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Q9EQQ9

- NCOAT_MOUSE

UniProt

Q9EQQ9 - NCOAT_MOUSE

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Protein

Bifunctional protein NCOAT

Gene
Mgea5, Hexc, Kiaa0679
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 H4.1 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.

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
Complete GO annotation...

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
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
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.2 Publications

Protein-protein interaction databases

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

Structurei

3D structure databases

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

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni583 – 916334Histone acetyltransferase activity By 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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 698698Missing in isoform 2. VSP_020870Add
BLAST
Alternative sequencei1 – 11M → MVRPRVWRSSRRVASQNGLR AFGPTDRGRRGAVAGGRRM in isoform 3. VSP_020871
Alternative sequencei699 – 72527NDLFF…FPKDE → MYTTHSCLYSFFLTFFLVCC LTRLYFQ in isoform 2. VSP_020872Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61S → T in BAE26311. 1 Publication
Sequence conflicti52 – 532GA → RT in BAE26311. 1 Publication
Sequence conflicti742 – 7421F → S in BAC97998. 1 Publication

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

« 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, 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: July 9, 2014
This is version 95 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

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