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

Protein O-GlcNAcase

Gene

Mgea5

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

Functioni

Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro) (PubMed:16517082). Does not bind acetyl-CoA and does not have histone acetyltransferase activity.By similarity1 Publication

Catalytic activityi

[Protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine + H2O = [protein]-L-serine + N-acetyl-D-glucosamine.1 Publication
[Protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine + H2O = [protein]-L-threonine + N-acetyl-D-glucosamine.1 Publication
Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.1 Publication

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
    Binding sitei67 – 671Substrate; via carbonyl oxygenBy similarity
    Binding sitei98 – 981SubstrateBy similarity
    Binding sitei174 – 1741Substrate1 Publication
    Active sitei175 – 1751Proton donorBy similarity
    Binding sitei219 – 2191SubstrateBy similarity
    Binding sitei285 – 2851SubstrateBy similarity
    Binding sitei313 – 3131SubstrateBy similarity
    Sitei413 – 4142Cleavage; by caspase-3By similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    BRENDAi2.3.1.48. 3474.
    3.2.1.169. 3474.

    Protein family/group databases

    CAZyiGH84. Glycoside Hydrolase Family 84.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein O-GlcNAcase1 Publication (EC:3.2.1.1691 Publication)
    Short name:
    OGA
    Alternative name(s):
    Beta-N-acetylhexosaminidase
    Beta-hexosaminidase
    Bifunctional protein NCOAT2 Publications
    Meningioma-expressed antigen 51 Publication
    N-acetyl-beta-D-glucosaminidase (EC:3.2.1.521 Publication)
    N-acetyl-beta-glucosaminidase
    Gene namesi
    Name:Mgea5
    Synonyms:Hexc, Kiaa0679
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589 Componenti: Chromosome 19

    Organism-specific databases

    MGIiMGI:1932139. Mgea5.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    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
    Mutagenesisi878 – 8781C → S: No effect on O-GlcNAcase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 916916Protein O-GlcNAcasePRO_0000252119Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei364 – 3641Phosphoserine1 Publication

    Post-translational modificationi

    Proteolytically cleaved by caspase-3 during apoptosis. The fragments interact with each other; cleavage does not decrease enzyme activity.By similarity

    Keywords - PTMi

    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

    BgeeiQ9EQQ9.
    CleanExiMM_MGEA5.
    ExpressionAtlasiQ9EQQ9. baseline and differential.
    GenevisibleiQ9EQQ9. MM.

    Interactioni

    Subunit structurei

    Monomer (By similarity). Interacts with CLOCK.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi217934. 4 interactions.
    IntActiQ9EQQ9. 2 interactions.
    MINTiMINT-2844950.
    STRINGi10090.ENSMUSP00000026243.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9EQQ9.
    SMRiQ9EQQ9. Positions 61-331, 717-916.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni278 – 2803Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 84 family.Curated

    Phylogenomic databases

    eggNOGiCOG0454.
    GeneTreeiENSGT00390000007726.
    HOVERGENiHBG053044.
    InParanoidiQ9EQQ9.
    KOiK15719.
    OMAiMSGDQEP.
    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. AlignAdd to basket

    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

            10         20         30         40         50
    MVQKESQAAL EERESERNAN PAAASGASLE QSVAPAPGED NPSGAGAAAV
    60 70 80 90 100
    VGAAGGARRF LCGVVEGFYG RPWVMEQRKE LFRRLQKWEL NTYLYAPKDD
    110 120 130 140 150
    YKHRMFWREM YSVEEAEQLM TLISAAREYE IEFIYAISPG LDITFSNPKE
    160 170 180 190 200
    VSTLKRKLDQ VSQFGCRSFA LLFDDIDHNM CAADKEVFSS FAHAQVSITN
    210 220 230 240 250
    EIYQYLGEPE TFLFCPTEYC GTFCYPNVSQ SPYLRTVGEK LLPGIEVLWT
    260 270 280 290 300
    GPKVVSKEIP VESIEEVSKI IKRAPVIWDN IHANDYDQKR LFLGPYKGRS
    310 320 330 340 350
    TELIPRLKGV LTNPNCEFEA NYVAIHTLAT WYKSNMNGVR KDVVMTDSED
    360 370 380 390 400
    STVSIQIKLE NEGSDEDIET DVLYSPQMAL KLALTEWLQE FGVPHQYSSR
    410 420 430 440 450
    QVAHSGAKTS VVDGTPLVAA PSLNATTVVT TVYQEPIMSQ GAALSGEPSV
    460 470 480 490 500
    LTKEEEKKQP DEEPMDMVVE KQEEAEHKND NQILTEIVEA KMAEELRPMD
    510 520 530 540 550
    TDKESMAESK SPEMSMQEDC IPDVAPMQTD EQTQKEQFVP GPNEKPLYTA
    560 570 580 590 600
    EPVTLEDLQL LADLFYLPYE HGPKGAQMLR EFQWLRANSS VVSVNCKGKD
    610 620 630 640 650
    SEKIEEWRSR AAKFEEMCAL VMGMFTRLSN CANRTILYDM YSYVWDIKSI
    660 670 680 690 700
    MSMVKSFVQW LGCRSHSSAQ FLIGDQEPWA FRGGLAGEFQ RLLPIDGAND
    710 720 730 740 750
    LFFQPPPLTP TSKVYTIRPY FPKDEASVYK ICREMYDDGV GFPFQSQPDL
    760 770 780 790 800
    IGDKLVGGLL SLSLDYCFVL EDEDGICGYA LGTVDVTPFI KKCKISWIPF
    810 820 830 840 850
    MQEKYTKPNG DKELSEAEKI MLSFHEEQEV LPETFLANFP SLIKMDIHKK
    860 870 880 890 900
    VTDPSVAKSM MACLLSSLKA NGSRGAFCEV RPDDKRILEF YSKLGCFEIA
    910
    KMEGFPKDVV ILGRSL
    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.Contaminating sequence. Potential poly-A sequence.Curated
    The sequence BAC97998.1 differs from that shown. Reason: Erroneous initiation. Curated
    The sequence BAE26311.1 differs from that shown. Reason: Erroneous initiation. Curated

    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:
    EMBLi
    GenBanki
    DDBJi
    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]
    XP_011245692.1. XM_011247390.1. [Q9EQQ9-3]
    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:
    EMBLi
    GenBanki
    DDBJi
    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]
    XP_011245692.1. XM_011247390.1. [Q9EQQ9-3]
    UniGeneiMm.122725.
    Mm.435821.
    Mm.440640.
    Mm.480399.

    3D structure databases

    ProteinModelPortaliQ9EQQ9.
    SMRiQ9EQQ9. Positions 61-331, 717-916.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi217934. 4 interactions.
    IntActiQ9EQQ9. 2 interactions.
    MINTiMINT-2844950.
    STRINGi10090.ENSMUSP00000026243.

    Protein family/group databases

    CAZyiGH84. Glycoside Hydrolase Family 84.

    PTM databases

    PhosphoSiteiQ9EQQ9.

    Proteomic databases

    MaxQBiQ9EQQ9.
    PaxDbiQ9EQQ9.
    PRIDEiQ9EQQ9.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi10724.
    MGIiMGI:1932139. Mgea5.
    RougeiSearch...

    Phylogenomic databases

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

    Enzyme and pathway databases

    BRENDAi2.3.1.48. 3474.
    3.2.1.169. 3474.

    Miscellaneous databases

    ChiTaRSiMgea5. mouse.
    NextBioi344519.
    PROiQ9EQQ9.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9EQQ9.
    CleanExiMM_MGEA5.
    ExpressionAtlasiQ9EQQ9. baseline and differential.
    GenevisibleiQ9EQQ9. MM.

    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.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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.
    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, CATALYTIC ACTIVITY, FUNCTION, 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 nameiOGA_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: July 22, 2015
    This is version 104 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    Was initially identified as a bi-functional protein that has an N-terminal domain with O-GlcNAcase activity and a C-terminal domain with histone acetyltransferase activity (PubMed:16356930). The histone acetyltransferase activity was detected only when the protein was expressed in mammalian cells, but not when expressed in bacterial cells, suggesting that the histone acetyltransferase activity might be due to the presence of a contaminant. Characterization of the human protein shows that this protein does not bind acetyl-CoA and therefore cannot have acetyltransferase activity.Curated

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    3. 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.