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O09000

- NCOA3_MOUSE

UniProt

O09000 - NCOA3_MOUSE

Protein

Nuclear receptor coactivator 3

Gene

Ncoa3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Plays a central role in creating a multisubunit coactivator complex, probably via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ER), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Displays histone acetyltransferase activity. Also involved in the coactivation of the NF-kappa-B pathway via its interaction with the NFKB1 subunit By similarity.By similarity

    Catalytic activityi

    Acetyl-CoA + [histone] = CoA + acetyl-[histone].

    Enzyme regulationi

    Coactivator activity on nuclear receptors and NF-kappa-B pathways is enhanced by various hormones, and the TNF cytokine, respectively. TNF stimulation probably enhances phosphorylation, which in turn activates coactivator function. In contrast, acetylation by CREBBP apparently suppresses coactivation of target genes by disrupting its association with nuclear receptors By similarity.By similarity

    GO - Molecular functioni

    1. chromatin binding Source: MGI
    2. histone acetyltransferase activity Source: UniProtKB-EC
    3. ligand-dependent nuclear receptor transcription coactivator activity Source: InterPro
    4. signal transducer activity Source: InterPro

    GO - Biological processi

    1. developmental growth Source: MGI
    2. labyrinthine layer morphogenesis Source: MGI
    3. mammary gland branching involved in thelarche Source: MGI
    4. multicellular organism growth Source: MGI
    5. regulation of transcription, DNA-templated Source: UniProtKB-KW
    6. transcription, DNA-templated Source: UniProtKB-KW
    7. vagina development Source: MGI

    Keywords - Molecular functioni

    Activator, Acyltransferase, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear receptor coactivator 3 (EC:2.3.1.48)
    Short name:
    NCoA-3
    Alternative name(s):
    Amplified in breast cancer-1 protein homolog
    Short name:
    AIB-1
    CBP-interacting protein
    Short name:
    p/CIP
    Short name:
    pCIP
    Receptor-associated coactivator 3
    Short name:
    RAC-3
    Steroid receptor coactivator protein 3
    Short name:
    SRC-3
    Thyroid hormone receptor activator molecule 1
    Short name:
    ACTR
    Short name:
    TRAM-1
    Gene namesi
    Name:Ncoa3
    Synonyms:Aib1, Pcip, Rac3, Tram1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1276535. Ncoa3.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus PROSITE-ProRule annotation
    Note: Mainly cytoplasmic and weakly nuclear. Upon TNF activation and subsequent phosphorylation, it translocates from the cytoplasm to the nucleus By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleoplasm Source: Reactome
    3. nucleus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Defects result in diverse phenotype of postnatal growth retardation, such as dwarfism, delayed puberty, abnormal reproductive function and mammary gland growth retardation.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 13981397Nuclear receptor coactivator 3PRO_0000094407Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei215 – 2151Phosphoserine1 Publication
    Modified residuei544 – 5441Phosphoserine1 Publication
    Modified residuei594 – 5941Phosphoserine; by CK1By similarity
    Modified residuei609 – 6091N6-acetyllysine; alternate1 Publication
    Modified residuei609 – 6091N6-acetyllysine; by CREBBP; alternateBy similarity
    Modified residuei612 – 6121N6-acetyllysine; alternate1 Publication
    Modified residuei612 – 6121N6-acetyllysine; by CREBBP; alternateBy similarity
    Modified residuei613 – 6131N6-acetyllysine; alternate1 Publication
    Modified residuei613 – 6131N6-acetyllysine; by CREBBP; alternateBy similarity
    Modified residuei680 – 6801N6-acetyllysineBy similarity
    Modified residuei720 – 7201Phosphoserine1 Publication
    Modified residuei847 – 8471Phosphoserine1 Publication
    Modified residuei850 – 8501Phosphoserine1 Publication

    Post-translational modificationi

    Acetylated by CREBBP. Acetylation occurs in the RID domain, and disrupts the interaction with nuclear receptors and regulates its function By similarity.By similarity
    Methylated by CARM1.1 Publication
    Phosphorylated by IKK complex. Regulated its function By similarity.By similarity

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    PaxDbiO09000.
    PRIDEiO09000.

    PTM databases

    PhosphoSiteiO09000.

    Expressioni

    Tissue specificityi

    Not expressed in all steroid sensitive tissues. Highly expressed in the female reproductive system, in both oocyte and smooth muscle cells of the oviduct, but not expressed in the uterine endometrium. Highly expressed in mammary glands. Expressed moderately in smooth muscle cells of both blood vessels and intestines, and weakly expressed in hepatocytes. In brain, highly expressed in neurons of the hyppocampus, and in mitral cell and granule layers of the olfactory bulb. Expressed moderately in the internal layer of cerebellum. Not expressed in the spinal chord, cardiac muscle, skeletal muscle, thymus and pancreas.1 Publication

    Gene expression databases

    CleanExiMM_NCOA3.
    MM_RAC3.
    GenevestigatoriO09000.

    Interactioni

    Subunit structurei

    Interacts with the histone acetyltransferase protein CREBBP. These two proteins are present in a complex containing NCOA2, IKKA, IKKB and IKBKG. Interacts with PCAF and NR3C1 By similarity. Interacts with CARM1. Interacts with CASP8AP2. Interacts with ATAD2 and this interaction is enhanced by estradiol By similarity. Interacts with PSMB9. Binds to CSNK1D By similarity. Found in a complex containing NCOA3, AR and MAK. Interacts with DDX5. Interacts with NPAS2 By similarity.By similarity

    Protein-protein interaction databases

    IntActiO09000. 12 interactions.
    MINTiMINT-1531012.
    STRINGi10090.ENSMUSP00000085416.

    Structurei

    3D structure databases

    ProteinModelPortaliO09000.
    SMRiO09000. Positions 35-365, 1052-1098.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 8358bHLHPROSITE-ProRule annotationAdd
    BLAST
    Domaini111 – 18171PASPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni949 – 1113165Interaction with CREBBPBy similarityAdd
    BLAST
    Regioni1104 – 1278175AcetyltransferaseAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi678 – 6825LXXLL motif 1
    Motifi730 – 7345LXXLL motif 2
    Motifi1041 – 10455LXXLL motif 3

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi429 – 664236Ser-richAdd
    BLAST
    Compositional biasi965 – 98723Poly-GlnAdd
    BLAST

    Domaini

    Contains three Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. Motifs 1 and 2 are essential for the association with nuclear receptors, and constitute the RID domain (Receptor-interacting domain) (By similarity).By similarity

    Sequence similaritiesi

    Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation
    Contains 1 PAS (PER-ARNT-SIM) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG315556.
    HOGENOMiHOG000230947.
    HOVERGENiHBG052583.

    Family and domain databases

    Gene3Di4.10.630.10. 2 hits.
    InterProiIPR011598. bHLH_dom.
    IPR010011. DUF1518.
    IPR028818. NCOA3.
    IPR009110. Nuc_rcpt_coact.
    IPR014920. Nuc_rcpt_coact_Ncoa-typ.
    IPR017426. Nuclear_rcpt_coactivator.
    IPR000014. PAS.
    IPR013767. PAS_fold.
    IPR014935. SRC-1.
    IPR008955. Src1_rcpt_coact.
    [Graphical view]
    PANTHERiPTHR10684. PTHR10684. 1 hit.
    PTHR10684:SF3. PTHR10684:SF3. 1 hit.
    PfamiPF07469. DUF1518. 1 hit.
    PF08815. Nuc_rec_co-act. 1 hit.
    PF00989. PAS. 1 hit.
    PF08832. SRC-1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038181. Nuclear_receptor_coactivator. 1 hit.
    SMARTiSM00353. HLH. 1 hit.
    SM00091. PAS. 1 hit.
    [Graphical view]
    SUPFAMiSSF47459. SSF47459. 1 hit.
    SSF55785. SSF55785. 2 hits.
    SSF69125. SSF69125. 1 hit.
    PROSITEiPS50888. BHLH. 1 hit.
    PS50112. PAS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O09000-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGLGESSLD PLAAESRKRK LPCDAPGQGL VYSGEKWRRE QESKYIEELA     50
    ELISANLSDI DNFNVKPDKC AILKETVRQI RQIKEQGKTI SSDDDVQKAD 100
    VSSTGQGVID KDSLGPLLLQ ALDGFLFVVN RDGNIVFVSE NVTQYLQYKQ 150
    EDLVNTSVYS ILHEPRRKDF LNTYQNPQLM EFLGLMRTRD KKAPYILIVR 200
    MLMKTHDILE DVNASPETRQ RYETMQCFAL SQPRAMLEEG EDLQCCMICV 250
    ARRVTAPFPS SPESFITRHD LSGKVVNIDT NSLRSSMRPG FEDIIRRCIQ 300
    RFFSLNDGQS WSQKRHYQEA YVHGHAETPV YRFSLADGTI VSAQTKSKLF 350
    RNPVTNDRHG FISTHFLQRE QNGYRPNPIP QDKGIRPPAA GCGVSMSPNQ 400
    NVQMMGSRTY GVPDPSNTGQ MGGARYGASS SVASLTPGQS LQSPSSYQNS 450
    SYGLSMSSPP HGSPGLGPNQ QNIMISPRNR GSPKMASHQF SPAAGAHSPM 500
    GPSGNTGSHS FSSSSLSALQ AISEGVGTSL LSTLSSPGPK LDNSPNMNIS 550
    QPSKVSGQDS KSPLGLYCEQ NPVESSVCQS NSRDPQVKKE SKESSGEVSE 600
    TPRGPLESKG HKKLLQLLTC SSDDRGHSSL TNSPLDPNCK DSSVSVTSPS 650
    GVSSSTSGTV SSTSNVHGSL LQEKHRILHK LLQNGNSPAE VAKITAEATG 700
    KDTSSTASCG EGTTRQEQLS PKKKENNALL RYLLDRDDPS DVLAKELQPQ 750
    ADSGDSKLSQ CSCSTNPSSG QEKDPKIKTE TNDEVSGDLD NLDAILGDLT 800
    SSDFYNNPTN GGHPGAKQQM FAGPSSLGLR SPQPVQSVRP PYNRAVSLDS 850
    PVSVGSGPPV KNVSAFPGLP KQPILAGNPR MMDSQENYGA NMGPNRNVPV 900
    NPTSSPGDWG LANSRASRME PLASSPLGRT GADYSATLPR PAMGGSVPTL 950
    PLRSNRLPGA RPSLQQQQQQ QQQQQQQQQQ QQQQQQQMLQ MRTGEIPMGM 1000
    GVNPYSPAVQ SNQPGSWPEG MLSMEQGPHG SQNRPLLRNS LDDLLGPPSN 1050
    AEGQSDERAL LDQLHTFLSN TDATGLEEID RALGIPELVN QGQALESKQD 1100
    VFQGQEAAVM MDQKAALYGQ TYPAQGPPLQ GGFNLQGQSP SFNSMMGQIS 1150
    QQGSFPLQGM HPRAGLVRPR TNTPKQLRMQ LQQRLQGQQF LNQSRQALEM 1200
    KMENPAGTAV MRPMMPQAFF NAQMAAQQKR ELMSHHLQQQ RMAMMMSQPQ 1250
    PQAFSPPPNV TASPSMDGVL AGSAMPQAPP QQFPYPANYG MGQPPEPAFG 1300
    RGSSPPSAMM SSRMGPSQNA MVQHPQPTPM YQPSDMKGWP SGNLARNGSF 1350
    PQQQFAPQGN PAAYNMVHMN SSGGHLGQMA MTPMPMSGMP MGPDQKYC 1398
    Length:1,398
    Mass (Da):151,574
    Last modified:August 1, 1998 - v2
    Checksum:iEF44E92735816C24
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF000581 mRNA. Translation: AAC05020.1.
    AK021229 mRNA. No translation available.
    UniGeneiMm.469663.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF000581 mRNA. Translation: AAC05020.1 .
    AK021229 mRNA. No translation available.
    UniGenei Mm.469663.

    3D structure databases

    ProteinModelPortali O09000.
    SMRi O09000. Positions 35-365, 1052-1098.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O09000. 12 interactions.
    MINTi MINT-1531012.
    STRINGi 10090.ENSMUSP00000085416.

    PTM databases

    PhosphoSitei O09000.

    Proteomic databases

    PaxDbi O09000.
    PRIDEi O09000.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    MGIi MGI:1276535. Ncoa3.

    Phylogenomic databases

    eggNOGi NOG315556.
    HOGENOMi HOG000230947.
    HOVERGENi HBG052583.

    Enzyme and pathway databases

    Reactomei REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

    Miscellaneous databases

    ChiTaRSi NCOA3. mouse.
    PROi O09000.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_NCOA3.
    MM_RAC3.
    Genevestigatori O09000.

    Family and domain databases

    Gene3Di 4.10.630.10. 2 hits.
    InterProi IPR011598. bHLH_dom.
    IPR010011. DUF1518.
    IPR028818. NCOA3.
    IPR009110. Nuc_rcpt_coact.
    IPR014920. Nuc_rcpt_coact_Ncoa-typ.
    IPR017426. Nuclear_rcpt_coactivator.
    IPR000014. PAS.
    IPR013767. PAS_fold.
    IPR014935. SRC-1.
    IPR008955. Src1_rcpt_coact.
    [Graphical view ]
    PANTHERi PTHR10684. PTHR10684. 1 hit.
    PTHR10684:SF3. PTHR10684:SF3. 1 hit.
    Pfami PF07469. DUF1518. 1 hit.
    PF08815. Nuc_rec_co-act. 1 hit.
    PF00989. PAS. 1 hit.
    PF08832. SRC-1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038181. Nuclear_receptor_coactivator. 1 hit.
    SMARTi SM00353. HLH. 1 hit.
    SM00091. PAS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47459. SSF47459. 1 hit.
    SSF55785. SSF55785. 2 hits.
    SSF69125. SSF69125. 1 hit.
    PROSITEi PS50888. BHLH. 1 hit.
    PS50112. PAS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function."
      Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K., Rosenfeld M.G.
      Nature 387:677-684(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CREBBP; ESR AND RARA.
    2. "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] OF 1360-1398.
      Strain: C57BL/6J.
      Tissue: Embryonic stem cell.
    3. "The steroid receptor coactivator SRC-3 (p/CIP/RAC3/AIB1/ACTR/TRAM-1) is required for normal growth, puberty, female reproductive function, and mammary gland development."
      Xu J., Liao L., Ning G., Yoshida-Komiya H., Deng C., O'Malley B.W.
      Proc. Natl. Acad. Sci. U.S.A. 97:6379-6384(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    4. "Regulation of transcription by a protein methyltransferase."
      Chen D., Ma H., Hong H., Koh S.S., Huang S.-M., Schurter B.T., Aswad D.W., Stallcup M.R.
      Science 284:2174-2177(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CARM1.
    5. "A transcriptional switch mediated by cofactor methylation."
      Xu W., Chen H., Du K., Asahara H., Tini M., Emerson B.M., Montminy M., Evans R.M.
      Science 294:2507-2511(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION BY CARM1.
    6. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-544; SER-720; SER-847 AND SER-850, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-609; LYS-612 AND LYS-613, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiNCOA3_MOUSE
    AccessioniPrimary (citable) accession number: O09000
    Secondary accession number(s): Q9CRD5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 138 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, 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