CTBP1
entrez
1487
canonical
uniprot
Q13363
canonical
ensembl
ENSG00000159692
resolver
ensp
ENSP00000290921
resolver
ensp
ENSP00000372411
resolver
ensp
ENSP00000422148
resolver
ensp
ENSP00000515195
resolver
ensp
ENSP00000515212
resolver
ensp
ENSP00000515213
resolver
ensp
ENSP00000579059
resolver
ensp
ENSP00000579060
resolver
ensp
ENSP00000579061
resolver
ensp
ENSP00000579062
resolver
ensp
ENSP00000579063
resolver
ensp
ENSP00000579064
resolver
ensp
ENSP00000579066
resolver
ensp
ENSP00000579069
resolver
ensp
ENSP00000579072
resolver
ensp
ENSP00000579073
resolver
ensp
ENSP00000579075
resolver
ensp
ENSP00000579077
resolver
ensp
ENSP00000597707
resolver
ensp
ENSP00000597708
resolver
ensp
ENSP00000597710
resolver
ensp
ENSP00000597713
resolver
ensp
ENSP00000611651
resolver
ensp
ENSP00000611654
resolver
enst
ENST00000503594
resolver
enst
ENST00000703164
resolver
enst
ENST00000703165
resolver
enst
ENST00000909001
resolver
enst
ENST00000909002
resolver
enst
ENST00000909003
resolver
enst
ENST00000909004
resolver
enst
ENST00000909005
resolver
enst
ENST00000909007
resolver
enst
ENST00000909010
resolver
enst
ENST00000909013
resolver
enst
ENST00000909014
resolver
enst
ENST00000909016
resolver
enst
ENST00000909018
resolver
enst
ENST00000927648
resolver
enst
ENST00000927649
resolver
enst
ENST00000927654
resolver
enst
ENST00000941592
resolver
enst
ENST00000941595
resolver
genesymbol
CTBP1
resolver
genesymbol_syn
CTBP
resolver
hgnc
HGNC:2494
resolver
uniprot
H0Y8U5
resolver
uniprot
Q4W5N3
resolver
uniprot
Q7Z2Q5
resolver
uniprot
X5D8Y5
resolver
uniprot_entry
CTBP1_HUMAN
resolver
uniprot_entry
H0Y8U5_HUMAN
resolver
uniprot_entry
X5D8Y5_HUMAN
resolver
uniprot_sec
Q4W5N3
resolver
uniprot_sec
Q7Z2Q5
resolver
amino_acid_sequence
MGSSHLLNKGLPLGVRPPIMNGPLHPRPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLKNCVNKDHLTAATHWASMDPAVVHPELNGAAYRYPPGVVGVAPTGIPAAVEGIVPSAMSLSHGLPPVAHPPHAPSPGQTVKPEADRDHASDQL
uniprot
proteins
disease_involvement
DISEASE: Hypotonia, ataxia, developmental delay, and tooth enamel defect syndrome (HADDTS) [MIM:617915]: An autosomal dominant disorder characterized by delayed motor development, intellectual disability, failure to thrive, hypotonia, ataxia, and tooth enamel defects. {ECO:0000269|PubMed:27094857}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
1.1.1.-
uniprot
proteins
function
FUNCTION: 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. {ECO:0000269|PubMed:12419229, ECO:0000269|PubMed:15542832, ECO:0000269|PubMed:18212045, ECO:0000269|PubMed:19103759, ECO:0000269|PubMed:9858600}.
uniprot
proteins
mass_dalton
47535
uniprot
proteins
mutagenesis
MUTAGEN 52; /note="A->E: Loss of interaction with SIMC1. No effect on its proteolytic processing mediated by CAPN3."; /evidence="ECO:0000269|PubMed:23707407"; MUTAGEN 66; /note="V->R: Loss of interaction with SIMC1. Reduced proteolytic processing mediated by CAPN3."; /evidence="ECO:0000269|PubMed:23707407"; MUTAGEN 134; /note="C->A: Strongly reduces E1A binding; when associated with A-138; A-141 and A-150."; /evidence="ECO:0000269|PubMed:12419229"; MUTAGEN 138; /note="N->A: Strongly reduces E1A binding; when associated with A-134; A-141 and A-150."; /evidence="ECO:0000269|PubMed:12419229"; MUTAGEN 141..142; /note="RR->AA: Strongly reduces E1A binding; when associated with A-163 and A-171."; /evidence="ECO:0000269|PubMed:12419229"; MUTAGEN 141; /note="R->A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-150."; /evidence="ECO:0000269|PubMed:12419229"; MUTAGEN 150; /note="L->A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-141."; /evidence="ECO:0000269|PubMed:12419229"; MUTAGEN 163; /note="R->A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-171."; /evidence="ECO:0000269|PubMed:12419229"; MUTAGEN 171; /note="R->A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-163."; /evidence="ECO:0000269|PubMed:12419229"; MUTAGEN 181; /note="G->V: Strongly reduces E1A binding; when associated with V-183 and A-204."; /evidence="ECO:0000269|PubMed:12419229"; MUTAGEN 183; /note="G->A: Reduced proteolytic processing mediated by CAPN3; when associated with A-186."; /evidence="ECO:0000269|PubMed:23707407"; MUTAGEN 183; /note="G->V: Strongly reduces E1A binding; when associated with V-181 and A-204."; /evidence="ECO:0000269|PubMed:12419229"; MUTAGEN 186; /note="G->A: Reduced proteolytic processing mediated by CAPN3; when associated with A-183."; /evidence="ECO:0000269|PubMed:23707407"; MUTAGEN 204; /note="D->A: Strongly reduces E1A binding; when associated with V-181 and V-183."; /evidence="ECO:0000269|PubMed:12419229"; MUTAGEN 204; /note="D->L: Reduced proteolytic processing mediated by CAPN3."; /evidence="ECO:0000269|PubMed:23707407"; MUTAGEN 266; /note="R->A: Strongly reduces E1A binding; when associated with A-290; A-295 and A-315."; /evidence="ECO:0000269|PubMed:12419229"; MUTAGEN 290; /note="D->A: Strongly reduces E1A binding; when associated with A-266; A-295 and A-315."; /evidence="ECO:0000269|PubMed:12419229"; MUTAGEN 295; /note="E->A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-315."; /evidence="ECO:0000269|PubMed:12419229"; MUTAGEN 315; /note="H->A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-295."; /evidence="ECO:0000269|PubMed:12419229"; MUTAGEN 422; /note="S->A: Abolishes phosphorylation by HIPK2 and prevents UV-induced clearance."; /evidence="ECO:0000269|PubMed:14567915
uniprot
proteins
post_translational_modification
PTM: The level of phosphorylation appears to be regulated during the cell cycle. Phosphorylation by HIPK2 on Ser-422 induces proteasomal degradation. {ECO:0000269|PubMed:14567915, ECO:0000269|PubMed:8440238}.; PTM: ADP-ribosylated; when cells are exposed to brefeldin A. {ECO:0000250}.; PTM: Sumoylation on Lys-428 is promoted by the E3 SUMO-protein ligase CBX4. {ECO:0000269|PubMed:12679040}.
uniprot
proteins
protein_family
D-isomer specific 2-hydroxyacid dehydrogenase family
uniprot
proteins
pubmed
11462050
uniprot
proteins
pubmed
11509661
uniprot
proteins
pubmed
11568182
uniprot
proteins
pubmed
12372828
uniprot
proteins
pubmed
12419229
uniprot
proteins
pubmed
12679040
uniprot
proteins
pubmed
14567915
uniprot
proteins
pubmed
15060175
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15542832
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
15897867
uniprot
proteins
pubmed
16061479
uniprot
proteins
pubmed
16393996
uniprot
proteins
pubmed
16609867
uniprot
proteins
pubmed
16702210
uniprot
proteins
pubmed
17085477
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
18212045
uniprot
proteins
pubmed
19103759
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23707407
uniprot
proteins
pubmed
23747199
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25728771
uniprot
proteins
pubmed
27094857
uniprot
proteins
pubmed
7479821
uniprot
proteins
pubmed
8440238
uniprot
proteins
pubmed
9858600
uniprot
proteins
sequence_length
440
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12679040}. Nucleus {ECO:0000269|PubMed:12679040}.
uniprot
proteins