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Q68CP4

- HGNAT_HUMAN

UniProt

Q68CP4 - HGNAT_HUMAN

Protein

Heparan-alpha-glucosaminide N-acetyltransferase

Gene

HGSNAT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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.4 Publications

    Catalytic activityi

    Acetyl-CoA + heparan sulfate alpha-D-glucosaminide = CoA + heparan sulfate N-acetyl-alpha-D-glucosaminide.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei297 – 29711 Publication

    GO - Molecular functioni

    1. heparan-alpha-glucosaminide N-acetyltransferase activity Source: UniProtKB-EC
    2. transferase activity, transferring acyl groups Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. glycosaminoglycan catabolic process Source: Reactome
    3. glycosaminoglycan metabolic process Source: Reactome
    4. lysosomal transport Source: UniProtKB
    5. protein oligomerization Source: UniProtKB
    6. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Enzyme and pathway databases

    BRENDAi2.3.1.78. 2681.
    ReactomeiREACT_120752. HS-GAG degradation.
    SABIO-RKQ68CP4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heparan-alpha-glucosaminide N-acetyltransferase (EC:2.3.1.78)
    Alternative name(s):
    Transmembrane protein 76
    Gene namesi
    Name:HGSNAT
    Synonyms:TMEM76
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:26527. HGSNAT.

    Subcellular locationi

    Lysosome membrane 3 Publications; Multi-pass membrane protein 3 Publications
    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.

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. lysosomal membrane Source: UniProtKB

    Keywords - Cellular componenti

    Lysosome, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti104 – 1041C → 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. 1 Publication
    VAR_063983
    Natural varianti165 – 1651L → P in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. 3 Publications
    VAR_063984
    Natural varianti280 – 2801I → R in MPS3C. 1 Publication
    VAR_063986
    Natural varianti290 – 2901G → R in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum.
    VAR_063987
    Natural varianti301 – 3011N → K in MPS3C; retained in the endoplasmic reticulum and loss of enzymatic activity. 1 Publication
    VAR_063988
    Natural varianti311 – 3111P → L in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. 2 Publications
    VAR_030083
    Natural varianti372 – 3721R → C in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. 3 Publications
    VAR_030084
    Natural varianti372 – 3721R → H in MPS3C; Retained in the endoplasmic reticulum and loss of enzymatic activity. 1 Publication
    VAR_063989
    Natural varianti431 – 4311W → 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. 2 Publications
    VAR_063990
    Natural varianti452 – 4521G → S in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. 1 Publication
    VAR_030085
    Natural varianti499 – 4991E → K in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. 3 Publications
    VAR_030086
    Natural varianti510 – 5101M → K in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. 1 Publication
    VAR_030087
    Natural varianti514 – 5141G → E in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. 1 Publication
    VAR_063992
    Natural varianti517 – 5171A → E in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. 1 Publication
    VAR_063993
    Natural varianti546 – 5461S → F in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. 3 Publications
    VAR_063994
    Natural varianti567 – 5671S → C in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. 1 Publication
    VAR_063996
    Natural varianti569 – 5691S → L in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity. 2 Publications
    VAR_030088
    Natural varianti590 – 5901D → V in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity. 1 Publication
    VAR_030089
    Natural varianti599 – 5991P → L in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity. 1 Publication
    VAR_030090
    Natural varianti643 – 6431A → 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. 2 Publications
    Corresponds to variant rs112029032 [ dbSNP | Ensembl ].
    VAR_063997

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi107 – 1071C → S: Loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation. 1 Publication
    Mutagenesisi151 – 1511C → S: Loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation. 1 Publication
    Mutagenesisi179 – 1791C → S: Loss of intralysosomal proteolytic cleavage and enzymatic activity. 1 Publication
    Mutagenesisi236 – 2361L → A: Displayed both lysosomal and plasma membrane localization, reduced intralysosomal proteolytic cleavage and enzymatic activity; when associated with A-209. 1 Publication
    Mutagenesisi237 – 2371I → A: Displayed both lysosomal and plasma membrane localization, reduced intralysosomal proteolytic cleavage and enzymatic activity; when associated with A-208. 1 Publication
    Mutagenesisi297 – 2971H → A: Loss of enzymatic activity, but correctly targeted and processed. 1 Publication
    Mutagenesisi333 – 3331C → S: No loss of intralysosomal proteolytic cleavage and enzymatic activity. 1 Publication
    Mutagenesisi402 – 4021C → S: No loss of intralysosomal proteolytic cleavage and enzymatic activity. 1 Publication
    Mutagenesisi462 – 4621C → S: Complete loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation. 1 Publication
    Mutagenesisi479 – 4791H → A: Loss of intralysosomal proteolytic cleavage and enzymatic activity, retained in the endoplasmic reticulum. 1 Publication
    Mutagenesisi633 – 6331H → A: Loss of intralysosomal proteolytic cleavage and enzymatic activity, retained in the endoplasmic reticulum. 1 Publication
    Mutagenesisi652 – 66312Missing: Loss of intralysosomal proteolytic cleavage and enzymatic activity. Localized in the plasma membrane. Add
    BLAST

    Keywords - Diseasei

    Disease mutation, Mucopolysaccharidosis

    Organism-specific databases

    MIMi252930. phenotype.
    Orphaneti79271. Sanfilippo syndrome type C.
    PharmGKBiPA162390851.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 663663Heparan-alpha-glucosaminide N-acetyltransferasePRO_0000273153Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi94 – 941N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi142 – 1421N-linked (GlcNAc...)2 Publications
    Disulfide bondi151 ↔ 462Curated
    Glycosylationi162 – 1621N-linked (GlcNAc...)Sequence Analysis
    Modified residuei245 – 2451Phosphoserine1 Publication

    Post-translational modificationi

    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.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ68CP4.
    PaxDbiQ68CP4.
    PRIDEiQ68CP4.

    PTM databases

    PhosphoSiteiQ68CP4.

    Expressioni

    Tissue specificityi

    Widely expressed, with highest level in leukocytes, heart, liver, skeletal muscle, lung, placenta and liver.2 Publications

    Gene expression databases

    ArrayExpressiQ68CP4.
    BgeeiQ68CP4.
    CleanExiHS_HGSNAT.
    GenevestigatoriQ68CP4.

    Organism-specific databases

    HPAiHPA029578.

    Interactioni

    Subunit structurei

    Homooligomer. Homooligomerization is necessary for enzyme activity.1 Publication

    Protein-protein interaction databases

    IntActiQ68CP4. 2 interactions.
    STRINGi9606.ENSP00000368965.

    Structurei

    3D structure databases

    ProteinModelPortaliQ68CP4.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 190190Lumenal, vesicleSequence AnalysisAdd
    BLAST
    Topological domaini212 – 27564CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini297 – 3026Lumenal, vesicleSequence Analysis
    Topological domaini324 – 34522CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini367 – 3748Lumenal, vesicleSequence Analysis
    Topological domaini396 – 42025CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini442 – 50059Lumenal, vesicleSequence AnalysisAdd
    BLAST
    Topological domaini522 – 5298CytoplasmicSequence Analysis
    Topological domaini551 – 56414Lumenal, vesicleSequence AnalysisAdd
    BLAST
    Topological domaini586 – 5927CytoplasmicSequence Analysis
    Topological domaini614 – 63421Lumenal, vesicleSequence AnalysisAdd
    BLAST
    Topological domaini656 – 6638CytoplasmicSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei191 – 21121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei276 – 29621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei303 – 32321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei346 – 36621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei375 – 39521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei421 – 44121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei501 – 52121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei530 – 55021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei565 – 58521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei593 – 61321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei635 – 65521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni624 – 63512Lysosomal targeting regionAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi4 – 6461Ala-richAdd
    BLAST

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG4299.
    HOGENOMiHOG000006803.
    HOVERGENiHBG081599.
    InParanoidiQ68CP4.
    KOiK10532.
    OrthoDBiEOG7PS1F9.
    PhylomeDBiQ68CP4.
    TreeFamiTF324790.

    Family and domain databases

    InterProiIPR012429. DUF1624.
    [Graphical view]
    PfamiPF07786. DUF1624. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative initiation. Align

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

    Isoform 1 (identifier: Q68CP4-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MTGARASAAE QRRAGRSGQA RAAERAAGMS GAGRALAALL LAASVLSAAL    50
    LAPGGSSGRD AQAAPPRDLD KKRHAELKMD QALLLIHNEL LWTNLTVYWK 100
    SECCYHCLFQ VLVNVPQSPK AGKPSAAAAS VSTQHGSILQ LNDTLEEKEV 150
    CRLEYRFGEF GNYSLLVKNI HNGVSEIACD LAVNEDPVDS NLPVSIAFLI 200
    GLAVIIVISF LRLLLSLDDF NNWISKAISS RETDRLINSE LGSPSRTDPL 250
    DGDVQPATWR LSALPPRLRS VDTFRGIALI LMVFVNYGGG KYWYFKHASW 300
    NGLTVADLVF PWFVFIMGSS IFLSMTSILQ RGCSKFRLLG KIAWRSFLLI 350
    CIGIIIVNPN YCLGPLSWDK VRIPGVLQRL GVTYFVVAVL ELLFAKPVPE 400
    HCASERSCLS LRDITSSWPQ WLLILVLEGL WLGLTFLLPV PGCPTGYLGP 450
    GGIGDFGKYP NCTGGAAGYI DRLLLGDDHL YQHPSSAVLY HTEVAYDPEG 500
    ILGTINSIVM AFLGVQAGKI LLYYKARTKD ILIRFTAWCC ILGLISVALT 550
    KVSENEGFIP VNKNLWSLSY VTTLSSFAFF ILLVLYPVVD VKGLWTGTPF 600
    FYPGMNSILV YVGHEVFENY FPFQWKLKDN QSHKEHLTQN IVATALWVLI 650
    AYILYRKKIF WKI 663

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

    Length:663
    Mass (Da):73,293
    Last modified:January 23, 2007 - v2
    Checksum:iB05648474A3587B5
    GO
    Isoform 2 (identifier: Q68CP4-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:635
    Mass (Da):70,496
    Checksum:i177CDCFCF76CDB36
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti104 – 1041C → 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. 1 Publication
    VAR_063983
    Natural varianti165 – 1651L → P in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. 3 Publications
    VAR_063984
    Natural varianti265 – 2651P → Q Rare polymorphism that does not influence neither stability, nor activity, nor cellular localization of the enzyme. 4 Publications
    VAR_063985
    Natural varianti280 – 2801I → R in MPS3C. 1 Publication
    VAR_063986
    Natural varianti290 – 2901G → R in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum.
    VAR_063987
    Natural varianti301 – 3011N → K in MPS3C; retained in the endoplasmic reticulum and loss of enzymatic activity. 1 Publication
    VAR_063988
    Natural varianti311 – 3111P → L in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. 2 Publications
    VAR_030083
    Natural varianti372 – 3721R → C in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. 3 Publications
    VAR_030084
    Natural varianti372 – 3721R → H in MPS3C; Retained in the endoplasmic reticulum and loss of enzymatic activity. 1 Publication
    VAR_063989
    Natural varianti431 – 4311W → 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. 2 Publications
    VAR_063990
    Natural varianti452 – 4521G → S in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. 1 Publication
    VAR_030085
    Natural varianti499 – 4991E → K in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. 3 Publications
    VAR_030086
    Natural varianti509 – 5091V → L Rare polymorphism; no loss of enzymatic activity. 1 Publication
    VAR_063991
    Natural varianti510 – 5101M → K in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. 1 Publication
    VAR_030087
    Natural varianti514 – 5141G → E in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. 1 Publication
    VAR_063992
    Natural varianti517 – 5171A → E in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. 1 Publication
    VAR_063993
    Natural varianti546 – 5461S → F in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. 3 Publications
    VAR_063994
    Natural varianti551 – 5511K → Q Rare polymorphism; no loss of enzymatic activity. 2 Publications
    Corresponds to variant rs73569592 [ dbSNP | Ensembl ].
    VAR_063995
    Natural varianti567 – 5671S → C in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity; retained in the endoplasmic reticulum. 1 Publication
    VAR_063996
    Natural varianti569 – 5691S → L in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity. 2 Publications
    VAR_030088
    Natural varianti590 – 5901D → V in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity. 1 Publication
    VAR_030089
    Natural varianti599 – 5991P → L in MPS3C; results in a negligible amount of protein synthesis and very low enzyme activity. 1 Publication
    VAR_030090
    Natural varianti643 – 6431A → 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. 2 Publications
    Corresponds to variant rs112029032 [ dbSNP | Ensembl ].
    VAR_063997

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2828Missing in isoform 2. 1 PublicationVSP_040504Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK304441 mRNA. Translation: BAG65262.1.
    AC113191 Genomic DNA. No translation available.
    CR749838 mRNA. Translation: CAH18694.1.
    CCDSiCCDS47852.1. [Q68CP4-2]
    RefSeqiNP_689632.2. NM_152419.2. [Q68CP4-2]
    UniGeneiHs.600384.

    Genome annotation databases

    EnsembliENST00000379644; ENSP00000368965; ENSG00000165102. [Q68CP4-2]
    GeneIDi138050.
    KEGGihsa:138050.
    UCSCiuc003xpx.4. human. [Q68CP4-1]

    Polymorphism databases

    DMDMi124007195.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK304441 mRNA. Translation: BAG65262.1 .
    AC113191 Genomic DNA. No translation available.
    CR749838 mRNA. Translation: CAH18694.1 .
    CCDSi CCDS47852.1. [Q68CP4-2 ]
    RefSeqi NP_689632.2. NM_152419.2. [Q68CP4-2 ]
    UniGenei Hs.600384.

    3D structure databases

    ProteinModelPortali Q68CP4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q68CP4. 2 interactions.
    STRINGi 9606.ENSP00000368965.

    PTM databases

    PhosphoSitei Q68CP4.

    Polymorphism databases

    DMDMi 124007195.

    Proteomic databases

    MaxQBi Q68CP4.
    PaxDbi Q68CP4.
    PRIDEi Q68CP4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379644 ; ENSP00000368965 ; ENSG00000165102 . [Q68CP4-2 ]
    GeneIDi 138050.
    KEGGi hsa:138050.
    UCSCi uc003xpx.4. human. [Q68CP4-1 ]

    Organism-specific databases

    CTDi 138050.
    GeneCardsi GC08P042995.
    H-InvDB HIX0007487.
    HGNCi HGNC:26527. HGSNAT.
    HPAi HPA029578.
    MIMi 252930. phenotype.
    610453. gene.
    neXtProti NX_Q68CP4.
    Orphaneti 79271. Sanfilippo syndrome type C.
    PharmGKBi PA162390851.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4299.
    HOGENOMi HOG000006803.
    HOVERGENi HBG081599.
    InParanoidi Q68CP4.
    KOi K10532.
    OrthoDBi EOG7PS1F9.
    PhylomeDBi Q68CP4.
    TreeFami TF324790.

    Enzyme and pathway databases

    BRENDAi 2.3.1.78. 2681.
    Reactomei REACT_120752. HS-GAG degradation.
    SABIO-RK Q68CP4.

    Miscellaneous databases

    ChiTaRSi HGSNAT. human.
    GeneWikii HGSNAT.
    GenomeRNAii 138050.
    NextBioi 83735.
    PROi Q68CP4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q68CP4.
    Bgeei Q68CP4.
    CleanExi HS_HGSNAT.
    Genevestigatori Q68CP4.

    Family and domain databases

    InterProi IPR012429. DUF1624.
    [Graphical view ]
    Pfami PF07786. DUF1624. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Placenta.
    6. 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. 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. 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.

    Entry informationi

    Entry nameiHGNAT_HUMAN
    AccessioniPrimary (citable) accession number: Q68CP4
    Secondary accession number(s): B4E2V0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2007
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 85 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Miscellaneous

    A signal sequence is predicted but has been shown not to be cleaved in the reticulum endoplasmic.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

    External Data

    Dasty 3