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Protein

Heparan-alpha-glucosaminide N-acetyltransferase

Gene

HGSNAT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei2971 Publication1

GO - Molecular functioni

GO - Biological processi

  • glycosaminoglycan catabolic process Source: Reactome
  • lysosomal transport Source: UniProtKB
  • protein oligomerization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BioCyciZFISH:HS15282-MONOMER.
BRENDAi2.3.1.78. 2681.
ReactomeiR-HSA-2024096. HS-GAG degradation.
R-HSA-6798695. Neutrophil degranulation.
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
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:26527. HGSNAT.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 190Lumenal, vesicleSequence analysisAdd BLAST190
Transmembranei191 – 211HelicalSequence analysisAdd BLAST21
Topological domaini212 – 275CytoplasmicSequence analysisAdd BLAST64
Transmembranei276 – 296HelicalSequence analysisAdd BLAST21
Topological domaini297 – 302Lumenal, vesicleSequence analysis6
Transmembranei303 – 323HelicalSequence analysisAdd BLAST21
Topological domaini324 – 345CytoplasmicSequence analysisAdd BLAST22
Transmembranei346 – 366HelicalSequence analysisAdd BLAST21
Topological domaini367 – 374Lumenal, vesicleSequence analysis8
Transmembranei375 – 395HelicalSequence analysisAdd BLAST21
Topological domaini396 – 420CytoplasmicSequence analysisAdd BLAST25
Transmembranei421 – 441HelicalSequence analysisAdd BLAST21
Topological domaini442 – 500Lumenal, vesicleSequence analysisAdd BLAST59
Transmembranei501 – 521HelicalSequence analysisAdd BLAST21
Topological domaini522 – 529CytoplasmicSequence analysis8
Transmembranei530 – 550HelicalSequence analysisAdd BLAST21
Topological domaini551 – 564Lumenal, vesicleSequence analysisAdd BLAST14
Transmembranei565 – 585HelicalSequence analysisAdd BLAST21
Topological domaini586 – 592CytoplasmicSequence analysis7
Transmembranei593 – 613HelicalSequence analysisAdd BLAST21
Topological domaini614 – 634Lumenal, vesicleSequence analysisAdd BLAST21
Transmembranei635 – 655HelicalSequence analysisAdd BLAST21
Topological domaini656 – 663CytoplasmicSequence analysis8

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • lysosomal membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Membrane

Pathology & Biotechi

Involvement in diseasei

Mucopolysaccharidosis 3C (MPS3C)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:252930
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07581282A → V in MPS3C; shows practically no enzyme activity. 1 Publication1
Natural variantiVAR_063983104C → F in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum; loss of intralysosomal proteolytic cleavage. 4 Publications1
Natural variantiVAR_075813141L → P in MPS3C; shows practically no enzyme activity. 1 Publication1
Natural variantiVAR_063984165L → P in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. 5 Publications1
Natural variantiVAR_063986280I → R in MPS3C. 1 Publication1
Natural variantiVAR_063987290G → R in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. 3 Publications1
Natural variantiVAR_063988301N → K in MPS3C; retained in the endoplasmic reticulum; loss of enzymatic activity. 2 Publications1
Natural variantiVAR_030083311P → L in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. 4 Publications1
Natural variantiVAR_030084372R → C in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. 4 Publications1
Natural variantiVAR_063989372R → H in MPS3C; retained in the endoplasmic reticulum; loss of enzymatic activity. 2 Publications1
Natural variantiVAR_063990431W → C in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. 4 Publications1
Natural variantiVAR_030085452G → S in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. 3 Publications1
Natural variantiVAR_075816452G → V in MPS3C; shows practically no enzyme activity. 1 Publication1
Natural variantiVAR_075817473L → P in MPS3C; shows practically no enzyme activity. 1 Publication1
Natural variantiVAR_030086499E → K in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. 5 Publications1
Natural variantiVAR_030087510M → K in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. 3 Publications1
Natural variantiVAR_063992514G → E in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. 2 Publications1
Natural variantiVAR_063993517A → E in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. 3 Publications1
Natural variantiVAR_063994546S → F in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. 6 Publications1
Natural variantiVAR_063996567S → C in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. 3 Publications1
Natural variantiVAR_030088569S → L in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity. 4 Publications1
Natural variantiVAR_030089590D → V in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity. 3 Publications1
Natural variantiVAR_030090599P → L in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity. 3 Publications1
Natural variantiVAR_063997643A → T in RP73 and MPS3C; unknown pathological significance; may act as a modifier of disease severity in patients with retinitis pigmentosa; has a negligible effect on the enzyme expression; moderately reduced enzyme activity. 5 PublicationsCorresponds to variant rs112029032dbSNPEnsembl.1
Retinitis pigmentosa 73 (RP73)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:616544
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075814152R → W in RP73. 1 Publication1
Natural variantiVAR_075815161G → A in RP73. 1 Publication1
Natural variantiVAR_063997643A → T in RP73 and MPS3C; unknown pathological significance; may act as a modifier of disease severity in patients with retinitis pigmentosa; has a negligible effect on the enzyme expression; moderately reduced enzyme activity. 5 PublicationsCorresponds to variant rs112029032dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi107C → S: Loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation. 1 Publication1
Mutagenesisi151C → S: Loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation. 1 Publication1
Mutagenesisi179C → S: Loss of intralysosomal proteolytic cleavage and enzymatic activity. 1 Publication1
Mutagenesisi236L → A: Displayed both lysosomal and plasma membrane localization, reduced intralysosomal proteolytic cleavage and enzymatic activity; when associated with A-209. 1 Publication1
Mutagenesisi237I → A: Displayed both lysosomal and plasma membrane localization, reduced intralysosomal proteolytic cleavage and enzymatic activity; when associated with A-208. 1 Publication1
Mutagenesisi297H → A: Loss of enzymatic activity, but correctly targeted and processed. 1 Publication1
Mutagenesisi333C → S: No loss of intralysosomal proteolytic cleavage and enzymatic activity. 1 Publication1
Mutagenesisi402C → S: No loss of intralysosomal proteolytic cleavage and enzymatic activity. 1 Publication1
Mutagenesisi462C → S: Complete loss of intralysosomal proteolytic cleavage and enzymatic activity. Reduced oligomer formation. 1 Publication1
Mutagenesisi479H → A: Loss of intralysosomal proteolytic cleavage and enzymatic activity, retained in the endoplasmic reticulum. 1 Publication1
Mutagenesisi633H → A: Loss of intralysosomal proteolytic cleavage and enzymatic activity, retained in the endoplasmic reticulum. 1 Publication1
Mutagenesisi652 – 663Missing : Loss of intralysosomal proteolytic cleavage and enzymatic activity. Localized in the plasma membrane. Add BLAST12

Keywords - Diseasei

Disease mutation, Mucopolysaccharidosis, Retinitis pigmentosa

Organism-specific databases

DisGeNETi138050.
MalaCardsiHGSNAT.
MIMi252930. phenotype.
616544. phenotype.
OpenTargetsiENSG00000165102.
Orphaneti79271. Sanfilippo syndrome type C.
PharmGKBiPA162390851.

Polymorphism and mutation databases

BioMutaiHGSNAT.
DMDMi124007195.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002731531 – 663Heparan-alpha-glucosaminide N-acetyltransferaseAdd BLAST663

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi94N-linked (GlcNAc...)Sequence analysis1
Glycosylationi142N-linked (GlcNAc...)1 Publication1
Disulfide bondi151 ↔ 462Curated
Glycosylationi162N-linked (GlcNAc...)Sequence analysis1
Modified residuei243PhosphoserineCombined sources1
Modified residuei245PhosphoserineCombined sources1

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.
PeptideAtlasiQ68CP4.
PRIDEiQ68CP4.

PTM databases

iPTMnetiQ68CP4.
PhosphoSitePlusiQ68CP4.
SwissPalmiQ68CP4.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000165102.
CleanExiHS_HGSNAT.
ExpressionAtlasiQ68CP4. baseline and differential.
GenevisibleiQ68CP4. HS.

Organism-specific databases

HPAiHPA029578.

Interactioni

Subunit structurei

Homooligomer. Homooligomerization is necessary for enzyme activity.1 Publication

Protein-protein interaction databases

IntActiQ68CP4. 2 interactors.
STRINGi9606.ENSP00000368965.

Structurei

3D structure databases

ProteinModelPortaliQ68CP4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni624 – 635Lysosomal targeting regionAdd BLAST12

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi4 – 64Ala-richAdd BLAST61

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4683. Eukaryota.
COG4299. LUCA.
GeneTreeiENSGT00390000001491.
HOGENOMiHOG000006803.
HOVERGENiHBG081599.
InParanoidiQ68CP4.
KOiK10532.
OMAiNSERCYH.
OrthoDBiEOG091G042R.
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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_07581282A → V in MPS3C; shows practically no enzyme activity. 1 Publication1
Natural variantiVAR_063983104C → F in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum; loss of intralysosomal proteolytic cleavage. 4 Publications1
Natural variantiVAR_075813141L → P in MPS3C; shows practically no enzyme activity. 1 Publication1
Natural variantiVAR_075814152R → W in RP73. 1 Publication1
Natural variantiVAR_075815161G → A in RP73. 1 Publication1
Natural variantiVAR_063984165L → P in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. 5 Publications1
Natural variantiVAR_063985265P → Q Rare polymorphism; does not influence stability; does not influence activity; does not influence cellular localization of the enzyme. 7 Publications1
Natural variantiVAR_063986280I → R in MPS3C. 1 Publication1
Natural variantiVAR_063987290G → R in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. 3 Publications1
Natural variantiVAR_063988301N → K in MPS3C; retained in the endoplasmic reticulum; loss of enzymatic activity. 2 Publications1
Natural variantiVAR_030083311P → L in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. 4 Publications1
Natural variantiVAR_030084372R → C in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. 4 Publications1
Natural variantiVAR_063989372R → H in MPS3C; retained in the endoplasmic reticulum; loss of enzymatic activity. 2 Publications1
Natural variantiVAR_063990431W → C in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. 4 Publications1
Natural variantiVAR_030085452G → S in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. 3 Publications1
Natural variantiVAR_075816452G → V in MPS3C; shows practically no enzyme activity. 1 Publication1
Natural variantiVAR_075817473L → P in MPS3C; shows practically no enzyme activity. 1 Publication1
Natural variantiVAR_030086499E → K in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. 5 Publications1
Natural variantiVAR_063991509V → L Rare polymorphism; no loss of enzymatic activity. 3 Publications1
Natural variantiVAR_030087510M → K in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. 3 Publications1
Natural variantiVAR_063992514G → E in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. 2 Publications1
Natural variantiVAR_063993517A → E in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. 3 Publications1
Natural variantiVAR_063994546S → F in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. 6 Publications1
Natural variantiVAR_063995551K → Q Rare polymorphism; no loss of enzymatic activity. 4 PublicationsCorresponds to variant rs73569592dbSNPEnsembl.1
Natural variantiVAR_063996567S → C in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity; retained in the endoplasmic reticulum. 3 Publications1
Natural variantiVAR_030088569S → L in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity. 4 Publications1
Natural variantiVAR_030089590D → V in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity. 3 Publications1
Natural variantiVAR_030090599P → L in MPS3C; results in a negligible amount of protein synthesis; very low enzyme activity. 3 Publications1
Natural variantiVAR_063997643A → T in RP73 and MPS3C; unknown pathological significance; may act as a modifier of disease severity in patients with retinitis pigmentosa; has a negligible effect on the enzyme expression; moderately reduced enzyme activity. 5 PublicationsCorresponds to variant rs112029032dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0405041 – 28Missing in isoform 2. 1 PublicationAdd BLAST28

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.5. human. [Q68CP4-1]

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ68CP4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ68CP4. 2 interactors.
STRINGi9606.ENSP00000368965.

PTM databases

iPTMnetiQ68CP4.
PhosphoSitePlusiQ68CP4.
SwissPalmiQ68CP4.

Polymorphism and mutation databases

BioMutaiHGSNAT.
DMDMi124007195.

Proteomic databases

MaxQBiQ68CP4.
PaxDbiQ68CP4.
PeptideAtlasiQ68CP4.
PRIDEiQ68CP4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379644; ENSP00000368965; ENSG00000165102. [Q68CP4-2]
GeneIDi138050.
KEGGihsa:138050.
UCSCiuc003xpx.5. human. [Q68CP4-1]

Organism-specific databases

CTDi138050.
DisGeNETi138050.
GeneCardsiHGSNAT.
H-InvDBHIX0007487.
HGNCiHGNC:26527. HGSNAT.
HPAiHPA029578.
MalaCardsiHGSNAT.
MIMi252930. phenotype.
610453. gene.
616544. phenotype.
neXtProtiNX_Q68CP4.
OpenTargetsiENSG00000165102.
Orphaneti79271. Sanfilippo syndrome type C.
PharmGKBiPA162390851.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4683. Eukaryota.
COG4299. LUCA.
GeneTreeiENSGT00390000001491.
HOGENOMiHOG000006803.
HOVERGENiHBG081599.
InParanoidiQ68CP4.
KOiK10532.
OMAiNSERCYH.
OrthoDBiEOG091G042R.
PhylomeDBiQ68CP4.
TreeFamiTF324790.

Enzyme and pathway databases

BioCyciZFISH:HS15282-MONOMER.
BRENDAi2.3.1.78. 2681.
ReactomeiR-HSA-2024096. HS-GAG degradation.
R-HSA-6798695. Neutrophil degranulation.
SABIO-RKQ68CP4.

Miscellaneous databases

ChiTaRSiHGSNAT. human.
GeneWikiiHGSNAT.
GenomeRNAii138050.
PROiQ68CP4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000165102.
CleanExiHS_HGSNAT.
ExpressionAtlasiQ68CP4. baseline and differential.
GenevisibleiQ68CP4. HS.

Family and domain databases

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

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: November 30, 2016
This is version 108 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.