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Protein

N-sulphoglucosamine sulphohydrolase

Gene

SGSH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes a step in lysosomal heparan sulfate degradation.3 Publications

Catalytic activityi

N-sulfo-D-glucosamine + H2O = D-glucosamine + sulfate.3 Publications

Cofactori

Ca2+1 PublicationNote: Binds 1 Ca2+ ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi31CalciumCombined sources1 Publication1
Metal bindingi32CalciumCombined sources1 Publication1
Metal bindingi70Calcium; via 3-oxoalanineCombined sources1 Publication1
Metal bindingi273CalciumCombined sources1 Publication1
Metal bindingi274CalciumCombined sources1 Publication1

GO - Molecular functioni

GO - Biological processi

  • glycosaminoglycan catabolic process Source: UniProtKB
  • heparan sulfate proteoglycan catabolic process Source: UniProtKB

Keywordsi

Molecular functionHydrolase
LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.10.1.1. 2681.
ReactomeiR-HSA-2024096. HS-GAG degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
N-sulphoglucosamine sulphohydrolase (EC:3.10.1.13 Publications)
Alternative name(s):
Sulfoglucosamine sulfamidase
Sulphamidase
Gene namesi
Name:SGSH
Synonyms:HSS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:10818. SGSH.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • lysosomal lumen Source: Reactome
  • lysosome Source: UniProtKB

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Involvement in diseasei

Mucopolysaccharidosis 3A (MPS3A)16 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA severe 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. MPS3A is characterized by earlier onset, rapid progression of symptoms and shorter survival.
See also OMIM:252900
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05467032D → E in MPS3A. 1 Publication1
Natural variantiVAR_05467132D → G in MPS3A. 1 Publication1
Natural variantiVAR_00738840Y → N in MPS3A; intermediate. 1 Publication1
Natural variantiVAR_05467242N → K in MPS3A; does not yield active enzyme; the reduction in 62 kDa precursor and 56 kDa mature forms suggests an increased degradation of the mutant enzyme. 1 Publication1
Natural variantiVAR_00738944A → T in MPS3A; severe. 1 Publication1
Natural variantiVAR_00739066S → W in MPS3A; intermediate/severe; common mutation in Italy. 3 PublicationsCorresponds to variant dbSNP:rs104894637Ensembl.1
Natural variantiVAR_00739174R → C in MPS3A; intermediate/severe; the mutant is enzymatically inactive; rapid degradation rather than decrease in synthesis is responsible for the low steady state level of the mutant protein in cells; the majority of newly synthesized protein probably occurs in the endoplasmic reticulum. 6 PublicationsCorresponds to variant dbSNP:rs104894636Ensembl.1
Natural variantiVAR_00739274R → H in MPS3A. Corresponds to variant dbSNP:rs778336949Ensembl.1
Natural variantiVAR_00739379T → P in MPS3A; severe. 1 PublicationCorresponds to variant dbSNP:rs779703983Ensembl.1
Natural variantiVAR_00739484 – 85Missing in MPS3A. 2
Natural variantiVAR_05467384H → Y in MPS3A. 1 Publication1
Natural variantiVAR_00739585Q → R in MPS3A. 1 Publication1
Natural variantiVAR_05467488M → T in MPS3A. 1 Publication1
Natural variantiVAR_00739690G → R in MPS3A. Corresponds to variant dbSNP:rs774010006Ensembl.1
Natural variantiVAR_054675106S → R in MPS3A; shows 3.3% activity of the expressed wild-type enzyme; rapid degradation rather than decrease in synthesis is responsible for the low steady state level of the mutant protein in cells. 1 Publication1
Natural variantiVAR_007397122G → R in MPS3A; intermediate. 2 PublicationsCorresponds to variant dbSNP:rs761607612Ensembl.1
Natural variantiVAR_007398128P → L in MPS3A; intermediate. 2 PublicationsCorresponds to variant dbSNP:rs104894642Ensembl.1
Natural variantiVAR_007399131V → M in MPS3A. Corresponds to variant dbSNP:rs370636303Ensembl.1
Natural variantiVAR_007400139T → M in MPS3A. Corresponds to variant dbSNP:rs775112689Ensembl.1
Natural variantiVAR_007401146L → P in MPS3A; severe. 1 PublicationCorresponds to variant dbSNP:rs749358773Ensembl.1
Natural variantiVAR_007402150R → Q in MPS3A; severe. 1 PublicationCorresponds to variant dbSNP:rs104894638Ensembl.1
Natural variantiVAR_054676150R → W in MPS3A. 1 Publication1
Natural variantiVAR_054677163L → P in MPS3A; the mutant is enzymatically inactive; rapid degradation rather than decrease in synthesis is responsible for the low steady state level of the mutant protein in cells; the mutant protein shows instability in the lysosomes. 1 Publication1
Natural variantiVAR_007403179D → N in MPS3A; severe. 1 PublicationCorresponds to variant dbSNP:rs774773010Ensembl.1
Natural variantiVAR_007404182R → C in MPS3A; intermediate. 1 PublicationCorresponds to variant dbSNP:rs529855742Ensembl.1
Natural variantiVAR_054678191G → R in MPS3A; the mutant is enzymatically inactive; rapid degradation rather than decrease in synthesis is responsible for the low steady state level of the mutant protein in cells; the majority of newly synthesized protein probably occurs in the endoplasmic reticulum. 1 PublicationCorresponds to variant dbSNP:rs753666460Ensembl.1
Natural variantiVAR_007405193F → L in MPS3A. 1
Natural variantiVAR_007406206R → P in MPS3A; the mutant enzyme retains 8% residual activity. 2 PublicationsCorresponds to variant dbSNP:rs104894643Ensembl.1
Natural variantiVAR_007408227P → R in MPS3A; severe. 1 PublicationCorresponds to variant dbSNP:rs774602372Ensembl.1
Natural variantiVAR_007409234A → G in MPS3A. Corresponds to variant dbSNP:rs113641837Ensembl.1
Natural variantiVAR_054679235D → N in MPS3A; does not yield active enzyme; the reduction in 62 kDa precursor and 56 kDa mature forms suggests an increased degradation of the mutant enzyme. 2 PublicationsCorresponds to variant dbSNP:rs753472891Ensembl.1
Natural variantiVAR_007410235D → V in MPS3A. Corresponds to variant dbSNP:rs763800418Ensembl.1
Natural variantiVAR_007411245R → H in MPS3A; severe; common mutation in Western Europe and Australia. 3 PublicationsCorresponds to variant dbSNP:rs104894635Ensembl.1
Natural variantiVAR_054680251G → A in MPS3A. 2 PublicationsCorresponds to variant dbSNP:rs144461610Ensembl.1
Natural variantiVAR_054681273D → N in MPS3A. 1 Publication1
Natural variantiVAR_054682288P → S in MPS3A. 1 Publication1
Natural variantiVAR_054683293P → S in MPS3A; does not yield active enzyme; the reduction in 62 kDa precursor and 56 kDa mature forms suggests an increased degradation of the mutant enzyme. 1 PublicationCorresponds to variant dbSNP:rs143947056Ensembl.1
Natural variantiVAR_054684293P → T in MPS3A. 1 Publication1
Natural variantiVAR_007412298S → P in MPS3A; associated with a slowly progressive clinical phenotype; rapidly degraded but small amounts of the mutant protein are correctly transported to the lysosome; low but significant residual enzymatic activity. 3 PublicationsCorresponds to variant dbSNP:rs138504221Ensembl.1
Natural variantiVAR_054685300E → V in MPS3A. 1 Publication1
Natural variantiVAR_054687307Q → P in MPS3A. 1 Publication1
Natural variantiVAR_007413321T → A in MPS3A. Corresponds to variant dbSNP:rs758756630Ensembl.1
Natural variantiVAR_054688322I → S in MPS3A. 1 Publication1
Natural variantiVAR_007414354A → P in MPS3A. 1 Publication1
Natural variantiVAR_054689355E → K in MPS3A. 1 PublicationCorresponds to variant dbSNP:rs766938111Ensembl.1
Natural variantiVAR_007416364S → R in MPS3A. 1
Natural variantiVAR_007417369E → K in MPS3A; intermediate. 2 PublicationsCorresponds to variant dbSNP:rs104894640Ensembl.1
Natural variantiVAR_054690374Y → H in MPS3A. 1 Publication1
Natural variantiVAR_007418377R → C in MPS3A; severe; does not yield active enzyme; the reduction in 62 kDa precursor and 56 kDa mature forms suggests an increased degradation of the mutant enzyme. 2 PublicationsCorresponds to variant dbSNP:rs772311757Ensembl.1
Natural variantiVAR_007419377R → H in MPS3A. Corresponds to variant dbSNP:rs746037899Ensembl.1
Natural variantiVAR_007420380Q → R in MPS3A. Corresponds to variant dbSNP:rs144143780Ensembl.1
Natural variantiVAR_054691381H → HQR in MPS3A. 1
Natural variantiVAR_007421386L → R in MPS3A. 1 Publication1
Natural variantiVAR_007422389N → K in MPS3A. Corresponds to variant dbSNP:rs764057581Ensembl.1
Natural variantiVAR_054693403Missing in MPS3A; the mutant is enzymatically inactive; rapid degradation rather than decrease in synthesis is responsible for the low steady state level of the mutant protein in cells. 1 Publication1
Natural variantiVAR_054694432 – 435YRAR → W in MPS3A. 4
Natural variantiVAR_054695433R → Q in MPS3A; severe. 1 PublicationCorresponds to variant dbSNP:rs104894641Ensembl.1
Natural variantiVAR_054696433R → W in MPS3A; the mutant is enzymatically inactive; rapid degradation rather than decrease in synthesis is responsible for the low steady state level of the mutant protein in cells; the majority of newly synthesized protein probably occurs in the endoplasmic reticulum. 2 PublicationsCorresponds to variant dbSNP:rs777267343Ensembl.1
Natural variantiVAR_054697436 – 438Missing in MPS3A. 1 Publication3
Natural variantiVAR_007423447E → K in MPS3A. Corresponds to variant dbSNP:rs104894639Ensembl.1
Natural variantiVAR_054698486V → F in MPS3A. 1 Publication1

Keywords - Diseasei

Disease mutation, Mucopolysaccharidosis

Organism-specific databases

DisGeNETi6448.
MalaCardsiSGSH.
MIMi252900. phenotype.
OpenTargetsiENSG00000181523.
Orphaneti79269. Sanfilippo syndrome type A.
PharmGKBiPA35726.

Polymorphism and mutation databases

BioMutaiSGSH.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 201 PublicationAdd BLAST20
ChainiPRO_000003343321 – 502N-sulphoglucosamine sulphohydrolaseAdd BLAST482

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi41N-linked (GlcNAc...)Combined sources3 Publications1
Modified residuei703-oxoalanine (Cys)1 Publication1
Glycosylationi142N-linked (GlcNAc...)Sequence analysis1
Glycosylationi151N-linked (GlcNAc...)Combined sources1 Publication1
Disulfide bondi183 ↔ 194Combined sources1 Publication
Glycosylationi264N-linked (GlcNAc...)Combined sources2 Publications1
Glycosylationi413N-linked (GlcNAc...)Combined sources2 Publications1
Disulfide bondi481 ↔ 495Combined sources1 Publication

Post-translational modificationi

The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP51688.
MaxQBiP51688.
PaxDbiP51688.
PeptideAtlasiP51688.
PRIDEiP51688.

PTM databases

iPTMnetiP51688.
PhosphoSitePlusiP51688.

Expressioni

Gene expression databases

BgeeiENSG00000181523.
CleanExiHS_SGSH.
ExpressionAtlasiP51688. baseline and differential.
GenevisibleiP51688. HS.

Organism-specific databases

HPAiHPA023436.
HPA023451.

Interactioni

Protein-protein interaction databases

BioGridi112346. 11 interactors.
IntActiP51688. 1 interactor.
STRINGi9606.ENSP00000314606.

Structurei

Secondary structure

1502
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi24 – 32Combined sources9
Helixi38 – 40Combined sources3
Beta strandi43 – 45Combined sources3
Helixi48 – 54Combined sources7
Beta strandi57 – 64Combined sources8
Helixi70 – 77Combined sources8
Helixi83 – 86Combined sources4
Turni94 – 96Combined sources3
Helixi107 – 113Combined sources7
Beta strandi117 – 122Combined sources6
Turni129 – 131Combined sources3
Beta strandi135 – 139Combined sources5
Helixi145 – 149Combined sources5
Helixi152 – 164Combined sources13
Beta strandi171 – 176Combined sources6
Turni184 – 186Combined sources3
Helixi188 – 190Combined sources3
Turni195 – 198Combined sources4
Beta strandi199 – 201Combined sources3
Turni202 – 204Combined sources3
Turni217 – 219Combined sources3
Helixi230 – 259Combined sources30
Helixi263 – 265Combined sources3
Beta strandi266 – 274Combined sources9
Helixi287 – 290Combined sources4
Beta strandi294 – 297Combined sources4
Turni303 – 306Combined sources4
Beta strandi307 – 314Combined sources8
Helixi315 – 317Combined sources3
Helixi318 – 325Combined sources8
Beta strandi334 – 336Combined sources3
Helixi349 – 352Combined sources4
Beta strandi360 – 369Combined sources10
Beta strandi373 – 381Combined sources9
Beta strandi384 – 389Combined sources6
Turni390 – 393Combined sources4
Helixi400 – 403Combined sources4
Helixi406 – 417Combined sources12
Helixi427 – 431Combined sources5
Beta strandi435 – 440Combined sources6
Turni441 – 443Combined sources3
Helixi455 – 457Combined sources3
Helixi458 – 474Combined sources17
Turni478 – 484Combined sources7
Beta strandi485 – 487Combined sources3
Beta strandi491 – 497Combined sources7
Beta strandi500 – 502Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4MHXX-ray2.00A/B1-502[»]
4MIVX-ray2.40A/B/C/D/E/F/G/H1-502[»]
ProteinModelPortaliP51688.
SMRiP51688.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi26 – 29Poly-Leu4

Sequence similaritiesi

Belongs to the sulfatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3867. Eukaryota.
COG3119. LUCA.
GeneTreeiENSGT00390000013080.
HOGENOMiHOG000234731.
HOVERGENiHBG012598.
InParanoidiP51688.
KOiK01565.
OMAiKEDRHHE.
OrthoDBiEOG091G073U.
PhylomeDBiP51688.
TreeFamiTF323156.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiView protein in InterPro
IPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR032506. DUF4976.
IPR024607. Sulfatase_CS.
IPR000917. Sulfatase_N.
PfamiView protein in Pfam
PF16347. DUF4976. 1 hit.
PF00884. Sulfatase. 1 hit.
SUPFAMiSSF53649. SSF53649. 2 hits.
PROSITEiView protein in PROSITE
PS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P51688-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSCPVPACCA LLLVLGLCRA RPRNALLLLA DDGGFESGAY NNSAIATPHL
60 70 80 90 100
DALARRSLLF RNAFTSVSSC SPSRASLLTG LPQHQNGMYG LHQDVHHFNS
110 120 130 140 150
FDKVRSLPLL LSQAGVRTGI IGKKHVGPET VYPFDFAYTE ENGSVLQVGR
160 170 180 190 200
NITRIKLLVR KFLQTQDDRP FFLYVAFHDP HRCGHSQPQY GTFCEKFGNG
210 220 230 240 250
ESGMGRIPDW TPQAYDPLDV LVPYFVPNTP AARADLAAQY TTVGRMDQGV
260 270 280 290 300
GLVLQELRDA GVLNDTLVIF TSDNGIPFPS GRTNLYWPGT AEPLLVSSPE
310 320 330 340 350
HPKRWGQVSE AYVSLLDLTP TILDWFSIPY PSYAIFGSKT IHLTGRSLLP
360 370 380 390 400
ALEAEPLWAT VFGSQSHHEV TMSYPMRSVQ HRHFRLVHNL NFKMPFPIDQ
410 420 430 440 450
DFYVSPTFQD LLNRTTAGQP TGWYKDLRHY YYRARWELYD RSRDPHETQN
460 470 480 490 500
LATDPRFAQL LEMLRDQLAK WQWETHDPWV CAPDGVLEEK LSPQCQPLHN

EL
Length:502
Mass (Da):56,695
Last modified:October 1, 1996 - v1
Checksum:i90C5CDAB4DCC3808
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05467032D → E in MPS3A. 1 Publication1
Natural variantiVAR_05467132D → G in MPS3A. 1 Publication1
Natural variantiVAR_00738840Y → N in MPS3A; intermediate. 1 Publication1
Natural variantiVAR_05467242N → K in MPS3A; does not yield active enzyme; the reduction in 62 kDa precursor and 56 kDa mature forms suggests an increased degradation of the mutant enzyme. 1 Publication1
Natural variantiVAR_00738944A → T in MPS3A; severe. 1 Publication1
Natural variantiVAR_00739066S → W in MPS3A; intermediate/severe; common mutation in Italy. 3 PublicationsCorresponds to variant dbSNP:rs104894637Ensembl.1
Natural variantiVAR_00739174R → C in MPS3A; intermediate/severe; the mutant is enzymatically inactive; rapid degradation rather than decrease in synthesis is responsible for the low steady state level of the mutant protein in cells; the majority of newly synthesized protein probably occurs in the endoplasmic reticulum. 6 PublicationsCorresponds to variant dbSNP:rs104894636Ensembl.1
Natural variantiVAR_00739274R → H in MPS3A. Corresponds to variant dbSNP:rs778336949Ensembl.1
Natural variantiVAR_00739379T → P in MPS3A; severe. 1 PublicationCorresponds to variant dbSNP:rs779703983Ensembl.1
Natural variantiVAR_00739484 – 85Missing in MPS3A. 2
Natural variantiVAR_05467384H → Y in MPS3A. 1 Publication1
Natural variantiVAR_00739585Q → R in MPS3A. 1 Publication1
Natural variantiVAR_05467488M → T in MPS3A. 1 Publication1
Natural variantiVAR_00739690G → R in MPS3A. Corresponds to variant dbSNP:rs774010006Ensembl.1
Natural variantiVAR_054675106S → R in MPS3A; shows 3.3% activity of the expressed wild-type enzyme; rapid degradation rather than decrease in synthesis is responsible for the low steady state level of the mutant protein in cells. 1 Publication1
Natural variantiVAR_007397122G → R in MPS3A; intermediate. 2 PublicationsCorresponds to variant dbSNP:rs761607612Ensembl.1
Natural variantiVAR_007398128P → L in MPS3A; intermediate. 2 PublicationsCorresponds to variant dbSNP:rs104894642Ensembl.1
Natural variantiVAR_007399131V → M in MPS3A. Corresponds to variant dbSNP:rs370636303Ensembl.1
Natural variantiVAR_007400139T → M in MPS3A. Corresponds to variant dbSNP:rs775112689Ensembl.1
Natural variantiVAR_007401146L → P in MPS3A; severe. 1 PublicationCorresponds to variant dbSNP:rs749358773Ensembl.1
Natural variantiVAR_007402150R → Q in MPS3A; severe. 1 PublicationCorresponds to variant dbSNP:rs104894638Ensembl.1
Natural variantiVAR_054676150R → W in MPS3A. 1 Publication1
Natural variantiVAR_054677163L → P in MPS3A; the mutant is enzymatically inactive; rapid degradation rather than decrease in synthesis is responsible for the low steady state level of the mutant protein in cells; the mutant protein shows instability in the lysosomes. 1 Publication1
Natural variantiVAR_007403179D → N in MPS3A; severe. 1 PublicationCorresponds to variant dbSNP:rs774773010Ensembl.1
Natural variantiVAR_007404182R → C in MPS3A; intermediate. 1 PublicationCorresponds to variant dbSNP:rs529855742Ensembl.1
Natural variantiVAR_054678191G → R in MPS3A; the mutant is enzymatically inactive; rapid degradation rather than decrease in synthesis is responsible for the low steady state level of the mutant protein in cells; the majority of newly synthesized protein probably occurs in the endoplasmic reticulum. 1 PublicationCorresponds to variant dbSNP:rs753666460Ensembl.1
Natural variantiVAR_007405193F → L in MPS3A. 1
Natural variantiVAR_007406206R → P in MPS3A; the mutant enzyme retains 8% residual activity. 2 PublicationsCorresponds to variant dbSNP:rs104894643Ensembl.1
Natural variantiVAR_007407226V → A1 Publication1
Natural variantiVAR_007408227P → R in MPS3A; severe. 1 PublicationCorresponds to variant dbSNP:rs774602372Ensembl.1
Natural variantiVAR_007409234A → G in MPS3A. Corresponds to variant dbSNP:rs113641837Ensembl.1
Natural variantiVAR_054679235D → N in MPS3A; does not yield active enzyme; the reduction in 62 kDa precursor and 56 kDa mature forms suggests an increased degradation of the mutant enzyme. 2 PublicationsCorresponds to variant dbSNP:rs753472891Ensembl.1
Natural variantiVAR_007410235D → V in MPS3A. Corresponds to variant dbSNP:rs763800418Ensembl.1
Natural variantiVAR_007411245R → H in MPS3A; severe; common mutation in Western Europe and Australia. 3 PublicationsCorresponds to variant dbSNP:rs104894635Ensembl.1
Natural variantiVAR_054680251G → A in MPS3A. 2 PublicationsCorresponds to variant dbSNP:rs144461610Ensembl.1
Natural variantiVAR_054681273D → N in MPS3A. 1 Publication1
Natural variantiVAR_054682288P → S in MPS3A. 1 Publication1
Natural variantiVAR_054683293P → S in MPS3A; does not yield active enzyme; the reduction in 62 kDa precursor and 56 kDa mature forms suggests an increased degradation of the mutant enzyme. 1 PublicationCorresponds to variant dbSNP:rs143947056Ensembl.1
Natural variantiVAR_054684293P → T in MPS3A. 1 Publication1
Natural variantiVAR_007412298S → P in MPS3A; associated with a slowly progressive clinical phenotype; rapidly degraded but small amounts of the mutant protein are correctly transported to the lysosome; low but significant residual enzymatic activity. 3 PublicationsCorresponds to variant dbSNP:rs138504221Ensembl.1
Natural variantiVAR_054685300E → V in MPS3A. 1 Publication1
Natural variantiVAR_054686304R → L1 PublicationCorresponds to variant dbSNP:rs745884647Ensembl.1
Natural variantiVAR_054687307Q → P in MPS3A. 1 Publication1
Natural variantiVAR_007413321T → A in MPS3A. Corresponds to variant dbSNP:rs758756630Ensembl.1
Natural variantiVAR_054688322I → S in MPS3A. 1 Publication1
Natural variantiVAR_007414354A → P in MPS3A. 1 Publication1
Natural variantiVAR_054689355E → K in MPS3A. 1 PublicationCorresponds to variant dbSNP:rs766938111Ensembl.1
Natural variantiVAR_007415361V → I. Corresponds to variant dbSNP:rs9894254Ensembl.1
Natural variantiVAR_007416364S → R in MPS3A. 1
Natural variantiVAR_007417369E → K in MPS3A; intermediate. 2 PublicationsCorresponds to variant dbSNP:rs104894640Ensembl.1
Natural variantiVAR_061884372M → I. Corresponds to variant dbSNP:rs58786455Ensembl.1
Natural variantiVAR_054690374Y → H in MPS3A. 1 Publication1
Natural variantiVAR_007418377R → C in MPS3A; severe; does not yield active enzyme; the reduction in 62 kDa precursor and 56 kDa mature forms suggests an increased degradation of the mutant enzyme. 2 PublicationsCorresponds to variant dbSNP:rs772311757Ensembl.1
Natural variantiVAR_007419377R → H in MPS3A. Corresponds to variant dbSNP:rs746037899Ensembl.1
Natural variantiVAR_007420380Q → R in MPS3A. Corresponds to variant dbSNP:rs144143780Ensembl.1
Natural variantiVAR_054691381H → HQR in MPS3A. 1
Natural variantiVAR_007421386L → R in MPS3A. 1 Publication1
Natural variantiVAR_054692387V → M1 PublicationCorresponds to variant dbSNP:rs62620232Ensembl.1
Natural variantiVAR_007422389N → K in MPS3A. Corresponds to variant dbSNP:rs764057581Ensembl.1
Natural variantiVAR_052517394M → I. Corresponds to variant dbSNP:rs34297805Ensembl.1
Natural variantiVAR_054693403Missing in MPS3A; the mutant is enzymatically inactive; rapid degradation rather than decrease in synthesis is responsible for the low steady state level of the mutant protein in cells. 1 Publication1
Natural variantiVAR_054694432 – 435YRAR → W in MPS3A. 4
Natural variantiVAR_054695433R → Q in MPS3A; severe. 1 PublicationCorresponds to variant dbSNP:rs104894641Ensembl.1
Natural variantiVAR_054696433R → W in MPS3A; the mutant is enzymatically inactive; rapid degradation rather than decrease in synthesis is responsible for the low steady state level of the mutant protein in cells; the majority of newly synthesized protein probably occurs in the endoplasmic reticulum. 2 PublicationsCorresponds to variant dbSNP:rs777267343Ensembl.1
Natural variantiVAR_054697436 – 438Missing in MPS3A. 1 Publication3
Natural variantiVAR_007423447E → K in MPS3A. Corresponds to variant dbSNP:rs104894639Ensembl.1
Natural variantiVAR_007424456R → H Does not affect enzyme activity; cells transfected with the mutant enzyme contain a 62 kDa precursor and a 56 kDa mature form as cells transfected with the wild-type enzyme. 6 PublicationsCorresponds to variant dbSNP:rs7503034Ensembl.1
Natural variantiVAR_054698486V → F in MPS3A. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30894 mRNA. Translation: AAA86530.1.
U60111
, U60107, U60108, U60109, U60110 Genomic DNA. Translation: AAB17952.1.
AK291257 mRNA. Translation: BAF83946.1.
BC047318 mRNA. Translation: AAH47318.1.
CCDSiCCDS11770.1.
RefSeqiNP_000190.1. NM_000199.3.
UniGeneiHs.31074.

Genome annotation databases

EnsembliENST00000326317; ENSP00000314606; ENSG00000181523.
GeneIDi6448.
KEGGihsa:6448.
UCSCiuc002jxz.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30894 mRNA. Translation: AAA86530.1.
U60111
, U60107, U60108, U60109, U60110 Genomic DNA. Translation: AAB17952.1.
AK291257 mRNA. Translation: BAF83946.1.
BC047318 mRNA. Translation: AAH47318.1.
CCDSiCCDS11770.1.
RefSeqiNP_000190.1. NM_000199.3.
UniGeneiHs.31074.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4MHXX-ray2.00A/B1-502[»]
4MIVX-ray2.40A/B/C/D/E/F/G/H1-502[»]
ProteinModelPortaliP51688.
SMRiP51688.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112346. 11 interactors.
IntActiP51688. 1 interactor.
STRINGi9606.ENSP00000314606.

PTM databases

iPTMnetiP51688.
PhosphoSitePlusiP51688.

Polymorphism and mutation databases

BioMutaiSGSH.

Proteomic databases

EPDiP51688.
MaxQBiP51688.
PaxDbiP51688.
PeptideAtlasiP51688.
PRIDEiP51688.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000326317; ENSP00000314606; ENSG00000181523.
GeneIDi6448.
KEGGihsa:6448.
UCSCiuc002jxz.5. human.

Organism-specific databases

CTDi6448.
DisGeNETi6448.
GeneCardsiSGSH.
HGNCiHGNC:10818. SGSH.
HPAiHPA023436.
HPA023451.
MalaCardsiSGSH.
MIMi252900. phenotype.
605270. gene.
neXtProtiNX_P51688.
OpenTargetsiENSG00000181523.
Orphaneti79269. Sanfilippo syndrome type A.
PharmGKBiPA35726.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3867. Eukaryota.
COG3119. LUCA.
GeneTreeiENSGT00390000013080.
HOGENOMiHOG000234731.
HOVERGENiHBG012598.
InParanoidiP51688.
KOiK01565.
OMAiKEDRHHE.
OrthoDBiEOG091G073U.
PhylomeDBiP51688.
TreeFamiTF323156.

Enzyme and pathway databases

BRENDAi3.10.1.1. 2681.
ReactomeiR-HSA-2024096. HS-GAG degradation.

Miscellaneous databases

ChiTaRSiSGSH. human.
GeneWikiiSGSH.
GenomeRNAii6448.
PROiP51688.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000181523.
CleanExiHS_SGSH.
ExpressionAtlasiP51688. baseline and differential.
GenevisibleiP51688. HS.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiView protein in InterPro
IPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR032506. DUF4976.
IPR024607. Sulfatase_CS.
IPR000917. Sulfatase_N.
PfamiView protein in Pfam
PF16347. DUF4976. 1 hit.
PF00884. Sulfatase. 1 hit.
SUPFAMiSSF53649. SSF53649. 2 hits.
PROSITEiView protein in PROSITE
PS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSPHM_HUMAN
AccessioniPrimary (citable) accession number: P51688
Secondary accession number(s): A8K5E2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: March 15, 2017
This is version 152 of the entry and version 1 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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.