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P51688

- SPHM_HUMAN

UniProt

P51688 - SPHM_HUMAN

Protein

N-sulphoglucosamine sulphohydrolase

Gene

SGSH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    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 – 311CalciumBy similarity
    Metal bindingi32 – 321CalciumBy similarity
    Metal bindingi70 – 701Calcium; via 3-oxoalanineBy similarity
    Metal bindingi273 – 2731CalciumBy similarity
    Metal bindingi274 – 2741CalciumBy similarity

    GO - Molecular functioni

    1. catalytic activity Source: ProtInc
    2. metal ion binding Source: UniProtKB-KW
    3. N-sulfoglucosamine sulfohydrolase activity Source: UniProtKB-EC
    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

    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

    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.16 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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 PublicationAdd
    BLAST
    Chaini21 – 502482N-sulphoglucosamine sulphohydrolasePRO_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...)Sequence Analysis
    Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis
    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

    1
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

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

    Sequence similaritiesi

    Belongs to the sulfatase family.Curated

    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

    « Hide

    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

    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: October 1, 2014
    This is version 128 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