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Protein

Protein O-GlcNAcase

Gene

MGEA5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Isoform 1: 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:11148210). Does not bind acetyl-CoA and does not have histone acetyltransferase activity (PubMed:24088714).5 Publications
Isoform 3: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc as substrate but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro), but has about six times lower specific activity than isoform 1.1 Publication

Catalytic activityi

[Protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine + H2O = [protein]-L-serine + N-acetyl-D-glucosamine.1 Publication5 Publications
[Protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine + H2O = [protein]-L-threonine + N-acetyl-D-glucosamine.1 Publication5 Publications
Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.6 Publications

Enzyme regulationi

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

Kineticsi

  1. KM=1.1 mM for pNP-GlcNAc1 Publication

Vmax=652 µmol/min/mg enzyme with pNP-GLcNAc as substrate1 Publication

pH dependencei

Optimum pH is 5.7-7.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei67 – 671Substrate; via carbonyl oxygenBy similarity
Binding sitei98 – 981SubstrateBy similarity
Binding sitei174 – 1741SubstrateBy similarity
Active sitei175 – 1751Proton donor1 Publication
Binding sitei219 – 2191SubstrateBy similarity
Binding sitei285 – 2851SubstrateBy similarity
Binding sitei313 – 3131SubstrateBy similarity
Sitei413 – 4142Cleavage; by caspase-31 Publication

GO - Molecular functioni

  1. beta-N-acetylglucosaminidase activity Source: UniProtKB
  2. histone acetyltransferase activity Source: Ensembl
  3. 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: UniProtKB
  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 deglycosylation Source: UniProtKB
  18. protein targeting to membrane Source: Ensembl
  19. response to steroid hormone Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

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:
Protein O-GlcNAcase2 Publications (EC:3.2.1.1691 Publication5 Publications)
Short name:
OGA1 Publication
Alternative name(s):
Beta-N-acetylglucosaminidase1 Publication (EC:3.2.1.-6 Publications)
Beta-N-acetylhexosaminidase
Beta-hexosaminidase
Meningioma-expressed antigen 51 Publication
N-acetyl-beta-D-glucosaminidase
N-acetyl-beta-glucosaminidase
Nuclear cytoplasmic O-GlcNAcase and acetyltransferase
Short name:
NCOAT
Gene namesi
Name:MGEA5
Synonyms:HEXC, KIAA0679, MEA5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:7056. MGEA5.

Subcellular locationi

Isoform 3 : Nucleus 1 Publication
Isoform 1 : Cytoplasm 3 Publications

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. membrane Source: UniProtKB
  3. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi69 – 691Y → K or Q: Strongly reduces affinity for glycopeptide substrates. Nearly abolishes enzyme activity. 2 Publications
Mutagenesisi69 – 691Y → S: Strongly reduces affinity for glycopeptide substrates. Nearly abolishes enzyme activity. 2 Publications
Mutagenesisi174 – 1741D → A: Nearly abolishes enzyme activity. 1 Publication
Mutagenesisi175 – 1751D → A: Nearly abolishes enzyme activity. 1 Publication
Mutagenesisi175 – 1751D → N: Nearly abolishes enzyme activity. 1 Publication
Mutagenesisi255 – 2551V → G or T: Nearly abolishes enzyme activity. 1 Publication
Mutagenesisi286 – 2861Y → S: Nearly abolishes enzyme activity. 1 Publication
Mutagenesisi287 – 2871D → A: Nearly abolishes enzyme activity. 1 Publication
Mutagenesisi413 – 4131D → A: Abrogates cleavage by caspase-3. 1 Publication
Mutagenesisi679 – 6791W → N: Nearly abolishes enzyme activity. 1 Publication

Organism-specific databases

PharmGKBiPA30787.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 916916Protein O-GlcNAcasePRO_0000252118Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei364 – 3641Phosphoserine4 Publications

Post-translational modificationi

Proteolytically cleaved by caspase-3 during apoptosis. The fragments interact with each other; cleavage does not decrease enzyme activity.2 Publications

Keywords - PTMi

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

BgeeiO60502.
CleanExiHS_MGEA5.
ExpressionAtlasiO60502. baseline and differential.
GenevestigatoriO60502.

Organism-specific databases

HPAiHPA036141.

Interactioni

Subunit structurei

Monomer (PubMed:11788610). Interacts with CLOCK (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi115948. 27 interactions.
IntActiO60502. 17 interactions.
STRINGi9606.ENSP00000354850.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YDQX-ray2.60T402-408[»]
ProteinModelPortaliO60502.
SMRiO60502. 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.
InParanoidiO60502.
KOiK15719.
OMAiMSGDQEP.
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. AlignAdd to basket

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

        10         20         30         40         50
MVQKESQATL EERESELSSN PAASAGASLE PPAAPAPGED NPAGAGGAAV
60 70 80 90 100
AGAAGGARRF 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
QVAHSGAKAS VVDGTPLVAA PSLNATTVVT TVYQEPIMSQ GAALSGEPTT
460 470 480 490 500
LTKEEEKKQP DEEPMDMVVE KQEETDHKND NQILSEIVEA KMAEELKPMD
510 520 530 540 550
TDKESIAESK SPEMSMQEDC ISDIAPMQTD EQTNKEQFVP GPNEKPLYTA
560 570 580 590 600
EPVTLEDLQL LADLFYLPYE HGPKGAQMLR EFQWLRANSS VVSVNCKGKD
610 620 630 640 650
SEKIEEWRSR AAKFEEMCGL VMGMFTRLSN CANRTILYDM YSYVWDIKSI
660 670 680 690 700
MSMVKSFVQW LGCRSHSSAQ FLIGDQEPWA FRGGLAGEFQ RLLPIDGAND
710 720 730 740 750
LFFQPPPLTP TSKVYTIRPY FPKDEASVYK ICREMYDDGV GLPFQSQPDL
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):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.Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAA31654.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YDQX-ray2.60T402-408[»]
ProteinModelPortaliO60502.
SMRiO60502. Positions 61-331, 717-916.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115948. 27 interactions.
IntActiO60502. 17 interactions.
STRINGi9606.ENSP00000354850.

Chemistry

BindingDBiO60502.
ChEMBLiCHEMBL5921.

Protein family/group databases

CAZyiGH84. Glycoside Hydrolase Family 84.

PTM databases

PhosphoSiteiO60502.

Proteomic databases

MaxQBiO60502.
PaxDbiO60502.
PRIDEiO60502.

Protocols and materials databases

DNASUi10724.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi10724.
GeneCardsiGC10M103534.
HGNCiHGNC:7056. MGEA5.
HPAiHPA036141.
MIMi604039. gene.
neXtProtiNX_O60502.
PharmGKBiPA30787.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0454.
GeneTreeiENSGT00390000007726.
HOVERGENiHBG053044.
InParanoidiO60502.
KOiK15719.
OMAiMSGDQEP.
OrthoDBiEOG7P02H7.
PhylomeDBiO60502.
TreeFamiTF313732.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiMGEA5. human.
GeneWikiiMGEA5.
GenomeRNAii10724.
NextBioi40709.
PMAP-CutDBO60502.
PROiO60502.
SOURCEiSearch...

Gene expression databases

BgeeiO60502.
CleanExiHS_MGEA5.
ExpressionAtlasiO60502. baseline and differential.
GenevestigatoriO60502.

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. "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(1997) [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(2000) [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(2000) [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(1997) [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(2001) [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(2003) [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(2003) [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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, PTM, SUBCELLULAR LOCATION.
  10. "Identification of Asp174 and Asp175 as the key catalytic residues of human O-GlcNAcase by functional analysis of site-directed mutants."
    Cetinbas N., Macauley M.S., Stubbs K.A., Drapala R., Vocadlo D.J.
    Biochemistry 45:3835-3844(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-174 AND ASP-175.
  11. "Characterization of beta-N-acetylglucosaminidase cleavage by caspase-3 during apoptosis."
    Butkinaree C., Cheung W.D., Park S., Park K., Barber M., Hart G.W.
    J. Biol. Chem. 283:23557-23566(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PTM, SITE, MUTAGENESIS OF ASP-413, CATALYTIC ACTIVITY.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Human OGA binds substrates in a conserved peptide recognition groove."
    Schimpl M., Schuttelkopf A.W., Borodkin V.S., van Aalten D.M.
    Biochem. J. 432:1-7(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF TYR-69; ASP-175; VAL-255; TYR-286; ASP-287 AND TRP-679.
  16. "Isoforms of human O-GlcNAcase show distinct catalytic efficiencies."
    Li J., Huang C.L., Zhang L.W., Lin L., Li Z.H., Zhang F.W., Wang P.
    Biochemistry (Mosc.) 75:938-943(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF ISOFORMS 1 AND 3, CATALYTIC ACTIVITY.
  17. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Structure of a bacterial putative acetyltransferase defines the fold of the human O-GlcNAcase C-terminal domain."
    Rao F.V., Schuttelkopf A.W., Dorfmueller H.C., Ferenbach A.T., Navratilova I., van Aalten D.M.
    Open Biol. 3:130021-130021(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: LACK OF ACETYLTRANSFERASE ACTIVITY, FUNCTION.
  22. "Synergy of peptide and sugar in O-GlcNAcase substrate recognition."
    Schimpl M., Borodkin V.S., Gray L.J., van Aalten D.M.
    Chem. Biol. 19:173-178(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 402-408, MUTAGENESIS OF TYR-69, FUNCTION, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiOGA_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: January 7, 2015
This is version 115 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

Caution

The mouse and rat orthologs were initially identified as bi-functional proteins containing an N-terminal domain with O-GlcNAcase activity and a C-terminal domain with histone acetyltransferase activity. 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. Comparison of the human protein with a bacterial putative acetyltransferase (AC Q2CEE2) shows that the residues important for acetyl-CoA binding are not conserved, and that the residues proposed to be important for histone acetyltransferase activity are not in a position where they could participate in catalysis. Characterization of the human protein shows that it does not bind acetyl-CoA and therefore cannot have acetyltransferase activity.1 Publication1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.