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Entry version 208 (10 Apr 2019)
Sequence version 2 (15 Jul 1999)
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Protein

C-terminal-binding protein 1

Gene

CTBP1

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>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
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei100NADBy similarity1
Binding sitei204NADBy similarity1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei266By similarity1
Binding sitei290NADBy similarity1
Active sitei295By similarity1
Active sitei315Proton donorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi180 – 185NADBy similarity6
Nucleotide bindingi237 – 243NADBy similarity7
Nucleotide bindingi264 – 266NADBy similarity3
Nucleotide bindingi315 – 318NADBy similarity4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-3769402 Deactivation of the beta-catenin transactivating complex
R-HSA-3899300 SUMOylation of transcription cofactors
R-HSA-4641265 Repression of WNT target genes
R-HSA-5339700 TCF7L2 mutants don't bind CTBP

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q13363

SIGNOR Signaling Network Open Resource

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SIGNORi
Q13363

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
C-terminal-binding protein 1 (EC:1.1.1.-)
Short name:
CtBP1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CTBP1
Synonyms:CTBP
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000159692.15

Human Gene Nomenclature Database

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HGNCi
HGNC:2494 CTBP1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
602618 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q13363

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Hypotonia, ataxia, developmental delay, and tooth enamel defect syndrome (HADDTS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disorder characterized by delayed motor development, intellectual disability, failure to thrive, hypotonia, ataxia, and tooth enamel defects.
See also OMIM:617915
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_080622342R → W in HADDTS. 1 PublicationCorresponds to variant dbSNP:rs869320802Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNET

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DisGeNETi
1487

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
CTBP1

MalaCards human disease database

More...
MalaCardsi
CTBP1
MIMi617915 phenotype

Open Targets

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OpenTargetsi
ENSG00000159692

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA26995

Chemistry databases

Drug and drug target database

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DrugBanki
DB01942 Formic Acid

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
CTBP1

Domain mapping of disease mutations (DMDM)

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DMDMi
6014741

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000760411 – 440C-terminal-binding protein 1Add BLAST440

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei300PhosphoserineCombined sources1
Modified residuei422Phosphoserine; by HIPK21 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki428Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

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EPDi
Q13363

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q13363

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q13363

PeptideAtlas

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PeptideAtlasi
Q13363

PRoteomics IDEntifications database

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PRIDEi
Q13363

ProteomicsDB human proteome resource

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ProteomicsDBi
59349
59350 [Q13363-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q13363

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q13363

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q13363

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in germinal center B-cells.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000159692 Expressed in 242 organ(s), highest expression level in oviduct epithelium

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q13363 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q13363 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB004217
HPA018987
HPA044971

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 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 MCRIP1 (unphosphorylated form, via the PXDLS motif); competitively inhibiting CTBP-ZEB1 interaction (PubMed:25728771). Interacts with Bassoon/BSN; this interaction targets and anchors CTBP1 to presynapses (By similarity).By similarity16 Publications
(Microbial infection) Interacts with Epstein-Barr virus EBNA3 and EBNA6.2 Publications
(Microbial infection) Interacts with adenovirus E1A protein (via its C-terminus); the interaction disrupts the interaction of CTBP1 with RBBP8.1 Publication
(Microbial infection) Interacts with human adenovirus 5 E1A protein; this interaction seems to potentiate viral replication.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
107869, 188 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q13363

Database of interacting proteins

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DIPi
DIP-24245N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
Q13363

Protein interaction database and analysis system

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IntActi
Q13363, 55 interactors

Molecular INTeraction database

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MINTi
Q13363

STRING: functional protein association networks

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STRINGi
9606.ENSP00000290921

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q13363

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1440
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1MX3X-ray1.95A28-353[»]
4LCEX-ray2.38A28-353[»]
4U6QX-ray2.30A28-353[»]
4U6SX-ray2.10A28-353[»]
6CDFX-ray2.60A28-379[»]
6CDRX-ray2.40A28-379[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q13363

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q13363

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q13363

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 70Interaction with GLIS2 1By similarityAdd BLAST70
Regioni288 – 360Interaction with GLIS2 2By similarityAdd BLAST73

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0067 Eukaryota
COG0111 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000157061

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000136701

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG001898

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q13363

KEGG Orthology (KO)

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KOi
K04496

Identification of Orthologs from Complete Genome Data

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OMAi
TADSTMC

Database of Orthologous Groups

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OrthoDBi
700058at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q13363

TreeFam database of animal gene trees

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TreeFami
TF313593

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View 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

Pfam protein domain database

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Pfami
View protein in Pfam
PF00389 2-Hacid_dh, 1 hit
PF02826 2-Hacid_dh_C, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF51735 SSF51735, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00065 D_2_HYDROXYACID_DH_1, 1 hit
PS00671 D_2_HYDROXYACID_DH_3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 10 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 10 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0Y8W7H0Y8W7_HUMAN
C-terminal-binding protein 1
CTBP1
287Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0Y8U5H0Y8U5_HUMAN
C-terminal-binding protein 1
CTBP1
184Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
D6RAX2D6RAX2_HUMAN
C-terminal-binding protein 1
CTBP1
186Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E7EPF8E7EPF8_HUMAN
C-terminal-binding protein 1
CTBP1
202Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E7ESU7E7ESU7_HUMAN
C-terminal-binding protein 1
CTBP1
171Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PGB1E9PGB1_HUMAN
C-terminal-binding protein 1
CTBP1
145Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0Y9M9H0Y9M9_HUMAN
C-terminal-binding protein 1
CTBP1
145Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E7EUB3E7EUB3_HUMAN
C-terminal-binding protein 1
CTBP1
168Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0Y913H0Y913_HUMAN
C-terminal-binding protein 1
CTBP1
24Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0D9SGE6A0A0D9SGE6_HUMAN
C-terminal-binding protein 1
CTBP1
69Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_080622342R → W in HADDTS. 1 PublicationCorresponds to variant dbSNP:rs869320802Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0433051 – 13MGSSH…KGLPL → MS in isoform 2. 1 PublicationAdd BLAST13

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS3348.1 [Q13363-1]
CCDS43203.1 [Q13363-2]

NCBI Reference Sequences

More...
RefSeqi
NP_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]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.208597

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000290921; ENSP00000290921; ENSG00000159692 [Q13363-1]
ENST00000382952; ENSP00000372411; ENSG00000159692 [Q13363-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1487

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:1487

UCSC genome browser

More...
UCSCi
uc003gcu.2 human [Q13363-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

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

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[»]
6CDFX-ray2.60A28-379[»]
6CDRX-ray2.40A28-379[»]
ProteinModelPortaliQ13363
SMRiQ13363
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107869, 188 interactors
CORUMiQ13363
DIPiDIP-24245N
ELMiQ13363
IntActiQ13363, 55 interactors
MINTiQ13363
STRINGi9606.ENSP00000290921

Chemistry databases

BindingDBiQ13363
DrugBankiDB01942 Formic Acid

PTM databases

iPTMnetiQ13363
PhosphoSitePlusiQ13363
SwissPalmiQ13363

Polymorphism and mutation databases

BioMutaiCTBP1
DMDMi6014741

Proteomic databases

EPDiQ13363
jPOSTiQ13363
PaxDbiQ13363
PeptideAtlasiQ13363
PRIDEiQ13363
ProteomicsDBi59349
59350 [Q13363-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
1487
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1487
DisGeNETi1487
EuPathDBiHostDB:ENSG00000159692.15

GeneCards: human genes, protein and diseases

More...
GeneCardsi
CTBP1
GeneReviewsiCTBP1
HGNCiHGNC:2494 CTBP1
HPAiCAB004217
HPA018987
HPA044971
MalaCardsiCTBP1
MIMi602618 gene
617915 phenotype
neXtProtiNX_Q13363
OpenTargetsiENSG00000159692
PharmGKBiPA26995

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0067 Eukaryota
COG0111 LUCA
GeneTreeiENSGT00940000157061
HOGENOMiHOG000136701
HOVERGENiHBG001898
InParanoidiQ13363
KOiK04496
OMAiTADSTMC
OrthoDBi700058at2759
PhylomeDBiQ13363
TreeFamiTF313593

Enzyme and pathway databases

ReactomeiR-HSA-3769402 Deactivation of the beta-catenin transactivating complex
R-HSA-3899300 SUMOylation of transcription cofactors
R-HSA-4641265 Repression of WNT target genes
R-HSA-5339700 TCF7L2 mutants don't bind CTBP
SignaLinkiQ13363
SIGNORiQ13363

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
CTBP1 human
EvolutionaryTraceiQ13363

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
CTBP1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
1487

Protein Ontology

More...
PROi
PR:Q13363

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000159692 Expressed in 242 organ(s), highest expression level in oviduct epithelium
ExpressionAtlasiQ13363 baseline and differential
GenevisibleiQ13363 HS

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCTBP1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q13363
Secondary accession number(s): Q4W5N3, Q7Z2Q5
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1999
Last modified: April 10, 2019
This is version 208 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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