Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P56545

- CTBP2_HUMAN

UniProt

P56545 - CTBP2_HUMAN

Protein

C-terminal-binding protein 2

Gene

CTBP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (15 Jul 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. NAD binding Source: InterPro
    2. oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: InterPro
    3. protein binding Source: IntAct
    4. 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. transcription, DNA-templated Source: UniProtKB-KW
    4. viral genome replication Source: ProtInc
    5. white fat cell differentiation Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase, Repressor

    Keywords - Biological processi

    Differentiation, Transcription, Transcription regulation

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    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: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:2495. CTBP2.

    Subcellular locationi

    Nucleus Curated. 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

    Keywords - Cellular componenti

    Cell junction, Nucleus, Synapse

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26996.

    PTM / Processingi

    Molecule processing

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

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP56545.
    PaxDbiP56545.
    PRIDEiP56545.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP56545.
    BgeeiP56545.
    CleanExiHS_CTBP2.
    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
    HIC1Q145262EBI-741533,EBI-2507362
    PPP1R15AO758072EBI-741533,EBI-714746
    PROX1Q927862EBI-741533,EBI-3912635
    SOX13Q9UN792EBI-741533,EBI-3928516
    Zbp1A2APF72EBI-741533,EBI-6115394From a different organism.

    Protein-protein interaction databases

    BioGridi107870. 72 interactions.
    IntActiP56545. 37 interactions.
    MINTiMINT-1188878.
    STRINGi9606.ENSP00000311825.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOVERGENiHBG001898.
    KOiK04496.
    OrthoDBiEOG761BT9.
    PhylomeDBiP56545.
    TreeFamiTF313593.

    Family and domain databases

    Gene3Di3.40.50.720. 2 hits.
    InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
    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. Align

    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

    MALVDKHKVK RQRLDRICEG IRPQIMNGPL HPRPLVALLD GRDCTVEMPI    50
    LKDLATVAFC DAQSTQEIHE KVLNEAVGAM MYHTITLTRE DLEKFKALRV 100
    IVRIGSGYDN VDIKAAGELG IAVCNIPSAA VEETADSTIC HILNLYRRNT 150
    WLYQALREGT RVQSVEQIRE VASGAARIRG ETLGLIGFGR TGQAVAVRAK 200
    AFGFSVIFYD PYLQDGIERS LGVQRVYTLQ DLLYQSDCVS LHCNLNEHNH 250
    HLINDFTIKQ MRQGAFLVNA ARGGLVDEKA LAQALKEGRI RGAALDVHES 300
    EPFSFAQGPL KDAPNLICTP HTAWYSEQAS LEMREAAATE IRRAITGRIP 350
    ESLRNCVNKE FFVTSAPWSV IDQQAIHPEL NGATYRYPPG IVGVAPGGLP 400
    AAMEGIIPGG IPVTHNLPTV AHPSQAPSPN QPTKHGDNRE HPNEQ 445
    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:
    EMBL
    GenBank
    DDBJ
    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_005269561.1. [P56545-1]
    XP_005269619.1. XM_005269562.2. [P56545-1]
    XP_005269621.1. XM_005269564.1. [P56545-1]
    XP_005269622.1. XM_005269565.1. [P56545-1]
    XP_005269624.1. XM_005269567.1. [P56545-1]
    XP_005269625.1. XM_005269568.2. [P56545-1]
    XP_005269626.1. XM_005269569.1. [P56545-1]
    XP_005269627.1. XM_005269570.1. [P56545-1]
    XP_005269628.1. XM_005269571.1. [P56545-1]
    XP_005269629.1. XM_005269572.2. [P56545-1]
    XP_006717704.1. XM_006717641.1. [P56545-1]
    XP_006717705.1. XM_006717642.1. [P56545-1]
    XP_006717706.1. XM_006717643.1. [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 databases

    DMDMi3182976.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS7643.1. [P56545-1 ]
    CCDS7644.1. [P56545-2 ]
    RefSeqi NP_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_005269561.1. [P56545-1 ]
    XP_005269619.1. XM_005269562.2. [P56545-1 ]
    XP_005269621.1. XM_005269564.1. [P56545-1 ]
    XP_005269622.1. XM_005269565.1. [P56545-1 ]
    XP_005269624.1. XM_005269567.1. [P56545-1 ]
    XP_005269625.1. XM_005269568.2. [P56545-1 ]
    XP_005269626.1. XM_005269569.1. [P56545-1 ]
    XP_005269627.1. XM_005269570.1. [P56545-1 ]
    XP_005269628.1. XM_005269571.1. [P56545-1 ]
    XP_005269629.1. XM_005269572.2. [P56545-1 ]
    XP_006717704.1. XM_006717641.1. [P56545-1 ]
    XP_006717705.1. XM_006717642.1. [P56545-1 ]
    XP_006717706.1. XM_006717643.1. [P56545-1 ]
    UniGenei Hs.501345.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2OME X-ray 2.80 A/B/C/D/E/F/G/H 31-364 [» ]
    4LCJ X-ray 2.86 A/B/C/D/E/F/G/H 31-362 [» ]
    ProteinModelPortali P56545.
    SMRi P56545. Positions 33-362.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107870. 72 interactions.
    IntActi P56545. 37 interactions.
    MINTi MINT-1188878.
    STRINGi 9606.ENSP00000311825.

    Polymorphism databases

    DMDMi 3182976.

    Proteomic databases

    MaxQBi P56545.
    PaxDbi P56545.
    PRIDEi P56545.

    Protocols and materials databases

    DNASUi 1488.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000309035 ; ENSP00000311825 ; ENSG00000175029 . [P56545-2 ]
    ENST00000337195 ; ENSP00000338615 ; ENSG00000175029 . [P56545-1 ]
    ENST00000411419 ; ENSP00000410474 ; ENSG00000175029 . [P56545-1 ]
    ENST00000494626 ; ENSP00000436285 ; ENSG00000175029 . [P56545-1 ]
    ENST00000531469 ; ENSP00000434630 ; ENSG00000175029 . [P56545-1 ]
    GeneIDi 1488.
    KEGGi hsa:1488.
    UCSCi uc001lie.4. human. [P56545-2 ]
    uc001lif.4. human. [P56545-1 ]

    Organism-specific databases

    CTDi 1488.
    GeneCardsi GC10M126666.
    HGNCi HGNC:2495. CTBP2.
    HPAi CAB031916.
    HPA023559.
    HPA023564.
    HPA044971.
    MIMi 602619. gene.
    neXtProti NX_P56545.
    PharmGKBi PA26996.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0111.
    HOVERGENi HBG001898.
    KOi K04496.
    OrthoDBi EOG761BT9.
    PhylomeDBi P56545.
    TreeFami TF313593.

    Enzyme and pathway databases

    SignaLinki P56545.

    Miscellaneous databases

    ChiTaRSi CTBP2. human.
    EvolutionaryTracei P56545.
    GeneWikii CTBP2.
    GenomeRNAii 1488.
    NextBioi 6111.
    PROi P56545.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P56545.
    Bgeei P56545.
    CleanExi HS_CTBP2.
    Genevestigatori P56545.

    Family and domain databases

    Gene3Di 3.40.50.720. 2 hits.
    InterProi IPR006139. D-isomer_2_OHA_DH_cat_dom.
    IPR006140. D-isomer_DH_NAD-bd.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF00389. 2-Hacid_dh. 1 hit.
    PF02826. 2-Hacid_dh_C. 1 hit.
    [Graphical view ]
    PROSITEi PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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: October 1, 2014
    This is version 144 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