GA0X-ray3.40A1-350[»]
DisProtiDP00499.
ProteinModelPortaliQ9Z2F5.
SMRiQ9Z2F5. Positions 15-345.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Z2F5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 5959Interaction with GLIS2 1By similarityAdd
BLAST
Regioni277 – 34973Interaction with GLIS2 2By similarityAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0067. Eukaryota.
COG0111. LUCA.
HOGENOMiHOG000136701.
HOVERGENiHBG001898.
InParanoidiQ9Z2F5.
KOiK04496.
OMAiDRDHPSD.
PhylomeDBiQ9Z2F5.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR029752. D-isomer_DH_CS1.
IPR006140. D-isomer_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Z2F5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGVRPPIMN GPMHPRPLVA LLDGRDCTVE MPILKDVATV AFCDAQSTQE
60 70 80 90 100
IHEKVLNEAV GALMYHTITL TREDLEKFKA LRIIVRIGSG FDNIDIKSAG
110 120 130 140 150
DLGIAVCNVP AASVEETADS TLCHILNLYR RTTWLHQALR EGTRVQSVEQ
160 170 180 190 200
IREVASGAAR IRGETLGIIG LGRVGQAVAL RAKAFGFNVL FYDPYLSDGI
210 220 230 240 250
ERALGLQRVS TLQDLLFHSD CVTLHCGLNE HNHHLINDFT VKQMRQGAFL
260 270 280 290 300
VNTARGGLVD EKALAQALKE GRIRGAALDV HESEPFSFSQ GPLKDAPNLI
310 320 330 340 350
CTPHAAWYSE QASIEMREEA AREIRRAITG RIPDSLKNCV NKDHLTAATH
360 370 380 390 400
WASMDPAVVH PELNGAAYSR YPPGVVSVAP TGIPAAVEGI VPSAMSLSHG
410 420 430
LPPVAHPPHA PSPGQTVKPE ADRDHTTDQL
Length:430
Mass (Da):46,628
Last modified:June 1, 2001 - v3
Checksum:i0A36DBF27E6A8605
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti175 – 1751G → S AA sequence (PubMed:10364211).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF067795 mRNA. Translation: AAC79427.2.
RefSeqiNP_062074.2. NM_019201.3.
UniGeneiRn.3946.

Genome annotation databases

GeneIDi29382.
KEGGirno:29382.
UCSCiRGD:2441. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF067795 mRNA. Translation: AAC79427.2.
RefSeqiNP_062074.2. NM_019201.3.
UniGeneiRn.3946.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HKUX-ray2.30A1-350[»]
1HL3X-ray3.10A1-350[»]
2HU2X-ray2.85A1-350[»]
3GA0X-ray3.40A1-350[»]
DisProtiDP00499.
ProteinModelPortaliQ9Z2F5.
SMRiQ9Z2F5. Positions 15-345.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248034. 4 interactions.
IntActiQ9Z2F5. 2 interactions.
MINTiMINT-216829.
STRINGi10116.ENSRNOP00000062945.

PTM databases

iPTMnetiQ9Z2F5.
PhosphoSiteiQ9Z2F5.

Proteomic databases

PaxDbiQ9Z2F5.
PRIDEiQ9Z2F5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29382.
KEGGirno:29382.
UCSCiRGD:2441. rat.

Organism-specific databases

CTDi1487.
RGDi2441. Ctbp1.

Phylogenomic databases

eggNOGiKOG0067. Eukaryota.
COG0111. LUCA.
HOGENOMiHOG000136701.
HOVERGENiHBG001898.
InParanoidiQ9Z2F5.
KOiK04496.
OMAiDRDHPSD.
PhylomeDBiQ9Z2F5.

Miscellaneous databases

EvolutionaryTraceiQ9Z2F5.
PROiQ9Z2F5.

Gene expression databases

GenevisibleiQ9Z2F5. RN.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR029752. D-isomer_DH_CS1.
IPR006140. D-isomer_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. Cited for: SEQUENCE REVISION TO 259.
  3. Lubec G., Diao W.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 275-294, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.
  4. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ADP-RIBOSYLATION, SUBCELLULAR LOCATION.
  5. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-349 IN COMPLEX WITH NADH, FUNCTION, MUTAGENESIS OF ALA-41 AND VAL-55.
  6. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-350 IN COMPLEX WITH NAD AND ZNF217, INTERACTION WITH ZNF217.
  7. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-350 OF MUTANT GLU-172, NAD BINDING, SUBUNIT, MUTAGENESIS OF GLY-172.

Entry informationi

Entry nameiCTBP1_RAT
AccessioniPrimary (citable) accession number: Q9Z2F5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.