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O60502

- NCOAT_HUMAN

UniProt

O60502 - NCOAT_HUMAN

Protein

Bifunctional protein NCOAT

Gene

MGEA5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 2 (01 Mar 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. Acetylates 'Lys-8' of histone H4 and 'Lys-14' of histone H3.2 Publications

    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].

    Enzyme regulationi

    Inhibited by N-acetylglucosamine and not N-acetylgalactosamine.1 Publication

    Kineticsi

    1. KM=1.1 mM for pNP-GlcNAc2 Publications

    Vmax=652 µmol/min/mg enzyme with pNP-GLcNAc as substrate2 Publications

    pH dependencei

    Optimum pH is 5.7-7.2 Publications

    Sites

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

    GO - Molecular functioni

    1. histone acetyltransferase activity Source: UniProtKB-EC
    2. hyalurononglucosaminidase activity Source: ProtInc

    GO - Biological processi

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

    Keywords - Molecular functioni

    Acyltransferase, Glycosidase, Hydrolase, Transferase

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03036-MONOMER.
    BRENDAi3.2.1.35. 2681.

    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, MEA5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:7056. MGEA5.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30787.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 916916Bifunctional protein NCOATPRO_0000252118Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei364 – 3641Phosphoserine4 Publications
    Disulfide bondi777 ↔ 793By similarity

    Post-translational modificationi

    Proteolytically cleaved by caspase-3.

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiO60502.
    PaxDbiO60502.
    PRIDEiO60502.

    PTM databases

    PhosphoSiteiO60502.

    Miscellaneous databases

    PMAP-CutDBO60502.

    Expressioni

    Tissue specificityi

    Ubiquitous. Shows highest expression in the brain, placenta and pancreas.2 Publications

    Gene expression databases

    ArrayExpressiO60502.
    BgeeiO60502.
    CleanExiHS_MGEA5.
    GenevestigatoriO60502.

    Organism-specific databases

    HPAiHPA036141.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi115948. 23 interactions.
    IntActiO60502. 17 interactions.
    STRINGi9606.ENSP00000354850.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YDQX-ray2.60T402-408[»]
    ProteinModelPortaliO60502.
    SMRiO60502. 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 bindingBy similarityAdd
    BLAST

    Phylogenomic databases

    eggNOGiCOG0454.
    HOVERGENiHBG053044.
    InParanoidiO60502.
    KOiK15719.
    OMAiLIKVDIH.
    OrthoDBiEOG7P02H7.
    PhylomeDBiO60502.
    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O60502-1) [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

    MVQKESQATL EERESELSSN PAASAGASLE PPAAPAPGED NPAGAGGAAV    50
    AGAAGGARRF 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
    QVAHSGAKAS VVDGTPLVAA PSLNATTVVT TVYQEPIMSQ GAALSGEPTT 450
    LTKEEEKKQP DEEPMDMVVE KQEETDHKND NQILSEIVEA KMAEELKPMD 500
    TDKESIAESK SPEMSMQEDC ISDIAPMQTD EQTNKEQFVP GPNEKPLYTA 550
    EPVTLEDLQL LADLFYLPYE HGPKGAQMLR EFQWLRANSS VVSVNCKGKD 600
    SEKIEEWRSR AAKFEEMCGL VMGMFTRLSN CANRTILYDM YSYVWDIKSI 650
    MSMVKSFVQW LGCRSHSSAQ FLIGDQEPWA FRGGLAGEFQ RLLPIDGAND 700
    LFFQPPPLTP TSKVYTIRPY FPKDEASVYK ICREMYDDGV GLPFQSQPDL 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):102,915
    Last modified:March 1, 2001 - v2
    Checksum:i01F8A64A9B1475C6
    GO
    Isoform 2 (identifier: O60502-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         346-398: Missing.
         691-704: Missing.

    Show »
    Length:849
    Mass (Da):95,331
    Checksum:iA65EFD64BE0AD17C
    GO
    Isoform 3 (identifier: O60502-3) [UniParc]FASTAAdd to Basket

    Also known as: MGEA5s

    The sequence of this isoform differs from the canonical sequence as follows:
         663-677: CRSHSSAQFLIGDQE → RCTRNNLFSSNILSL
         678-916: Missing.

    Show »
    Length:677
    Mass (Da):76,193
    Checksum:iBF83DEF3ABDE4AA8
    GO
    Isoform 4 (identifier: O60502-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         346-398: Missing.

    Show »
    Length:863
    Mass (Da):96,932
    Checksum:iD6AB77EE6830F570
    GO

    Sequence cautioni

    The sequence AAH47877.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence BAA31654.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti46 – 461G → E.
    Corresponds to variant rs3740421 [ dbSNP | Ensembl ].
    VAR_027761
    Natural varianti602 – 6021E → K.1 Publication
    Corresponds to variant rs17853930 [ dbSNP | Ensembl ].
    VAR_027762

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei346 – 39853Missing in isoform 2 and isoform 4. CuratedVSP_020866Add
    BLAST
    Alternative sequencei663 – 67715CRSHS…IGDQE → RCTRNNLFSSNILSL in isoform 3. 1 PublicationVSP_020867Add
    BLAST
    Alternative sequencei678 – 916239Missing in isoform 3. 1 PublicationVSP_020868Add
    BLAST
    Alternative sequencei691 – 70414Missing in isoform 2. CuratedVSP_020869Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF036144 mRNA. Translation: AAD05385.2.
    AF307332 mRNA. Translation: AAG21428.1.
    AB014579 mRNA. Translation: BAA31654.2. Different initiation.
    AC010789 Genomic DNA. No translation available.
    CH471066 Genomic DNA. Translation: EAW49744.1.
    CH471066 Genomic DNA. Translation: EAW49741.1.
    CH471066 Genomic DNA. Translation: EAW49742.1.
    BC001343 mRNA. Translation: AAH01343.1.
    BC039583 mRNA. Translation: AAH39583.2.
    BC047877 mRNA. Translation: AAH47877.1. Sequence problems.
    CCDSiCCDS44471.1. [O60502-4]
    CCDS7520.1. [O60502-1]
    PIRiT00360.
    RefSeqiNP_001135906.1. NM_001142434.1. [O60502-4]
    NP_036347.1. NM_012215.3. [O60502-1]
    UniGeneiHs.500842.

    Genome annotation databases

    EnsembliENST00000357797; ENSP00000350445; ENSG00000198408. [O60502-2]
    ENST00000361464; ENSP00000354850; ENSG00000198408. [O60502-1]
    ENST00000370094; ENSP00000359112; ENSG00000198408. [O60502-3]
    ENST00000439817; ENSP00000409973; ENSG00000198408. [O60502-4]
    GeneIDi10724.
    KEGGihsa:10724.
    UCSCiuc001ktv.2. human. [O60502-1]
    uc001ktw.2. human. [O60502-3]
    uc009xws.2. human. [O60502-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF036144 mRNA. Translation: AAD05385.2 .
    AF307332 mRNA. Translation: AAG21428.1 .
    AB014579 mRNA. Translation: BAA31654.2 . Different initiation.
    AC010789 Genomic DNA. No translation available.
    CH471066 Genomic DNA. Translation: EAW49744.1 .
    CH471066 Genomic DNA. Translation: EAW49741.1 .
    CH471066 Genomic DNA. Translation: EAW49742.1 .
    BC001343 mRNA. Translation: AAH01343.1 .
    BC039583 mRNA. Translation: AAH39583.2 .
    BC047877 mRNA. Translation: AAH47877.1 . Sequence problems.
    CCDSi CCDS44471.1. [O60502-4 ]
    CCDS7520.1. [O60502-1 ]
    PIRi T00360.
    RefSeqi NP_001135906.1. NM_001142434.1. [O60502-4 ]
    NP_036347.1. NM_012215.3. [O60502-1 ]
    UniGenei Hs.500842.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YDQ X-ray 2.60 T 402-408 [» ]
    ProteinModelPortali O60502.
    SMRi O60502. Positions 46-388, 717-916.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115948. 23 interactions.
    IntActi O60502. 17 interactions.
    STRINGi 9606.ENSP00000354850.

    Chemistry

    BindingDBi O60502.
    ChEMBLi CHEMBL5921.

    Protein family/group databases

    CAZyi GH84. Glycoside Hydrolase Family 84.

    PTM databases

    PhosphoSitei O60502.

    Proteomic databases

    MaxQBi O60502.
    PaxDbi O60502.
    PRIDEi O60502.

    Protocols and materials databases

    DNASUi 10724.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357797 ; ENSP00000350445 ; ENSG00000198408 . [O60502-2 ]
    ENST00000361464 ; ENSP00000354850 ; ENSG00000198408 . [O60502-1 ]
    ENST00000370094 ; ENSP00000359112 ; ENSG00000198408 . [O60502-3 ]
    ENST00000439817 ; ENSP00000409973 ; ENSG00000198408 . [O60502-4 ]
    GeneIDi 10724.
    KEGGi hsa:10724.
    UCSCi uc001ktv.2. human. [O60502-1 ]
    uc001ktw.2. human. [O60502-3 ]
    uc009xws.2. human. [O60502-2 ]

    Organism-specific databases

    CTDi 10724.
    GeneCardsi GC10M103534.
    HGNCi HGNC:7056. MGEA5.
    HPAi HPA036141.
    MIMi 604039. gene.
    neXtProti NX_O60502.
    PharmGKBi PA30787.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0454.
    HOVERGENi HBG053044.
    InParanoidi O60502.
    KOi K15719.
    OMAi LIKVDIH.
    OrthoDBi EOG7P02H7.
    PhylomeDBi O60502.
    TreeFami TF313732.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS03036-MONOMER.
    BRENDAi 3.2.1.35. 2681.

    Miscellaneous databases

    ChiTaRSi MGEA5. human.
    GeneWikii MGEA5.
    GenomeRNAii 10724.
    NextBioi 40709.
    PMAP-CutDB O60502.
    PROi O60502.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60502.
    Bgeei O60502.
    CleanExi HS_MGEA5.
    Genevestigatori O60502.

    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. "Novel immunogenic antigen homologous to hyaluronidase in meningioma."
      Heckel D., Comtesse N., Brass N., Blin N., Zang K.D., Meese E.
      Hum. Mol. Genet. 7:1859-1872(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
      Tissue: Meningioma.
    2. "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: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    3. "Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain."
      Gao Y., Wells L., Comer F.I., Parker G.J., Hart G.W.
      J. Biol. Chem. 276:9838-9845(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain.
    4. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    5. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    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. "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), VARIANT LYS-602.
      Tissue: Cervix, Eye and Skin.
    9. "Dynamic O-glycosylation of nuclear and cytosolic proteins: further characterization of the nucleocytoplasmic beta-N-acetylglucosaminidase, O-GlcNAcase."
      Wells L., Gao Y., Mahoney J.A., Vosseller K., Chen C., Rosen A., Hart G.W.
      J. Biol. Chem. 277:1755-1761(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, PTM, SUBCELLULAR LOCATION.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNCOAT_HUMAN
    AccessioniPrimary (citable) accession number: O60502
    Secondary accession number(s): B7WPB9
    , D3DR79, E9PGF9, O75166, Q86WV0, Q8IV98, Q9BVA5, Q9HAR0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 112 of the entry and version 2 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, Multifunctional enzyme, 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

    External Data

    Dasty 3