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Protein O-GlcNAcase (OGA) (EC 3.2.1.169) (Beta-N-acetylglucosaminidase) (EC 3.2.1.-) (Beta-N-acetylhexosaminidase) (Beta-hexosaminidase) (Meningioma-expressed antigen 5) (N-acetyl-beta-D-glucosaminidase) (N-acetyl-beta-glucosaminidase) (Nuclear cytoplasmic O-GlcNAcase and acetyltransferase) (NCOAT)

 OGA_HUMAN               Reviewed;         916 AA.
O60502; B7WPB9; D3DR79; E9PGF9; O75166; Q86WV0; Q8IV98; Q9BVA5;
Q9HAR0;
03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 2.
22-NOV-2017, entry version 140.
RecName: Full=Protein O-GlcNAcase {ECO:0000303|PubMed:11148210, ECO:0000303|PubMed:11788610};
Short=OGA {ECO:0000303|PubMed:20863279};
EC=3.2.1.169 {ECO:0000269|PubMed:11148210, ECO:0000269|PubMed:11788610, ECO:0000269|PubMed:18586680, ECO:0000269|PubMed:20863279, ECO:0000269|PubMed:22365600, ECO:0000305|PubMed:20673219};
AltName: Full=Beta-N-acetylglucosaminidase {ECO:0000303|PubMed:11148210};
EC=3.2.1.- {ECO:0000269|PubMed:11148210, ECO:0000269|PubMed:11788610, ECO:0000269|PubMed:18586680, ECO:0000269|PubMed:20673219, ECO:0000269|PubMed:20863279, ECO:0000269|PubMed:22365600};
AltName: Full=Beta-N-acetylhexosaminidase;
AltName: Full=Beta-hexosaminidase;
AltName: Full=Meningioma-expressed antigen 5 {ECO:0000303|PubMed:9811929};
AltName: Full=N-acetyl-beta-D-glucosaminidase;
AltName: Full=N-acetyl-beta-glucosaminidase;
AltName: Full=Nuclear cytoplasmic O-GlcNAcase and acetyltransferase;
Short=NCOAT;
Name=MGEA5; Synonyms=HEXC, KIAA0679, MEA5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
TISSUE=Meningioma;
PubMed=9811929; DOI=10.1093/hmg/7.12.1859;
Heckel D., Comtesse N., Brass N., Blin N., Zang K.D., Meese E.;
"Novel immunogenic antigen homologous to hyaluronidase in
meningioma.";
Hum. Mol. Genet. 7:1859-1872(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 3), SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=11341771; DOI=10.1006/bbrc.2001.4815;
Comtesse N., Maldener E., Meese E.;
"Identification of a nuclear variant of MGEA5, a cytoplasmic
hyaluronidase and a beta-N-acetylglucosaminidase.";
Biochem. Biophys. Res. Commun. 283:634-640(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL
PROPERTIES, ENZYME REGULATION, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Brain;
PubMed=11148210; DOI=10.1074/jbc.M010420200;
Gao Y., Wells L., Comer F.I., Parker G.J., Hart G.W.;
"Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning
and characterization of a neutral, cytosolic beta-N-
acetylglucosaminidase from human brain.";
J. Biol. Chem. 276:9838-9845(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9734811; DOI=10.1093/dnares/5.3.169;
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
Nomura N., Ohara O.;
"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.";
DNA Res. 5:169-176(1998).
[5]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
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.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
LYS-602.
TISSUE=Cervix, Eye, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
PTM, AND SUBCELLULAR LOCATION.
PubMed=11788610; DOI=10.1074/jbc.M109656200;
Wells L., Gao Y., Mahoney J.A., Vosseller K., Chen C., Rosen A.,
Hart G.W.;
"Dynamic O-glycosylation of nuclear and cytosolic proteins: further
characterization of the nucleocytoplasmic beta-N-
acetylglucosaminidase, O-GlcNAcase.";
J. Biol. Chem. 277:1755-1761(2002).
[10]
ACTIVE SITE, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-174 AND
ASP-175.
PubMed=16533067; DOI=10.1021/bi052370b;
Cetinbas N., Macauley M.S., Stubbs K.A., Drapala R., Vocadlo D.J.;
"Identification of Asp174 and Asp175 as the key catalytic residues of
human O-GlcNAcase by functional analysis of site-directed mutants.";
Biochemistry 45:3835-3844(2006).
[11]
PTM, SITE, MUTAGENESIS OF ASP-413, AND CATALYTIC ACTIVITY.
PubMed=18586680; DOI=10.1074/jbc.M804116200;
Butkinaree C., Cheung W.D., Park S., Park K., Barber M., Hart G.W.;
"Characterization of beta-N-acetylglucosaminidase cleavage by caspase-
3 during apoptosis.";
J. Biol. Chem. 283:23557-23566(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-69; ASP-175;
VAL-255; TYR-286; ASP-287 AND TRP-679.
PubMed=20863279; DOI=10.1042/BJ20101338;
Schimpl M., Schuttelkopf A.W., Borodkin V.S., van Aalten D.M.;
"Human OGA binds substrates in a conserved peptide recognition
groove.";
Biochem. J. 432:1-7(2010).
[16]
FUNCTION OF ISOFORMS 1 AND 3, AND CATALYTIC ACTIVITY.
PubMed=20673219; DOI=10.1134/S0006297910070175;
Li J., Huang C.L., Zhang L.W., Lin L., Li Z.H., Zhang F.W., Wang P.;
"Isoforms of human O-GlcNAcase show distinct catalytic efficiencies.";
Biochemistry (Mosc.) 75:938-943(2010).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
LACK OF ACETYLTRANSFERASE ACTIVITY, AND FUNCTION.
PubMed=24088714; DOI=10.1098/rsob.130021;
Rao F.V., Schuttelkopf A.W., Dorfmueller H.C., Ferenbach A.T.,
Navratilova I., van Aalten D.M.;
"Structure of a bacterial putative acetyltransferase defines the fold
of the human O-GlcNAcase C-terminal domain.";
Open Biol. 3:130021-130021(2013).
[23]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 402-408, MUTAGENESIS OF
TYR-69, FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=22365600; DOI=10.1016/j.chembiol.2012.01.011;
Schimpl M., Borodkin V.S., Gray L.J., van Aalten D.M.;
"Synergy of peptide and sugar in O-GlcNAcase substrate recognition.";
Chem. Biol. 19:173-178(2012).
-!- FUNCTION: 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).
{ECO:0000269|PubMed:11148210, ECO:0000269|PubMed:11788610,
ECO:0000269|PubMed:20673219, ECO:0000269|PubMed:22365600,
ECO:0000269|PubMed:24088714}.
-!- FUNCTION: 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. {ECO:0000269|PubMed:20673219}.
-!- CATALYTIC ACTIVITY: [Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-
L-serine + H(2)O = [protein]-L-serine + N-acetyl-D-glucosamine.
{ECO:0000269|PubMed:11148210, ECO:0000269|PubMed:11788610,
ECO:0000269|PubMed:18586680, ECO:0000269|PubMed:20863279,
ECO:0000269|PubMed:22365600, ECO:0000305|PubMed:20673219}.
-!- CATALYTIC ACTIVITY: [Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-
L-threonine + H(2)O = [protein]-L-threonine + N-acetyl-D-
glucosamine. {ECO:0000269|PubMed:11148210,
ECO:0000269|PubMed:11788610, ECO:0000269|PubMed:18586680,
ECO:0000269|PubMed:20863279, ECO:0000269|PubMed:22365600,
ECO:0000305|PubMed:20673219}.
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing N-acetyl-
D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
{ECO:0000269|PubMed:11148210, ECO:0000269|PubMed:11788610,
ECO:0000269|PubMed:18586680, ECO:0000269|PubMed:20673219,
ECO:0000269|PubMed:20863279, ECO:0000269|PubMed:22365600}.
-!- ENZYME REGULATION: Inhibited by N-acetylglucosamine and not N-
acetylgalactosamine. {ECO:0000269|PubMed:11148210}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.1 mM for pNP-GlcNAc {ECO:0000269|PubMed:11788610};
Vmax=652 umol/min/mg enzyme with pNP-GLcNAc as substrate
{ECO:0000269|PubMed:11788610};
pH dependence:
Optimum pH is 5.7-7. {ECO:0000269|PubMed:11148210};
-!- SUBUNIT: Monomer (PubMed:11788610). Interacts with CLOCK (By
similarity). {ECO:0000250|UniProtKB:Q9EQQ9,
ECO:0000269|PubMed:11788610}.
-!- SUBCELLULAR LOCATION: Isoform 3: Nucleus
{ECO:0000269|PubMed:11341771}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm
{ECO:0000269|PubMed:11148210, ECO:0000269|PubMed:11341771,
ECO:0000269|PubMed:11788610}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=O60502-1; Sequence=Displayed;
Name=2;
IsoId=O60502-2; Sequence=VSP_020866, VSP_020869;
Name=3; Synonyms=MGEA5s;
IsoId=O60502-3; Sequence=VSP_020867, VSP_020868;
Name=4;
IsoId=O60502-4; Sequence=VSP_020866;
-!- TISSUE SPECIFICITY: Ubiquitous. Shows highest expression in the
brain, placenta and pancreas. {ECO:0000269|PubMed:11148210,
ECO:0000269|PubMed:11341771}.
-!- PTM: Proteolytically cleaved by caspase-3 during apoptosis. The
fragments interact with each other; cleavage does not decrease
enzyme activity. {ECO:0000269|PubMed:11788610,
ECO:0000269|PubMed:18586680}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 84 family.
{ECO:0000305}.
-!- 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. {ECO:0000269|PubMed:24088714,
ECO:0000305|PubMed:24088714}.
-!- SEQUENCE CAUTION:
Sequence=AAH47877.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAA31654.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF036144; AAD05385.2; -; mRNA.
EMBL; AF307332; AAG21428.1; -; mRNA.
EMBL; AB014579; BAA31654.2; ALT_INIT; mRNA.
EMBL; AC010789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471066; EAW49744.1; -; Genomic_DNA.
EMBL; CH471066; EAW49741.1; -; Genomic_DNA.
EMBL; CH471066; EAW49742.1; -; Genomic_DNA.
EMBL; BC001343; AAH01343.1; -; mRNA.
EMBL; BC039583; AAH39583.2; -; mRNA.
EMBL; BC047877; AAH47877.1; ALT_SEQ; mRNA.
CCDS; CCDS44471.1; -. [O60502-4]
CCDS; CCDS7520.1; -. [O60502-1]
PIR; T00360; T00360.
RefSeq; NP_001135906.1; NM_001142434.1. [O60502-4]
RefSeq; NP_036347.1; NM_012215.3. [O60502-1]
UniGene; Hs.500842; -.
PDB; 2YDQ; X-ray; 2.60 A; T=402-408.
PDB; 5M7R; X-ray; 2.35 A; A/B=1-916.
PDB; 5M7S; X-ray; 2.40 A; A/B=1-916.
PDB; 5M7T; X-ray; 2.60 A; A/B=1-916.
PDB; 5M7U; X-ray; 2.30 A; A/B=1-916.
PDB; 5TKE; X-ray; 2.48 A; A/B=60-400, A/B=553-704.
PDB; 5UHK; X-ray; 2.97 A; A/C=56-400, B/D=544-705.
PDB; 5UHL; X-ray; 3.14 A; A/C=56-400, B/D=544-705.
PDB; 5UHO; X-ray; 3.21 A; A/C=56-400, B/D=544-705.
PDB; 5UHP; X-ray; 2.79 A; A/B/C/D=14-400, E/F/G/H=554-705.
PDB; 5UN8; X-ray; 2.13 A; A/B/C/D=60-400, A/B/C/D=553-704.
PDB; 5UN9; X-ray; 2.50 A; A/B=60-400, A/B=553-704.
PDB; 5VVO; X-ray; 2.60 A; A/B=60-400, A/B=553-704.
PDB; 5VVT; X-ray; 2.80 A; A/C=60-400, A/C=553-704.
PDB; 5VVU; X-ray; 2.70 A; A/C=60-400, A/C=553-704.
PDB; 5VVV; X-ray; 2.80 A; A/C=60-400, A/C=553-704.
PDB; 5VVX; X-ray; 2.90 A; A/C=60-400, A/C=553-704.
PDBsum; 2YDQ; -.
PDBsum; 5M7R; -.
PDBsum; 5M7S; -.
PDBsum; 5M7T; -.
PDBsum; 5M7U; -.
PDBsum; 5TKE; -.
PDBsum; 5UHK; -.
PDBsum; 5UHL; -.
PDBsum; 5UHO; -.
PDBsum; 5UHP; -.
PDBsum; 5UN8; -.
PDBsum; 5UN9; -.
PDBsum; 5VVO; -.
PDBsum; 5VVT; -.
PDBsum; 5VVU; -.
PDBsum; 5VVV; -.
PDBsum; 5VVX; -.
ProteinModelPortal; O60502; -.
SMR; O60502; -.
BioGrid; 115948; 36.
IntAct; O60502; 20.
STRING; 9606.ENSP00000354850; -.
BindingDB; O60502; -.
ChEMBL; CHEMBL5921; -.
CAZy; GH84; Glycoside Hydrolase Family 84.
iPTMnet; O60502; -.
PhosphoSitePlus; O60502; -.
BioMuta; MGEA5; -.
EPD; O60502; -.
MaxQB; O60502; -.
PaxDb; O60502; -.
PeptideAtlas; O60502; -.
PRIDE; O60502; -.
DNASU; 10724; -.
Ensembl; ENST00000357797; ENSP00000350445; ENSG00000198408. [O60502-2]
Ensembl; ENST00000361464; ENSP00000354850; ENSG00000198408. [O60502-1]
Ensembl; ENST00000370094; ENSP00000359112; ENSG00000198408. [O60502-3]
Ensembl; ENST00000439817; ENSP00000409973; ENSG00000198408. [O60502-4]
GeneID; 10724; -.
KEGG; hsa:10724; -.
UCSC; uc001ktv.3; human. [O60502-1]
CTD; 10724; -.
DisGeNET; 10724; -.
EuPathDB; HostDB:ENSG00000198408.13; -.
GeneCards; MGEA5; -.
HGNC; HGNC:7056; MGEA5.
HPA; HPA036141; -.
HPA; HPA076501; -.
MIM; 604039; gene.
neXtProt; NX_O60502; -.
OpenTargets; ENSG00000198408; -.
PharmGKB; PA30787; -.
eggNOG; KOG3698; Eukaryota.
eggNOG; ENOG410XPBQ; LUCA.
GeneTree; ENSGT00390000007726; -.
HOVERGEN; HBG053044; -.
InParanoid; O60502; -.
KO; K15719; -.
OMA; WLGCRSQ; -.
OrthoDB; EOG091G02T9; -.
PhylomeDB; O60502; -.
TreeFam; TF313732; -.
BioCyc; MetaCyc:HS03036-MONOMER; -.
BRENDA; 3.2.1.35; 2681.
ChiTaRS; MGEA5; human.
GeneWiki; MGEA5; -.
GenomeRNAi; 10724; -.
PMAP-CutDB; O60502; -.
PRO; PR:O60502; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000198408; -.
CleanEx; HS_MGEA5; -.
ExpressionAtlas; O60502; baseline and differential.
Genevisible; O60502; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0102167; F:[protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine O-N-acetyl-alpha-D-glucosaminase activity; IEA:UniProtKB-EC.
GO; GO:0102571; F:[protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine/L-threonine O-N-acetyl-alpha-D-glucosaminase activity; IEA:UniProtKB-EC.
GO; GO:0102166; F:[protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine O-N-acetyl-alpha-D-glucosaminase activity; IEA:UniProtKB-EC.
GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; IDA:UniProtKB.
GO; GO:0004415; F:hyalurononglucosaminidase activity; TAS:ProtInc.
GO; GO:0006516; P:glycoprotein catabolic process; TAS:ProtInc.
GO; GO:0006044; P:N-acetylglucosamine metabolic process; IDA:UniProtKB.
GO; GO:0006517; P:protein deglycosylation; IDA:UniProtKB.
GO; GO:0006493; P:protein O-linked glycosylation; NAS:ParkinsonsUK-UCL.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR011496; Beta-N-acetylglucosaminidase.
InterPro; IPR017853; Glycoside_hydrolase_SF.
Pfam; PF07555; NAGidase; 1.
SUPFAM; SSF51445; SSF51445; 1.
SUPFAM; SSF55729; SSF55729; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Glycosidase; Hydrolase; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome.
CHAIN 1 916 Protein O-GlcNAcase.
/FTId=PRO_0000252118.
REGION 278 280 Substrate binding.
{ECO:0000250|UniProtKB:Q2CEE3}.
ACT_SITE 175 175 Proton donor.
{ECO:0000305|PubMed:16533067}.
BINDING 67 67 Substrate; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q2CEE3}.
BINDING 98 98 Substrate.
{ECO:0000250|UniProtKB:Q0TR53}.
BINDING 174 174 Substrate.
{ECO:0000250|UniProtKB:Q0TR53}.
BINDING 219 219 Substrate.
{ECO:0000250|UniProtKB:Q2CEE3}.
BINDING 285 285 Substrate.
{ECO:0000250|UniProtKB:Q2CEE3}.
BINDING 313 313 Substrate.
{ECO:0000250|UniProtKB:Q2CEE3}.
SITE 413 414 Cleavage; by caspase-3.
{ECO:0000269|PubMed:18586680}.
MOD_RES 364 364 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 346 398 Missing (in isoform 2 and isoform 4).
{ECO:0000305}.
/FTId=VSP_020866.
VAR_SEQ 663 677 CRSHSSAQFLIGDQE -> RCTRNNLFSSNILSL (in
isoform 3). {ECO:0000303|PubMed:9811929}.
/FTId=VSP_020867.
VAR_SEQ 678 916 Missing (in isoform 3).
{ECO:0000303|PubMed:9811929}.
/FTId=VSP_020868.
VAR_SEQ 691 704 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_020869.
VARIANT 46 46 G -> E (in dbSNP:rs3740421).
/FTId=VAR_027761.
VARIANT 602 602 E -> K (in dbSNP:rs17853930).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_027762.
MUTAGEN 69 69 Y->K,Q: Strongly reduces affinity for
glycopeptide substrates. Nearly abolishes
enzyme activity.
{ECO:0000269|PubMed:20863279,
ECO:0000269|PubMed:22365600}.
MUTAGEN 69 69 Y->S: Strongly reduces affinity for
glycopeptide substrates. Nearly abolishes
enzyme activity.
{ECO:0000269|PubMed:20863279,
ECO:0000269|PubMed:22365600}.
MUTAGEN 174 174 D->A: Nearly abolishes enzyme activity.
{ECO:0000269|PubMed:16533067}.
MUTAGEN 175 175 D->A: Nearly abolishes enzyme activity.
{ECO:0000269|PubMed:16533067}.
MUTAGEN 175 175 D->N: Nearly abolishes enzyme activity.
{ECO:0000269|PubMed:20863279}.
MUTAGEN 255 255 V->G,T: Nearly abolishes enzyme activity.
{ECO:0000269|PubMed:20863279}.
MUTAGEN 286 286 Y->S: Nearly abolishes enzyme activity.
{ECO:0000269|PubMed:20863279}.
MUTAGEN 287 287 D->A: Nearly abolishes enzyme activity.
{ECO:0000269|PubMed:20863279}.
MUTAGEN 413 413 D->A: Abrogates cleavage by caspase-3.
{ECO:0000269|PubMed:18586680}.
MUTAGEN 679 679 W->N: Nearly abolishes enzyme activity.
{ECO:0000269|PubMed:20863279}.
TURN 54 57 {ECO:0000244|PDB:5UHP}.
STRAND 61 66 {ECO:0000244|PDB:5UN8}.
STRAND 69 71 {ECO:0000244|PDB:5UN8}.
HELIX 75 87 {ECO:0000244|PDB:5UN8}.
STRAND 92 95 {ECO:0000244|PDB:5UN8}.
HELIX 101 103 {ECO:0000244|PDB:5UN8}.
TURN 104 108 {ECO:0000244|PDB:5UN8}.
HELIX 113 128 {ECO:0000244|PDB:5UN8}.
STRAND 132 137 {ECO:0000244|PDB:5UN8}.
TURN 140 142 {ECO:0000244|PDB:5UN8}.
HELIX 148 162 {ECO:0000244|PDB:5UN8}.
TURN 163 165 {ECO:0000244|PDB:5UN8}.
STRAND 168 172 {ECO:0000244|PDB:5UN8}.
HELIX 182 187 {ECO:0000244|PDB:5UN8}.
HELIX 191 205 {ECO:0000244|PDB:5UN8}.
STRAND 212 215 {ECO:0000244|PDB:5UN8}.
HELIX 221 223 {ECO:0000244|PDB:5UN8}.
STRAND 224 226 {ECO:0000244|PDB:5UN8}.
TURN 228 230 {ECO:0000244|PDB:5M7R}.
HELIX 232 240 {ECO:0000244|PDB:5UN8}.
STRAND 245 249 {ECO:0000244|PDB:5UN8}.
STRAND 252 255 {ECO:0000244|PDB:5UN8}.
HELIX 261 271 {ECO:0000244|PDB:5UN8}.
STRAND 276 279 {ECO:0000244|PDB:5UN8}.
HELIX 285 287 {ECO:0000244|PDB:5UHK}.
HELIX 301 306 {ECO:0000244|PDB:5UN8}.
STRAND 308 312 {ECO:0000244|PDB:5UN8}.
HELIX 318 321 {ECO:0000244|PDB:5UN8}.
HELIX 322 332 {ECO:0000244|PDB:5UN8}.
TURN 334 337 {ECO:0000244|PDB:5UHL}.
HELIX 376 388 {ECO:0000244|PDB:5UN8}.
TURN 389 391 {ECO:0000244|PDB:5M7R}.
STRAND 542 544 {ECO:0000244|PDB:5M7T}.
HELIX 555 564 {ECO:0000244|PDB:5UN8}.
HELIX 573 587 {ECO:0000244|PDB:5UN8}.
HELIX 589 591 {ECO:0000244|PDB:5UN8}.
HELIX 605 628 {ECO:0000244|PDB:5UN8}.
HELIX 634 661 {ECO:0000244|PDB:5UN8}.
TURN 662 666 {ECO:0000244|PDB:5M7R}.
TURN 680 683 {ECO:0000244|PDB:5UN8}.
HELIX 684 692 {ECO:0000244|PDB:5UN8}.
TURN 694 699 {ECO:0000244|PDB:5UN8}.
TURN 710 712 {ECO:0000244|PDB:5M7R}.
SEQUENCE 916 AA; 102915 MW; 01F8A64A9B1475C6 CRC64;
MVQKESQATL EERESELSSN PAASAGASLE PPAAPAPGED NPAGAGGAAV AGAAGGARRF
LCGVVEGFYG RPWVMEQRKE LFRRLQKWEL NTYLYAPKDD YKHRMFWREM YSVEEAEQLM
TLISAAREYE IEFIYAISPG LDITFSNPKE VSTLKRKLDQ VSQFGCRSFA LLFDDIDHNM
CAADKEVFSS FAHAQVSITN EIYQYLGEPE TFLFCPTEYC GTFCYPNVSQ SPYLRTVGEK
LLPGIEVLWT GPKVVSKEIP VESIEEVSKI IKRAPVIWDN IHANDYDQKR LFLGPYKGRS
TELIPRLKGV LTNPNCEFEA NYVAIHTLAT WYKSNMNGVR KDVVMTDSED STVSIQIKLE
NEGSDEDIET DVLYSPQMAL KLALTEWLQE FGVPHQYSSR QVAHSGAKAS VVDGTPLVAA
PSLNATTVVT TVYQEPIMSQ GAALSGEPTT LTKEEEKKQP DEEPMDMVVE KQEETDHKND
NQILSEIVEA KMAEELKPMD TDKESIAESK SPEMSMQEDC ISDIAPMQTD EQTNKEQFVP
GPNEKPLYTA EPVTLEDLQL LADLFYLPYE HGPKGAQMLR EFQWLRANSS VVSVNCKGKD
SEKIEEWRSR AAKFEEMCGL VMGMFTRLSN CANRTILYDM YSYVWDIKSI MSMVKSFVQW
LGCRSHSSAQ FLIGDQEPWA FRGGLAGEFQ RLLPIDGAND LFFQPPPLTP TSKVYTIRPY
FPKDEASVYK ICREMYDDGV GLPFQSQPDL IGDKLVGGLL SLSLDYCFVL EDEDGICGYA
LGTVDVTPFI KKCKISWIPF MQEKYTKPNG DKELSEAEKI MLSFHEEQEV LPETFLANFP
SLIKMDIHKK VTDPSVAKSM MACLLSSLKA NGSRGAFCEV RPDDKRILEF YSKLGCFEIA
KMEGFPKDVV ILGRSL


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