HGSNAT
entrez
138050
canonical
uniprot
Q68CP4
canonical
ensembl
ENSG00000165102
resolver
ensp
ENSP00000368965
resolver
ensp
ENSP00000572515
resolver
ensp
ENSP00000572516
resolver
ensp
ENSP00000572518
resolver
ensp
ENSP00000789466
resolver
genesymbol
HGSNAT
resolver
genesymbol_syn
TMEM76
resolver
hgnc
HGNC:26527
resolver
uniprot
B4E2V0
resolver
uniprot
Q8IVU6
resolver
uniprot_entry
HGNAT_HUMAN
resolver
uniprot_entry
Q8IVU6_HUMAN
resolver
uniprot_sec
B4E2V0
resolver
amino_acid_sequence
MTGARASAAEQRRAGRSGQARAAERAAGMSGAGRALAALLLAASVLSAALLAPGGSSGRDAQAAPPRDLDKKRHAELKMDQALLLIHNELLWTNLTVYWKSECCYHCLFQVLVNVPQSPKAGKPSAAAASVSTQHGSILQLNDTLEEKEVCRLEYRFGEFGNYSLLVKNIHNGVSEIACDLAVNEDPVDSNLPVSIAFLIGLAVIIVISFLRLLLSLDDFNNWISKAISSRETDRLINSELGSPSRTDPLDGDVQPATWRLSALPPRLRSVDTFRGIALILMVFVNYGGGKYWYFKHASWNGLTVADLVFPWFVFIMGSSIFLSMTSILQRGCSKFRLLGKIAWRSFLLICIGIIIVNPNYCLGPLSWDKVRIPGVLQRLGVTYFVVAVLELLFAKPVPEHCASERSCLSLRDITSSWPQWLLILVLEGLWLGLTFLLPVPGCPTGYLGPGGIGDFGKYPNCTGGAAGYIDRLLLGDDHLYQHPSSAVLYHTEVAYDPEGILGTINSIVMAFLGVQAGKILLYYKARTKDILIRFTAWCCILGLISVALTKVSENEGFIPVNKNLWSLSYVTTLSSFAFFILLVLYPVVDVKGLWTGTPFFYPGMNSILVYVGHEVFENYFPFQWKLKDNQSHKEHLTQNIVATALWVLIAYILYRKKIFWKI
uniprot
proteins
disease_involvement
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. {ECO:0000269|PubMed:16960811, ECO:0000269|PubMed:17033958, ECO:0000269|PubMed:17397050, ECO:0000269|PubMed:18024218, ECO:0000269|PubMed:19479962, ECO:0000269|PubMed:19823584, ECO:0000269|PubMed:20583299, ECO:0000269|PubMed:20825431, ECO:0000269|PubMed:28101780}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Retinitis pigmentosa 73 (RP73) [MIM:616544]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. {ECO:0000269|PubMed:25859010}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.3.1.78
uniprot
proteins
function
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. {ECO:0000269|PubMed:16960811, ECO:0000269|PubMed:17033958, ECO:0000269|PubMed:19823584, ECO:0000269|PubMed:20650889}.
uniprot
proteins
mass_dalton
73293
uniprot
proteins
mutagenesis
MUTAGEN 107; /note="C->S: Loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation."; /evidence="ECO:0000269|PubMed:20650889"; MUTAGEN 151; /note="C->S: Loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation."; /evidence="ECO:0000269|PubMed:20650889"; MUTAGEN 179; /note="C->S: Loss of intralysosomal proteolytic cleavage and enzymatic activity."; /evidence="ECO:0000269|PubMed:20650889"; MUTAGEN 236; /note="L->A: Displayed both lysosomal and plasma membrane localization, reduced intralysosomal proteolytic cleavage and enzymatic activity; when associated with A-209."; /evidence="ECO:0000269|PubMed:20650889"; MUTAGEN 237; /note="I->A: Displayed both lysosomal and plasma membrane localization, reduced intralysosomal proteolytic cleavage and enzymatic activity; when associated with A-208."; /evidence="ECO:0000269|PubMed:20650889"; MUTAGEN 297; /note="H->A: Loss of enzymatic activity, but correctly targeted and processed."; /evidence="ECO:0000269|PubMed:20650889"; MUTAGEN 333; /note="C->S: No loss of intralysosomal proteolytic cleavage and enzymatic activity."; /evidence="ECO:0000269|PubMed:20650889"; MUTAGEN 402; /note="C->S: No loss of intralysosomal proteolytic cleavage and enzymatic activity."; /evidence="ECO:0000269|PubMed:20650889"; MUTAGEN 462; /note="C->S: Complete loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation."; /evidence="ECO:0000269|PubMed:20650889"; MUTAGEN 479; /note="H->A: Loss of intralysosomal proteolytic cleavage and enzymatic activity, retained in the endoplasmic reticulum."; /evidence="ECO:0000269|PubMed:20650889"; MUTAGEN 633; /note="H->A: Loss of intralysosomal proteolytic cleavage and enzymatic activity, retained in the endoplasmic reticulum."; /evidence="ECO:0000269|PubMed:20650889"; MUTAGEN 652..663; /note="Missing: Loss of intralysosomal proteolytic cleavage and enzymatic activity. Localized in the plasma membrane.
uniprot
proteins
post_translational_modification
PTM: 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.; PTM: Glycosylated. {ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19823584}.
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
16421571
uniprot
proteins
pubmed
16960811
uniprot
proteins
pubmed
17033958
uniprot
proteins
pubmed
17397050
uniprot
proteins
pubmed
17897319
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18024218
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19479962
uniprot
proteins
pubmed
19823584
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20583299
uniprot
proteins
pubmed
20650889
uniprot
proteins
pubmed
20825431
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
25859010
uniprot
proteins
pubmed
28101780
uniprot
proteins
sequence_length
663
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:16960811, ECO:0000269|PubMed:17033958, ECO:0000269|PubMed:17897319}; Multi-pass membrane protein {ECO:0000269|PubMed:16960811, ECO:0000269|PubMed:17033958, ECO:0000269|PubMed:17897319}. 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.
uniprot
proteins
transmembrane_region
TRANSMEM 191..211; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 276..296; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 303..323; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 346..366; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 375..395; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 421..441; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 501..521; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 530..550; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 565..585; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 593..613; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 635..655; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins