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Q68CP4 (HGNAT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Heparan-alpha-glucosaminide N-acetyltransferase

EC=2.3.1.78
Alternative name(s):
Transmembrane protein 76
Gene names
Name:HGSNAT
Synonyms:TMEM76
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length663 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 663663Heparan-alpha-glucosaminide N-acetyltransferase
PRO_0000273153

Regions

Topological domain1 – 190190Lumenal, vesicle Potential
Transmembrane191 – 21121Helical; Potential
Topological domain212 – 27564Cytoplasmic Potential
Transmembrane276 – 29621Helical; Potential
Topological domain297 – 3026Lumenal, vesicle Potential
Transmembrane303 – 32321Helical; Potential
Topological domain324 – 34522Cytoplasmic Potential
Transmembrane346 – 36621Helical; Potential
Topological domain367 – 3748Lumenal, vesicle Potential
Transmembrane375 – 39521Helical; Potential
Topological domain396 – 42025Cytoplasmic Potential
Transmembrane421 – 44121Helical; Potential
Topological domain442 – 50059Lumenal, vesicle Potential
Transmembrane501 – 52121Helical; Potential
Topological domain522 – 5298Cytoplasmic Potential
Transmembrane530 – 55021Helical; Potential
Topological domain551 – 56414Lumenal, vesicle Potential
Transmembrane565 – 58521Helical; Potential
Topological domain586 – 5927Cytoplasmic Potential
Transmembrane593 – 61321Helical; Potential
Topological domain614 – 63421Lumenal, vesicle Potential
Transmembrane635 – 65521Helical; Potential
Topological domain656 – 6638Cytoplasmic Potential
Region624 – 63512Lysosomal targeting region
Compositional bias4 – 6461Ala-rich

Sites

Active site2971 Ref.9

Amino acid modifications

Modified residue2451Phosphoserine Ref.10
Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation1421N-linked (GlcNAc...) Ref.7
Glycosylation1621N-linked (GlcNAc...) Potential
Disulfide bond151 ↔ 462 Probable

Natural variations

Alternative sequence1 – 2828Missing in isoform 2.
VSP_040504
Natural variant1041C → 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 variant1651L → 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 variant2651P → 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 variant2801I → R in MPS3C. Ref.13
VAR_063986
Natural variant2901G → 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 variant3011N → K in MPS3C; retained in the endoplasmic reticulum and loss of enzymatic activity. Ref.8 Ref.13
VAR_063988
Natural variant3111P → 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 variant3721R → 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 variant3721R → H in MPS3C; Retained in the endoplasmic reticulum and loss of enzymatic activity. Ref.8 Ref.11
VAR_063989
Natural variant4311W → 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 variant4521G → 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 variant4991E → 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 variant5091V → L Rare polymorphism; no loss of enzymatic activity. Ref.8 Ref.14 Ref.15
VAR_063991
Natural variant5101M → 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 variant5141G → 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 variant5171A → 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 variant5461S → 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 variant5511K → Q Rare polymorphism; no loss of enzymatic activity. Ref.8 Ref.11 Ref.14 Ref.15
Corresponds to variant rs73569592 [ dbSNP | Ensembl ].
VAR_063995
Natural variant5671S → 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 variant5691S → 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 variant5901D → 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 variant5991P → 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 variant6431A → 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
Corresponds to variant rs112029032 [ dbSNP | Ensembl ].
VAR_063997

Experimental info

Mutagenesis1071C → S: Loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation. Ref.9
Mutagenesis1511C → S: Loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation. Ref.9
Mutagenesis1791C → S: Loss of intralysosomal proteolytic cleavage and enzymatic activity. Ref.9
Mutagenesis2361L → A: Displayed both lysosomal and plasma membrane localization, reduced intralysosomal proteolytic cleavage and enzymatic activity; when associated with A-209. Ref.9
Mutagenesis2371I → A: Displayed both lysosomal and plasma membrane localization, reduced intralysosomal proteolytic cleavage and enzymatic activity; when associated with A-208. Ref.9
Mutagenesis2971H → A: Loss of enzymatic activity, but correctly targeted and processed. Ref.9
Mutagenesis3331C → S: No loss of intralysosomal proteolytic cleavage and enzymatic activity. Ref.9
Mutagenesis4021C → S: No loss of intralysosomal proteolytic cleavage and enzymatic activity. Ref.9
Mutagenesis4621C → S: Complete loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation. Ref.9
Mutagenesis4791H → A: Loss of intralysosomal proteolytic cleavage and enzymatic activity, retained in the endoplasmic reticulum. Ref.9
Mutagenesis6331H → A: Loss of intralysosomal proteolytic cleavage and enzymatic activity, retained in the endoplasmic reticulum. Ref.9
Mutagenesis652 – 66312Missing: Loss of intralysosomal proteolytic cleavage and enzymatic activity. Localized in the plasma membrane.

Sequences

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

Last modified January 23, 2007. Version 2.
Checksum: B05648474A3587B5

FASTA66373,293
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 177CDCFCF76CDB36
Show »

FASTA63570,496

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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].
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.
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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK304441 mRNA. Translation: BAG65262.1.
AC113191 Genomic DNA. No translation available.
CR749838 mRNA. Translation: CAH18694.1.
CCDSCCDS47852.1. [Q68CP4-2]
RefSeqNP_689632.2. NM_152419.2. [Q68CP4-2]
UniGeneHs.600384.

3D structure databases

ProteinModelPortalQ68CP4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ68CP4. 2 interactions.
STRING9606.ENSP00000368965.

PTM databases

PhosphoSiteQ68CP4.

Polymorphism databases

DMDM124007195.

Proteomic databases

MaxQBQ68CP4.
PaxDbQ68CP4.
PRIDEQ68CP4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379644; ENSP00000368965; ENSG00000165102. [Q68CP4-2]
ENST00000458501; ENSP00000389524; ENSG00000165102. [Q68CP4-1]
GeneID138050.
KEGGhsa:138050.
UCSCuc003xpx.4. human. [Q68CP4-1]

Organism-specific databases

CTD138050.
GeneCardsGC08P042995.
H-InvDBHIX0007487.
HGNCHGNC:26527. HGSNAT.
HPAHPA029578.
MIM252930. phenotype.
610453. gene.
neXtProtNX_Q68CP4.
Orphanet79271. Sanfilippo syndrome type C.
PharmGKBPA162390851.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4299.
HOGENOMHOG000006803.
HOVERGENHBG081599.
InParanoidQ68CP4.
KOK10532.
OrthoDBEOG7PS1F9.
PhylomeDBQ68CP4.
TreeFamTF324790.

Enzyme and pathway databases

BRENDA2.3.1.78. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
SABIO-RKQ68CP4.

Gene expression databases

ArrayExpressQ68CP4.
BgeeQ68CP4.
CleanExHS_HGSNAT.
GenevestigatorQ68CP4.

Family and domain databases

InterProIPR012429. DUF1624.
[Graphical view]
PfamPF07786. DUF1624. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHGSNAT. human.
GeneWikiHGSNAT.
GenomeRNAi138050.
NextBio83735.
PROQ68CP4.
SOURCESearch...

Entry information

Entry nameHGNAT_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 83 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

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 8

Human chromosome 8: entries, gene names and cross-references to MIM