Q13363 (CTBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
C-terminal-binding protein 1
Short name=CtBP1
EC=1.1.1.-

Gene names

Name:	CTBP1
Synonyms:	CTBP

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	440 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Functions in brown adipose tissue (BAT) differentiation. Corepressor targeting diverse transcription regulators such as GLIS2. Has dehydrogenase activity. Ref.2 Ref.13 Ref.20 Ref.22
Cofactor	NAD. Required for efficient interaction with E1A. Cofactor binding induces a conformation change. Ref.22
Subunit structure	Interacts with the C-terminus of adenovirus E1A protein, ELK3 and CTIP via their consensus motif P-X-[DNS]-L-[STVA]. Can form homodimers or heterodimers of CTBP1 and CTBP2. Interacts with FOXP2, HDAC4, HDAC5 and HDAC9. Interacts with GLIS2 but not GLIS1 or GLIS3. Interacts with PRDM16; represses white adipose tissue (WAT)-specific genes expression By similarity. Interacts with FOXP1, HIPK2, PNN and NRIP1. Interacts with ZFHX1B and WIZ. Interacts with Epstein-Barr virus EBNA3 and EBNA6. Interaction with non acetylated SATB1 stabalizes its attachment to DNA and promotes transcription repression. Interacts with MECOM. 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.20 Ref.22
Subcellular location	Cytoplasm. Nucleus Ref.11.
Post-translational modification	The level of phosphorylation appears to be regulated during the cell cycle. Phosphorylated upon DNA damage, probably by ATM or ATR. Phosphorylation by HIPK2 on Ser-422 induces proteasomal degradation. Ref.6 Ref.12 Ref.19 ADP-ribosylated; when cells are exposed to brefeldin A By similarity. Sumoylation on Lys-428 is promoted by the E3 SUMO-protein ligase CBX4.
Sequence similarities	Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.

Ontologies

Keywords
Biological process	Differentiation Host-virus interaction Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Ligand	NAD
Molecular function	Oxidoreductase Repressor
PTM	ADP-ribosylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Uncategorized	regulation of transcription from RNA polymerase II promoter by nuclear hormone receptor Inferred from mutant phenotype. Source: BHF-UCL
Biological process	interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cell proliferation Traceable author statement. Source: ProtInc negative regulation of histone H4 acetylation Inferred from mutant phenotype. Source: BHF-UCL negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: BHF-UCL positive regulation of histone deacetylation Inferred from mutant phenotype. Source: BHF-UCL protein phosphorylation Traceable author statement. Source: ProtInc regulation of cell cycle Inferred from mutant phenotype. Source: BHF-UCL regulation of transcription by chromatin organization Inferred from mutant phenotype. Source: BHF-UCL transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW viral genome replication Traceable author statement. Source: ProtInc white fat cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell transcriptional repressor complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	NAD binding Inferred from sequence or structural similarity. Source: UniProtKB 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. Source: ProtInc protein domain specific binding Inferred from physical interaction. Source: UniProtKB transcription factor binding Inferred from physical interaction Ref.17. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HEMGN	Q9BXL5	2	EBI-908846,EBI-3916399
HIC1	Q14526	4	EBI-908846,EBI-2507362
THAP11	Q96EK4	2	EBI-908846,EBI-1790529

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 440

440

C-terminal-binding protein 1

PRO_0000076041

Regions

Nucleotide binding

180 – 185

6

NAD By similarity

Nucleotide binding

237 – 243

7

NAD By similarity

Nucleotide binding

264 – 266

3

NAD By similarity

Nucleotide binding

315 – 318

4

NAD By similarity

Region

1 – 70

70

Interaction with GLIS2 1 By similarity

Region

288 – 360

73

Interaction with GLIS2 2 By similarity

Sites

Active site

266

1

By similarity

Active site

295

1

By similarity

Active site

315

1

Proton donor By similarity

Binding site

100

1

NAD By similarity

Binding site

204

1

NAD By similarity

Binding site

290

1

NAD By similarity

Amino acid modifications

Modified residue

300

1

Phosphoserine Ref.19

Modified residue

422

1

Phosphoserine; by HIPK2 Ref.12

Cross-link

428

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.11

Experimental info

Mutagenesis

134

1

C → A: Strongly reduces E1A binding; when associated with A-138; A-141 and A-150. Ref.22

Mutagenesis

138

1

N → A: Strongly reduces E1A binding; when associated with A-134; A-141 and A-150. Ref.22

Mutagenesis

141 – 142

2

RR → AA: Strongly reduces E1A binding; when associated with A-163 and A-171. Ref.22

Mutagenesis

141

1

R → A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-150. Ref.22

Mutagenesis

150

1

L → A: Strongly reduces E1A binding; when associated with A-134; A-138 and A-141. Ref.22

Mutagenesis

163

1

R → A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-171. Ref.22

Mutagenesis

171

1

R → A: Strongly reduces E1A binding; when associated with A-141; A-142 and A-163. Ref.22

Mutagenesis

181

1

G → V: Strongly reduces E1A binding; when associated with V-183 and A-204. Ref.22

Mutagenesis

183

1

G → V: Strongly reduces E1A binding; when associated with V-181 and A-204. Ref.22

Mutagenesis

204

1

D → A: Strongly reduces E1A binding; when associated with V-181 and V-183. Ref.22

Mutagenesis

266

1

R → A: Strongly reduces E1A binding; when associated with A-290; A-295 and A-315. Ref.22

Mutagenesis

290

1

D → A: Strongly reduces E1A binding; when associated with A-266; A-295 and A-315. Ref.22

Mutagenesis

295

1

E → A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-315. Ref.22

Mutagenesis

315

1

H → A: Strongly reduces E1A binding; when associated with A-266; A-290 and A-295. Ref.22

Mutagenesis

422

1

S → A: Abolishes phosphorylation by HIPK2 and prevents UV-induced clearance. Ref.12

Secondary structure

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440

Helix Strand Turn

Details...

Beta strand

29 – 34

6

Turn

39 – 41

3

Helix

42 – 45

4

Turn

46 – 48

3

Beta strand

50 – 53

4

Helix

59 – 61

3

Helix

64 – 69

6

Beta strand

70 – 75

6

Beta strand

77 – 79

3

Helix

83 – 86

4

Beta strand

94 – 100

7

Helix

107 – 112

6

Beta strand

116 – 118

3

Helix

125 – 141

17

Helix

143 – 151

9

Helix

159 – 165

7

Turn

166 – 168

3

Beta strand

176 – 180

5

Helix

184 – 194

11

Turn

195 – 197

3

Beta strand

199 – 203

5

Helix

211 – 215

5

Helix

223 – 229

7

Beta strand

231 – 235

5

Beta strand

246 – 248

3

Helix

249 – 252

4

Beta strand

259 – 263

5

Helix

272 – 280

9

Beta strand

283 – 290

8

Beta strand

293 – 296

4

Turn

303 – 306

4

Beta strand

308 – 312

5

Helix

321 – 340

20

Turn

343 – 346

4

Beta strand

348 – 350

3

Sequences

	Sequence		Length	Mass (Da)
	Q13363 [UniParc]. Last modified July 15, 1999. Version 2. Checksum: F071DD30B385603F	FASTA	440	47,535
	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

References

	« Hide 'large scale' referencesShow '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: 7479821] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 98-108, INTERACTION WITH 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: 9858600] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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. , 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: 15815621] [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. , 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[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: 8440238] [Abstract] Cited for: INTERACTION WITH 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: 11568182] [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: 11462050] [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: 11509661] [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: 12372828] [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: 12679040] [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: 14567915] [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: 15542832] [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: 15060175] [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: 16061479] [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: 15897867] [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: 16609867] [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: 16702210] [Abstract] Cited for: INTERACTION WITH WIZ.
[19]	"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 SER-300, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[20]	"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: 19103759] [Abstract] Cited for: FUNCTION, INTERACTION WITH SATB1.
[21]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]	"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: 12419229] [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: EAW82601.1.
BC011655 mRNA. Translation: AAH11655.1.

IPI

IPI00012835.

RefSeq

NP_001012632.1. NM_001012614.1.
NP_001319.1. NM_001328.2.

UniGene

Hs.208597.
Hs.594321.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MX3	X-ray	1.95	A	28-353	[»]

ProteinModelPortal

Q13363.

SMR

Q13363. Positions 28-352.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24245N.

IntAct

Q13363. 10 interactions.

MINT

MINT-94454.

STRING

Q13363.

PTM databases

PhosphoSite

Q13363.

Polymorphism databases

DMDM

6014741.

Proteomic databases

PRIDE

Q13363.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000290921; ENSP00000290921; ENSG00000159692.

GeneID

1487.

KEGG

hsa:1487.

UCSC

uc003gcv.1. human.

Organism-specific databases

CTD

1487.

GeneCards

GC04M001205.

HGNC

HGNC:2494. CTBP1.

HPA

CAB004217.
HPA018987.

MIM

602618. gene.

neXtProt

NX_Q13363.

PharmGKB

PA26995.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG15622.

HOGENOM

HBG731446.

HOVERGEN

HBG001898.

InParanoid

Q13363.

OMA

PIMNGPM.

OrthoDB

EOG4HHP2H.

PhylomeDB

Q13363.

Enzyme and pathway databases

Pathway_Interaction_DB

wnt_canonical_pathway. Canonical Wnt signaling pathway.
ps1pathway. Presenilin action in Notch and Wnt signaling.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.

Gene expression databases

ArrayExpress

Q13363.

Bgee

Q13363.

CleanEx

HS_CTBP1.

Genevestigator

Q13363.

GermOnline

ENSG00000159692. Homo sapiens.

Family and domain databases

InterPro

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

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 2 hits.

KO

K04496.

Pfam

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

PROSITE

PS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00670. D_2_HYDROXYACID_DH_2. False negative.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

6105.

SOURCE

Search...

Entry information

Entry name

CTBP1_HUMAN

Accession

Primary (citable) accession number: Q13363
Secondary accession number(s): Q4W5N3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 15, 1999
Last modified:	January 25, 2012
This is version 132 of the entry and version 2 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.