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P51688

- SPHM_HUMAN

UniProt

P51688 - SPHM_HUMAN

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Protein
N-sulphoglucosamine sulphohydrolase
Gene
SGSH, HSS
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Binds 1 calcium ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi31 – 311Calcium By similarity
Metal bindingi32 – 321Calcium By similarity
Metal bindingi70 – 701Calcium; via 3-oxoalanine By similarity
Metal bindingi273 – 2731Calcium By similarity
Metal bindingi274 – 2741Calcium By similarity

GO - Molecular functioni

  1. N-sulfoglucosamine sulfohydrolase activity Source: UniProtKB-EC
  2. catalytic activity Source: ProtInc
  3. metal ion binding Source: UniProtKB-KW
  4. sulfuric ester hydrolase activity Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. glycosaminoglycan catabolic process Source: Reactome
  3. glycosaminoglycan metabolic process Source: Reactome
  4. proteoglycan metabolic process Source: ProtInc
  5. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_120752. HS-GAG degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
N-sulphoglucosamine sulphohydrolase (EC:3.10.1.1)
Alternative name(s):
Sulfoglucosamine sulfamidase
Sulphamidase
Gene namesi
Name:SGSH
Synonyms:HSS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:10818. SGSH.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. lysosomal lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Involvement in diseasei

Mucopolysaccharidosis 3A (MPS3A) [MIM:252900]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.16 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321D → E in MPS3A. 1 Publication
VAR_054670
Natural varianti32 – 321D → G in MPS3A. 1 Publication
VAR_054671
Natural varianti40 – 401Y → N in MPS3A; intermediate. 1 Publication
VAR_007388
Natural varianti42 – 421N → 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 Publication
VAR_054672
Natural varianti44 – 441A → T in MPS3A; severe. 1 Publication
VAR_007389
Natural varianti66 – 661S → W in MPS3A; intermediate/severe; common mutation in Italy. 3 Publications
VAR_007390
Natural varianti74 – 741R → 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 Publications
VAR_007391
Natural varianti74 – 741R → H in MPS3A.
VAR_007392
Natural varianti79 – 791T → P in MPS3A; severe. 1 Publication
VAR_007393
Natural varianti84 – 852Missing in MPS3A.
VAR_007394
Natural varianti84 – 841H → Y in MPS3A. 1 Publication
VAR_054673
Natural varianti85 – 851Q → R in MPS3A. 1 Publication
VAR_007395
Natural varianti88 – 881M → T in MPS3A. 1 Publication
VAR_054674
Natural varianti90 – 901G → R in MPS3A.
VAR_007396
Natural varianti106 – 1061S → 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 Publication
VAR_054675
Natural varianti122 – 1221G → R in MPS3A; intermediate. 2 Publications
VAR_007397
Natural varianti128 – 1281P → L in MPS3A; intermediate. 2 Publications
VAR_007398
Natural varianti131 – 1311V → M in MPS3A.
VAR_007399
Natural varianti139 – 1391T → M in MPS3A.
VAR_007400
Natural varianti146 – 1461L → P in MPS3A; severe. 1 Publication
VAR_007401
Natural varianti150 – 1501R → Q in MPS3A; severe. 1 Publication
VAR_007402
Natural varianti150 – 1501R → W in MPS3A. 1 Publication
VAR_054676
Natural varianti163 – 1631L → 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 Publication
VAR_054677
Natural varianti179 – 1791D → N in MPS3A; severe. 1 Publication
VAR_007403
Natural varianti182 – 1821R → C in MPS3A; intermediate. 1 Publication
VAR_007404
Natural varianti191 – 1911G → 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 Publication
VAR_054678
Natural varianti193 – 1931F → L in MPS3A.
VAR_007405
Natural varianti206 – 2061R → P in MPS3A; the mutant enzyme retains 8% residual activity. 2 Publications
VAR_007406
Natural varianti227 – 2271P → R in MPS3A; severe. 1 Publication
VAR_007408
Natural varianti234 – 2341A → G in MPS3A.
Corresponds to variant rs113641837 [ dbSNP | Ensembl ].
VAR_007409
Natural varianti235 – 2351D → 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 Publications
VAR_054679
Natural varianti235 – 2351D → V in MPS3A.
VAR_007410
Natural varianti245 – 2451R → H in MPS3A; severe; common mutation in Western Europe and Australia. 3 Publications
VAR_007411
Natural varianti251 – 2511G → A in MPS3A. 2 Publications
Corresponds to variant rs144461610 [ dbSNP | Ensembl ].
VAR_054680
Natural varianti273 – 2731D → N in MPS3A. 1 Publication
VAR_054681
Natural varianti288 – 2881P → S in MPS3A. 1 Publication
VAR_054682
Natural varianti293 – 2931P → 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 Publication
VAR_054683
Natural varianti293 – 2931P → T in MPS3A. 1 Publication
VAR_054684
Natural varianti298 – 2981S → 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 Publications
Corresponds to variant rs138504221 [ dbSNP | Ensembl ].
VAR_007412
Natural varianti300 – 3001E → V in MPS3A. 1 Publication
VAR_054685
Natural varianti307 – 3071Q → P in MPS3A. 1 Publication
VAR_054687
Natural varianti321 – 3211T → A in MPS3A.
VAR_007413
Natural varianti322 – 3221I → S in MPS3A. 1 Publication
VAR_054688
Natural varianti354 – 3541A → P in MPS3A. 1 Publication
VAR_007414
Natural varianti355 – 3551E → K in MPS3A. 1 Publication
VAR_054689
Natural varianti364 – 3641S → R in MPS3A.
VAR_007416
Natural varianti369 – 3691E → K in MPS3A; intermediate. 2 Publications
VAR_007417
Natural varianti374 – 3741Y → H in MPS3A. 1 Publication
VAR_054690
Natural varianti377 – 3771R → 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 Publications
VAR_007418
Natural varianti377 – 3771R → H in MPS3A.
VAR_007419
Natural varianti380 – 3801Q → R in MPS3A.
VAR_007420
Natural varianti381 – 3811H → HQR in MPS3A.
VAR_054691
Natural varianti386 – 3861L → R in MPS3A. 1 Publication
VAR_007421
Natural varianti389 – 3891N → K in MPS3A.
VAR_007422
Natural varianti403 – 4031Missing 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 Publication
VAR_054693
Natural varianti432 – 4354YRAR → W in MPS3A.
VAR_054694
Natural varianti433 – 4331R → Q in MPS3A; severe. 1 Publication
VAR_054695
Natural varianti433 – 4331R → 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 Publications
VAR_054696
Natural varianti436 – 4383Missing in MPS3A.
VAR_054697
Natural varianti447 – 4471E → K in MPS3A.
VAR_007423
Natural varianti486 – 4861V → F in MPS3A. 1 Publication
VAR_054698

Keywords - Diseasei

Disease mutation, Mucopolysaccharidosis

Organism-specific databases

MIMi252900. phenotype.
Orphaneti79269. Sanfilippo syndrome type A.
PharmGKBiPA35726.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20201 Publication
Add
BLAST
Chaini21 – 502482N-sulphoglucosamine sulphohydrolase
PRO_0000033433Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi41 – 411N-linked (GlcNAc...)2 Publications
Modified residuei70 – 7013-oxoalanine (Cys) By similarity
Glycosylationi142 – 1421N-linked (GlcNAc...) Reviewed prediction
Glycosylationi151 – 1511N-linked (GlcNAc...) Reviewed prediction
Glycosylationi264 – 2641N-linked (GlcNAc...)1 Publication
Glycosylationi413 – 4131N-linked (GlcNAc...)1 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 By similarity.

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP51688.
PaxDbiP51688.
PRIDEiP51688.

PTM databases

PhosphoSiteiP51688.

Expressioni

Gene expression databases

ArrayExpressiP51688.
BgeeiP51688.
CleanExiHS_SGSH.
GenevestigatoriP51688.

Organism-specific databases

HPAiHPA023436.
HPA023451.

Interactioni

Protein-protein interaction databases

BioGridi112346. 8 interactions.
IntActiP51688. 1 interaction.
STRINGi9606.ENSP00000314606.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 329
Helixi38 – 403
Beta strandi43 – 453
Helixi48 – 547
Beta strandi57 – 648
Helixi70 – 778
Helixi83 – 864
Turni94 – 963
Helixi107 – 1137
Beta strandi117 – 1226
Turni129 – 1313
Beta strandi135 – 1395
Helixi145 – 1495
Helixi152 – 16413
Beta strandi171 – 1766
Turni184 – 1863
Helixi188 – 1903
Turni195 – 1984
Beta strandi199 – 2013
Turni202 – 2043
Turni217 – 2193
Helixi230 – 25930
Helixi263 – 2653
Beta strandi266 – 2749
Helixi287 – 2904
Beta strandi294 – 2974
Turni303 – 3064
Beta strandi307 – 3148
Helixi315 – 3173
Helixi318 – 3258
Beta strandi334 – 3363
Helixi349 – 3524
Beta strandi360 – 36910
Beta strandi373 – 3819
Beta strandi384 – 3896
Turni390 – 3934
Helixi400 – 4034
Helixi406 – 41712
Helixi427 – 4315
Beta strandi435 – 4406
Turni441 – 4433
Helixi455 – 4573
Helixi458 – 47417
Turni478 – 4847
Beta strandi485 – 4873
Beta strandi491 – 4977
Beta strandi500 – 5023

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MHXX-ray2.00A/B1-502[»]
4MIVX-ray2.40A/B/C/D/E/F/G/H1-502[»]
ProteinModelPortaliP51688.
SMRiP51688. Positions 20-479.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi26 – 294Poly-Leu

Sequence similaritiesi

Belongs to the sulfatase family.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3119.
HOGENOMiHOG000234731.
HOVERGENiHBG012598.
InParanoidiP51688.
KOiK01565.
OMAiRDPHETQ.
PhylomeDBiP51688.
TreeFamiTF323156.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view]
PfamiPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 2 hits.
PROSITEiPS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P51688-1 [UniParc]FASTAAdd to Basket

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MSCPVPACCA LLLVLGLCRA RPRNALLLLA DDGGFESGAY NNSAIATPHL    50
DALARRSLLF RNAFTSVSSC SPSRASLLTG LPQHQNGMYG LHQDVHHFNS 100
FDKVRSLPLL LSQAGVRTGI IGKKHVGPET VYPFDFAYTE ENGSVLQVGR 150
NITRIKLLVR KFLQTQDDRP FFLYVAFHDP HRCGHSQPQY GTFCEKFGNG 200
ESGMGRIPDW TPQAYDPLDV LVPYFVPNTP AARADLAAQY TTVGRMDQGV 250
GLVLQELRDA GVLNDTLVIF TSDNGIPFPS GRTNLYWPGT AEPLLVSSPE 300
HPKRWGQVSE AYVSLLDLTP TILDWFSIPY PSYAIFGSKT IHLTGRSLLP 350
ALEAEPLWAT VFGSQSHHEV TMSYPMRSVQ HRHFRLVHNL NFKMPFPIDQ 400
DFYVSPTFQD LLNRTTAGQP TGWYKDLRHY YYRARWELYD RSRDPHETQN 450
LATDPRFAQL LEMLRDQLAK WQWETHDPWV CAPDGVLEEK LSPQCQPLHN 500
EL 502
Length:502
Mass (Da):56,695
Last modified:October 1, 1996 - v1
Checksum:i90C5CDAB4DCC3808
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321D → E in MPS3A. 1 Publication
VAR_054670
Natural varianti32 – 321D → G in MPS3A. 1 Publication
VAR_054671
Natural varianti40 – 401Y → N in MPS3A; intermediate. 1 Publication
VAR_007388
Natural varianti42 – 421N → 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 Publication
VAR_054672
Natural varianti44 – 441A → T in MPS3A; severe. 1 Publication
VAR_007389
Natural varianti66 – 661S → W in MPS3A; intermediate/severe; common mutation in Italy. 3 Publications
VAR_007390
Natural varianti74 – 741R → 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 Publications
VAR_007391
Natural varianti74 – 741R → H in MPS3A.
VAR_007392
Natural varianti79 – 791T → P in MPS3A; severe. 1 Publication
VAR_007393
Natural varianti84 – 852Missing in MPS3A.
VAR_007394
Natural varianti84 – 841H → Y in MPS3A. 1 Publication
VAR_054673
Natural varianti85 – 851Q → R in MPS3A. 1 Publication
VAR_007395
Natural varianti88 – 881M → T in MPS3A. 1 Publication
VAR_054674
Natural varianti90 – 901G → R in MPS3A.
VAR_007396
Natural varianti106 – 1061S → 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 Publication
VAR_054675
Natural varianti122 – 1221G → R in MPS3A; intermediate. 2 Publications
VAR_007397
Natural varianti128 – 1281P → L in MPS3A; intermediate. 2 Publications
VAR_007398
Natural varianti131 – 1311V → M in MPS3A.
VAR_007399
Natural varianti139 – 1391T → M in MPS3A.
VAR_007400
Natural varianti146 – 1461L → P in MPS3A; severe. 1 Publication
VAR_007401
Natural varianti150 – 1501R → Q in MPS3A; severe. 1 Publication
VAR_007402
Natural varianti150 – 1501R → W in MPS3A. 1 Publication
VAR_054676
Natural varianti163 – 1631L → 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 Publication
VAR_054677
Natural varianti179 – 1791D → N in MPS3A; severe. 1 Publication
VAR_007403
Natural varianti182 – 1821R → C in MPS3A; intermediate. 1 Publication
VAR_007404
Natural varianti191 – 1911G → 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 Publication
VAR_054678
Natural varianti193 – 1931F → L in MPS3A.
VAR_007405
Natural varianti206 – 2061R → P in MPS3A; the mutant enzyme retains 8% residual activity. 2 Publications
VAR_007406
Natural varianti226 – 2261V → A.1 Publication
VAR_007407
Natural varianti227 – 2271P → R in MPS3A; severe. 1 Publication
VAR_007408
Natural varianti234 – 2341A → G in MPS3A.
Corresponds to variant rs113641837 [ dbSNP | Ensembl ].
VAR_007409
Natural varianti235 – 2351D → 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 Publications
VAR_054679
Natural varianti235 – 2351D → V in MPS3A.
VAR_007410
Natural varianti245 – 2451R → H in MPS3A; severe; common mutation in Western Europe and Australia. 3 Publications
VAR_007411
Natural varianti251 – 2511G → A in MPS3A. 2 Publications
Corresponds to variant rs144461610 [ dbSNP | Ensembl ].
VAR_054680
Natural varianti273 – 2731D → N in MPS3A. 1 Publication
VAR_054681
Natural varianti288 – 2881P → S in MPS3A. 1 Publication
VAR_054682
Natural varianti293 – 2931P → 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 Publication
VAR_054683
Natural varianti293 – 2931P → T in MPS3A. 1 Publication
VAR_054684
Natural varianti298 – 2981S → 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 Publications
Corresponds to variant rs138504221 [ dbSNP | Ensembl ].
VAR_007412
Natural varianti300 – 3001E → V in MPS3A. 1 Publication
VAR_054685
Natural varianti304 – 3041R → L.1 Publication
VAR_054686
Natural varianti307 – 3071Q → P in MPS3A. 1 Publication
VAR_054687
Natural varianti321 – 3211T → A in MPS3A.
VAR_007413
Natural varianti322 – 3221I → S in MPS3A. 1 Publication
VAR_054688
Natural varianti354 – 3541A → P in MPS3A. 1 Publication
VAR_007414
Natural varianti355 – 3551E → K in MPS3A. 1 Publication
VAR_054689
Natural varianti361 – 3611V → I.
Corresponds to variant rs9894254 [ dbSNP | Ensembl ].
VAR_007415
Natural varianti364 – 3641S → R in MPS3A.
VAR_007416
Natural varianti369 – 3691E → K in MPS3A; intermediate. 2 Publications
VAR_007417
Natural varianti372 – 3721M → I.
Corresponds to variant rs58786455 [ dbSNP | Ensembl ].
VAR_061884
Natural varianti374 – 3741Y → H in MPS3A. 1 Publication
VAR_054690
Natural varianti377 – 3771R → 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 Publications
VAR_007418
Natural varianti377 – 3771R → H in MPS3A.
VAR_007419
Natural varianti380 – 3801Q → R in MPS3A.
VAR_007420
Natural varianti381 – 3811H → HQR in MPS3A.
VAR_054691
Natural varianti386 – 3861L → R in MPS3A. 1 Publication
VAR_007421
Natural varianti387 – 3871V → M.1 Publication
Corresponds to variant rs62620232 [ dbSNP | Ensembl ].
VAR_054692
Natural varianti389 – 3891N → K in MPS3A.
VAR_007422
Natural varianti394 – 3941M → I.
Corresponds to variant rs34297805 [ dbSNP | Ensembl ].
VAR_052517
Natural varianti403 – 4031Missing 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 Publication
VAR_054693
Natural varianti432 – 4354YRAR → W in MPS3A.
VAR_054694
Natural varianti433 – 4331R → Q in MPS3A; severe. 1 Publication
VAR_054695
Natural varianti433 – 4331R → 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 Publications
VAR_054696
Natural varianti436 – 4383Missing in MPS3A.
VAR_054697
Natural varianti447 – 4471E → K in MPS3A.
VAR_007423
Natural varianti456 – 4561R → 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 Publications
Corresponds to variant rs7503034 [ dbSNP | Ensembl ].
VAR_007424
Natural varianti486 – 4861V → F in MPS3A. 1 Publication
VAR_054698

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS11770.1.
RefSeqi NP_000190.1. NM_000199.3.
UniGenei Hs.31074.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4MHX X-ray 2.00 A/B 1-502 [» ]
4MIV X-ray 2.40 A/B/C/D/E/F/G/H 1-502 [» ]
ProteinModelPortali P51688.
SMRi P51688. Positions 20-479.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112346. 8 interactions.
IntActi P51688. 1 interaction.
STRINGi 9606.ENSP00000314606.

PTM databases

PhosphoSitei P51688.

Proteomic databases

MaxQBi P51688.
PaxDbi P51688.
PRIDEi P51688.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000326317 ; ENSP00000314606 ; ENSG00000181523 .
GeneIDi 6448.
KEGGi hsa:6448.
UCSCi uc002jxz.4. human.

Organism-specific databases

CTDi 6448.
GeneCardsi GC17M078183.
HGNCi HGNC:10818. SGSH.
HPAi HPA023436.
HPA023451.
MIMi 252900. phenotype.
605270. gene.
neXtProti NX_P51688.
Orphaneti 79269. Sanfilippo syndrome type A.
PharmGKBi PA35726.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3119.
HOGENOMi HOG000234731.
HOVERGENi HBG012598.
InParanoidi P51688.
KOi K01565.
OMAi RDPHETQ.
PhylomeDBi P51688.
TreeFami TF323156.

Enzyme and pathway databases

Reactomei REACT_120752. HS-GAG degradation.

Miscellaneous databases

ChiTaRSi SGSH. human.
GeneWikii SGSH.
GenomeRNAii 6448.
NextBioi 25061.
PROi P51688.
SOURCEi Search...

Gene expression databases

ArrayExpressi P51688.
Bgeei P51688.
CleanExi HS_SGSH.
Genevestigatori P51688.

Family and domain databases

Gene3Di 3.40.720.10. 1 hit.
InterProi IPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view ]
Pfami PF00884. Sulfatase. 1 hit.
[Graphical view ]
SUPFAMi SSF53649. SSF53649. 2 hits.
PROSITEi PS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the sulphamidase gene and identification of mutations in Sanfilippo A syndrome."
    Scott H.S., Blanch L., Guo X.-H., Freeman C., Orsborn A., Baker E., Sutherland G.R., Morris C.P., Hopwood J.J.
    Nat. Genet. 11:465-467(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 21-45.
    Tissue: Kidney and Testis.
  2. Karageorgos L.E., Guo X.H., Blanch L., Weber B., Anson D.S., Scott H.S., Hopwood J.J.
    Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pancreas.
  5. "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
    Zhang H., Li X.-J., Martin D.B., Aebersold R.
    Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-41 AND ASN-264.
  6. "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-41 AND ASN-413.
    Tissue: Liver.
  7. Cited for: VARIANTS MPS3A, VARIANT HIS-456.
  8. "Novel mutations in Sanfilippo A syndrome: implications for enzyme function."
    Weber B., Guo X.-H., Wraith J.E., Cooper A., Kleijer W.J., Bunge S., Hopwood J.J.
    Hum. Mol. Genet. 6:1573-1579(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MPS3A.
  9. "Identification of 16 sulfamidase gene mutations including the common R74C in patients with mucopolysaccharidosis type IIIA (Sanfilippo A)."
    Bunge S., Ince H., Steglich C., Kleijer W.J., Beck M., Zaremba J., van Diggelen O.P., Weber B., Hopwood J.J., Gal A.
    Hum. Mutat. 10:479-485(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MPS3A.
  10. "Identification of molecular defects in Italian Sanfilippo A patients including 13 novel mutations."
    di Natale P., Balzano N., Esposito S., Villani G.R.D.
    Hum. Mutat. 11:313-320(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MPS3A ASN-40; THR-44; TRP-66; CYS-74; ARG-122; LEU-128; PRO-146; GLN-150; ASN-179; CYS-182; ARG-227; LYS-369 AND CYS-377, VARIANTS ALA-226 AND HIS-456.
  11. "Mutation 1091delC is highly prevalent in Spanish Sanfilippo syndrome type A patients."
    Montfort M., Vilageliu L., Garcia-Giralt N., Guidi S., Coll M.J., Chabas A., Grinberg D.
    Hum. Mutat. 12:274-279(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MPS3A ARG-85; PRO-206; PRO-354 AND ARG-386.
  12. "Mutational analysis of Sanfilippo syndrome type A (MPS IIIA): identification of 13 novel mutations."
    Beesley C.E., Young E.P., Vellodi A., Winchester B.G.
    J. Med. Genet. 37:704-707(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MPS3A GLY-32; TRP-66; CYS-74; PRO-79; TYR-84; ARG-122; TRP-150; ASN-235; HIS-245; ASN-273; PRO-298; SER-322; LYS-355; HIS-374; GLN-ARG-381 INS; TRP-433; 436-TRP--LEU-438 DEL AND PHE-486, VARIANT HIS-456.
  13. "Identification and characterization of mutations underlying Sanfilippo syndrome type A (mucopolysaccharidosis type IIIA)."
    Lee-Chen G.J., Lin S.P., Ko M.H., Chuang C.K., Chen C.P., Lee H.H., Cheng S.C., Shen C.H., Tseng K.L., Li C.L.
    Clin. Genet. 61:192-197(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MPS3A LYS-42; ASN-235; SER-293 AND CYS-377, VARIANT HIS-456, CHARACTERIZATION OF VARIANTS MPS3A LYS-42; ASN-235; SER-293 AND CYS-377, CHARACTERIZATION OF VARIANT HIS-456.
  14. "Sanfilippo syndrome in Turkey: identification of novel mutations in subtypes A and B."
    Emre S., Terzioglu M., Tokatli A., Coskun T., Ozalp I., Weber B., Hopwood J.J.
    Hum. Mutat. 19:184-185(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MPS3A CYS-74 AND SER-288.
  15. Cited for: VARIANTS MPS3A LEU-128; LYS-369 AND GLN-433, VARIANT HIS-456.
  16. "Transport, enzymatic activity, and stability of mutant sulfamidase (SGSH) identified in patients with mucopolysaccharidosis type III A."
    Muschol N., Storch S., Ballhausen D., Beesley C., Westermann J.-C., Gal A., Ullrich K., Hopwood J.J., Winchester B., Braulke T.
    Hum. Mutat. 23:559-566(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MPS3A CYS-74; ARG-106; PRO-163; ARG-191; TYR-403 DEL AND TRP-433, CHARACTERIZATION OF VARIANTS MPS3A CYS-74; ARG-106; PRO-163; ARG-191; TYR-403 DEL AND TRP-433.
  17. "An adult Sanfilippo type A patient with homozygous mutation R206P in the sulfamidase gene."
    Gabrielli O., Coppa G.V., Bruni S., Villani G.R.D., Pontarelli G., Di Natale P.
    Am. J. Med. Genet. A 133:85-89(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MPS3A PRO-206, VARIANT HIS-456, CHARACTERIZATION OF VARIANT MPS3A PRO-206.
  18. "Early diagnosis of mucopolysaccharidosis III A with a nonsense mutation and two de novo missense mutations in SGSH gene."
    Bekri S., Armana G., De Ricaud D., Osenda M., Maire I., Van Obberghen E., Froissart R.
    J. Inherit. Metab. Dis. 28:601-602(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MPS3A VAL-300 AND PRO-307.
  19. "Gene symbol: SGSH. Disease: Sanfilippo type A syndrome, mucopolysaccharidosis IIIA."
    Di Natale P., Pontarelli G., Villani G.R.D., Di Domenico C.
    Hum. Genet. 119:679-679(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MPS3A THR-293, VARIANTS LEU-304 AND MET-387.
  20. "Strategies and clinical outcome of 250 cycles of Preimplantation Genetic Diagnosis for single gene disorders."
    Fiorentino F., Biricik A., Nuccitelli A., De Palma R., Kahraman S., Iacobelli M., Trengia V., Caserta D., Bonu M.A., Borini A., Baldi M.
    Hum. Reprod. 21:670-684(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MPS3A THR-88.
  21. "The mutation p.Ser298Pro in the sulphamidase gene (SGSH) is associated with a slowly progressive clinical phenotype in mucopolysaccharidosis type IIIA (Sanfilippo A syndrome)."
    Meyer A., Kossow K., Gal A., Steglich C., Muehlhausen C., Ullrich K., Braulke T., Muschol N.
    Hum. Mutat. 29:770-770(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MPS3A GLU-32; CYS-74; HIS-245; ALA-251 AND PRO-298, ASSOCIATION OF VARIANT MPS3A PRO-298 WITH SLOWLY PROGRESSIVE PHENOTYPE.
  22. "Residual activity and proteasomal degradation of p.Ser298Pro sulfamidase identified in patients with a mild clinical phenotype of Sanfilippo A syndrome."
    Muschol N., Pohl S., Meyer A., Gal A., Ullrich K., Braulke T.
    Am. J. Med. Genet. A 155A:1634-1639(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MPS3A TRP-66; CYS-74; HIS-245; ALA-251 AND PRO-298, CHARACTERIZATION OF VARIANT MPS3A PRO-298.

Entry informationi

Entry nameiSPHM_HUMAN
AccessioniPrimary (citable) accession number: P51688
Secondary accession number(s): A8K5E2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 127 of the entry and version 1 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

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

External Data

Dasty 3

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