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Protein

C-terminal-binding protein 1

Gene

CTBP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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.5 Publications

Cofactori

NAD+1 PublicationNote: NAD is required for efficient interaction with E1A. Cofactor binding induces a conformation change.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei100NADBy similarity1
Binding sitei204NADBy similarity1
Active sitei266By similarity1
Binding sitei290NADBy similarity1
Active sitei295By similarity1
Active sitei315Proton donorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi180 – 185NADBy similarity6
Nucleotide bindingi237 – 243NADBy similarity7
Nucleotide bindingi264 – 266NADBy similarity3
Nucleotide bindingi315 – 318NADBy similarity4

GO - Molecular functioni

  • DNA binding transcription factor activity Source: Ensembl
  • glyoxylate reductase (NADP) activity Source: GO_Central
  • hydroxypyruvate reductase activity Source: GO_Central
  • identical protein binding Source: IntAct
  • NAD binding Source: UniProtKB
  • protein C-terminus binding Source: ProtInc
  • protein domain specific binding Source: BHF-UCL
  • protein homodimerization activity Source: GO_Central
  • repressing transcription factor binding Source: BHF-UCL
  • RNA polymerase II transcription corepressor activity Source: BHF-UCL
  • transcription factor binding Source: UniProtKB

GO - Biological processi

  • negative regulation of cell proliferation Source: ProtInc
  • negative regulation of histone acetylation Source: BHF-UCL
  • negative regulation of histone H4 acetylation Source: BHF-UCL
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription by RNA polymerase II Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter by histone modification Source: BHF-UCL
  • positive regulation of histone deacetylation Source: BHF-UCL
  • protein phosphorylation Source: ProtInc
  • regulation of cell cycle Source: BHF-UCL
  • transcription, DNA-templated Source: UniProtKB-KW
  • viral genome replication Source: ProtInc
  • white fat cell differentiation Source: UniProtKB

Keywordsi

Molecular functionOxidoreductase, Repressor
Biological processDifferentiation, Host-virus interaction, Transcription, Transcription regulation
LigandNAD

Enzyme and pathway databases

ReactomeiR-HSA-3769402 Deactivation of the beta-catenin transactivating complex
R-HSA-4641265 Repression of WNT target genes
R-HSA-5339700 TCF7L2 mutants don't bind CTBP
SignaLinkiQ13363
SIGNORiQ13363

Names & Taxonomyi

Protein namesi
Recommended name:
C-terminal-binding protein 1 (EC:1.1.1.-)
Short name:
CtBP1
Gene namesi
Name:CTBP1
Synonyms:CTBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

EuPathDBiHostDB:ENSG00000159692.15
HGNCiHGNC:2494 CTBP1
MIMi602618 gene
neXtProtiNX_Q13363

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
Mutagenesisi134C → A: Strongly reduces E1A binding; when associated with A-138; A-141 and A-150. 1 Publication1
Mutagenesisi138N → A: Strongly reduces E1A binding; when associated with A-134; A-141 and A-150. 1 Publication1
Mutagenesisi141 – 142RR → AA: Strongly reduces E1A binding; when associated with A-163 and A-171. 1 Publication2
Mutagenesisi141R → A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-150. 1 Publication1
Mutagenesisi150L → A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-141. 1 Publication1
Mutagenesisi163R → A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-171. 1 Publication1
Mutagenesisi171R → A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-163. 1 Publication1
Mutagenesisi181G → V: Strongly reduces E1A binding; when associated with V-183 and A-204. 1 Publication1
Mutagenesisi183G → V: Strongly reduces E1A binding; when associated with V-181 and A-204. 1 Publication1
Mutagenesisi204D → A: Strongly reduces E1A binding; when associated with V-181 and V-183. 1 Publication1
Mutagenesisi266R → A: Strongly reduces E1A binding; when associated with A-290; A-295 and A-315. 1 Publication1
Mutagenesisi290D → A: Strongly reduces E1A binding; when associated with A-266; A-295 and A-315. 1 Publication1
Mutagenesisi295E → A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-315. 1 Publication1
Mutagenesisi315H → A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-295. 1 Publication1
Mutagenesisi422S → A: Abolishes phosphorylation by HIPK2 and prevents UV-induced clearance. 1 Publication1

Organism-specific databases

DisGeNETi1487
OpenTargetsiENSG00000159692
PharmGKBiPA26995

Chemistry databases

DrugBankiDB01942 Formic Acid

Polymorphism and mutation databases

BioMutaiCTBP1
DMDMi6014741

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000760411 – 440C-terminal-binding protein 1Add BLAST440

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei300PhosphoserineCombined sources1
Modified residuei422Phosphoserine; by HIPK21 Publication1
Cross-linki428Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

Post-translational modificationi

The level of phosphorylation appears to be regulated during the cell cycle. Phosphorylation by HIPK2 on Ser-422 induces proteasomal degradation.2 Publications
ADP-ribosylated; when cells are exposed to brefeldin A.By similarity
Sumoylation on Lys-428 is promoted by the E3 SUMO-protein ligase CBX4.1 Publication

Keywords - PTMi

ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ13363
PaxDbiQ13363
PeptideAtlasiQ13363
PRIDEiQ13363

PTM databases

iPTMnetiQ13363
PhosphoSitePlusiQ13363
SwissPalmiQ13363

Expressioni

Tissue specificityi

Expressed in germinal center B-cells.1 Publication

Gene expression databases

BgeeiENSG00000159692
CleanExiHS_CTBP1
ExpressionAtlasiQ13363 baseline and differential
GenevisibleiQ13363 HS

Organism-specific databases

HPAiCAB004217
HPA018987
HPA044971

Interactioni

Subunit structurei

Homo- or heterodimer. Heterodimer with CTBP2. Interacts with PRDM16; the interaction represses white adipose tissue (WAT)-specific genes expression. Interacts with GLIS2, FOXP2, HDAC4, HDAC5, HDAC9 and ZNF217. Interacts with adenovirus E1A protein (via its C-terminus); the interaction disrupts the interaction of CTBP1 with RBBP8. Interacts with Epstein-Barr virus EBNA3 and EBNA6. 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 FOXP1, HIPK2, PNN, NRIP1, MECOM, ZFHX1B and WIZ. Interacts with ZNF366 (via PXDLS motif) (PubMed:16393996, PubMed:17085477). Interaction with SATB1 (non-acetylated form); the interaction stabilizes its attachment to DNA and promotes transcription repression. 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 human adenovirus 5 E1A protein; this interaction seems to potentiate viral replication (PubMed:23747199). Interacts with MCRIP1 (unphosphorylated form, via the PXDLS motif); competitively inhibiting CTBP-ZEB1 interaction (PubMed:25728771).By similarity20 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein C-terminus binding Source: ProtInc
  • protein domain specific binding Source: BHF-UCL
  • protein homodimerization activity Source: GO_Central
  • repressing transcription factor binding Source: BHF-UCL
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107869, 175 interactors
CORUMiQ13363
DIPiDIP-24245N
ELMiQ13363
IntActiQ13363, 65 interactors
MINTiQ13363
STRINGi9606.ENSP00000290921

Chemistry databases

BindingDBiQ13363

Structurei

Secondary structure

1440
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi29 – 34Combined sources6
Turni39 – 41Combined sources3
Helixi42 – 45Combined sources4
Turni46 – 48Combined sources3
Beta strandi50 – 53Combined sources4
Helixi59 – 61Combined sources3
Helixi64 – 69Combined sources6
Beta strandi70 – 75Combined sources6
Beta strandi77 – 79Combined sources3
Helixi83 – 86Combined sources4
Beta strandi94 – 100Combined sources7
Helixi107 – 112Combined sources6
Beta strandi116 – 118Combined sources3
Turni121 – 124Combined sources4
Helixi125 – 141Combined sources17
Helixi143 – 151Combined sources9
Helixi159 – 165Combined sources7
Turni166 – 168Combined sources3
Beta strandi176 – 180Combined sources5
Helixi184 – 194Combined sources11
Turni195 – 197Combined sources3
Beta strandi199 – 203Combined sources5
Helixi211 – 215Combined sources5
Helixi223 – 229Combined sources7
Beta strandi231 – 235Combined sources5
Beta strandi246 – 248Combined sources3
Helixi249 – 252Combined sources4
Beta strandi259 – 263Combined sources5
Helixi267 – 269Combined sources3
Helixi272 – 280Combined sources9
Beta strandi283 – 290Combined sources8
Beta strandi293 – 296Combined sources4
Turni303 – 306Combined sources4
Beta strandi308 – 312Combined sources5
Helixi321 – 340Combined sources20
Turni343 – 346Combined sources4
Beta strandi348 – 350Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MX3X-ray1.95A28-353[»]
4LCEX-ray2.38A28-353[»]
4U6QX-ray2.30A28-353[»]
4U6SX-ray2.10A28-353[»]
ProteinModelPortaliQ13363
SMRiQ13363
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13363

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 70Interaction with GLIS2 1By similarityAdd BLAST70
Regioni288 – 360Interaction with GLIS2 2By similarityAdd BLAST73

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0067 Eukaryota
COG0111 LUCA
GeneTreeiENSGT00530000063021
HOGENOMiHOG000136701
HOVERGENiHBG001898
InParanoidiQ13363
KOiK04496
OMAiTADSTMC
OrthoDBiEOG091G08GS
PhylomeDBiQ13363
TreeFamiTF313593

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
IPR036291 NAD(P)-bd_dom_sf
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

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q13363-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGSSHLLNKG LPLGVRPPIM NGPLHPRPLV ALLDGRDCTV EMPILKDVAT
60 70 80 90 100
VAFCDAQSTQ EIHEKVLNEA VGALMYHTIT LTREDLEKFK ALRIIVRIGS
110 120 130 140 150
GFDNIDIKSA GDLGIAVCNV PAASVEETAD STLCHILNLY RRATWLHQAL
160 170 180 190 200
REGTRVQSVE QIREVASGAA RIRGETLGII GLGRVGQAVA LRAKAFGFNV
210 220 230 240 250
LFYDPYLSDG VERALGLQRV STLQDLLFHS DCVTLHCGLN EHNHHLINDF
260 270 280 290 300
TVKQMRQGAF LVNTARGGLV DEKALAQALK EGRIRGAALD VHESEPFSFS
310 320 330 340 350
QGPLKDAPNL ICTPHAAWYS EQASIEMREE AAREIRRAIT GRIPDSLKNC
360 370 380 390 400
VNKDHLTAAT HWASMDPAVV HPELNGAAYR YPPGVVGVAP TGIPAAVEGI
410 420 430 440
VPSAMSLSHG LPPVAHPPHA PSPGQTVKPE ADRDHASDQL
Length:440
Mass (Da):47,535
Last modified:July 15, 1999 - v2
Checksum:iF071DD30B385603F
GO
Isoform 2 (identifier: Q13363-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: MGSSHLLNKGLPL → MS

Note: No experimental confirmation available.
Show »
Length:429
Mass (Da):46,405
Checksum:i0366A6370016910B
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0433051 – 13MGSSH…KGLPL → MS in isoform 2. 1 PublicationAdd BLAST13

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37408 mRNA Translation: AAC62822.1
AF091555 mRNA Translation: AAD14597.1
AC092535 Genomic DNA Translation: AAY40989.1
CH471131 Genomic DNA Translation: EAW82599.1
CH471131 Genomic DNA Translation: EAW82600.1
CH471131 Genomic DNA Translation: EAW82601.1
BC011655 mRNA Translation: AAH11655.1
BC053320 mRNA Translation: AAH53320.1
CCDSiCCDS3348.1 [Q13363-1]
CCDS43203.1 [Q13363-2]
RefSeqiNP_001012632.1, NM_001012614.1 [Q13363-2]
NP_001319.1, NM_001328.2 [Q13363-1]
XP_016863253.1, XM_017007764.1 [Q13363-2]
XP_016863254.1, XM_017007765.1 [Q13363-2]
XP_016863255.1, XM_017007766.1 [Q13363-2]
XP_016863256.1, XM_017007767.1 [Q13363-2]
UniGeneiHs.208597

Genome annotation databases

EnsembliENST00000290921; ENSP00000290921; ENSG00000159692 [Q13363-1]
ENST00000382952; ENSP00000372411; ENSG00000159692 [Q13363-2]
GeneIDi1487
KEGGihsa:1487
UCSCiuc003gcu.2 human [Q13363-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiCTBP1_HUMAN
AccessioniPrimary (citable) accession number: Q13363
Secondary accession number(s): Q4W5N3, Q7Z2Q5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1999
Last modified: April 25, 2018
This is version 198 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health