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Reviewed, UniProtKB/Swiss-Prot P56545 (CTBP2_HUMAN)

Last modified February 9, 2010. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    C-terminal-binding protein 2
      Short name=CtBP2
Gene names
Name: CTBP2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Corepressor targeting diverse transcription regulators. Functions in brown adipose tissue (BAT) differentiation By similarity.

Isoform 2 probably acts as a scaffold for specialized synapses.

Subunit structure

Interacts with the C-terminus of adenovirus E1A protein. Can form homodimers or heterodimers of CTBP1 and CTBP2. Interacts with HIPK2 and ZNF217. Interacts with PRDM16; represses white adipose tissue (WAT)-specific genes expression By similarity. Interacts with PNN, NRIP1 and WIZ. Ref.10 Ref.11 Ref.12

Subcellular location

Nucleus Potential. Cell junction › synapse By similarity.

Tissue specificity

Ubiquitous. Highest levels in heart, skeletal muscle, and pancreas.

Post-translational modification

Isoform 2 is phosphorylated upon DNA damage, probably by ATM or ATR at Thr-179; Ser-181 and Ser-185. Phosphorylation by HIPK2 on Ser-428 induces proteasomal degradation By similarity. Ref.13

Sequence similarities

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

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Ontologies

Keywords
   Biological processDifferentiation
Transcription
Transcription regulation
   Cellular componentCell junction
Nucleus
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandNAD
   Molecular functionOxidoreductase
Repressor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processnegative regulation of cell proliferation Ref.1

Traceable author statement. Source: ProtInc

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription

Inferred from electronic annotation. Source: UniProtKB-KW

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

viral genome replication Ref.1

Traceable author statement. Source: ProtInc

white fat cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

synapse

Inferred from electronic annotation. Source: UniProtKB-SubCell

transcriptional repressor complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functionNAD or NADH binding

Inferred from electronic annotation. Source: InterPro

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

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from sequence or structural similarity. Source: UniProtKB

transcription repressor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

HIC1Q145261EBI-741533,EBI-2507362

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Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P56545-1)

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: P56545-2)

Also known as: Ribeye;

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MALVDKHKVKRQRLDRICEG → MPVPSRHINI...VSTMLAPEPS
Note: Contains a phosphothreonine at position 179. Contains a phosphoserine at position 181. Contains a phosphoserine at position 185.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier
Sequence conflict4551Y → H in AAG45951. Ref.2
Sequence conflict5391Q → E in AAG45951. Ref.2

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445C-terminal-binding protein 2
PRO_0000076044

Regions

Nucleotide binding186 – 1916NAD
Nucleotide binding243 – 2497NAD
Nucleotide binding270 – 2723NAD
Nucleotide binding321 – 3244NAD

Sites

Active site2721 By similarity
Active site3011 By similarity
Active site3211Proton donor By similarity
Binding site1061NAD By similarity
Binding site2101NAD
Binding site2961NAD

Amino acid modifications

Modified residue4281Phosphoserine By similarity

Natural variations

Alternative sequence1 – 2020MALVD…RICEG → MPVPSRHINIGRSQSWDAAG WYEGPWENAESLRPLGRRSS LTYGTAEGTWFEPNHRPQDA ALPVAAEPYLYREAVYNSVA ARKGSTPDFTFYDSRQAVMS GRSPLLPREYYSDPSGAARV PKEPPLYRDPGVSRPVPSYG VLGSRTSWDPMQGRSPALQD AGHLYRDPGGKMIPQGRQTQ SRAASPGRYGREQPDTRYGA EVPAYPLSQVFSDISERPID PAPARQVAPTCLVVDPSSAA APEGSTGVAPGALNRGYGPA RESIPSKMAYETYEADLSTF QGPGGKRTVLPEFLAFLRAE GLAEATLGALLQQGFDSPAV LATLEDADIKSVAPNLGQAR VLSRLANSCRTEMQLRRQDR GGPLPRARSSSFSHRSELLH GDLASLGAAAPLQTASPRAG DPARRPSSAPSQHLLETAAT YSAPGVGTHAPHFPSNSGYS SPTPCALTARLSPTYPLQAG VALTNPGPSNPLHPGPRTAY STAYTVPMELLKRERNVAAS PLPSPHGSPQVLRKPGAPLG PSTLPPASQSLHTPHSPYQK VARRTGAPIIVSTMLAPEPS in isoform 2.
VSP_027615
Natural variant471E → D: dbSNP rs3198926.
VAR_033844

Experimental info

Sequence conflict871L → F in AAG45951. Ref.2
Sequence conflict881T → N in AAG45951. Ref.2
Sequence conflict1121D → N in AAG45951. Ref.2
Sequence conflict4111I → T in AAH47018. Ref.8

Secondary structure

1 .................................................................. 445
Helix Strand Turn

Details...

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Sequences

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

Last modified July 15, 1998. Version 1.
Checksum: 0A8C21CEB36807FA

FASTA44548,945
        10         20         30         40         50         60 
MALVDKHKVK RQRLDRICEG IRPQIMNGPL HPRPLVALLD GRDCTVEMPI LKDLATVAFC 

        70         80         90        100        110        120 
DAQSTQEIHE KVLNEAVGAM MYHTITLTRE DLEKFKALRV IVRIGSGYDN VDIKAAGELG 

       130        140        150        160        170        180 
IAVCNIPSAA VEETADSTIC HILNLYRRNT WLYQALREGT RVQSVEQIRE VASGAARIRG 

       190        200        210        220        230        240 
ETLGLIGFGR TGQAVAVRAK AFGFSVIFYD PYLQDGIERS LGVQRVYTLQ DLLYQSDCVS 

       250        260        270        280        290        300 
LHCNLNEHNH HLINDFTIKQ MRQGAFLVNA ARGGLVDEKA LAQALKEGRI RGAALDVHES 

       310        320        330        340        350        360 
EPFSFAQGPL KDAPNLICTP HTAWYSEQAS LEMREAAATE IRRAITGRIP ESLRNCVNKE 

       370        380        390        400        410        420 
FFVTSAPWSV IDQQAIHPEL NGATYRYPPG IVGVAPGGLP AAMEGIIPGG IPVTHNLPTV 

       430        440 
AHPSQAPSPN QPTKHGDNRE HPNEQ

« Hide

Isoform 2 (Ribeye).

Checksum: 90EC841907295622
Show »

FASTA985106,187

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References

« Hide 'large scale' references
[1]"A novel C-terminal binding protein (CTBP2) is closely related to CTBP1, an adenovirus E1A-binding protein, and maps to human chromosome 21q21.3."
Katsanis N., Fisher E.M.C.
Genomics 47:294-299(1998) [PubMed: 9479502] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"RIBEYE, a component of synaptic ribbons: a protein's journey through evolution provides insight into synaptic ribbon function."
Schmitz F., Koenigstorfer A., Suedhof T.C.
Neuron 28:857-872(2000) [PubMed: 11163272] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Umbilical cord blood.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Melanoma.
[6]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed: 15164054] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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 (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Colon, Kidney, Pancreas and Placenta.
[9]"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: 7479821] [Abstract]
Cited for: PROTEIN SEQUENCE OF 263-272.
Tissue: B-cell and Cervix carcinoma.
[10]"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: 15542832] [Abstract]
Cited for: INTERACTION WITH PNN.
[11]"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: 15060175] [Abstract]
Cited for: INTERACTION WITH NRIP1.
[12]"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: 16702210] [Abstract]
Cited for: INTERACTION WITH WIZ.
[13]"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: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-179; SER-181 AND SER-185 (ISOFORM 2), MASS SPECTROMETRY.
[14]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[15]"Crystal structure of human CTBP2 dehydrogenase complexed with NAD(H)."
Structural genomics consortium (SGC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 31-364 IN COMPLEX WITH NAD.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF016507 mRNA. Translation: AAC39603.1.
AF222711 mRNA. Translation: AAG45951.1.
BT007012 mRNA. Translation: AAP35658.1.
AK290390 mRNA. Translation: BAF83079.1.
AL833398 mRNA. Translation: CAH10590.1.
AL596261, AL731571 Genomic DNA. Translation: CAH72472.1.
AL731571, AL596261 Genomic DNA. Translation: CAI16100.1.
AL731571 Genomic DNA. Translation: CAI16102.1.
CH471066 Genomic DNA. Translation: EAW49247.1.
CH471066 Genomic DNA. Translation: EAW49250.1.
BC002486 mRNA. Translation: AAH02486.1.
BC047018 mRNA. Translation: AAH47018.1.
BC052276 mRNA. Translation: AAH52276.1.
BC072020 mRNA. Translation: AAH72020.1.
IPIIPI00010120.
IPI00010136.
RefSeqNP_001077383.1.
NP_001320.1.
NP_073713.2.
UniGeneHs.501345

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2OMEX-ray2.80A/B/C/D/E/F/G/H31-364[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP56545. 8 interactions.
STRINGP56545.

Proteomic databases

PRIDEP56545.

Genome annotation databases

EnsemblENST00000337195; ENSP00000338615; ENSG00000175029; Homo sapiens. [Genome view]
ENST00000411419; ENSP00000410474; ENSG00000175029; Homo sapiens. [Genome view]
GeneID1488.
KEGGhsa:1488.
UCSCuc001lie.2. human.
uc001lif.2. human.

Organism-specific databases

CTD1488.
GeneCardsGC10M126666.
H-InvDBHIX0009290.
HGNCHGNC:2495. CTBP2.
MIM602619. gene.
PharmGKBPA24460.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG17991.
HOVERGENP56545.
PhylomeDBP56545.

Gene expression databases

ArrayExpressP56545.
BgeeP56545.
CleanExHS_CTBP2.
GenevestigatorP56545.
GermOnlineENSG00000175029. Homo sapiens.

Family and domain databases

InterProIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR006140. D-isomer_2_OHA_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
PROSITEPS00065. D_2_HYDROXYACID_DH_1. False negative.
PS00670. D_2_HYDROXYACID_DH_2. False negative.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio6111.
SOURCESearch...

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Entry information

Entry nameCTBP2_HUMAN
AccessionPrimary (citable) accession number: P56545
Secondary accession number(s): A8K2X5 expand/collapse secondary AC list , O43449, Q5SQP7, Q69YI3, Q86SV0, Q9H2T8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: February 9, 2010
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Relevant documents

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents