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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

  • glyoxylate reductase (NADP) activity Source: GO_Central
  • hydroxypyruvate reductase activity Source: GO_Central
  • NAD binding Source: UniProtKB
  • PDZ domain binding Source: CAFA
  • protein homodimerization activity Source: UniProtKB
  • transcription corepressor activity Source: RGD
  • transferase activity, transferring acyl groups Source: RGD

GO - Biological processi

  • membrane fusion Source: RGD
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • presynapse to nucleus signaling pathway Source: SynGO
  • transcription, DNA-templated Source: UniProtKB-KW
  • white fat cell differentiation Source: UniProtKB

Keywordsi

Molecular functionOxidoreductase, Repressor
Biological processDifferentiation, Transcription, Transcription regulation
LigandNAD

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2441. Ctbp1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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

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 and ZFHX1B. Interacts with ZNF366 (via PXDLS motif) (By similarity). 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

  • PDZ domain binding Source: CAFA
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi248034. 4 interactors.
IntActiQ9Z2F5. 3 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

InterProiView protein in InterPro
IPR006139. 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.
PfamiView protein in Pfam
PF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
PROSITEiView protein in PROSITE
PS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.

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.

Similar proteinsi

Entry informationi

Entry nameiCTBP1_RAT
AccessioniPrimary (citable) accession number: Q9Z2F5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: June 1, 2001
Last modified: September 27, 2017
This is version 157 of the entry and version 3 of the sequence. See 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