Reviewed, UniProtKB/Swiss-Prot P56545 (CTBP2_HUMAN)

Names and origin

Protein names

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

Gene names

Name:

CTBP2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	445 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Corepressor targeting diverse transcription regulators. Isoform 2 probably acts as a scaffold for specialized synapses By similarity.
Subunit structure	Interacts with the C-terminus of adenovirus E1A protein. Can form homodimers or heterodimers of CTBP1 and CTBP2. Interacts with HIPK2 By similarity. Interacts with PNN, NRIP1 and WIZ.
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.
Sequence similarities	Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.

Ontologies

Keywords
Cellular component	Cell junction Nucleus Synapse
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	negative regulation of cell proliferation Ref.1 Traceable author statement. Source: ProtInc oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW viral genome replication Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cell junction Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell synapse Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NAD 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
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
	Sequence conflict	455	1	Y → H in AAG45951. Ref.2
	Sequence conflict	539	1	Q → E in AAG45951. Ref.2

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

Sites

Active site

272

1

Potential

Active site

301

1

Potential

Active site

321

1

Potential

Amino acid modifications

Modified residue

428

1

Phosphoserine By similarity

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: dbSNP rs3198926.

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.8

Secondary structure

1

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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). 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: 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. , 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., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder 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. , 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. , 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00010120.
IPI00010136.

RefSeq

NP_001077383.1.
NP_001320.1.
NP_073713.2.

UniGene

Hs.501345

3D structure databases

PDBPDBe

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

ModBase

Search...

Protein-protein interaction databases

IntAct

P56545. 7 interactions.

Proteomic databases

PRIDE

P56545.

Genome annotation databases

Ensembl

ENSG00000175029. Homo sapiens. [Contig view]

GeneID

1488.

KEGG

hsa:1488.

UCSC

uc001lie.2. human.
uc001lif.2. human.

Organism-specific databases

GeneCards

GC10M126666.

H-InvDB

HIX0009290.

HGNC

HGNC:2495. CTBP2.

MIM

602619. gene.

PharmGKB

PA24460.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P56545.

OMA

P56545. GHLYRDP.

Gene expression databases

Bgee

P56545.

CleanEx

HS_CTBP2.

GermOnline

ENSG00000175029. Homo sapiens.

Family and domain databases

InterPro

IPR006139. D-isomer_2_OHA_DH.
IPR006140. D-isomer_2_OHA_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

Pfam

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

PROSITE

PS00065. 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]

ProtoNet

Search...

Other Resources

NextBio

6111.

SOURCE

Search...

Entry information

Entry name

CTBP2_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 15, 1998
Last modified:	July 7, 2009
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)