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Protein

Heparan-alpha-glucosaminide N-acetyltransferase

Gene

HGSNAT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

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

Keywordsi

Molecular functionAcyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.3.1.78 2681
ReactomeiR-HSA-2024096 HS-GAG degradation
R-HSA-2206291 MPS IIIC - Sanfilippo syndrome C
R-HSA-6798695 Neutrophil degranulation
SABIO-RKiQ68CP4

Protein family/group databases

TCDBi9.B.169.4.1 the integral membrane protein (8 -10 tmss) yeib or duf418 (yeib) family

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

EuPathDBiHostDB:ENSG00000165102.14
HGNCiHGNC:26527 HGSNAT
MIMi610453 gene
neXtProtiNX_Q68CP4

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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

Keywords - Cellular componenti

Lysosome, Membrane

Pathology & Biotechi

Involvement in diseasei

Mucopolysaccharidosis 3C (MPS3C)9 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
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

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...) asparagineSequence analysis1
Glycosylationi142N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi151 ↔ 462Curated
Glycosylationi162N-linked (GlcNAc...) asparagineSequence 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
ProteomicsDBi66009
66010 [Q68CP4-2]

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 Expressed in 226 organ(s), highest expression level in mucosa of stomach
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

BioGridi126499, 2 interactors
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
OMAiKHSSWNG
OrthoDBiEOG091G042R
PhylomeDBiQ68CP4
TreeFamiTF324790

Family and domain databases

InterProiView protein in InterPro
IPR012429 DUF1624
PfamiView protein in Pfam
PF07786 DUF1624, 1 hit

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.

This entry has 2 described isoforms and 5 potential isoforms that are computationally mapped.iShow all

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

Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E5RJN0E5RJN0_HUMAN
Heparan-alpha-glucosaminide N-acety...
HGSNAT
352Annotation score:
E5RGH7E5RGH7_HUMAN
Heparan-alpha-glucosaminide N-acety...
HGSNAT
184Annotation score:
E5RJC4E5RJC4_HUMAN
Heparan-alpha-glucosaminide N-acety...
HGSNAT
172Annotation score:
E5RH11E5RH11_HUMAN
Heparan-alpha-glucosaminide N-acety...
HGSNAT
97Annotation score:
H0YAZ0H0YAZ0_HUMAN
Heparan-alpha-glucosaminide N-acety...
HGSNAT
253Annotation score:

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 dbSNP:rs73569592Ensembl.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 dbSNP:rs112029032Ensembl.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

Similar proteinsi

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

BioGridi126499, 2 interactors
IntActiQ68CP4, 2 interactors
STRINGi9606.ENSP00000368965

Protein family/group databases

TCDBi9.B.169.4.1 the integral membrane protein (8 -10 tmss) yeib or duf418 (yeib) family

PTM databases

iPTMnetiQ68CP4
PhosphoSitePlusiQ68CP4
SwissPalmiQ68CP4

Polymorphism and mutation databases

BioMutaiHGSNAT
DMDMi124007195

Proteomic databases

MaxQBiQ68CP4
PaxDbiQ68CP4
PeptideAtlasiQ68CP4
PRIDEiQ68CP4
ProteomicsDBi66009
66010 [Q68CP4-2]

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
EuPathDBiHostDB:ENSG00000165102.14
GeneCardsiHGSNAT
H-InvDBiHIX0007487
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
OMAiKHSSWNG
OrthoDBiEOG091G042R
PhylomeDBiQ68CP4
TreeFamiTF324790

Enzyme and pathway databases

BRENDAi2.3.1.78 2681
ReactomeiR-HSA-2024096 HS-GAG degradation
R-HSA-2206291 MPS IIIC - Sanfilippo syndrome C
R-HSA-6798695 Neutrophil degranulation
SABIO-RKiQ68CP4

Miscellaneous databases

ChiTaRSiHGSNAT human
GeneWikiiHGSNAT
GenomeRNAii138050
PROiPR:Q68CP4
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000165102 Expressed in 226 organ(s), highest expression level in mucosa of stomach
CleanExiHS_HGSNAT
ExpressionAtlasiQ68CP4 baseline and differential
GenevisibleiQ68CP4 HS

Family and domain databases

InterProiView protein in InterPro
IPR012429 DUF1624
PfamiView protein in Pfam
PF07786 DUF1624, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiHGNAT_HUMAN
AccessioniPrimary (citable) accession number: Q68CP4
Secondary accession number(s): B4E2V0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: September 12, 2018
This is version 119 of the entry and version 2 of the sequence. See 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

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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