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Q68CP4

- HGNAT_HUMAN

UniProt

Q68CP4 - HGNAT_HUMAN

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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

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
Complete GO annotation...

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
Complete GO annotation...

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...)1 Publication
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

BgeeiQ68CP4.
CleanExiHS_HGSNAT.
ExpressionAtlasiQ68CP4. baseline and differential.
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.
GeneTreeiENSGT00390000001491.
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

        10         20         30         40         50
MTGARASAAE QRRAGRSGQA RAAERAAGMS GAGRALAALL LAASVLSAAL
60 70 80 90 100
LAPGGSSGRD AQAAPPRDLD KKRHAELKMD QALLLIHNEL LWTNLTVYWK
110 120 130 140 150
SECCYHCLFQ VLVNVPQSPK AGKPSAAAAS VSTQHGSILQ LNDTLEEKEV
160 170 180 190 200
CRLEYRFGEF GNYSLLVKNI HNGVSEIACD LAVNEDPVDS NLPVSIAFLI
210 220 230 240 250
GLAVIIVISF LRLLLSLDDF NNWISKAISS RETDRLINSE LGSPSRTDPL
260 270 280 290 300
DGDVQPATWR LSALPPRLRS VDTFRGIALI LMVFVNYGGG KYWYFKHASW
310 320 330 340 350
NGLTVADLVF PWFVFIMGSS IFLSMTSILQ RGCSKFRLLG KIAWRSFLLI
360 370 380 390 400
CIGIIIVNPN YCLGPLSWDK VRIPGVLQRL GVTYFVVAVL ELLFAKPVPE
410 420 430 440 450
HCASERSCLS LRDITSSWPQ WLLILVLEGL WLGLTFLLPV PGCPTGYLGP
460 470 480 490 500
GGIGDFGKYP NCTGGAAGYI DRLLLGDDHL YQHPSSAVLY HTEVAYDPEG
510 520 530 540 550
ILGTINSIVM AFLGVQAGKI LLYYKARTKD ILIRFTAWCC ILGLISVALT
560 570 580 590 600
KVSENEGFIP VNKNLWSLSY VTTLSSFAFF ILLVLYPVVD VKGLWTGTPF
610 620 630 640 650
FYPGMNSILV YVGHEVFENY FPFQWKLKDN QSHKEHLTQN IVATALWVLI
660
AYILYRKKIF WKI

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.
GeneTreei ENSGT00390000001491.
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

Bgeei Q68CP4.
CleanExi HS_HGSNAT.
ExpressionAtlasi Q68CP4. baseline and differential.
Genevestigatori Q68CP4.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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 29, 2014
This is version 86 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