Q9EQQ9 (NCOAT_MOUSE) 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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 By similarity. Acetylates 'Lys-8' of histone H4. Ref.6
Catalytic activity	[Protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine + H2O = [protein]-L-serine + N-acetyl-D-glucosamine. [Protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine + H2O = [protein]-L-threonine + N-acetyl-D-glucosamine. Acetyl-CoA + [histone] = CoA + acetyl-[histone].
Subunit structure	Monomer By similarity. Binds both acetylated and unacetylated histone H4 tail but acetylation on 'Lys-8' of histone H4 abolishes binding. Ref.6
Subcellular location	Nucleus By similarity. Cytoplasm By similarity.
Developmental stage	Expressed throughout development from blastocyst stage to embryonic day 16.5. Ref.7
Post-translational modification	Proteolytically cleaved by caspase-3 By similarity.
Biophysicochemical properties	Kinetic parameters: KM=0.49 mM for pNP-GLcNAc Ref.9 pH dependence: Optimum pH is 6.5-7.
Sequence caution	The sequence AAH41109.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence BAC97998.1 differs from that shown. Reason: Erroneous initiation. The sequence BAE26311.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Molecular function	Acyltransferase Glycosidase Hydrolase Transferase
PTM	Disulfide bond Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	N-acetylglucosamine metabolic process Inferred from electronic annotation. Source: Compara aging Inferred from electronic annotation. Source: Compara dATP metabolic process Inferred from electronic annotation. Source: Compara necrotic cell death Inferred from electronic annotation. Source: Compara negative regulation of cardiac muscle adaptation Inferred from electronic annotation. Source: Compara negative regulation of protein glycosylation Inferred from electronic annotation. Source: Compara positive regulation of DNA metabolic process Inferred from electronic annotation. Source: Compara positive regulation of calcium ion transport into cytosol Inferred from electronic annotation. Source: Compara positive regulation of cell killing Inferred from electronic annotation. Source: Compara positive regulation of glucose import Inferred from electronic annotation. Source: Compara positive regulation of growth hormone secretion Inferred from electronic annotation. Source: Compara positive regulation of insulin secretion Inferred from electronic annotation. Source: Compara positive regulation of mitochondrial depolarization Inferred from electronic annotation. Source: Compara positive regulation of protein complex disassembly Inferred from electronic annotation. Source: Compara positive regulation of proteolysis Inferred from electronic annotation. Source: Compara protein targeting to membrane Inferred from electronic annotation. Source: Compara response to steroid hormone stimulus Inferred from electronic annotation. Source: Compara
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 hydrolase activity, acting on glycosyl bonds Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9EQQ9-1)

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: Q9EQQ9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-698: Missing.
     699-725: NDLFFQPPPLTPTSKVYTIRPYFPKDE → MYTTHSCLYSFFLTFFLVCCLTRLYFQ

Note: No experimental confirmation available.

Isoform 3 (identifier: Q9EQQ9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVRPRVWRSSRRVASQNGLRAFGPTDRGRRGAVAGGRRM

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 916	916	Bifunctional protein NCOAT		PRO_0000252119
Regions
	Region	583 – 916	334	Histone acetyltransferase activity By similarity
	Region	695 – 814	120	Required for histone H4 binding
Sites
	Active site	175	1	Nucleophile; for O-GlcNAcase activity Ref.9
	Active site	177	1	Proton donor; for O-GlcNAcase activity Ref.9
Amino acid modifications
	Modified residue	364	1	Phosphoserine Ref.8 Ref.10
	Disulfide bond	777 ↔ 793		Ref.6
Natural variations
	Alternative sequence	1 – 698	698	Missing in isoform 2.		VSP_020870
	Alternative sequence	1	1	M → MVRPRVWRSSRRVASQNGLR AFGPTDRGRRGAVAGGRRM in isoform 3.		VSP_020871
	Alternative sequence	699 – 725	27	NDLFF…FPKDE → MYTTHSCLYSFFLTFFLVCC LTRLYFQ in isoform 2.		VSP_020872
Experimental info
	Mutagenesis	166	1	C → S: No change in substrate affinity but 60% reduction in O-GlcNAcase activity. Ref.9
	Mutagenesis	174	1	D → N: 2-fold increase in substrate affinity and 77% reduction in O-GlcNAcase activity. Regains appreciable level of catalytic efficiency in the acidic pH range. No recovery of activity in the presence of sodium azide. Ref.9
	Mutagenesis	175	1	D → A: 3-fold increase in substrate affinity and 90% reduction in O-GlcNAcase activity. Regains appreciable level of catalytic efficiency in the acidic pH range. 70% recovery of activity in the presence of sodium azide. Ref.9
	Mutagenesis	177	1	D → N: 2-fold decrease in substrate affinity and 96% reduction in O-GlcNAcase activity. Regains appreciable level of catalytic efficiency in the acidic pH range. 40% recovery of activity in the presence of sodium azide. Ref.9
	Mutagenesis	774	1	D → A: Disrupts ability to bind histone H4 as well as HAT activity. Ref.6
	Mutagenesis	777	1	C → A: Disrupts ability to bind histone H4 as well as HAT activity. Ref.6
	Mutagenesis	789	1	F → A: Disrupts ability to bind histone H4 as well as HAT activity. Ref.6
	Mutagenesis	793	1	C → A: Disrupts ability to bind histone H4 as well as HAT activity. Ref.6
	Mutagenesis	796	1	S → A: Disrupts ability to bind histone H4 as well as HAT activity. Ref.6
	Mutagenesis	853	1	D → N: Retains ability to bind histone H4. Ref.6
	Mutagenesis	878	1	C → S: No effect on O-GlcNAcase activity. Ref.9
	Mutagenesis	884	1	D → N: Retains ability to bind histone H4. Ref.6
	Mutagenesis	891	1	Y → F: Retains ability to bind histone H4. Ref.6
	Sequence conflict	6	1	S → T in BAE26311. Ref.3
	Sequence conflict	52 – 53	2	GA → RT in BAE26311. Ref.3
	Sequence conflict	742	1	F → S in BAC97998. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2001. Version 2. Checksum: B2FAC6F10E03C5CA	FASTA	916	103,162
	10 20 30 40 50 60 MVQKESQAAL EERESERNAN PAAASGASLE QSVAPAPGED NPSGAGAAAV VGAAGGARRF 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 QVAHSGAKTS VVDGTPLVAA 430 440 450 460 470 480 PSLNATTVVT TVYQEPIMSQ GAALSGEPSV LTKEEEKKQP DEEPMDMVVE KQEEAEHKND 490 500 510 520 530 540 NQILTEIVEA KMAEELRPMD TDKESMAESK SPEMSMQEDC IPDVAPMQTD EQTQKEQFVP 550 560 570 580 590 600 GPNEKPLYTA EPVTLEDLQL LADLFYLPYE HGPKGAQMLR EFQWLRANSS VVSVNCKGKD 610 620 630 640 650 660 SEKIEEWRSR AAKFEEMCAL VMGMFTRLSN CANRTILYDM YSYVWDIKSI MSMVKSFVQW 670 680 690 700 710 720 LGCRSHSSAQ FLIGDQEPWA FRGGLAGEFQ RLLPIDGAND LFFQPPPLTP TSKVYTIRPY 730 740 750 760 770 780 FPKDEASVYK ICREMYDDGV GFPFQSQPDL 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: 48F3308C6C616896	FASTA	218	24,718
	10 20 30 40 50 60 MYTTHSCLYS FFLTFFLVCC LTRLYFQASV YKICREMYDD GVGFPFQSQP DLIGDKLVGG 70 80 90 100 110 120 LLSLSLDYCF VLEDEDGICG YALGTVDVTP FIKKCKISWI PFMQEKYTKP NGDKELSEAE 130 140 150 160 170 180 KIMLSFHEEQ EVLPETFLAN FPSLIKMDIH KKVTDPSVAK SMMACLLSSL KANGSRGAFC 190 200 210 EVRPDDKRIL EFYSKLGCFE IAKMEGFPKD VVILGRSL
	Isoform 3 [UniParc]. Checksum: 677AA03C422AECBD	FASTA	954	107,395
	10 20 30 40 50 60 MVRPRVWRSS RRVASQNGLR AFGPTDRGRR GAVAGGRRMV QKESQAALEE RESERNANPA 70 80 90 100 110 120 AASGASLEQS VAPAPGEDNP SGAGAAAVVG AAGGARRFLC GVVEGFYGRP WVMEQRKELF 130 140 150 160 170 180 RRLQKWELNT YLYAPKDDYK HRMFWREMYS VEEAEQLMTL ISAAREYEIE FIYAISPGLD 190 200 210 220 230 240 ITFSNPKEVS TLKRKLDQVS QFGCRSFALL FDDIDHNMCA ADKEVFSSFA HAQVSITNEI 250 260 270 280 290 300 YQYLGEPETF LFCPTEYCGT FCYPNVSQSP YLRTVGEKLL PGIEVLWTGP KVVSKEIPVE 310 320 330 340 350 360 SIEEVSKIIK RAPVIWDNIH ANDYDQKRLF LGPYKGRSTE LIPRLKGVLT NPNCEFEANY 370 380 390 400 410 420 VAIHTLATWY KSNMNGVRKD VVMTDSEDST VSIQIKLENE GSDEDIETDV LYSPQMALKL 430 440 450 460 470 480 ALTEWLQEFG VPHQYSSRQV AHSGAKTSVV DGTPLVAAPS LNATTVVTTV YQEPIMSQGA 490 500 510 520 530 540 ALSGEPSVLT KEEEKKQPDE EPMDMVVEKQ EEAEHKNDNQ ILTEIVEAKM AEELRPMDTD 550 560 570 580 590 600 KESMAESKSP EMSMQEDCIP DVAPMQTDEQ TQKEQFVPGP NEKPLYTAEP VTLEDLQLLA 610 620 630 640 650 660 DLFYLPYEHG PKGAQMLREF QWLRANSSVV SVNCKGKDSE KIEEWRSRAA KFEEMCALVM 670 680 690 700 710 720 GMFTRLSNCA NRTILYDMYS YVWDIKSIMS MVKSFVQWLG CRSHSSAQFL IGDQEPWAFR 730 740 750 760 770 780 GGLAGEFQRL LPIDGANDLF FQPPPLTPTS KVYTIRPYFP KDEASVYKIC REMYDDGVGF 790 800 810 820 830 840 PFQSQPDLIG DKLVGGLLSL SLDYCFVLED EDGICGYALG TVDVTPFIKK CKISWIPFMQ 850 860 870 880 890 900 EKYTKPNGDK ELSEAEKIML SFHEEQEVLP ETFLANFPSL IKMDIHKKVT DPSVAKSMMA 910 920 930 940 950 CLLSSLKANG SRGAFCEVRP DDKRILEFYS KLGCFEIAKM EGFPKDVVIL GRSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mgea5, the murine homolog of a neutral-active cytosolic beta-N-acetylglucosaminidase, localized on chromosome 19." Csoka A.B. Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H. DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Embryonic tail.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-603 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-77 (ISOFORM 3). Strain: C57BL/6J and NOD. Tissue: Head, Mammary gland and Thymus.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: FVB/N-3. Tissue: Kidney and Mammary tumor.
[5]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 109-127, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[6]	"The histone acetyltransferase NCOAT contains a zinc finger-like motif involved in substrate recognition." Toleman C.A., Paterson A.J., Kudlow J.E. J. Biol. Chem. 281:3918-3925(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 157-167; 775-785 AND 875-886, FUNCTION, SUBUNIT, DISULFIDE BOND, MUTAGENESIS OF ASP-774; CYS-777; PHE-789; CYS-793; SER-796; ASP-853; ASP-884 AND TYR-891.
[7]	"Identification of a nuclear variant of MGEA5, a cytoplasmic hyaluronidase and a beta-N-acetylglucosaminidase." Comtesse N., Maldener E., Meese E. Biochem. Biophys. Res. Commun. 283:634-640(2001) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE.
[8]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, MASS SPECTROMETRY. Tissue: Embryonic brain.
[9]	"Location and characterization of the O-GlcNAcase active site." Toleman C., Paterson A.J., Kudlow J.E. Biochim. Biophys. Acta 1760:829-839(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF CYS-166; ASP-174; ASP-175; ASP-177 AND CYS-878.
[10]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF132214 mRNA. Translation: AAG43273.2. AK129188 mRNA. Translation: BAC97998.1. Different initiation. BC041109 mRNA. Translation: AAH41109.1. Sequence problems. BC054821 mRNA. Translation: AAH54821.1. AK012695 mRNA. Translation: BAB28416.1. AK014781 mRNA. Translation: BAB29550.1. AK077613 mRNA. Translation: BAC36900.1. AK088774 mRNA. Translation: BAC40564.1. AK145227 mRNA. Translation: BAE26311.1. Different initiation.
IPI	IPI00406624. IPI00655175. IPI00788404.
RefSeq	NP_076288.1. NM_023799.3.
UniGene	Mm.122725. Mm.440640. Mm.480399.
3D structure databases
ProteinModelPortal	Q9EQQ9.
SMR	Q9EQQ9. Positions 61-331.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-2844950.
Protein family/group databases
CAZy	GH84. Glycoside Hydrolase Family 84.
PTM databases
PhosphoSite	Q9EQQ9.
Proteomic databases
PaxDb	Q9EQQ9.
PRIDE	Q9EQQ9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000026243; ENSMUSP00000026243; ENSMUSG00000025220.
GeneID	76055.
KEGG	mmu:76055.
UCSC	uc008hrm.1. mouse. uc008hrn.1. mouse.
Organism-specific databases
CTD	10724.
MGI	MGI:1932139. Mgea5.
Rouge	Search...
Phylogenomic databases
eggNOG	COG0454.
GeneTree	ENSGT00390000007726.
HOVERGEN	HBG053044.
InParanoid	Q9EQQ9.
KO	K15719.
OMA	AHSGAKT.
OrthoDB	EOG469QT2.
Gene expression databases
ArrayExpress	Q9EQQ9.
Bgee	Q9EQQ9.
CleanEx	MM_MGEA5.
Genevestigator	Q9EQQ9.
GermOnline	ENSMUSG00000025220. Mus musculus.
Family and domain databases
Gene3D	3.40.630.30. 2 hits.
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR011496. Beta-N-acetylglucosaminidase. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF07555. NAGidase. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit. SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	MGEA5. mouse.
NextBio	344519.
SOURCE	Search...

Entry information

Entry name

NCOAT_MOUSE

Accession

Primary (citable) accession number: Q9EQQ9
Secondary accession number(s): Q3ULY7 , Q6ZQ71, Q8BK05, Q8BTT2, Q8CFX2, Q9CSJ4, Q9CUR7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	October 1, 2001
Last modified:	May 1, 2013
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program