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Reviewed, UniProtKB/Swiss-Prot Q9EQH5 (CTBP2_RAT)

Last modified January 19, 2010. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · 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
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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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. Isoform 2 probably acts as a scaffold for specialized synapses By similarity.

Subunit structure

Interacts with HIPK2, ZNF217 and PNN By similarity. Interacts with the transcription factors BKLF, delta EF1/AREB6/ZEB, EVI-1 and Friend of GATA (FOG) via the consensus motif P-X-[DNS]-L-[STVA]. Can form a complex with BKLF on a CACCC-box oligonucleotide. Can form homodimers or heterodimers of CTBP1 and CTBP2. Interacts with NRIP1 and WIZ. Interacts with PRDM16; represses white adipose tissue (WAT)-specific genes expression By similarity.

Subcellular location

Nucleus Potential. Cell junction › synapse By similarity.

Tissue specificity

Isoform 2 is specifically localized in synaptic ribbon (at protein level). Ref.1

Post-translational modification

Isoform 2 is phosphorylated upon DNA damage, probably by ATM or ATR at Thr-171 and Ser-177. Phosphorylation by HIPK2 on Ser-428 induces proteasomal degradation By similarity.

Sequence similarities

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

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Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9EQH5-1)

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: Q9EQH5-2)

Also known as: Ribeye;

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MALVDKHKVKRQRLDRICEG → MPVPSRHINI...VSTMLTPEPS
Note: Contains a phosphothreonine at position 171 (By similarity). Contains a phosphoserine at position 177 (By similarity).

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445C-terminal-binding protein 2
PRO_0000299356

Regions

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

Sites

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

Amino acid modifications

Modified residue4281Phosphoserine; by HIPK2 By similarity

Natural variations

Alternative sequence1 – 2020MALVD…RICEG → MPVPSRHINIGRSQSWDAAG WYEGPWENAGPPGRRSSLTY GPGEGVWCELVNHRAQDTES CLSREAFYNSLASRKGSVPD FTFYDSRQAVMSGRGSVLPQ DYYGDPSRGTRVPKEPPFYR DPGTSRPVPSYGVLGSRIPW EQVQGQLPALQDAGHLYRES GSKTVLHGQRTHCRAPSPGR YGREQPDSRLGIEVPTYSPN SSQVYNDICERPVDSTHARQ VAPTCLVVDPSSTAPTENST GVAPGSLNRGYGPTRESIHS KLAYENYEADLSTFQGPGGK RTVYPEFLALLRAEGVAEAT LAALLQQGFDSPAVLATLED ADIKSVAPNLGQARVLSRLV SSCRTEMQFRRQDRTGPPPR HRSSSFSHRSELLPNDTASL GTTALQFHPAGPLQTPSPRG GDLGRRPSSAPSQHLLETAA TYSAPVVGSQTPHLPSNSGY SSPTPCALTARLASSYPSQA GVALTANPGPSVPLHSSPRT AYSTSYTVPMELLKRERSVT ASPLPSPHASPQLLRKPGAA PVEPAALPPVRQSLHTPHPP YQKVARRTGAPIIVSTMLTP EPS in isoform 2.
VSP_027611

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Sequences

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

Last modified September 11, 2007. Version 2.
Checksum: 403012CDEB2E492B

FASTA44548,987
        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 VEETADSTVC 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 
FFVTSTPWSV IDQQAIHPEL NGATYRYPPG IVGVAPGGLP PAMEGIIPGG IPVTHNLPTV 

       430        440 
AHPSQAPSPN QPTKHGDNRE HPNEQ

« Hide

Isoform 2 (Ribeye).

Checksum: 41E08C4148B50424
Show »

FASTA988107,125

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References

« Hide 'large scale' references
[1]"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), TISSUE SPECIFICITY.
[2]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed: 15057822] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF222712 mRNA. Translation: AAG45952.1.
AABR03001613 Genomic DNA. No translation available.
AABR03000195 Genomic DNA. No translation available.
IPIIPI00189984.
IPI00476123.
RefSeqNP_445787.1.
UniGeneRn.138124

3D structure databases

HSSPHSSP built from PDB template 1MX3 based on UniProtKB Q13363.
SMRQ9EQH5. Positions 33-362.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9EQH5.

Genome annotation databases

EnsemblENSRNOT00000023574; ENSRNOP00000023574; ENSRNOG00000017326; Rattus norvegicus. [Genome view]
GeneID81717.
KEGGrno:81717.
NMPDRfig|10116.3.peg.3145.
UCSCNM_053335. rat.

Organism-specific databases

CTD81717.
RGD68372. Ctbp2.

Phylogenomic databases

eggNOGroNOG10005.
HOVERGENQ9EQH5.
OMATMEDADI.
OrthoDBEOG9X3KKH.

Gene expression databases

ArrayExpressQ9EQH5.
GenevestigatorQ9EQH5.

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

NextBio615359.

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Entry information

Entry nameCTBP2_RAT
AccessionPrimary (citable) accession number: Q9EQH5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: January 19, 2010
This is version 54 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

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