Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

C-terminal-binding protein 2

Gene

CTBP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Corepressor targeting diverse transcription regulators. Functions in brown adipose tissue (BAT) differentiation (By similarity).By similarity
Isoform 2 probably acts as a scaffold for specialized synapses.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei106 – 1061NADBy similarity
Binding sitei210 – 2101NAD1 Publication
Active sitei272 – 2721By similarity
Binding sitei296 – 2961NAD1 Publication
Active sitei301 – 3011By similarity
Active sitei321 – 3211Proton donorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi186 – 1916NAD1 Publication
Nucleotide bindingi243 – 2497NAD1 Publication
Nucleotide bindingi270 – 2723NAD1 Publication
Nucleotide bindingi321 – 3244NAD1 Publication

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. NAD binding Source: InterPro
  3. oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: InterPro
  4. transcription coactivator activity Source: Ensembl
  5. transcription corepressor activity Source: Ensembl

GO - Biological processi

  1. negative regulation of cell proliferation Source: ProtInc
  2. negative regulation of transcription, DNA-templated Source: UniProtKB
  3. positive regulation of chromatin binding Source: Ensembl
  4. positive regulation of retinoic acid receptor signaling pathway Source: MGI
  5. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  6. transcription, DNA-templated Source: UniProtKB-KW
  7. viral genome replication Source: ProtInc
  8. white fat cell differentiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Repressor

Keywords - Biological processi

Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiREACT_264499. TCF7L2 mutants don't bind CTBP.
REACT_264567. repression of WNT target genes.
SignaLinkiP56545.

Names & Taxonomyi

Protein namesi
Recommended name:
C-terminal-binding protein 2
Short name:
CtBP2
Gene namesi
Name:CTBP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:2495. CTBP2.

Subcellular locationi

  1. Nucleus Curated
  2. Cell junctionsynapse By similarity

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. nucleus Source: UniProtKB
  3. synapse Source: UniProtKB-SubCell
  4. transcriptional repressor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Nucleus, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26996.

Polymorphism and mutation databases

BioMutaiCTBP2.
DMDMi3182976.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 445445C-terminal-binding protein 2PRO_0000076044Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei428 – 4281Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP56545.
PaxDbiP56545.
PRIDEiP56545.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP56545.
CleanExiHS_CTBP2.
ExpressionAtlasiP56545. baseline and differential.
GenevestigatoriP56545.

Organism-specific databases

HPAiCAB031916.
HPA023559.
HPA023564.
HPA044971.

Interactioni

Subunit structurei

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.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BCL3P207492EBI-741533,EBI-958997
CCNHP519465EBI-741533,EBI-741406
CTBP1Q13363-23EBI-741533,EBI-10171858
FOXP2O154093EBI-741533,EBI-983612
FUNDC1Q8IVP53EBI-741533,EBI-3059266
HIC1Q145262EBI-741533,EBI-2507362
IKZF1Q134225EBI-741533,EBI-745305
IKZF2Q9UKS73EBI-741533,EBI-3893057
LCORQ96JN03EBI-741533,EBI-8833163
NOL4O94818-23EBI-741533,EBI-10190763
NOL4LQ96MY13EBI-741533,EBI-6660790
PLCB1Q9NQ663EBI-741533,EBI-3396023
PPP1R15AO758072EBI-741533,EBI-714746
PROX1Q927862EBI-741533,EBI-3912635
RAI2Q9Y5P34EBI-741533,EBI-746228
SOX13Q9UN792EBI-741533,EBI-3928516
TGIF1Q155835EBI-741533,EBI-714215
Zbp1A2APF72EBI-741533,EBI-6115394From a different organism.
ZNF750Q32MQ03EBI-741533,EBI-10240029

Protein-protein interaction databases

BioGridi107870. 90 interactions.
IntActiP56545. 44 interactions.
MINTiMINT-1188878.
STRINGi9606.ENSP00000311825.

Structurei

Secondary structure

1
445
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi35 – 384Combined sources
Helixi47 – 515Combined sources
Turni52 – 543Combined sources
Beta strandi56 – 594Combined sources
Helixi65 – 673Combined sources
Helixi70 – 756Combined sources
Beta strandi76 – 816Combined sources
Beta strandi83 – 853Combined sources
Helixi89 – 935Combined sources
Beta strandi100 – 1067Combined sources
Helixi113 – 1186Combined sources
Beta strandi122 – 1243Combined sources
Beta strandi128 – 1303Combined sources
Helixi131 – 14717Combined sources
Helixi149 – 1579Combined sources
Helixi165 – 1717Combined sources
Turni172 – 1743Combined sources
Beta strandi182 – 1865Combined sources
Helixi190 – 19910Combined sources
Helixi200 – 2023Combined sources
Beta strandi205 – 2095Combined sources
Helixi217 – 2204Combined sources
Helixi229 – 2357Combined sources
Beta strandi237 – 2415Combined sources
Helixi255 – 2584Combined sources
Beta strandi265 – 2695Combined sources
Helixi273 – 2753Combined sources
Helixi278 – 2869Combined sources
Beta strandi289 – 2968Combined sources
Beta strandi299 – 3024Combined sources
Turni309 – 3124Combined sources
Beta strandi314 – 3185Combined sources
Helixi327 – 34620Combined sources
Turni349 – 3524Combined sources
Beta strandi354 – 3563Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OMEX-ray2.80A/B/C/D/E/F/G/H31-364[»]
4LCJX-ray2.86A/B/C/D/E/F/G/H31-362[»]
ProteinModelPortaliP56545.
SMRiP56545. Positions 33-362.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP56545.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0111.
GeneTreeiENSGT00530000063021.
HOVERGENiHBG001898.
InParanoidiP56545.
KOiK04496.
OrthoDBiEOG761BT9.
PhylomeDBiP56545.
TreeFamiTF313593.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR006140. D-isomer_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
PROSITEiPS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P56545-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MALVDKHKVK RQRLDRICEG IRPQIMNGPL HPRPLVALLD GRDCTVEMPI
60 70 80 90 100
LKDLATVAFC DAQSTQEIHE KVLNEAVGAM MYHTITLTRE DLEKFKALRV
110 120 130 140 150
IVRIGSGYDN VDIKAAGELG IAVCNIPSAA VEETADSTIC HILNLYRRNT
160 170 180 190 200
WLYQALREGT RVQSVEQIRE VASGAARIRG ETLGLIGFGR TGQAVAVRAK
210 220 230 240 250
AFGFSVIFYD PYLQDGIERS LGVQRVYTLQ DLLYQSDCVS LHCNLNEHNH
260 270 280 290 300
HLINDFTIKQ MRQGAFLVNA ARGGLVDEKA LAQALKEGRI RGAALDVHES
310 320 330 340 350
EPFSFAQGPL KDAPNLICTP HTAWYSEQAS LEMREAAATE IRRAITGRIP
360 370 380 390 400
ESLRNCVNKE FFVTSAPWSV IDQQAIHPEL NGATYRYPPG IVGVAPGGLP
410 420 430 440
AAMEGIIPGG IPVTHNLPTV AHPSQAPSPN QPTKHGDNRE HPNEQ
Length:445
Mass (Da):48,945
Last modified:July 15, 1998 - v1
Checksum:i0A8C21CEB36807FA
GO
Isoform 2 (identifier: P56545-2) [UniParc]FASTAAdd to basket

Also known as: Ribeye

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MALVDKHKVKRQRLDRICEG → MPVPSRHINI...VSTMLAPEPS

Show »
Length:985
Mass (Da):106,187
Checksum:i90EC841907295622
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 871L → F in AAG45951 (PubMed:11163272).Curated
Sequence conflicti88 – 881T → N in AAG45951 (PubMed:11163272).Curated
Sequence conflicti112 – 1121D → N in AAG45951 (PubMed:11163272).Curated
Sequence conflicti411 – 4111I → T in AAH47018 (PubMed:15489334).Curated
Isoform 2 (identifier: P56545-2)
Sequence conflicti455 – 4551Y → H in AAG45951 (PubMed:11163272).Curated
Sequence conflicti539 – 5391Q → E in AAG45951 (PubMed:11163272).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti47 – 471E → D.
Corresponds to variant rs3198926 [ dbSNP | Ensembl ].
VAR_033844

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 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. 1 PublicationVSP_027615Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS7643.1. [P56545-1]
CCDS7644.1. [P56545-2]
RefSeqiNP_001077383.1. NM_001083914.1. [P56545-1]
NP_001277143.1. NM_001290214.1. [P56545-1]
NP_001277144.1. NM_001290215.1. [P56545-1]
NP_001320.1. NM_001329.2. [P56545-1]
NP_073713.2. NM_022802.2. [P56545-2]
XP_005269618.1. XM_005269561.2. [P56545-1]
XP_005269621.1. XM_005269564.2. [P56545-1]
XP_005269622.1. XM_005269565.2. [P56545-1]
XP_005269624.1. XM_005269567.2. [P56545-1]
XP_005269625.1. XM_005269568.3. [P56545-1]
XP_005269626.1. XM_005269569.2. [P56545-1]
XP_005269627.1. XM_005269570.2. [P56545-1]
XP_005269628.1. XM_005269571.2. [P56545-1]
XP_005269629.1. XM_005269572.3. [P56545-1]
XP_006717704.1. XM_006717641.2. [P56545-1]
XP_006717705.1. XM_006717642.2. [P56545-1]
XP_006717706.1. XM_006717643.2. [P56545-1]
UniGeneiHs.501345.

Genome annotation databases

EnsembliENST00000309035; ENSP00000311825; ENSG00000175029. [P56545-2]
ENST00000337195; ENSP00000338615; ENSG00000175029. [P56545-1]
ENST00000411419; ENSP00000410474; ENSG00000175029. [P56545-1]
ENST00000494626; ENSP00000436285; ENSG00000175029. [P56545-1]
ENST00000531469; ENSP00000434630; ENSG00000175029. [P56545-1]
GeneIDi1488.
KEGGihsa:1488.
UCSCiuc001lie.4. human. [P56545-2]
uc001lif.4. human. [P56545-1]

Polymorphism and mutation databases

BioMutaiCTBP2.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS7643.1. [P56545-1]
CCDS7644.1. [P56545-2]
RefSeqiNP_001077383.1. NM_001083914.1. [P56545-1]
NP_001277143.1. NM_001290214.1. [P56545-1]
NP_001277144.1. NM_001290215.1. [P56545-1]
NP_001320.1. NM_001329.2. [P56545-1]
NP_073713.2. NM_022802.2. [P56545-2]
XP_005269618.1. XM_005269561.2. [P56545-1]
XP_005269621.1. XM_005269564.2. [P56545-1]
XP_005269622.1. XM_005269565.2. [P56545-1]
XP_005269624.1. XM_005269567.2. [P56545-1]
XP_005269625.1. XM_005269568.3. [P56545-1]
XP_005269626.1. XM_005269569.2. [P56545-1]
XP_005269627.1. XM_005269570.2. [P56545-1]
XP_005269628.1. XM_005269571.2. [P56545-1]
XP_005269629.1. XM_005269572.3. [P56545-1]
XP_006717704.1. XM_006717641.2. [P56545-1]
XP_006717705.1. XM_006717642.2. [P56545-1]
XP_006717706.1. XM_006717643.2. [P56545-1]
UniGeneiHs.501345.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OMEX-ray2.80A/B/C/D/E/F/G/H31-364[»]
4LCJX-ray2.86A/B/C/D/E/F/G/H31-362[»]
ProteinModelPortaliP56545.
SMRiP56545. Positions 33-362.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107870. 90 interactions.
IntActiP56545. 44 interactions.
MINTiMINT-1188878.
STRINGi9606.ENSP00000311825.

Polymorphism and mutation databases

BioMutaiCTBP2.
DMDMi3182976.

Proteomic databases

MaxQBiP56545.
PaxDbiP56545.
PRIDEiP56545.

Protocols and materials databases

DNASUi1488.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000309035; ENSP00000311825; ENSG00000175029. [P56545-2]
ENST00000337195; ENSP00000338615; ENSG00000175029. [P56545-1]
ENST00000411419; ENSP00000410474; ENSG00000175029. [P56545-1]
ENST00000494626; ENSP00000436285; ENSG00000175029. [P56545-1]
ENST00000531469; ENSP00000434630; ENSG00000175029. [P56545-1]
GeneIDi1488.
KEGGihsa:1488.
UCSCiuc001lie.4. human. [P56545-2]
uc001lif.4. human. [P56545-1]

Organism-specific databases

CTDi1488.
GeneCardsiGC10M126666.
HGNCiHGNC:2495. CTBP2.
HPAiCAB031916.
HPA023559.
HPA023564.
HPA044971.
MIMi602619. gene.
neXtProtiNX_P56545.
PharmGKBiPA26996.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0111.
GeneTreeiENSGT00530000063021.
HOVERGENiHBG001898.
InParanoidiP56545.
KOiK04496.
OrthoDBiEOG761BT9.
PhylomeDBiP56545.
TreeFamiTF313593.

Enzyme and pathway databases

ReactomeiREACT_264499. TCF7L2 mutants don't bind CTBP.
REACT_264567. repression of WNT target genes.
SignaLinkiP56545.

Miscellaneous databases

ChiTaRSiCTBP2. human.
EvolutionaryTraceiP56545.
GeneWikiiCTBP2.
GenomeRNAii1488.
NextBioi6111.
PROiP56545.
SOURCEiSearch...

Gene expression databases

BgeeiP56545.
CleanExiHS_CTBP2.
ExpressionAtlasiP56545. baseline and differential.
GenevestigatoriP56545.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR006140. D-isomer_DH_NAD-bd.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
PROSITEiPS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "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.

Entry informationi

Entry nameiCTBP2_HUMAN
AccessioniPrimary (citable) accession number: P56545
Secondary accession number(s): A8K2X5
, D3DRF5, O43449, Q5SQP7, Q69YI3, Q86SV0, Q9H2T8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: April 29, 2015
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.