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O60502 (NCOAT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional protein NCOAT
Alternative name(s):
Meningioma-expressed antigen 5
Nuclear cytoplasmic O-GlcNAcase and acetyltransferase

Including the following 2 domains:

  1. 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
  2. Histone acetyltransferase
    Short name=HAT
    EC=2.3.1.48
Gene names
Name:MGEA5
Synonyms:HEXC, KIAA0679, MEA5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length916 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleaves GlcNAc but not GalNAc from glycopeptides. Can use p-nitrophenyl-beta-GlcNAc as substrate but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc. Possesses hyaluronidase activity. Acetylates 'Lys-8' of histone H4 and 'Lys-14' of histone H3. Ref.3 Ref.9

Catalytic activity

[Protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine + H2O = [protein]-L-serine + N-acetyl-D-glucosamine. Ref.3 Ref.9

[Protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine + H2O = [protein]-L-threonine + N-acetyl-D-glucosamine.

Acetyl-CoA + [histone] = CoA + acetyl-[histone]. Ref.3 Ref.9

Enzyme regulation

Inhibited by N-acetylglucosamine and not N-acetylgalactosamine. Ref.3

Subunit structure

Monomer. Binds both acetylated and unacetylated histone H4 tail but acetylation on 'Lys-8' of histone H4 abolishes binding. Interacts with CLOCK By similarity. Ref.9

Subcellular location

Isoform 3: Nucleus Ref.2 Ref.3 Ref.9.

Isoform 1: Cytoplasm Ref.2 Ref.3 Ref.9.

Tissue specificity

Ubiquitous. Shows highest expression in the brain, placenta and pancreas. Ref.2 Ref.3

Post-translational modification

Proteolytically cleaved by caspase-3.

Biophysicochemical properties

Kinetic parameters:

KM=1.1 mM for pNP-GlcNAc Ref.3 Ref.9

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

pH dependence:

Optimum pH is 5.7-7.

Sequence caution

The sequence AAH47877.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence BAA31654.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionAcyltransferase
Glycosidase
Hydrolase
Transferase
   PTMDisulfide bond
Phosphoprotein
   Technical term3D-structure
Complete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processN-acetylglucosamine metabolic process

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from electronic annotation. Source: Ensembl

dATP metabolic process

Inferred from electronic annotation. Source: Ensembl

glycoprotein catabolic process

Traceable author statement Ref.1. Source: ProtInc

necrotic cell death

Inferred from electronic annotation. Source: Ensembl

negative regulation of cardiac muscle adaptation

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein glycosylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of calcium ion transport into cytosol

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell killing

Inferred from electronic annotation. Source: Ensembl

positive regulation of glucose import

Inferred from electronic annotation. Source: Ensembl

positive regulation of growth hormone secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of insulin secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitochondrial depolarization

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein complex disassembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of proteolysis

Inferred from electronic annotation. Source: Ensembl

protein targeting to membrane

Inferred from electronic annotation. Source: Ensembl

response to steroid hormone

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionhistone acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

hyalurononglucosaminidase activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60502-1)

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.
Isoform 2 (identifier: O60502-2)

The sequence of this isoform differs from the canonical sequence as follows:
     346-398: Missing.
     691-704: Missing.
Isoform 3 (identifier: O60502-3)

Also known as: MGEA5s;

The sequence of this isoform differs from the canonical sequence as follows:
     663-677: CRSHSSAQFLIGDQE → RCTRNNLFSSNILSL
     678-916: Missing.
Isoform 4 (identifier: O60502-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 916916Bifunctional protein NCOAT
PRO_0000252118

Regions

Region583 – 916334Histone acetyltransferase activity By similarity
Region695 – 814120Required for histone H4 binding By similarity

Sites

Active site1751Nucleophile; for O-GlcNAcase activity By similarity
Active site1771Proton donor; for O-GlcNAcase activity By similarity

Amino acid modifications

Modified residue3641Phosphoserine Ref.10 Ref.12 Ref.13 Ref.15
Disulfide bond777 ↔ 793 By similarity

Natural variations

Alternative sequence346 – 39853Missing in isoform 2 and isoform 4.
VSP_020866
Alternative sequence663 – 67715CRSHS…IGDQE → RCTRNNLFSSNILSL in isoform 3.
VSP_020867
Alternative sequence678 – 916239Missing in isoform 3.
VSP_020868
Alternative sequence691 – 70414Missing in isoform 2.
VSP_020869
Natural variant461G → E.
Corresponds to variant rs3740421 [ dbSNP | Ensembl ].
VAR_027761
Natural variant6021E → K. Ref.8
Corresponds to variant rs17853930 [ dbSNP | Ensembl ].
VAR_027762

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 2.
Checksum: 01F8A64A9B1475C6

FASTA916102,915
        10         20         30         40         50         60 
MVQKESQATL EERESELSSN PAASAGASLE PPAAPAPGED NPAGAGGAAV AGAAGGARRF 

        70         80         90        100        110        120 
LCGVVEGFYG RPWVMEQRKE LFRRLQKWEL NTYLYAPKDD YKHRMFWREM YSVEEAEQLM 

       130        140        150        160        170        180 
TLISAAREYE IEFIYAISPG LDITFSNPKE VSTLKRKLDQ VSQFGCRSFA LLFDDIDHNM 

       190        200        210        220        230        240 
CAADKEVFSS FAHAQVSITN EIYQYLGEPE TFLFCPTEYC GTFCYPNVSQ SPYLRTVGEK 

       250        260        270        280        290        300 
LLPGIEVLWT GPKVVSKEIP VESIEEVSKI IKRAPVIWDN IHANDYDQKR LFLGPYKGRS 

       310        320        330        340        350        360 
TELIPRLKGV LTNPNCEFEA NYVAIHTLAT WYKSNMNGVR KDVVMTDSED STVSIQIKLE 

       370        380        390        400        410        420 
NEGSDEDIET DVLYSPQMAL KLALTEWLQE FGVPHQYSSR QVAHSGAKAS VVDGTPLVAA 

       430        440        450        460        470        480 
PSLNATTVVT TVYQEPIMSQ GAALSGEPTT LTKEEEKKQP DEEPMDMVVE KQEETDHKND 

       490        500        510        520        530        540 
NQILSEIVEA KMAEELKPMD TDKESIAESK SPEMSMQEDC ISDIAPMQTD EQTNKEQFVP 

       550        560        570        580        590        600 
GPNEKPLYTA EPVTLEDLQL LADLFYLPYE HGPKGAQMLR EFQWLRANSS VVSVNCKGKD 

       610        620        630        640        650        660 
SEKIEEWRSR AAKFEEMCGL VMGMFTRLSN CANRTILYDM YSYVWDIKSI MSMVKSFVQW 

       670        680        690        700        710        720 
LGCRSHSSAQ FLIGDQEPWA FRGGLAGEFQ RLLPIDGAND LFFQPPPLTP TSKVYTIRPY 

       730        740        750        760        770        780 
FPKDEASVYK ICREMYDDGV GLPFQSQPDL IGDKLVGGLL SLSLDYCFVL EDEDGICGYA 

       790        800        810        820        830        840 
LGTVDVTPFI KKCKISWIPF MQEKYTKPNG DKELSEAEKI MLSFHEEQEV LPETFLANFP 

       850        860        870        880        890        900 
SLIKMDIHKK VTDPSVAKSM MACLLSSLKA NGSRGAFCEV RPDDKRILEF YSKLGCFEIA 

       910 
KMEGFPKDVV ILGRSL 

« Hide

Isoform 2 [UniParc].

Checksum: A65EFD64BE0AD17C
Show »

FASTA84995,331
Isoform 3 (MGEA5s) [UniParc].

Checksum: BF83DEF3ABDE4AA8
Show »

FASTA67776,193
Isoform 4 [UniParc].

Checksum: D6AB77EE6830F570
Show »

FASTA86396,932

References

« Hide 'large scale' references
[1]"Novel immunogenic antigen homologous to hyaluronidase in meningioma."
Heckel D., Comtesse N., Brass N., Blin N., Zang K.D., Meese E.
Hum. Mol. Genet. 7:1859-1872(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
Tissue: Meningioma.
[2]"Identification of a nuclear variant of MGEA5, a cytoplasmic hyaluronidase and a beta-N-acetylglucosaminidase."
Comtesse N., Maldener E., Meese E.
Biochem. Biophys. Res. Commun. 283:634-640(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]"Dynamic O-glycosylation of nuclear and cytosolic proteins: cloning and characterization of a neutral, cytosolic beta-N-acetylglucosaminidase from human brain."
Gao Y., Wells L., Comer F.I., Parker G.J., Hart G.W.
J. Biol. Chem. 276:9838-9845(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain.
[4]"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[5]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[6]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LYS-602.
Tissue: Cervix, Eye and Skin.
[9]"Dynamic O-glycosylation of nuclear and cytosolic proteins: further characterization of the nucleocytoplasmic beta-N-acetylglucosaminidase, O-GlcNAcase."
Wells L., Gao Y., Mahoney J.A., Vosseller K., Chen C., Rosen A., Hart G.W.
J. Biol. Chem. 277:1755-1761(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, PTM, SUBCELLULAR LOCATION.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS7520.1. [O60502-1]
PIRT00360.
RefSeqNP_001135906.1. NM_001142434.1. [O60502-4]
NP_036347.1. NM_012215.3. [O60502-1]
UniGeneHs.500842.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YDQX-ray2.60T402-408[»]
ProteinModelPortalO60502.
SMRO60502. Positions 46-388, 717-916.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115948. 23 interactions.
IntActO60502. 14 interactions.
STRING9606.ENSP00000354850.

Chemistry

BindingDBO60502.
ChEMBLCHEMBL5921.

Protein family/group databases

CAZyGH84. Glycoside Hydrolase Family 84.

PTM databases

PhosphoSiteO60502.

Proteomic databases

MaxQBO60502.
PaxDbO60502.
PRIDEO60502.

Protocols and materials databases

DNASU10724.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357797; ENSP00000350445; ENSG00000198408. [O60502-2]
ENST00000361464; ENSP00000354850; ENSG00000198408. [O60502-1]
ENST00000370094; ENSP00000359112; ENSG00000198408. [O60502-3]
ENST00000439817; ENSP00000409973; ENSG00000198408.
GeneID10724.
KEGGhsa:10724.
UCSCuc001ktv.2. human. [O60502-1]
uc001ktw.2. human. [O60502-3]
uc009xws.2. human. [O60502-2]

Organism-specific databases

CTD10724.
GeneCardsGC10M103534.
HGNCHGNC:7056. MGEA5.
HPAHPA036141.
MIM604039. gene.
neXtProtNX_O60502.
PharmGKBPA30787.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0454.
HOVERGENHBG053044.
InParanoidO60502.
KOK15719.
OMALIKVDIH.
OrthoDBEOG7P02H7.
PhylomeDBO60502.
TreeFamTF313732.

Enzyme and pathway databases

BioCycMetaCyc:HS03036-MONOMER.
BRENDA3.2.1.35. 2681.

Gene expression databases

ArrayExpressO60502.
BgeeO60502.
CleanExHS_MGEA5.
GenevestigatorO60502.

Family and domain databases

Gene3D3.40.630.30. 2 hits.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR011496. Beta-N-acetylglucosaminidase.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF07555. NAGidase. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
SSF55729. SSF55729. 1 hit.
ProtoNetSearch...

Other

ChiTaRSMGEA5. human.
GeneWikiMGEA5.
GenomeRNAi10724.
NextBio40709.
PMAP-CutDBO60502.
PROO60502.
SOURCESearch...

Entry information

Entry nameNCOAT_HUMAN
AccessionPrimary (citable) accession number: O60502
Secondary accession number(s): B7WPB9 expand/collapse secondary AC list , D3DR79, E9PGF9, O75166, Q86WV0, Q8IV98, Q9BVA5, Q9HAR0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM