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O88712

- CTBP1_MOUSE

UniProt

O88712 - CTBP1_MOUSE

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Protein

C-terminal-binding protein 1

Gene

Ctbp1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Corepressor targeting diverse transcription regulators such as GLIS2 or BCL6. Has dehydrogenase activity. Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Functions in brown adipose tissue (BAT) differentiation.5 Publications

Cofactori

NAD(+)By similarityNote: Cofactor binding induces a conformational change.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei100 – 1001NADBy similarity
Binding sitei204 – 2041NADBy similarity
Active sitei266 – 2661By similarity
Binding sitei290 – 2901NADBy similarity
Active sitei295 – 2951By similarity
Active sitei315 – 3151Proton donorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi180 – 1856NADBy similarity
Nucleotide bindingi237 – 2437NADBy similarity
Nucleotide bindingi264 – 2663NADBy similarity
Nucleotide bindingi315 – 3184NADBy similarity

GO - Molecular functioni

  1. NAD binding Source: UniProtKB
  2. oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Source: InterPro
  3. RNA polymerase II transcription corepressor activity Source: Ensembl
  4. sequence-specific DNA binding transcription factor activity Source: MGI
  5. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. Golgi organization Source: Ensembl
  2. negative regulation of histone H4 acetylation Source: Ensembl
  3. negative regulation of transcription, DNA-templated Source: UniProtKB
  4. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  5. positive regulation of histone deacetylation Source: Ensembl
  6. regulation of cell cycle Source: Ensembl
  7. regulation of transcription by chromatin organization Source: Ensembl
  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_219771. deactivation of the beta-catenin transactivating complex.
REACT_233471. repression of WNT target genes.
REACT_254498. TCF7L2 mutants don't bind CTBP.

Names & Taxonomyi

Protein namesi
Recommended name:
C-terminal-binding protein 1 (EC:1.1.1.-)
Short name:
CtBP1
Gene namesi
Name:Ctbp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1201685. Ctbp1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. nucleus Source: UniProtKB
  3. transcriptional repressor complex Source: UniProtKB
  4. transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 441441C-terminal-binding protein 1PRO_0000076042Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei300 – 3001PhosphoserineBy similarity
Modified residuei423 – 4231PhosphoserineBy similarity
Cross-linki429 – 429Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Post-translational modificationi

ADP-ribosylated; when cells are exposed to brefeldin A.By similarity
The level of phosphorylation appears to be regulated during the cell cycle. Phosphorylation by HIPK2 on Ser-423 induces proteasomal degradation (By similarity).By similarity
Sumoylation on Lys-429 is promoted by the E3 SUMO-protein ligase CBX4.By similarity

Keywords - PTMi

ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO88712.
PaxDbiO88712.
PRIDEiO88712.

PTM databases

PhosphoSiteiO88712.

Expressioni

Tissue specificityi

Expressed in a wide range of adult tissues.1 Publication

Developmental stagei

Expressed throughout the developmental stages.1 Publication

Gene expression databases

BgeeiO88712.
CleanExiMM_CTBP1.
GenevestigatoriO88712.

Interactioni

Subunit structurei

Homo- or heterodimer. Heterodimer with CTBP2. Interacts with ELK3 (via its PXDLS motif). Interacts with RBBP8 (via its PXDLS motif). Interacts with PNN, MECOM, ZNF366 and ZFHX1B. Interaction with SATB1 (non-acetylated form); the interaction stabilizes its attachment to DNA and promotes transcription repression. Interacts with PRDM16; the interaction represses white adipose tissue (WAT)-specific genes expression. Interacts with GLIS2, HIPK2, FOXP1, FOXP2, HDAC4, HDAC5, HDAC9, NRIP1, WIZ and ZNF217. Interacts with BCL6; the interaction is required for BCL6 transcriptional autoinhibition and inhibition of some BCL6 target genes.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HIC1Q1452610EBI-604547,EBI-2507362From a different organism.
Zeb1Q643184EBI-604547,EBI-8560245

Protein-protein interaction databases

BioGridi198961. 13 interactions.
DIPiDIP-33907N.
IntActiO88712. 10 interactions.
MINTiMINT-146962.

Structurei

3D structure databases

ProteinModelPortaliO88712.
SMRiO88712. Positions 26-356.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 7070Interaction with GLIS2 1Add
BLAST
Regioni288 – 36073Interaction with GLIS2 2Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0111.
GeneTreeiENSGT00530000063021.
HOVERGENiHBG001898.
InParanoidiO88712.
KOiK04496.
OMAiDRDHPSD.
OrthoDBiEOG761BT9.
PhylomeDBiO88712.
TreeFamiTF313593.

Family and domain databases

Gene3Di3.40.50.720. 2 hits.
InterProiIPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR029752. D-isomer_DH_CS1.
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]
PROSITEiPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O88712-1) [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
MGSSHLLNKG LPLGVRPPIM NGPMHPRPLV ALLDGRDCTV EMPILKDVAT
60 70 80 90 100
VAFCDAQSTQ EIHEKVLNEA VGALMYHTIT LTREDLEKFK ALRIIVRIGS
110 120 130 140 150
GFDNIDIKSA GDLGIAVCNV PAASVEETAD STLCHILNLY RRTTWLHQAL
160 170 180 190 200
REGTRVQSVE QIREVASGAA RIRGETLGII GLGRVGQAVA LRAKAFGFNV
210 220 230 240 250
LFYDPYLSDG IERALGLQRV STLQDLLFHS DCVTLHCGLN EHNHHLINDF
260 270 280 290 300
TVKQMRQGAF LVNTARGGLV DEKALAQALK EGRIRGAALD VHESEPFSFS
310 320 330 340 350
QGPLKDAPNL ICTPHAAWYS EQASIEMREE AAREIRRAIT GRIPDSLKNC
360 370 380 390 400
VNKDHLTAAT HWASMDPAVV HPELNGAAYS RYPPGVVSVA PTGIPAAVEG
410 420 430 440
IVPSAMSLSH GLPPVAHPPH APSPGQTVKP EADRDHTSDQ L
Length:441
Mass (Da):47,745
Last modified:May 1, 2007 - v2
Checksum:i2105CC8D69D915F4
GO
Isoform 2 (identifier: O88712-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: MGSSHLLNKGLPL → MS

Show »
Length:430
Mass (Da):46,614
Checksum:i0A36DBF66E6A8605
GO
Isoform 3 (identifier: O88712-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-74: Missing.

Note: No experimental confirmation available.

Show »
Length:367
Mass (Da):39,848
Checksum:i0E71CBDFDBF2EDA9
GO

Sequence cautioni

The sequence BAE41586.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551D → G in BAE41586. (PubMed:16141072)Curated
Sequence conflicti55 – 551D → G in BAE42587. (PubMed:16141072)Curated
Sequence conflicti108 – 1081K → R in BAE35946. (PubMed:16141072)Curated
Sequence conflicti380 – 3801Missing in CAA09219. (PubMed:10369679)Curated
Sequence conflicti380 – 3801Missing in BAE35946. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7474Missing in isoform 3. 1 PublicationVSP_024737Add
BLAST
Alternative sequencei1 – 1313MGSSH…KGLPL → MS in isoform 2. 2 PublicationsVSP_024738Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ010483 mRNA. Translation: CAA09219.1.
AB033122 mRNA. Translation: BAA85180.1.
AK133816 mRNA. Translation: BAE21859.1.
AK160658 mRNA. Translation: BAE35946.1.
AK165276 mRNA. Translation: BAE38115.1.
AK170133 mRNA. Translation: BAE41586.1. Different initiation.
AK171650 mRNA. Translation: BAE42587.1.
BC013702 mRNA. Translation: AAH13702.1.
BC015071 mRNA. Translation: AAH15071.1.
BC042425 mRNA. Translation: AAH42425.1.
CCDSiCCDS19201.1. [O88712-1]
RefSeqiNP_001185788.1. NM_001198859.1.
NP_001185789.1. NM_001198860.1.
NP_001185790.1. NM_001198861.1. [O88712-2]
NP_038530.1. NM_013502.3. [O88712-1]
XP_006503773.1. XM_006503710.1. [O88712-3]
UniGeneiMm.7286.

Genome annotation databases

EnsembliENSMUST00000079746; ENSMUSP00000078682; ENSMUSG00000037373. [O88712-1]
GeneIDi13016.
KEGGimmu:13016.
UCSCiuc008xaj.2. mouse. [O88712-1]
uc008xak.2. mouse. [O88712-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ010483 mRNA. Translation: CAA09219.1 .
AB033122 mRNA. Translation: BAA85180.1 .
AK133816 mRNA. Translation: BAE21859.1 .
AK160658 mRNA. Translation: BAE35946.1 .
AK165276 mRNA. Translation: BAE38115.1 .
AK170133 mRNA. Translation: BAE41586.1 . Different initiation.
AK171650 mRNA. Translation: BAE42587.1 .
BC013702 mRNA. Translation: AAH13702.1 .
BC015071 mRNA. Translation: AAH15071.1 .
BC042425 mRNA. Translation: AAH42425.1 .
CCDSi CCDS19201.1. [O88712-1 ]
RefSeqi NP_001185788.1. NM_001198859.1.
NP_001185789.1. NM_001198860.1.
NP_001185790.1. NM_001198861.1. [O88712-2 ]
NP_038530.1. NM_013502.3. [O88712-1 ]
XP_006503773.1. XM_006503710.1. [O88712-3 ]
UniGenei Mm.7286.

3D structure databases

ProteinModelPortali O88712.
SMRi O88712. Positions 26-356.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198961. 13 interactions.
DIPi DIP-33907N.
IntActi O88712. 10 interactions.
MINTi MINT-146962.

PTM databases

PhosphoSitei O88712.

Proteomic databases

MaxQBi O88712.
PaxDbi O88712.
PRIDEi O88712.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000079746 ; ENSMUSP00000078682 ; ENSMUSG00000037373 . [O88712-1 ]
GeneIDi 13016.
KEGGi mmu:13016.
UCSCi uc008xaj.2. mouse. [O88712-1 ]
uc008xak.2. mouse. [O88712-2 ]

Organism-specific databases

CTDi 1487.
MGIi MGI:1201685. Ctbp1.

Phylogenomic databases

eggNOGi COG0111.
GeneTreei ENSGT00530000063021.
HOVERGENi HBG001898.
InParanoidi O88712.
KOi K04496.
OMAi DRDHPSD.
OrthoDBi EOG761BT9.
PhylomeDBi O88712.
TreeFami TF313593.

Enzyme and pathway databases

Reactomei REACT_219771. deactivation of the beta-catenin transactivating complex.
REACT_233471. repression of WNT target genes.
REACT_254498. TCF7L2 mutants don't bind CTBP.

Miscellaneous databases

ChiTaRSi Ctbp1. mouse.
NextBioi 282870.
PROi O88712.
SOURCEi Search...

Gene expression databases

Bgeei O88712.
CleanExi MM_CTBP1.
Genevestigatori O88712.

Family and domain databases

Gene3Di 3.40.50.720. 2 hits.
InterProi IPR006139. D-isomer_2_OHA_DH_cat_dom.
IPR029753. D-isomer_DH_CS.
IPR029752. D-isomer_DH_CS1.
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 PS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Net, a negative Ras-switchable TCF, contains a second inhibition domain, the CID, that mediates repression through interactions with CtBP and de-acetylation."
    Criqui-Filipe P., Ducret C., Maira S.-M., Wasylyk B.
    EMBO J. 18:3392-3403(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
  2. "Identification of CtBP1 and CtBP2 as corepressors of zinc finger-homeodomain factor deltaEF1."
    Furusawa T., Moribe H., Kondoh H., Higashi Y.
    Mol. Cell. Biol. 19:8581-8590(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: ICR.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Strain: C57BL/6J and NOD.
    Tissue: Spleen.
  4. "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] (ISOFORMS 1 AND 2).
    Strain: 129, FVB/N and FVB/N-3.
    Tissue: Mammary tumor and Salivary gland.
  5. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 98-108 AND 286-305, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  6. "Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting transcription repressor (MITR) contributes to transcriptional repression of the MEF2 transcription factor."
    Zhang C.L., McKinsey T.A., Lu J.R., Olson E.N.
    J. Biol. Chem. 276:35-39(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HDAC4; HDAC5 AND HDAC9.
  7. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIPK2.
  8. "Characterization of four autonomous repression domains in the corepressor receptor interacting protein 140."
    Christian M., Tullet J.M.A., Parker M.G.
    J. Biol. Chem. 279:15645-15651(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NRIP1.
  9. "Transcriptional and DNA binding activity of the Foxp1/2/4 family is modulated by heterotypic and homotypic protein interactions."
    Li S., Weidenfeld J., Morrisey E.E.
    Mol. Cell. Biol. 24:809-822(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FOXP1 AND FOXP2.
  10. "Kruppel-like zinc finger protein Gli-similar 2 (Glis2) represses transcription through interaction with C-terminal binding protein 1 (CtBP1)."
    Kim S.-C., Kim Y.-S., Jetten A.M.
    Nucleic Acids Res. 33:6805-6815(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GLIS2, FUNCTION, SUBCELLULAR LOCATION.
  11. "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.
  12. "Regulation of the brown and white fat gene programs through a PRDM16/CtBP transcriptional complex."
    Kajimura S., Seale P., Tomaru T., Erdjument-Bromage H., Cooper M.P., Ruas J.L., Chin S., Tempst P., Lazar M.A., Spiegelman B.M.
    Genes Dev. 22:1397-1409(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PRDM16, SUBCELLULAR LOCATION.
  13. "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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SATB1.

Entry informationi

Entry nameiCTBP1_MOUSE
AccessioniPrimary (citable) accession number: O88712
Secondary accession number(s): Q3TAT1
, Q3TDL5, Q3TUM5, Q91WI6, Q91YX3, Q9QYG2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 2007
Last modified: November 26, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3