O60502 (NCOAT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	916 AA.
Sequence status	Complete.
Protein existence	Evidence 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 By similarity. 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 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.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Acyltransferase Glycosidase Hydrolase Transferase
PTM	Disulfide bond Phosphoprotein
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	glycoprotein catabolic process Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	histone acetyltransferase activity Inferred from electronic annotation. Source: EC hyalurononglucosaminidase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 3 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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 916	916	Bifunctional protein NCOAT		PRO_0000252118
Regions
	Region	583 – 916	334	Histone acetyltransferase activity By similarity
	Region	695 – 814	120	Required for histone H4 binding By similarity
Sites
	Active site	175	1	Nucleophile; for O-GlcNAcase activity By similarity
	Active site	177	1	Proton donor; for O-GlcNAcase activity By similarity
Amino acid modifications
	Modified residue	364	1	Phosphoserine Ref.10 Ref.11 Ref.12 Ref.13
	Disulfide bond	777 ↔ 793		By similarity
Natural variations
	Alternative sequence	346 – 398	53	Missing in isoform 2.		VSP_020866
	Alternative sequence	663 – 677	15	CRSHS…IGDQE → RCTRNNLFSSNILSL in isoform 3.		VSP_020867
	Alternative sequence	678 – 916	239	Missing in isoform 3.		VSP_020868
	Alternative sequence	691 – 704	14	Missing in isoform 2.		VSP_020869
	Natural variant	46	1	G → E. Corresponds to variant rs3740421 [ dbSNP | Ensembl ].		VAR_027761
	Natural variant	602	1	E → K. Ref.8 Corresponds to variant rs17853930 [ dbSNP | Ensembl ].		VAR_027762

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 2. Checksum: 01F8A64A9B1475C6	FASTA	916	102,915
	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
	Isoform 2 [UniParc]. Checksum: A65EFD64BE0AD17C	FASTA	849	95,331
	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 KDVVMSRQVA HSGAKASVVD 370 380 390 400 410 420 GTPLVAAPSL NATTVVTTVY QEPIMSQGAA LSGEPTTLTK EEEKKQPDEE PMDMVVEKQE 430 440 450 460 470 480 ETDHKNDNQI LSEIVEAKMA EELKPMDTDK ESIAESKSPE MSMQEDCISD IAPMQTDEQT 490 500 510 520 530 540 NKEQFVPGPN EKPLYTAEPV TLEDLQLLAD LFYLPYEHGP KGAQMLREFQ WLRANSSVVS 550 560 570 580 590 600 VNCKGKDSEK IEEWRSRAAK FEEMCGLVMG MFTRLSNCAN RTILYDMYSY VWDIKSIMSM 610 620 630 640 650 660 VKSFVQWLGC RSHSSAQFLI GDQEPWAFRG GLAGEFQPPP LTPTSKVYTI RPYFPKDEAS 670 680 690 700 710 720 VYKICREMYD DGVGLPFQSQ PDLIGDKLVG GLLSLSLDYC FVLEDEDGIC GYALGTVDVT 730 740 750 760 770 780 PFIKKCKISW IPFMQEKYTK PNGDKELSEA EKIMLSFHEE QEVLPETFLA NFPSLIKMDI 790 800 810 820 830 840 HKKVTDPSVA KSMMACLLSS LKANGSRGAF CEVRPDDKRI LEFYSKLGCF EIAKMEGFPK DVVILGRSL
	Isoform 3 (MGEA5s) [UniParc]. Checksum: BF83DEF3ABDE4AA8	FASTA	677	76,193
	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 LGRCTRNNLF SSNILSL

References

	« Hide 'large scale' referencesShow '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: 9811929] [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: 11341771] [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: 11148210] [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: 9734811] [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: 12168954] [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(2004) [PubMed: 15164054] [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. , 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: 15489334] [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: 11788610] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, PTM, SUBCELLULAR LOCATION.
[10]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[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: 21269460] [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.
IPI	IPI00181391. IPI00465449. IPI00477231.
PIR	T00360.
RefSeq	NP_001135906.1. NM_001142434.1. NP_036347.1. NM_012215.3.
UniGene	Hs.500842.
3D structure databases
ProteinModelPortal	O60502.
SMR	O60502. Positions 46-703.
ModBase	Search...
Protein-protein interaction databases
IntAct	O60502. 12 interactions.
STRING	O60502.
Protein family/group databases
CAZy	GH84. Glycoside Hydrolase Family 84.
PTM databases
PhosphoSite	O60502.
Proteomic databases
PRIDE	O60502.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000361464; ENSP00000354850; ENSG00000198408.
GeneID	10724.
KEGG	hsa:10724.
UCSC	uc001ktv.1. human. uc001ktw.1. human. uc009xws.1. human.
Organism-specific databases
CTD	10724.
GeneCards	GC10M103534.
H-InvDB	HIX0035300.
HGNC	HGNC:7056. MGEA5.
HPA	HPA036141.
MIM	604039. gene.
neXtProt	NX_O60502.
PharmGKB	PA30787.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG06231.
GeneTree	ENSGT00390000007726.
HOGENOM	HBG357525.
HOVERGEN	HBG053044.
InParanoid	O60502.
OMA	KFEEMCG.
OrthoDB	EOG469QT2.
PhylomeDB	O60502.
Enzyme and pathway databases
BioCyc	MetaCyc:HS03036-MONOMER.
BRENDA	3.2.1.35. 2681.
Gene expression databases
ArrayExpress	O60502.
Bgee	O60502.
CleanEx	HS_MGEA5.
Genevestigator	O60502.
GermOnline	ENSG00000198408. Homo sapiens.
Family and domain databases
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR011496. Beta-N-acetylglucosaminidase. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Gene3D	G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 2 hits.
Pfam	PF07555. NAGidase. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit. SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...
Other
NextBio	40709.
PMAP-CutDB	O60502.
SOURCE	Search...

Entry information

Entry name

NCOAT_HUMAN

Accession

Primary (citable) accession number: O60502
Secondary accession number(s): B7WPB9 , D3DR79, O75166, Q86WV0, Q8IV98, Q9BVA5, Q9HAR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	March 1, 2001
Last modified:	January 25, 2012
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.