P56545 (CTBP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
C-terminal-binding protein 2
Short name=CtBP2

Gene names

Name:

CTBP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	445 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.11 Ref.12 Ref.13
Subcellular location	Nucleus Potential. Cell junction › synapse By similarity.
Tissue specificity	Ubiquitous. Highest levels in heart, skeletal muscle, and pancreas.
Sequence similarities	Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.

Ontologies

Keywords
Biological process	Differentiation Transcription Transcription regulation
Cellular component	Cell junction Nucleus Synapse
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	NAD
Molecular function	Oxidoreductase Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of cell proliferation Traceable author statement Ref.1. Source: ProtInc negative regulation of transcription, DNA-templated Inferred from sequence or structural similarity. Source: UniProtKB transcription, DNA-templated Inferred from electronic annotation. Source: UniProtKB-KW viral genome replication Traceable author statement Ref.1. Source: ProtInc white fat cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cell 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_function	NAD 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 transcription corepressor activity Inferred from electronic annotation. Source: Ensembl
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BCL3	P20749	2	EBI-741533,EBI-958997
CCNH	P51946	5	EBI-741533,EBI-741406
HIC1	Q14526	2	EBI-741533,EBI-2507362
PPP1R15A	O75807	2	EBI-741533,EBI-714746
PROX1	Q92786	2	EBI-741533,EBI-3912635
SOX13	Q9UN79	2	EBI-741533,EBI-3928516
Zbp1	A2APF7	2	EBI-741533,EBI-6115394	From a different organism.

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 445

445

C-terminal-binding protein 2

PRO_0000076044

Regions

Nucleotide binding

186 – 191

6

NAD

Nucleotide binding

243 – 249

7

NAD

Nucleotide binding

270 – 272

3

NAD

Nucleotide binding

321 – 324

4

NAD

Sites

Active site

272

1

By similarity

Active site

301

1

By similarity

Active site

321

1

Proton donor By similarity

Binding site

106

1

NAD By similarity

Binding site

210

1

NAD

Binding site

296

1

NAD

Natural variations

Alternative sequence

1 – 20

20

MALVD…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 variant

47

1

E → D.
Corresponds to variant rs3198926 [ dbSNP | Ensembl ].

VAR_033844

Experimental info

Sequence conflict

87

1

L → F in AAG45951. Ref.2

Sequence conflict

88

1

T → N in AAG45951. Ref.2

Sequence conflict

112

1

D → N in AAG45951. Ref.2

Sequence conflict

411

1

I → T in AAH47018. Ref.9

Isoform 2:

Sequence conflict

455

1

Y → H in AAG45951. Ref.2

Sequence conflict

539

1

Q → E in AAG45951. Ref.2

Secondary structure

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445

Helix Strand Turn

Details...

Beta strand

35 – 38

4

Helix

47 – 51

5

Turn

52 – 54

3

Beta strand

56 – 59

4

Helix

65 – 67

3

Helix

70 – 75

6

Beta strand

76 – 81

6

Beta strand

83 – 85

3

Helix

89 – 93

5

Beta strand

100 – 106

7

Helix

113 – 118

6

Beta strand

122 – 124

3

Beta strand

128 – 130

3

Helix

131 – 147

17

Helix

149 – 157

9

Helix

165 – 171

7

Turn

172 – 174

3

Beta strand

182 – 186

5

Helix

190 – 199

10

Helix

200 – 202

3

Beta strand

205 – 209

5

Helix

217 – 220

4

Helix

229 – 235

7

Beta strand

237 – 241

5

Helix

255 – 258

4

Beta strand

265 – 269

5

Helix

273 – 275

3

Helix

278 – 286

9

Beta strand

289 – 296

8

Beta strand

299 – 302

4

Turn

309 – 312

4

Beta strand

314 – 318

5

Helix

327 – 346

20

Turn

349 – 352

4

Beta strand

354 – 356

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 15, 1998. Version 1. Checksum: 0A8C21CEB36807FA	FASTA	445	48,945
	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
	Isoform 2 (Ribeye) [UniParc]. Checksum: 90EC841907295622	FASTA	985	106,187
	10 20 30 40 50 60 MPVPSRHINI GRSQSWDAAG WYEGPWENAE SLRPLGRRSS LTYGTAEGTW FEPNHRPQDA 70 80 90 100 110 120 ALPVAAEPYL YREAVYNSVA ARKGSTPDFT FYDSRQAVMS GRSPLLPREY YSDPSGAARV 130 140 150 160 170 180 PKEPPLYRDP GVSRPVPSYG VLGSRTSWDP MQGRSPALQD AGHLYRDPGG KMIPQGRQTQ 190 200 210 220 230 240 SRAASPGRYG REQPDTRYGA EVPAYPLSQV FSDISERPID PAPARQVAPT CLVVDPSSAA 250 260 270 280 290 300 APEGSTGVAP GALNRGYGPA RESIPSKMAY ETYEADLSTF QGPGGKRTVL PEFLAFLRAE 310 320 330 340 350 360 GLAEATLGAL LQQGFDSPAV LATLEDADIK SVAPNLGQAR VLSRLANSCR TEMQLRRQDR 370 380 390 400 410 420 GGPLPRARSS SFSHRSELLH GDLASLGAAA PLQTASPRAG DPARRPSSAP SQHLLETAAT 430 440 450 460 470 480 YSAPGVGTHA PHFPSNSGYS SPTPCALTAR LSPTYPLQAG VALTNPGPSN PLHPGPRTAY 490 500 510 520 530 540 STAYTVPMEL LKRERNVAAS PLPSPHGSPQ VLRKPGAPLG PSTLPPASQS LHTPHSPYQK 550 560 570 580 590 600 VARRTGAPII VSTMLAPEPS IRPQIMNGPL HPRPLVALLD GRDCTVEMPI LKDLATVAFC 610 620 630 640 650 660 DAQSTQEIHE KVLNEAVGAM MYHTITLTRE DLEKFKALRV IVRIGSGYDN VDIKAAGELG 670 680 690 700 710 720 IAVCNIPSAA VEETADSTIC HILNLYRRNT WLYQALREGT RVQSVEQIRE VASGAARIRG 730 740 750 760 770 780 ETLGLIGFGR TGQAVAVRAK AFGFSVIFYD PYLQDGIERS LGVQRVYTLQ DLLYQSDCVS 790 800 810 820 830 840 LHCNLNEHNH HLINDFTIKQ MRQGAFLVNA ARGGLVDEKA LAQALKEGRI RGAALDVHES 850 860 870 880 890 900 EPFSFAQGPL KDAPNLICTP HTAWYSEQAS LEMREAAATE IRRAITGRIP ESLRNCVNKE 910 920 930 940 950 960 FFVTSAPWSV IDQQAIHPEL NGATYRYPPG IVGVAPGGLP AAMEGIIPGG IPVTHNLPTV 970 980 AHPSQAPSPN QPTKHGDNRE HPNEQ

References

	« Hide 'large scale' referencesShow '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] [Europe PMC] [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] [Europe PMC] [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. , 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] [Europe PMC] [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] [Europe PMC] [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. , 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] [Europe PMC] [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. , 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].
[8]	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. , 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].
[9]	"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] (ISOFORM 1). Tissue: Colon, Kidney, Pancreas and Placenta.
[10]	"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: PROTEIN SEQUENCE OF 263-272, PHOSPHORYLATION. Tissue: B-cell and Cervix carcinoma.
[11]	"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: INTERACTION WITH PNN.
[12]	"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.
[13]	"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.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[15]	"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].
[16]	"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.

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.
CH471066 Genomic DNA. Translation: EAW49249.1.
BC002486 mRNA. Translation: AAH02486.1.
BC047018 mRNA. Translation: AAH47018.1.
BC052276 mRNA. Translation: AAH52276.1.
BC072020 mRNA. Translation: AAH72020.1.

RefSeq

NP_001077383.1. NM_001083914.1.
NP_001320.1. NM_001329.2.
NP_073713.2. NM_022802.2.
XP_005269618.1. XM_005269561.1.
XP_005269619.1. XM_005269562.1.
XP_005269620.1. XM_005269563.1.
XP_005269621.1. XM_005269564.1.
XP_005269622.1. XM_005269565.1.
XP_005269623.1. XM_005269566.1.
XP_005269624.1. XM_005269567.1.
XP_005269625.1. XM_005269568.1.
XP_005269626.1. XM_005269569.1.
XP_005269627.1. XM_005269570.1.
XP_005269628.1. XM_005269571.1.
XP_005269629.1. XM_005269572.1.

UniGene

Hs.501345.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2OME	X-ray	2.80	A/B/C/D/E/F/G/H	31-364	[»]

ProteinModelPortal

P56545.

SMR

P56545. Positions 33-362.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

107870. 66 interactions.

IntAct

P56545. 37 interactions.

MINT

MINT-1188878.

STRING

9606.ENSP00000311825.

Polymorphism databases

DMDM

3182976.

Proteomic databases

PaxDb

P56545.

PRIDE

P56545.

Protocols and materials databases

DNASU

1488.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000309035; ENSP00000311825; ENSG00000175029.
ENST00000337195; ENSP00000338615; ENSG00000175029.
ENST00000411419; ENSP00000410474; ENSG00000175029.
ENST00000494626; ENSP00000436285; ENSG00000175029.
ENST00000531469; ENSP00000434630; ENSG00000175029.

GeneID

1488.

KEGG

hsa:1488.

UCSC

uc001lif.4. human.

Organism-specific databases

CTD

1488.

GeneCards

GC10M126666.

HGNC

HGNC:2495. CTBP2.

HPA

CAB031916.
HPA023559.
HPA023564.
HPA044971.

MIM

602619. gene.

neXtProt

NX_P56545.

PharmGKB

PA26996.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0111.

HOVERGEN

HBG001898.

KO

K04496.

OrthoDB

EOG761BT9.

TreeFam

TF313593.

Enzyme and pathway databases

SignaLink

P56545.

Gene expression databases

ArrayExpress

P56545.

Bgee

P56545.

CleanEx

HS_CTBP2.

Genevestigator

P56545.

Family and domain databases

Gene3D

3.40.50.720. 2 hits.

InterPro

IPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR006140. D-isomer_2_OHA_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Pfam

PF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]

PROSITE

PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CTBP2. human.

EvolutionaryTrace

P56545.

GeneWiki

CTBP2.

GenomeRNAi

1488.

NextBio

6111.

PRO

P56545.

SOURCE

Search...

Entry information

Entry name

CTBP2_HUMAN

Accession

Primary (citable) accession number: P56545
Secondary accession number(s): A8K2X5 , D3DRF5, O43449, Q5SQP7, Q69YI3, Q86SV0, Q9H2T8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 15, 1998
Last modified:	February 19, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.