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Q9EQQ9

- NCOAT_MOUSE

UniProt

Q9EQQ9 - NCOAT_MOUSE

Protein

Bifunctional protein NCOAT

Gene

Mgea5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 2 (01 Oct 2001)
      Previous versions | rss
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    Functioni

    Cleaves GlcNAc but not GalNAc from glycopeptides. Can use p-nitrophenyl-beta-GlcNAc as substrate but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc. Possesses hyaluronidase activity By similarity. Acetylates 'Lys-8' of histone H4.By similarity1 Publication

    Catalytic activityi

    [Protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine + H2O = [protein]-L-serine + N-acetyl-D-glucosamine.
    [Protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine + H2O = [protein]-L-threonine + N-acetyl-D-glucosamine.
    Acetyl-CoA + [histone] = CoA + acetyl-[histone].

    Kineticsi

    1. KM=0.49 mM for pNP-GlcNAc1 Publication

    pH dependencei

    Optimum pH is 6.5-7.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei175 – 1751Nucleophile; for O-GlcNAcase activity1 Publication
    Active sitei177 – 1771Proton donor; for O-GlcNAcase activity1 Publication

    GO - Molecular functioni

    1. histone acetyltransferase activity Source: UniProtKB-EC
    2. hydrolase activity, acting on glycosyl bonds Source: UniProtKB-KW

    GO - Biological processi

    1. aging Source: Ensembl
    2. dATP metabolic process Source: Ensembl
    3. N-acetylglucosamine metabolic process Source: Ensembl
    4. necrotic cell death Source: Ensembl
    5. negative regulation of cardiac muscle adaptation Source: Ensembl
    6. negative regulation of protein glycosylation Source: Ensembl
    7. positive regulation of calcium ion transport into cytosol Source: Ensembl
    8. positive regulation of cell killing Source: Ensembl
    9. positive regulation of DNA metabolic process Source: Ensembl
    10. positive regulation of glucose import Source: Ensembl
    11. positive regulation of growth hormone secretion Source: Ensembl
    12. positive regulation of insulin secretion Source: Ensembl
    13. positive regulation of mitochondrial depolarization Source: Ensembl
    14. positive regulation of protein complex disassembly Source: Ensembl
    15. positive regulation of proteolysis Source: Ensembl
    16. protein targeting to membrane Source: Ensembl
    17. response to steroid hormone Source: Ensembl

    Keywords - Molecular functioni

    Acyltransferase, Glycosidase, Hydrolase, Transferase

    Protein family/group databases

    CAZyiGH84. Glycoside Hydrolase Family 84.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional protein NCOAT
    Alternative name(s):
    Meningioma-expressed antigen 5
    Nuclear cytoplasmic O-GlcNAcase and acetyltransferase
    Including the following 2 domains:
    Protein O-GlcNAcase (EC:3.2.1.169)
    Alternative name(s):
    Glycoside hydrolase O-GlcNAcase
    Hexosaminidase C
    N-acetyl-beta-D-glucosaminidase
    N-acetyl-beta-glucosaminidase
    O-GlcNAcase
    Short name:
    OGA
    Histone acetyltransferase (EC:2.3.1.48)
    Short name:
    HAT
    Gene namesi
    Name:Mgea5
    Synonyms:Hexc, Kiaa0679
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:1932139. Mgea5.

    Subcellular locationi

    Nucleus By similarity. Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi166 – 1661C → S: No change in substrate affinity but 60% reduction in O-GlcNAcase activity. 1 Publication
    Mutagenesisi174 – 1741D → N: 2-fold increase in substrate affinity and 77% reduction in O-GlcNAcase activity. Regains appreciable level of catalytic efficiency in the acidic pH range. No recovery of activity in the presence of sodium azide. 1 Publication
    Mutagenesisi175 – 1751D → A: 3-fold increase in substrate affinity and 90% reduction in O-GlcNAcase activity. Regains appreciable level of catalytic efficiency in the acidic pH range. 70% recovery of activity in the presence of sodium azide. 1 Publication
    Mutagenesisi177 – 1771D → N: 2-fold decrease in substrate affinity and 96% reduction in O-GlcNAcase activity. Regains appreciable level of catalytic efficiency in the acidic pH range. 40% recovery of activity in the presence of sodium azide. 1 Publication
    Mutagenesisi774 – 7741D → A: Disrupts ability to bind histone H4 as well as HAT activity. 1 Publication
    Mutagenesisi777 – 7771C → A: Disrupts ability to bind histone H4 as well as HAT activity. 1 Publication
    Mutagenesisi789 – 7891F → A: Disrupts ability to bind histone H4 as well as HAT activity. 1 Publication
    Mutagenesisi793 – 7931C → A: Disrupts ability to bind histone H4 as well as HAT activity. 1 Publication
    Mutagenesisi796 – 7961S → A: Disrupts ability to bind histone H4 as well as HAT activity. 1 Publication
    Mutagenesisi853 – 8531D → N: Retains ability to bind histone H4. 1 Publication
    Mutagenesisi878 – 8781C → S: No effect on O-GlcNAcase activity. 1 Publication
    Mutagenesisi884 – 8841D → N: Retains ability to bind histone H4. 1 Publication
    Mutagenesisi891 – 8911Y → F: Retains ability to bind histone H4. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 916916Bifunctional protein NCOATPRO_0000252119Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei364 – 3641Phosphoserine1 Publication
    Disulfide bondi777 ↔ 7931 Publication

    Post-translational modificationi

    Proteolytically cleaved by caspase-3.By similarity

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiQ9EQQ9.
    PaxDbiQ9EQQ9.
    PRIDEiQ9EQQ9.

    PTM databases

    PhosphoSiteiQ9EQQ9.

    Expressioni

    Developmental stagei

    Expressed throughout development from blastocyst stage to embryonic day 16.5.1 Publication

    Inductioni

    Expression in the liver oscillates in a circadian manner with peak levels at CT8-CT12.1 Publication

    Gene expression databases

    ArrayExpressiQ9EQQ9.
    BgeeiQ9EQQ9.
    CleanExiMM_MGEA5.
    GenevestigatoriQ9EQQ9.

    Interactioni

    Subunit structurei

    Monomer By similarity. Binds both acetylated and unacetylated histone H4 tail but acetylation on 'Lys-8' of histone H4 abolishes binding. Interacts with CLOCK.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi217934. 4 interactions.
    IntActiQ9EQQ9. 2 interactions.
    MINTiMINT-2844950.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9EQQ9.
    SMRiQ9EQQ9. Positions 46-388, 717-916.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni583 – 916334Histone acetyltransferase activityBy similarityAdd
    BLAST
    Regioni695 – 814120Required for histone H4 bindingAdd
    BLAST

    Phylogenomic databases

    eggNOGiCOG0454.
    GeneTreeiENSGT00390000007726.
    HOVERGENiHBG053044.
    InParanoidiQ9EQQ9.
    KOiK15719.
    OMAiLIKVDIH.
    OrthoDBiEOG7P02H7.
    PhylomeDBiQ9EQQ9.
    TreeFamiTF313732.

    Family and domain databases

    Gene3Di3.40.630.30. 2 hits.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR011496. Beta-N-acetylglucosaminidase.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF07555. NAGidase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF55729. SSF55729. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9EQQ9-1) [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

    MVQKESQAAL EERESERNAN PAAASGASLE QSVAPAPGED NPSGAGAAAV    50
    VGAAGGARRF LCGVVEGFYG RPWVMEQRKE LFRRLQKWEL NTYLYAPKDD 100
    YKHRMFWREM YSVEEAEQLM TLISAAREYE IEFIYAISPG LDITFSNPKE 150
    VSTLKRKLDQ VSQFGCRSFA LLFDDIDHNM CAADKEVFSS FAHAQVSITN 200
    EIYQYLGEPE TFLFCPTEYC GTFCYPNVSQ SPYLRTVGEK LLPGIEVLWT 250
    GPKVVSKEIP VESIEEVSKI IKRAPVIWDN IHANDYDQKR LFLGPYKGRS 300
    TELIPRLKGV LTNPNCEFEA NYVAIHTLAT WYKSNMNGVR KDVVMTDSED 350
    STVSIQIKLE NEGSDEDIET DVLYSPQMAL KLALTEWLQE FGVPHQYSSR 400
    QVAHSGAKTS VVDGTPLVAA PSLNATTVVT TVYQEPIMSQ GAALSGEPSV 450
    LTKEEEKKQP DEEPMDMVVE KQEEAEHKND NQILTEIVEA KMAEELRPMD 500
    TDKESMAESK SPEMSMQEDC IPDVAPMQTD EQTQKEQFVP GPNEKPLYTA 550
    EPVTLEDLQL LADLFYLPYE HGPKGAQMLR EFQWLRANSS VVSVNCKGKD 600
    SEKIEEWRSR AAKFEEMCAL VMGMFTRLSN CANRTILYDM YSYVWDIKSI 650
    MSMVKSFVQW LGCRSHSSAQ FLIGDQEPWA FRGGLAGEFQ RLLPIDGAND 700
    LFFQPPPLTP TSKVYTIRPY FPKDEASVYK ICREMYDDGV GFPFQSQPDL 750
    IGDKLVGGLL SLSLDYCFVL EDEDGICGYA LGTVDVTPFI KKCKISWIPF 800
    MQEKYTKPNG DKELSEAEKI MLSFHEEQEV LPETFLANFP SLIKMDIHKK 850
    VTDPSVAKSM MACLLSSLKA NGSRGAFCEV RPDDKRILEF YSKLGCFEIA 900
    KMEGFPKDVV ILGRSL 916
    Length:916
    Mass (Da):103,162
    Last modified:October 1, 2001 - v2
    Checksum:iB2FAC6F10E03C5CA
    GO
    Isoform 2 (identifier: Q9EQQ9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-698: Missing.
         699-725: NDLFFQPPPLTPTSKVYTIRPYFPKDE → MYTTHSCLYSFFLTFFLVCCLTRLYFQ

    Note: No experimental confirmation available.

    Show »
    Length:218
    Mass (Da):24,718
    Checksum:i48F3308C6C616896
    GO
    Isoform 3 (identifier: Q9EQQ9-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MVRPRVWRSSRRVASQNGLRAFGPTDRGRRGAVAGGRRM

    Note: No experimental confirmation available.

    Show »
    Length:954
    Mass (Da):107,395
    Checksum:i677AA03C422AECBD
    GO

    Sequence cautioni

    The sequence AAH41109.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence BAC97998.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAE26311.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61S → T in BAE26311. (PubMed:16141072)Curated
    Sequence conflicti52 – 532GA → RT in BAE26311. (PubMed:16141072)Curated
    Sequence conflicti742 – 7421F → S in BAC97998. (PubMed:14621295)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 698698Missing in isoform 2. 1 PublicationVSP_020870Add
    BLAST
    Alternative sequencei1 – 11M → MVRPRVWRSSRRVASQNGLR AFGPTDRGRRGAVAGGRRM in isoform 3. 1 PublicationVSP_020871
    Alternative sequencei699 – 72527NDLFF…FPKDE → MYTTHSCLYSFFLTFFLVCC LTRLYFQ in isoform 2. 1 PublicationVSP_020872Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF132214 mRNA. Translation: AAG43273.2.
    AK129188 mRNA. Translation: BAC97998.1. Different initiation.
    BC041109 mRNA. Translation: AAH41109.1. Sequence problems.
    BC054821 mRNA. Translation: AAH54821.1.
    AK012695 mRNA. Translation: BAB28416.1.
    AK014781 mRNA. Translation: BAB29550.1.
    AK077613 mRNA. Translation: BAC36900.1.
    AK088774 mRNA. Translation: BAC40564.1.
    AK145227 mRNA. Translation: BAE26311.1. Different initiation.
    CCDSiCCDS29866.1. [Q9EQQ9-1]
    RefSeqiNP_076288.1. NM_023799.3. [Q9EQQ9-1]
    UniGeneiMm.122725.
    Mm.435821.
    Mm.440640.
    Mm.480399.

    Genome annotation databases

    EnsembliENSMUST00000026243; ENSMUSP00000026243; ENSMUSG00000025220. [Q9EQQ9-1]
    GeneIDi76055.
    KEGGimmu:76055.
    UCSCiuc008hrm.1. mouse. [Q9EQQ9-2]
    uc008hrn.1. mouse. [Q9EQQ9-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF132214 mRNA. Translation: AAG43273.2 .
    AK129188 mRNA. Translation: BAC97998.1 . Different initiation.
    BC041109 mRNA. Translation: AAH41109.1 . Sequence problems.
    BC054821 mRNA. Translation: AAH54821.1 .
    AK012695 mRNA. Translation: BAB28416.1 .
    AK014781 mRNA. Translation: BAB29550.1 .
    AK077613 mRNA. Translation: BAC36900.1 .
    AK088774 mRNA. Translation: BAC40564.1 .
    AK145227 mRNA. Translation: BAE26311.1 . Different initiation.
    CCDSi CCDS29866.1. [Q9EQQ9-1 ]
    RefSeqi NP_076288.1. NM_023799.3. [Q9EQQ9-1 ]
    UniGenei Mm.122725.
    Mm.435821.
    Mm.440640.
    Mm.480399.

    3D structure databases

    ProteinModelPortali Q9EQQ9.
    SMRi Q9EQQ9. Positions 46-388, 717-916.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 217934. 4 interactions.
    IntActi Q9EQQ9. 2 interactions.
    MINTi MINT-2844950.

    Protein family/group databases

    CAZyi GH84. Glycoside Hydrolase Family 84.

    PTM databases

    PhosphoSitei Q9EQQ9.

    Proteomic databases

    MaxQBi Q9EQQ9.
    PaxDbi Q9EQQ9.
    PRIDEi Q9EQQ9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000026243 ; ENSMUSP00000026243 ; ENSMUSG00000025220 . [Q9EQQ9-1 ]
    GeneIDi 76055.
    KEGGi mmu:76055.
    UCSCi uc008hrm.1. mouse. [Q9EQQ9-2 ]
    uc008hrn.1. mouse. [Q9EQQ9-1 ]

    Organism-specific databases

    CTDi 10724.
    MGIi MGI:1932139. Mgea5.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG0454.
    GeneTreei ENSGT00390000007726.
    HOVERGENi HBG053044.
    InParanoidi Q9EQQ9.
    KOi K15719.
    OMAi LIKVDIH.
    OrthoDBi EOG7P02H7.
    PhylomeDBi Q9EQQ9.
    TreeFami TF313732.

    Miscellaneous databases

    ChiTaRSi MGEA5. mouse.
    NextBioi 344519.
    PROi Q9EQQ9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9EQQ9.
    Bgeei Q9EQQ9.
    CleanExi MM_MGEA5.
    Genevestigatori Q9EQQ9.

    Family and domain databases

    Gene3Di 3.40.630.30. 2 hits.
    InterProi IPR016181. Acyl_CoA_acyltransferase.
    IPR011496. Beta-N-acetylglucosaminidase.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF07555. NAGidase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    SSF55729. SSF55729. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Mgea5, the murine homolog of a neutral-active cytosolic beta-N-acetylglucosaminidase, localized on chromosome 19."
      Csoka A.B.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
      DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Embryonic tail.
    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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-603 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-77 (ISOFORM 3).
      Strain: C57BL/6J and NOD.
      Tissue: Head, Mammary gland and Thymus.
    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] (ISOFORM 1).
      Strain: FVB/N-3.
      Tissue: Kidney and Mammary tumor.
    5. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 109-127, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    6. "The histone acetyltransferase NCOAT contains a zinc finger-like motif involved in substrate recognition."
      Toleman C.A., Paterson A.J., Kudlow J.E.
      J. Biol. Chem. 281:3918-3925(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 157-167; 775-785 AND 875-886, FUNCTION, SUBUNIT, DISULFIDE BOND, MUTAGENESIS OF ASP-774; CYS-777; PHE-789; CYS-793; SER-796; ASP-853; ASP-884 AND TYR-891.
    7. "Identification of a nuclear variant of MGEA5, a cytoplasmic hyaluronidase and a beta-N-acetylglucosaminidase."
      Comtesse N., Maldener E., Meese E.
      Biochem. Biophys. Res. Commun. 283:634-640(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    9. "Location and characterization of the O-GlcNAcase active site."
      Toleman C., Paterson A.J., Kudlow J.E.
      Biochim. Biophys. Acta 1760:829-839(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-166; ASP-174; ASP-175; ASP-177 AND CYS-878.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    11. "Glucose sensor O-GlcNAcylation coordinates with phosphorylation to regulate circadian clock."
      Kaasik K., Kivimae S., Allen J.J., Chalkley R.J., Huang Y., Baer K., Kissel H., Burlingame A.L., Shokat K.M., Ptacek L.J., Fu Y.H.
      Cell Metab. 17:291-302(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CLOCK, INDUCTION.

    Entry informationi

    Entry nameiNCOAT_MOUSE
    AccessioniPrimary (citable) accession number: Q9EQQ9
    Secondary accession number(s): Q3ULY7
    , Q6ZQ71, Q8BK05, Q8BTT2, Q8CFX2, Q9CSJ4, Q9CUR7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: October 1, 2001
    Last modified: October 1, 2014
    This is version 96 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, Multifunctional enzyme, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

    External Data

    Dasty 3