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Q9EQQ9

- OGA_MOUSE

UniProt

Q9EQQ9 - OGA_MOUSE

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Protein

Protein O-GlcNAcase

Gene

Mgea5

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  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

Glycosidase, Hydrolase

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: Chromosome 19

Organism-specific databases

MGIiMGI:1932139. Mgea5.

Subcellular locationi

Nucleus By similarity. Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
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.
GenevestigatoriQ9EQQ9.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

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

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.
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

        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. Reason: 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]
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.
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 61-331, 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

Bgeei Q9EQQ9.
CleanExi MM_MGEA5.
ExpressionAtlasi Q9EQQ9. baseline and differential.
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.
  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: November 26, 2014
This is version 98 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, 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