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Q13363 (CTBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 158. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
C-terminal-binding protein 1

Short name=CtBP1
EC=1.1.1.-
Gene names
Name:CTBP1
Synonyms:CTBP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length440 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.2 Ref.13 Ref.21 Ref.22 Ref.24

Cofactor

NAD. Required for efficient interaction with E1A. Cofactor binding induces a conformation change. Ref.24

Subunit structure

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, ZNF366, ZFHX1B and WIZ. 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. Ref.1 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.22 Ref.24

Subcellular location

Cytoplasm. Nucleus Ref.11.

Tissue specificity

Expressed in germinal center B-cells. Ref.21

Post-translational modification

The level of phosphorylation appears to be regulated during the cell cycle. Phosphorylation by HIPK2 on Ser-422 induces proteasomal degradation.

ADP-ribosylated; when cells are exposed to brefeldin A By similarity.

Sumoylation on Lys-428 is promoted by the E3 SUMO-protein ligase CBX4. Ref.11

Sequence similarities

Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.

Ontologies

Keywords
   Biological processDifferentiation
Host-virus interaction
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandNAD
   Molecular functionOxidoreductase
Repressor
   PTMADP-ribosylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi organization

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Traceable author statement Ref.1. Source: ProtInc

negative regulation of histone H4 acetylation

Inferred from mutant phenotype PubMed 21102443. Source: BHF-UCL

negative regulation of histone acetylation

Inferred from mutant phenotype PubMed 21102443. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 19162039PubMed 21102443. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of histone deacetylation

Inferred from mutant phenotype PubMed 21102443. Source: BHF-UCL

protein phosphorylation

Traceable author statement Ref.6. Source: ProtInc

regulation of cell cycle

Inferred from mutant phenotype PubMed 21102443. Source: BHF-UCL

regulation of transcription by chromatin organization

Inferred from mutant phenotype PubMed 21102443. Source: BHF-UCL

viral genome replication

Traceable author statement Ref.1. Source: ProtInc

white fat cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

transcriptional repressor complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionNAD binding

Inferred from sequence or structural similarity. Source: UniProtKB

RNA polymerase II transcription corepressor activity

Inferred from direct assay PubMed 16287852PubMed 19162039. Source: BHF-UCL

oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor

Inferred from electronic annotation. Source: InterPro

protein C-terminus binding

Traceable author statement Ref.6. Source: ProtInc

protein binding

Inferred from physical interaction Ref.7PubMed 12052894Ref.16PubMed 19505873. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction PubMed 18374649. Source: UniProtKB

repressing transcription factor binding

Inferred from physical interaction PubMed 19162039. Source: BHF-UCL

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

transcription factor binding

Inferred from physical interaction Ref.17. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13363-1)

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.
Isoform 2 (identifier: Q13363-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: MGSSHLLNKGLPL → MS
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 440440C-terminal-binding protein 1
PRO_0000076041

Regions

Nucleotide binding180 – 1856NAD By similarity
Nucleotide binding237 – 2437NAD By similarity
Nucleotide binding264 – 2663NAD By similarity
Nucleotide binding315 – 3184NAD By similarity
Region1 – 7070Interaction with GLIS2 1 By similarity
Region288 – 36073Interaction with GLIS2 2 By similarity

Sites

Active site2661 By similarity
Active site2951 By similarity
Active site3151Proton donor By similarity
Binding site1001NAD By similarity
Binding site2041NAD By similarity
Binding site2901NAD By similarity

Amino acid modifications

Modified residue3001Phosphoserine Ref.20
Modified residue4221Phosphoserine; by HIPK2 Ref.12
Cross-link428Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.11

Natural variations

Alternative sequence1 – 1313MGSSH…KGLPL → MS in isoform 2.
VSP_043305

Experimental info

Mutagenesis1341C → A: Strongly reduces E1A binding; when associated with A-138; A-141 and A-150. Ref.24
Mutagenesis1381N → A: Strongly reduces E1A binding; when associated with A-134; A-141 and A-150. Ref.24
Mutagenesis141 – 1422RR → AA: Strongly reduces E1A binding; when associated with A-163 and A-171. Ref.24
Mutagenesis1411R → A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-150. Ref.24
Mutagenesis1501L → A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-141. Ref.24
Mutagenesis1631R → A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-171. Ref.24
Mutagenesis1711R → A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-163. Ref.24
Mutagenesis1811G → V: Strongly reduces E1A binding; when associated with V-183 and A-204. Ref.24
Mutagenesis1831G → V: Strongly reduces E1A binding; when associated with V-181 and A-204. Ref.24
Mutagenesis2041D → A: Strongly reduces E1A binding; when associated with V-181 and V-183. Ref.24
Mutagenesis2661R → A: Strongly reduces E1A binding; when associated with A-290; A-295 and A-315. Ref.24
Mutagenesis2901D → A: Strongly reduces E1A binding; when associated with A-266; A-295 and A-315. Ref.24
Mutagenesis2951E → A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-315. Ref.24
Mutagenesis3151H → A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-295. Ref.24
Mutagenesis4221S → A: Abolishes phosphorylation by HIPK2 and prevents UV-induced clearance. Ref.12

Secondary structure

................................................................... 440
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: F071DD30B385603F

FASTA44047,535
        10         20         30         40         50         60 
MGSSHLLNKG LPLGVRPPIM NGPLHPRPLV ALLDGRDCTV EMPILKDVAT VAFCDAQSTQ 

        70         80         90        100        110        120 
EIHEKVLNEA VGALMYHTIT LTREDLEKFK ALRIIVRIGS GFDNIDIKSA GDLGIAVCNV 

       130        140        150        160        170        180 
PAASVEETAD STLCHILNLY RRATWLHQAL REGTRVQSVE QIREVASGAA RIRGETLGII 

       190        200        210        220        230        240 
GLGRVGQAVA LRAKAFGFNV LFYDPYLSDG VERALGLQRV STLQDLLFHS DCVTLHCGLN 

       250        260        270        280        290        300 
EHNHHLINDF TVKQMRQGAF LVNTARGGLV DEKALAQALK EGRIRGAALD VHESEPFSFS 

       310        320        330        340        350        360 
QGPLKDAPNL ICTPHAAWYS EQASIEMREE AAREIRRAIT GRIPDSLKNC VNKDHLTAAT 

       370        380        390        400        410        420 
HWASMDPAVV HPELNGAAYR YPPGVVGVAP TGIPAAVEGI VPSAMSLSHG LPPVAHPPHA 

       430        440 
PSPGQTVKPE ADRDHASDQL 

« Hide

Isoform 2 [UniParc].

Checksum: 0366A6370016910B
Show »

FASTA42946,405

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of a cellular phosphoprotein that interacts with a conserved C-terminal domain of adenovirus E1A involved in negative modulation of oncogenic transformation."
Schaeper U., Boyd J.M., Verma S., Uhlmann E., Subramanian T., Chinnadurai G.
Proc. Natl. Acad. Sci. U.S.A. 92:10467-10471(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 98-108, INTERACTION WITH RBBP8 AND ADENOVIRUS E1A.
Tissue: B-cell and Cervix carcinoma.
[2]"C-terminal binding protein is a transcriptional repressor that interacts with a specific class of vertebrate polycomb proteins."
Sewalt R.G.A.B., Gunster M.J., van der Vlag J., Satijn D.P.E., Otte A.P.
Mol. Cell. Biol. 19:777-787(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SEQUENCE REVISION, FUNCTION.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain and Lung.
[6]"A region in the C-terminus of adenovirus 2/5 E1a protein is required for association with a cellular phosphoprotein and important for the negative modulation of T24-ras mediated transformation, tumorigenesis and metastasis."
Boyd J.M., Subramanian T., Schaeper U., la Regina M., Bayley S., Chinnadurai G.
EMBO J. 12:469-478(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ADENOVIRUS E1A, PHOSPHORYLATION.
[7]"Interaction of EVI1 with cAMP-responsive element-binding protein-binding protein (CBP) and p300/CBP-associated factor (P/CAF) results in reversible acetylation of EVI1 and in co-localization in nuclear speckles."
Chakraborty S., Senyuk V., Sitailo S., Chi Y., Nucifora G.
J. Biol. Chem. 276:44936-44943(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MECOM.
[8]"Physical and functional interactions between the corepressor CtBP and the Epstein-Barr virus nuclear antigen EBNA3C."
Touitou R., Hickabottom M., Parker G., Crook T., Allday M.J.
J. Virol. 75:7749-7755(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EBV EBNA6.
[9]"Acetylation of nuclear hormone receptor-interacting protein RIP140 regulates binding of the transcriptional corepressor CtBP."
Vo N., Fjeld C., Goodman R.H.
Mol. Cell. Biol. 21:6181-6188(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NRIP1.
[10]"Two nonconsensus sites in the Epstein-Barr virus oncoprotein EBNA3A cooperate to bind the co-repressor carboxyl-terminal-binding protein (CtBP)."
Hickabottom M., Parker G.A., Freemont P., Crook T., Allday M.J.
J. Biol. Chem. 277:47197-47204(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EBV EBNA3.
[11]"The polycomb protein Pc2 is a SUMO E3."
Kagey M.H., Melhuish T.A., Wotton D.
Cell 113:127-137(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-428, SUBCELLULAR LOCATION.
[12]"Homeodomain interacting protein kinase 2 promotes apoptosis by downregulating the transcriptional corepressor CtBP."
Zhang Q., Yoshimatsu Y., Hildebrand J., Frisch S.M., Goodman R.H.
Cell 115:177-186(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIPK2, PHOSPHORYLATION AT SER-422, MUTAGENESIS OF SER-422.
[13]"Nuclear speckle-associated protein Pnn/DRS binds to the transcriptional corepressor CtBP and relieves CtBP-mediated repression of the E-cadherin gene."
Alpatov R., Munguba G.C., Caton P., Joo J.H., Shi Y., Shi Y., Hunt M.E., Sugrue S.P.
Mol. Cell. Biol. 24:10223-10235(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSCRIPTIONAL REPRESSION, INTERACTION WITH PNN.
[14]"Multiple domains of the receptor-interacting protein 140 contribute to transcription inhibition."
Castet A., Boulahtouf A., Versini G., Bonnet S., Augereau P., Vignon F., Khochbin S., Jalaguier S., Cavailles V.
Nucleic Acids Res. 32:1957-1966(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NRIP1.
[15]"Pc2-mediated sumoylation of Smad-interacting protein 1 attenuates transcriptional repression of E-cadherin."
Long J., Zuo D., Park M.
J. Biol. Chem. 280:35477-35489(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZFHX1B.
[16]"Oligomerization of Evi-1 regulated by the PR domain contributes to recruitment of corepressor CtBP."
Nitta E., Izutsu K., Yamaguchi Y., Imai Y., Ogawa S., Chiba S., Kurokawa M., Hirai H.
Oncogene 24:6165-6173(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MECOM.
[17]"The FoxP subclass in Xenopus laevis development."
Schoen C., Wochnik A., Roessner A., Donow C., Knoechel W.
Dev. Genes Evol. 216:641-646(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FOXP1.
[18]"Zinc finger protein Wiz links G9a/GLP histone methyltransferases to the co-repressor molecule CtBP."
Ueda J., Tachibana M., Ikura T., Shinkai Y.
J. Biol. Chem. 281:20120-20128(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH WIZ.
[19]"ZNF366 is an estrogen receptor corepressor that acts through CtBP and histone deacetylases."
Lopez-Garcia J., Periyasamy M., Thomas R.S., Christian M., Leao M., Jat P., Kindle K.B., Heery D.M., Parker M.G., Buluwela L., Kamalati T., Ali S.
Nucleic Acids Res. 34:6126-6136(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZNF366.
[20]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[21]"CtBP is an essential corepressor for BCL6 autoregulation."
Mendez L.M., Polo J.M., Yu J.J., Krupski M., Ding B.B., Melnick A., Ye B.H.
Mol. Cell. Biol. 28:2175-2186(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS COREPRESSOR, INTERACTION WITH BCL6, TISSUE SPECIFICITY.
[22]"Acetylation-dependent interaction of SATB1 and CtBP1 mediates transcriptional repression by SATB1."
Purbey P.K., Singh S., Notani D., Kumar P.P., Limaye A.S., Galande S.
Mol. Cell. Biol. 29:1321-1337(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SATB1.
[23]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Transcription corepressor CtBP is an NAD(+)-regulated dehydrogenase."
Kumar V., Carlson J.E., Ohgi K.A., Edwards T.A., Rose D.W., Escalante C.R., Rosenfeld M.G., Aggarwal A.K.
Mol. Cell 10:857-869(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 28-353 IN COMPLEX WITH NAD, FUNCTION, COFACTOR, MUTAGENESIS OF CYS-134; ASN-138; ARG-141; 141-ARG-ARG-142; LEU-150; ARG-163; ARG-171; GLY-181; GLY-183; ASP-204; ARG-266; ASP-290; GLU-295 AND HIS-315, DIMERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS3348.1. [Q13363-1]
CCDS43203.1. [Q13363-2]
RefSeqNP_001012632.1. NM_001012614.1. [Q13363-2]
NP_001319.1. NM_001328.2. [Q13363-1]
UniGeneHs.208597.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MX3X-ray1.95A28-353[»]
4LCEX-ray2.38A28-353[»]
ProteinModelPortalQ13363.
SMRQ13363. Positions 28-352.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107869. 90 interactions.
DIPDIP-24245N.
IntActQ13363. 24 interactions.
MINTMINT-94454.
STRING9606.ENSP00000290921.

PTM databases

PhosphoSiteQ13363.

Polymorphism databases

DMDM6014741.

Proteomic databases

MaxQBQ13363.
PaxDbQ13363.
PRIDEQ13363.

Protocols and materials databases

DNASU1487.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000290921; ENSP00000290921; ENSG00000159692. [Q13363-1]
ENST00000382952; ENSP00000372411; ENSG00000159692. [Q13363-2]
GeneID1487.
KEGGhsa:1487.
UCSCuc003gcu.1. human. [Q13363-2]
uc003gcv.1. human. [Q13363-1]

Organism-specific databases

CTD1487.
GeneCardsGC04M001205.
HGNCHGNC:2494. CTBP1.
HPACAB004217.
HPA018987.
HPA044971.
MIM602618. gene.
neXtProtNX_Q13363.
PharmGKBPA26995.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0111.
HOGENOMHOG000136701.
HOVERGENHBG001898.
InParanoidQ13363.
KOK04496.
OMADRDHPSD.
OrthoDBEOG761BT9.
PhylomeDBQ13363.
TreeFamTF313593.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ13363.

Gene expression databases

ArrayExpressQ13363.
BgeeQ13363.
CleanExHS_CTBP1.
GenevestigatorQ13363.

Family and domain databases

Gene3D3.40.50.720. 2 hits.
InterProIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR006140. D-isomer_2_OHA_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
PROSITEPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCTBP1. human.
EvolutionaryTraceQ13363.
GeneWikiCTBP1.
GenomeRNAi1487.
NextBio6105.
PROQ13363.
SOURCESearch...

Entry information

Entry nameCTBP1_HUMAN
AccessionPrimary (citable) accession number: Q13363
Secondary accession number(s): Q4W5N3, Q7Z2Q5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1999
Last modified: July 9, 2014
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM