Q68CP4 (HGNAT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Heparan-alpha-glucosaminide N-acetyltransferase
EC=2.3.1.78

Alternative name(s):
Transmembrane protein 76

Gene names

Name:	HGSNAT
Synonyms:	TMEM76

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	663 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Lysosomal acetyltransferase that acetylates the non-reducing terminal alpha-glucosamine residue of intralysosomal heparin or heparan sulfate, converting it into a substrate for luminal alpha-N-acetyl glucosaminidase. Ref.4 Ref.8 Ref.9 Ref.11
Catalytic activity	Acetyl-CoA + heparan sulfate alpha-D-glucosaminide = CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide. Ref.4
Subunit structure	Homooligomer. Homooligomerization is necessary for enzyme activity. Ref.9
Subcellular location	Lysosome membrane; Multi-pass membrane protein. Note: Colocalizes with the lysosomal marker LAMP2. The signal peptide is not cleaved upon translocation into the endoplasmic reticulum; the precursor is probably targeted to the lysosomes via the adapter protein complex-mediated pathway that involves tyrosine- and/or dileucine-based conserved amino acid motifs in the last C-terminus 16-amino acid domain. Ref.4 Ref.5 Ref.11
Tissue specificity	Widely expressed, with highest level in leukocytes, heart, liver, skeletal muscle, lung, placenta and liver. Ref.4 Ref.11
Post-translational modification	Undergoes intralysosomal proteolytic cleavage; occurs within the end of the first and/or the beginning of the second luminal domain and is essential for the activation of the enzyme. Glycosylated. Ref.8
Involvement in disease	Mucopolysaccharidosis 3C (MPS3C) [MIM:252930]: A form of mucopolysaccharidosis type 3, an autosomal recessive lysosomal storage disease due to impaired degradation of heparan sulfate. MPS3 is characterized by severe central nervous system degeneration, but only mild somatic disease. Onset of clinical features usually occurs between 2 and 6 years; severe neurologic degeneration occurs in most patients between 6 and 10 years of age, and death occurs typically during the second or third decade of life. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15
Miscellaneous	A signal sequence is predicted but has been shown not to be cleaved in the reticulum endoplasmic.

Ontologies

Keywords
Cellular component	Lysosome Membrane
Coding sequence diversity	Alternative initiation
Disease	Disease mutation Mucopolysaccharidosis
Domain	Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Traceable author statement. Source: Reactome glycosaminoglycan catabolic process Traceable author statement. Source: Reactome lysosomal transport Inferred from direct assay Ref.9. Source: UniProtKB protein oligomerization Inferred from direct assay Ref.9. Source: UniProtKB small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW lysosomal membrane Inferred from direct assay Ref.8Ref.9. Source: UniProtKB
Molecular_function	heparan-alpha-glucosaminide N-acetyltransferase activity Inferred from electronic annotation. Source: EC transferase activity, transferring acyl groups Inferred from direct assay Ref.8Ref.9. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]

Note: Isoform 1 and isoform 2 are correctly targeted to the lysosomal compartment and are functional enzymes.

Isoform 1 (identifier: Q68CP4-1)

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.

Note: Intralysosomal proteolytic cleavage is faster and enzymatic activity higher than isoform 2.

Isoform 2 (identifier: Q68CP4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 663	663	Heparan-alpha-glucosaminide N-acetyltransferase		PRO_0000273153
Regions
	Topological domain	1 – 190	190	Lumenal, vesicle Potential
	Transmembrane	191 – 211	21	Helical; Potential
	Topological domain	212 – 275	64	Cytoplasmic Potential
	Transmembrane	276 – 296	21	Helical; Potential
	Topological domain	297 – 302	6	Lumenal, vesicle Potential
	Transmembrane	303 – 323	21	Helical; Potential
	Topological domain	324 – 345	22	Cytoplasmic Potential
	Transmembrane	346 – 366	21	Helical; Potential
	Topological domain	367 – 374	8	Lumenal, vesicle Potential
	Transmembrane	375 – 395	21	Helical; Potential
	Topological domain	396 – 420	25	Cytoplasmic Potential
	Transmembrane	421 – 441	21	Helical; Potential
	Topological domain	442 – 500	59	Lumenal, vesicle Potential
	Transmembrane	501 – 521	21	Helical; Potential
	Topological domain	522 – 529	8	Cytoplasmic Potential
	Transmembrane	530 – 550	21	Helical; Potential
	Topological domain	551 – 564	14	Lumenal, vesicle Potential
	Transmembrane	565 – 585	21	Helical; Potential
	Topological domain	586 – 592	7	Cytoplasmic Potential
	Transmembrane	593 – 613	21	Helical; Potential
	Topological domain	614 – 634	21	Lumenal, vesicle Potential
	Transmembrane	635 – 655	21	Helical; Potential
	Topological domain	656 – 663	8	Cytoplasmic Potential
	Region	624 – 635	12	Lysosomal targeting region
	Compositional bias	4 – 64	61	Ala-rich
Sites
	Active site	297	1	Ref.9
Amino acid modifications
	Modified residue	239	1	Phosphoserine By similarity
	Modified residue	245	1	Phosphoserine Ref.10
	Glycosylation	94	1	N-linked (GlcNAc...) Potential
	Glycosylation	142	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	162	1	N-linked (GlcNAc...) Potential
	Disulfide bond	151 ↔ 462		Probable
Natural variations
	Alternative sequence	1 – 28	28	Missing in isoform 2.		VSP_040504
	Natural variant	104	1	C → F in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum and loss of intralysosomal proteolytic cleavage. Ref.8 Ref.9 Ref.11 Ref.15		VAR_063983
	Natural variant	165	1	L → P in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. Ref.8 Ref.12 Ref.13 Ref.14 Ref.15		VAR_063984
	Natural variant	265	1	P → Q Rare polymorphism that does not influence neither stability, nor activity, nor cellular localization of the enzyme. Ref.8 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15		VAR_063985
	Natural variant	280	1	I → R in MPS3C. Ref.13		VAR_063986
	Natural variant	290	1	G → R in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. Ref.8 Ref.15		VAR_063987
	Natural variant	301	1	N → K in MPS3C; retained in the endoplasmic reticulum and loss of enzymatic activity. Ref.8 Ref.13		VAR_063988
	Natural variant	311	1	P → L in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. Ref.8 Ref.11 Ref.14 Ref.15		VAR_030083
	Natural variant	372	1	R → C in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. Ref.11 Ref.13 Ref.14 Ref.15		VAR_030084
	Natural variant	372	1	R → H in MPS3C; Retained in the endoplasmic reticulum and loss of enzymatic activity. Ref.8 Ref.11		VAR_063989
	Natural variant	431	1	W → C in MPS3C; associated with T-643 on the same allele in a MPS3C patient; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. Ref.8 Ref.11 Ref.14 Ref.15		VAR_063990
	Natural variant	452	1	G → S in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. Ref.8 Ref.11 Ref.15		VAR_030085
	Natural variant	499	1	E → K in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. Ref.8 Ref.11 Ref.13 Ref.14 Ref.15		VAR_030086
	Natural variant	509	1	V → L Rare polymorphism; no loss of enzymatic activity. Ref.8 Ref.14 Ref.15		VAR_063991
	Natural variant	510	1	M → K in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. Ref.8 Ref.11 Ref.15		VAR_030087
	Natural variant	514	1	G → E in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. Ref.14 Ref.15		VAR_063992
	Natural variant	517	1	A → E in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. Ref.8 Ref.14 Ref.15		VAR_063993
	Natural variant	546	1	S → F in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. Ref.8 Ref.12 Ref.13 Ref.14 Ref.15		VAR_063994
	Natural variant	551	1	K → Q Rare polymorphism; no loss of enzymatic activity. Ref.8 Ref.11 Ref.14 Ref.15		VAR_063995
	Natural variant	567	1	S → C in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. Ref.8 Ref.13 Ref.15		VAR_063996
	Natural variant	569	1	S → L in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity. Ref.8 Ref.11 Ref.14 Ref.15		VAR_030088
	Natural variant	590	1	D → V in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity. Ref.8 Ref.11 Ref.15		VAR_030089
	Natural variant	599	1	P → L in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity. Ref.8 Ref.11 Ref.15		VAR_030090
	Natural variant	643	1	A → T Rare polymorphism associated with C-431 on the same allele in a MPS3C patient; has a negligible effect on the enzyme expression; no loss of enzymatic activity. Ref.8 Ref.11 Ref.14 Ref.15		VAR_063997
Experimental info
	Mutagenesis	107	1	C → S: Loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation. Ref.9
	Mutagenesis	151	1	C → S: Loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation. Ref.9
	Mutagenesis	179	1	C → S: Loss of intralysosomal proteolytic cleavage and enzymatic activity. Ref.9
	Mutagenesis	236	1	L → A: Displayed both lysosomal and plasma membrane localization, reduced intralysosomal proteolytic cleavage and enzymatic activity; when associated with A-209. Ref.9
	Mutagenesis	237	1	I → A: Displayed both lysosomal and plasma membrane localization, reduced intralysosomal proteolytic cleavage and enzymatic activity; when associated with A-208. Ref.9
	Mutagenesis	297	1	H → A: Loss of enzymatic activity, but correctly targeted and processed. Ref.9
	Mutagenesis	333	1	C → S: No loss of intralysosomal proteolytic cleavage and enzymatic activity. Ref.9
	Mutagenesis	402	1	C → S: No loss of intralysosomal proteolytic cleavage and enzymatic activity. Ref.9
	Mutagenesis	462	1	C → S: Complete loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation. Ref.9
	Mutagenesis	479	1	H → A: Loss of intralysosomal proteolytic cleavage and enzymatic activity, retained in the endoplasmic reticulum. Ref.9
	Mutagenesis	633	1	H → A: Loss of intralysosomal proteolytic cleavage and enzymatic activity, retained in the endoplasmic reticulum. Ref.9
	Mutagenesis	652 – 663	12	Missing: Loss of intralysosomal proteolytic cleavage and enzymatic activity. Localized in the plasma membrane.

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: B05648474A3587B5	FASTA	663	73,293
	10 20 30 40 50 60 MTGARASAAE QRRAGRSGQA RAAERAAGMS GAGRALAALL LAASVLSAAL LAPGGSSGRD 70 80 90 100 110 120 AQAAPPRDLD KKRHAELKMD QALLLIHNEL LWTNLTVYWK SECCYHCLFQ VLVNVPQSPK 130 140 150 160 170 180 AGKPSAAAAS VSTQHGSILQ LNDTLEEKEV CRLEYRFGEF GNYSLLVKNI HNGVSEIACD 190 200 210 220 230 240 LAVNEDPVDS NLPVSIAFLI GLAVIIVISF LRLLLSLDDF NNWISKAISS RETDRLINSE 250 260 270 280 290 300 LGSPSRTDPL DGDVQPATWR LSALPPRLRS VDTFRGIALI LMVFVNYGGG KYWYFKHASW 310 320 330 340 350 360 NGLTVADLVF PWFVFIMGSS IFLSMTSILQ RGCSKFRLLG KIAWRSFLLI CIGIIIVNPN 370 380 390 400 410 420 YCLGPLSWDK VRIPGVLQRL GVTYFVVAVL ELLFAKPVPE HCASERSCLS LRDITSSWPQ 430 440 450 460 470 480 WLLILVLEGL WLGLTFLLPV PGCPTGYLGP GGIGDFGKYP NCTGGAAGYI DRLLLGDDHL 490 500 510 520 530 540 YQHPSSAVLY HTEVAYDPEG ILGTINSIVM AFLGVQAGKI LLYYKARTKD ILIRFTAWCC 550 560 570 580 590 600 ILGLISVALT KVSENEGFIP VNKNLWSLSY VTTLSSFAFF ILLVLYPVVD VKGLWTGTPF 610 620 630 640 650 660 FYPGMNSILV YVGHEVFENY FPFQWKLKDN QSHKEHLTQN IVATALWVLI AYILYRKKIF WKI
	Isoform 2 [UniParc]. Checksum: 177CDCFCF76CDB36	FASTA	635	70,496
	10 20 30 40 50 60 MSGAGRALAA LLLAASVLSA ALLAPGGSSG RDAQAAPPRD LDKKRHAELK MDQALLLIHN 70 80 90 100 110 120 ELLWTNLTVY WKSECCYHCL FQVLVNVPQS PKAGKPSAAA ASVSTQHGSI LQLNDTLEEK 130 140 150 160 170 180 EVCRLEYRFG EFGNYSLLVK NIHNGVSEIA CDLAVNEDPV DSNLPVSIAF LIGLAVIIVI 190 200 210 220 230 240 SFLRLLLSLD DFNNWISKAI SSRETDRLIN SELGSPSRTD PLDGDVQPAT WRLSALPPRL 250 260 270 280 290 300 RSVDTFRGIA LILMVFVNYG GGKYWYFKHA SWNGLTVADL VFPWFVFIMG SSIFLSMTSI 310 320 330 340 350 360 LQRGCSKFRL LGKIAWRSFL LICIGIIIVN PNYCLGPLSW DKVRIPGVLQ RLGVTYFVVA 370 380 390 400 410 420 VLELLFAKPV PEHCASERSC LSLRDITSSW PQWLLILVLE GLWLGLTFLL PVPGCPTGYL 430 440 450 460 470 480 GPGGIGDFGK YPNCTGGAAG YIDRLLLGDD HLYQHPSSAV LYHTEVAYDP EGILGTINSI 490 500 510 520 530 540 VMAFLGVQAG KILLYYKART KDILIRFTAW CCILGLISVA LTKVSENEGF IPVNKNLWSL 550 560 570 580 590 600 SYVTTLSSFA FFILLVLYPV VDVKGLWTGT PFFYPGMNSI LVYVGHEVFE NYFPFQWKLK 610 620 630 DNQSHKEHLT QNIVATALWV LIAYILYRKK IFWKI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Trachea.
[2]	"DNA sequence and analysis of human chromosome 8." Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S. Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 265-663 (ISOFORMS 1/2). Tissue: Uterus.
[4]	"Identification of the gene encoding the enzyme deficient in mucopolysaccharidosis IIIC (Sanfilippo disease type C)." Fan X., Zhang H., Zhang S., Bagshaw R.D., Tropak M.B., Callahan J.W., Mahuran D.J. Am. J. Hum. Genet. 79:738-744(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN MPS3C, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[5]	"Integral and associated lysosomal membrane proteins." Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H., Elsaesser H.-P., Mann M., Hasilik A. Traffic 8:1676-1686(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Placenta.
[6]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[7]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-142, MASS SPECTROMETRY. Tissue: Liver.
[8]	"Protein misfolding as an underlying molecular defect in mucopolysaccharidosis III type C." Feldhammer M., Durand S., Pshezhetsky A.V. PLoS ONE 4:E7434-E7434(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, GLYCOSYLATION, CHARACTERIZATION OF VARIANTS PHE-104; PRO-165; GLN-265; ARG-290; LYS-301; LEU-311; HIS-372; CYS-431; SER-452; LYS-499; LEU-509; LYS-510; GLU-517; PHE-546; GLN-551; CYS-567; LEU-569; VAL-590; LEU-599 AND THR-643.
[9]	"Analysis of the biogenesis of heparan sulfate acetyl-CoA:alpha-glucosaminide N-acetyltransferase provides insights into the mechanism underlying its complete deficiency in mucopolysaccharidosis IIIC." Durand S., Feldhammer M., Bonneil E., Thibault P., Pshezhetsky A.V. J. Biol. Chem. 285:31233-31242(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ACTIVE SITE, ALTERNATIVE INITIATION (ISOFORMS 1 AND 2), SUBUNIT, CHARACTERIZATION OF VARIANT PHE-104, MUTAGENESIS OF CYS-107; CYS-151; CYS-179; LEU-236; ILE-237; HIS-297; CYS-333; CYS-402; CYS-462; HIS-479 AND HIS-633, MASS SPECTROMETRY.
[10]	"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-245, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Mutations in TMEM76 cause mucopolysaccharidosis IIIC (Sanfilippo C syndrome)." Hrebicek M., Mrazova L., Seyrantepe V., Durand S., Roslin N.M., Noskova L., Hartmannova H., Ivanek R., Cizkova A., Poupetova H., Sikora J., Urinovska J., Stranecky V., Zeman J., Lepage P., Roquis D., Verner A., Ausseil J. , Beesley C.E., Maire I., Poorthuis B.J.H.M., van de Kamp J., van Diggelen O.P., Wevers R.A., Hudson T.J., Fujiwara T.M., Majewski J., Morgan K., Kmoch S., Pshezhetsky A.V. Am. J. Hum. Genet. 79:807-819(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS3C PHE-104; LEU-311; CYS-372; HIS-372; CYS-431; SER-452; LYS-499; LYS-510; LEU-569; VAL-590 AND LEU-599, VARIANTS GLN-265; GLN-551 AND THR-643, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[12]	"Mutational analysis of the HGSNAT gene in Italian patients with mucopolysaccharidosis IIIC (Sanfilippo C syndrome). Mutation in brief #959. Online." Fedele A.O., Filocamo M., Di Rocco M., Sersale G., Luebke T., di Natale P., Cosma M.P., Ballabio A. Hum. Mutat. 28:523-523(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS3C PRO-165 AND PHE-546, VARIANT GLN-265.
[13]	"Clinical and genetic spectrum of Sanfilippo type C (MPS IIIC) disease in The Netherlands." Ruijter G.J.G., Valstar M.J., van de Kamp J.M., van der Helm R.M., Durand S., van Diggelen O.P., Wevers R.A., Poorthuis B.J., Pshezhetsky A.V., Wijburg F.A. Mol. Genet. Metab. 93:104-111(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS3C PRO-165; ARG-280; LYS-301; CYS-372; LYS-499; PHE-546 AND CYS-567, VARIANT GLN-265.
[14]	"Sanfilippo syndrome type C: mutation spectrum in the heparan sulfate acetyl-CoA: alpha-glucosaminide N-acetyltransferase (HGSNAT) gene." Feldhammer M., Durand S., Mrazova L., Boucher R.-M., Laframboise R., Steinfeld R., Wraith J.E., Michelakakis H., van Diggelen O.P., Hrebicek M., Kmoch S., Pshezhetsky A.V. Hum. Mutat. 30:918-925(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS3C PRO-165; LEU-311; CYS-372; CYS-431; LYS-499; GLU-514; GLU-517; PHE-546 AND LEU-569, VARIANTS GLN-265; LEU-509; GLN-551 AND THR-643, CHARACTERIZATION OF VARIANT MPS3C CYS-431, CHARACTERIZATION OF VARIANTS GLN-265; LEU-509; GLN-551 AND THR-643.
[15]	"Functional analysis of the HGSNAT gene in patients with mucopolysaccharidosis IIIC (Sanfilippo C Syndrome)." Fedele A.O., Hopwood J.J. Hum. Mutat. 31:E1574-E1586(2010) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS MPS3C PHE-104; PRO-165; ARG-290; LEU-311; CYS-372; CYS-431; SER-452; LYS-499; LYS-510; GLU-514; GLU-517; PHE-546; CYS-567; LEU-569; VAL-590 AND LEU-599, CHARACTERIZATION OF VARIANTS GLN-265; LEU-509; GLN-551 AND THR-643.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK304441 mRNA. Translation: BAG65262.1. AC113191 Genomic DNA. No translation available. CR749838 mRNA. Translation: CAH18694.1.
IPI	IPI00739149. IPI00908672.
RefSeq	NP_689632.2. NM_152419.2.
UniGene	Hs.600384.
3D structure databases
ProteinModelPortal	Q68CP4.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q68CP4. 2 interactions.
STRING	9606.ENSP00000368965.
PTM databases
PhosphoSite	Q68CP4.
Polymorphism databases
DMDM	124007195.
Proteomic databases
PaxDb	Q68CP4.
PRIDE	Q68CP4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000379644; ENSP00000368965; ENSG00000165102. ENST00000458501; ENSP00000389524; ENSG00000165102.
GeneID	138050.
KEGG	hsa:138050.
UCSC	uc003xpx.4. human.
Organism-specific databases
CTD	138050.
GeneCards	GC08P042995.
H-InvDB	HIX0007487.
HGNC	HGNC:26527. HGSNAT.
HPA	HPA029578.
MIM	252930. phenotype. 610453. gene.
neXtProt	NX_Q68CP4.
Orphanet	79271. Sanfilippo syndrome type C.
PharmGKB	PA162390851.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG4299.
HOGENOM	HOG000006803.
HOVERGEN	HBG081599.
InParanoid	Q68CP4.
KO	K10532.
OrthoDB	EOG4548Z7.
Enzyme and pathway databases
BRENDA	2.3.1.78. 2681.
Reactome	REACT_111217. Metabolism. REACT_116125. Disease.
SABIO-RK	Q68CP4.
Gene expression databases
ArrayExpress	Q68CP4.
Bgee	Q68CP4.
CleanEx	HS_HGSNAT.
Genevestigator	Q68CP4.
Family and domain databases
InterPro	IPR012429. DUF1624. [Graphical view]
Pfam	PF07786. DUF1624. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	HGSNAT. human.
GenomeRNAi	138050.
NextBio	83735.
SOURCE	Search...

Entry information

Entry name

HGNAT_HUMAN

Accession

Primary (citable) accession number: Q68CP4
Secondary accession number(s): B4E2V0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2007
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 72 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.