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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)DescriptionActionsGraphical viewLength
Binding sitei89NAD2 Publications1
Binding sitei193NAD2 Publications1
Active sitei255By similarity1
Binding sitei279NAD2 Publications1
Active sitei284By similarity1
Active sitei304Proton donorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi169 – 174NAD2 Publications6
Nucleotide bindingi226 – 232NAD2 Publications7
Nucleotide bindingi253 – 255NAD2 Publications3

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)DescriptionActionsGraphical viewLength
Mutagenesisi41A → E: Strongly reduces interaction with E1A. 1 Publication1
Mutagenesisi55V → R: Strongly reduces interaction with E1A. 1 Publication1
Mutagenesisi172G → E: Loss dimerization and of NAD binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000760431 – 430C-terminal-binding protein 1Add BLAST430

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei289PhosphoserineBy similarity1
Modified residuei412PhosphoserineBy similarity1
Cross-linki418Glycyl 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.
PhosphoSitePlusiQ9Z2F5.

Expressioni

Gene expression databases

BgeeiENSRNOG00000005428.
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 MCRIP1 (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 interactors.
IntActiQ9Z2F5. 2 interactors.
MINTiMINT-216829.
STRINGi10116.ENSRNOP00000062945.

Structurei

Secondary structure

1430
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi18 – 23Combined sources6
Turni28 – 30Combined sources3
Helixi31 – 34Combined sources4
Turni35 – 37Combined sources3
Beta strandi39 – 42Combined sources4
Helixi48 – 50Combined sources3
Helixi53 – 58Combined sources6
Beta strandi59 – 64Combined sources6
Beta strandi66 – 68Combined sources3
Helixi72 – 76Combined sources5
Beta strandi83 – 89Combined sources7
Beta strandi92 – 94Combined sources3
Helixi96 – 101Combined sources6
Beta strandi105 – 107Combined sources3
Beta strandi111 – 113Combined sources3
Helixi114 – 130Combined sources17
Helixi132 – 140Combined sources9
Helixi148 – 154Combined sources7
Turni155 – 157Combined sources3
Beta strandi165 – 169Combined sources5
Helixi173 – 183Combined sources11
Turni184 – 186Combined sources3
Beta strandi188 – 192Combined sources5
Beta strandi194 – 196Combined sources3
Helixi200 – 203Combined sources4
Helixi212 – 218Combined sources7
Beta strandi220 – 224Combined sources5
Beta strandi230 – 232Combined sources3
Helixi238 – 243Combined sources6
Beta strandi248 – 252Combined sources5
Helixi256 – 258Combined sources3
Helixi261 – 269Combined sources9
Beta strandi272 – 279Combined sources8
Beta strandi282 – 285Combined sources4
Beta strandi288 – 291Combined sources4
Turni292 – 295Combined sources4
Beta strandi297 – 301Combined sources5
Helixi310 – 329Combined sources20
Turni332 – 334Combined sources3
Beta strandi337 – 340Combined sources4
Helixi342 – 344Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9Z2F5.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 59Interaction with GLIS2 1By similarityAdd BLAST59
Regioni277 – 349Interaction with GLIS2 2By similarityAdd BLAST73

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0067. Eukaryota.
COG0111. LUCA.
HOGENOMiHOG000136701.
HOVERGENiHBG001898.
InParanoidiQ9Z2F5.
KOiK04496.
OrthoDBiEOG091G08GS.
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)DescriptionActionsGraphical viewLength
Sequence conflicti175G → S AA sequence (PubMed:10364211).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF067795 mRNA. Translation: AAC79427.2.
RefSeqiNP_062074.2. NM_019201.3.
XP_017454636.1. XM_017599147.1.
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.
XP_017454636.1. XM_017599147.1.
UniGeneiRn.3946.

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ9Z2F5.
PhosphoSitePlusiQ9Z2F5.

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.
OrthoDBiEOG091G08GS.
PhylomeDBiQ9Z2F5.

Miscellaneous databases

EvolutionaryTraceiQ9Z2F5.
PROiQ9Z2F5.

Gene expression databases

BgeeiENSRNOG00000005428.
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...

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: November 30, 2016
This is version 151 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.