Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P51688 (SPHM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-sulphoglucosamine sulphohydrolase

EC=3.10.1.1
Alternative name(s):
Sulfoglucosamine sulfamidase
Sulphamidase
Gene names
Name:SGSH
Synonyms:HSS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length502 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 calcium ion per subunit By similarity.

Subcellular location

Lysosome.

Post-translational modification

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.

Involvement in disease

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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22

Sequence similarities

Belongs to the sulfatase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.1
Chain21 – 502482N-sulphoglucosamine sulphohydrolase
PRO_0000033433

Regions

Compositional bias26 – 294Poly-Leu

Sites

Metal binding311Calcium By similarity
Metal binding321Calcium By similarity
Metal binding701Calcium; via 3-oxoalanine By similarity
Metal binding2731Calcium By similarity
Metal binding2741Calcium By similarity

Amino acid modifications

Modified residue7013-oxoalanine (Cys) By similarity
Glycosylation411N-linked (GlcNAc...) Ref.5 Ref.6
Glycosylation1421N-linked (GlcNAc...) Potential
Glycosylation1511N-linked (GlcNAc...) Potential
Glycosylation2641N-linked (GlcNAc...) Ref.5
Glycosylation4131N-linked (GlcNAc...) Ref.6

Natural variations

Natural variant321D → E in MPS3A. Ref.21
VAR_054670
Natural variant321D → G in MPS3A. Ref.12
VAR_054671
Natural variant401Y → N in MPS3A; intermediate. Ref.10
VAR_007388
Natural variant421N → 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. Ref.13
VAR_054672
Natural variant441A → T in MPS3A; severe. Ref.10
VAR_007389
Natural variant661S → W in MPS3A; intermediate/severe; common mutation in Italy. Ref.10 Ref.12 Ref.22
VAR_007390
Natural variant741R → 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. Ref.10 Ref.12 Ref.14 Ref.16 Ref.21 Ref.22
VAR_007391
Natural variant741R → H in MPS3A.
VAR_007392
Natural variant791T → P in MPS3A; severe. Ref.12
VAR_007393
Natural variant84 – 852Missing in MPS3A.
VAR_007394
Natural variant841H → Y in MPS3A. Ref.12
VAR_054673
Natural variant851Q → R in MPS3A. Ref.11
VAR_007395
Natural variant881M → T in MPS3A. Ref.20
VAR_054674
Natural variant901G → R in MPS3A.
VAR_007396
Natural variant1061S → 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. Ref.16
VAR_054675
Natural variant1221G → R in MPS3A; intermediate. Ref.10 Ref.12
VAR_007397
Natural variant1281P → L in MPS3A; intermediate. Ref.10 Ref.15
VAR_007398
Natural variant1311V → M in MPS3A.
VAR_007399
Natural variant1391T → M in MPS3A.
VAR_007400
Natural variant1461L → P in MPS3A; severe. Ref.10
VAR_007401
Natural variant1501R → Q in MPS3A; severe. Ref.10
VAR_007402
Natural variant1501R → W in MPS3A. Ref.12
VAR_054676
Natural variant1631L → 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. Ref.16
VAR_054677
Natural variant1791D → N in MPS3A; severe. Ref.10
VAR_007403
Natural variant1821R → C in MPS3A; intermediate. Ref.10
VAR_007404
Natural variant1911G → 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. Ref.16
VAR_054678
Natural variant1931F → L in MPS3A.
VAR_007405
Natural variant2061R → P in MPS3A; the mutant enzyme retains 8% residual activity. Ref.11 Ref.17
VAR_007406
Natural variant2261V → A. Ref.10
VAR_007407
Natural variant2271P → R in MPS3A; severe. Ref.10
VAR_007408
Natural variant2341A → G in MPS3A.
Corresponds to variant rs113641837 [ dbSNP | Ensembl ].
VAR_007409
Natural variant2351D → 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. Ref.12 Ref.13
VAR_054679
Natural variant2351D → V in MPS3A.
VAR_007410
Natural variant2451R → H in MPS3A; severe; common mutation in Western Europe and Australia. Ref.12 Ref.21 Ref.22
VAR_007411
Natural variant2511G → A in MPS3A. Ref.21 Ref.22
Corresponds to variant rs144461610 [ dbSNP | Ensembl ].
VAR_054680
Natural variant2731D → N in MPS3A. Ref.12
VAR_054681
Natural variant2881P → S in MPS3A. Ref.14
VAR_054682
Natural variant2931P → 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. Ref.13
VAR_054683
Natural variant2931P → T in MPS3A. Ref.19
VAR_054684
Natural variant2981S → 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. Ref.12 Ref.21 Ref.22
Corresponds to variant rs138504221 [ dbSNP | Ensembl ].
VAR_007412
Natural variant3001E → V in MPS3A. Ref.18
VAR_054685
Natural variant3041R → L. Ref.19
VAR_054686
Natural variant3071Q → P in MPS3A. Ref.18
VAR_054687
Natural variant3211T → A in MPS3A.
VAR_007413
Natural variant3221I → S in MPS3A. Ref.12
VAR_054688
Natural variant3541A → P in MPS3A. Ref.11
VAR_007414
Natural variant3551E → K in MPS3A. Ref.12
VAR_054689
Natural variant3611V → I.
Corresponds to variant rs9894254 [ dbSNP | Ensembl ].
VAR_007415
Natural variant3641S → R in MPS3A.
VAR_007416
Natural variant3691E → K in MPS3A; intermediate. Ref.10 Ref.15
VAR_007417
Natural variant3721M → I.
Corresponds to variant rs58786455 [ dbSNP | Ensembl ].
VAR_061884
Natural variant3741Y → H in MPS3A. Ref.12
VAR_054690
Natural variant3771R → 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. Ref.10 Ref.13
VAR_007418
Natural variant3771R → H in MPS3A.
VAR_007419
Natural variant3801Q → R in MPS3A.
VAR_007420
Natural variant3811H → HQR in MPS3A.
VAR_054691
Natural variant3861L → R in MPS3A. Ref.11
VAR_007421
Natural variant3871V → M. Ref.19
Corresponds to variant rs62620232 [ dbSNP | Ensembl ].
VAR_054692
Natural variant3891N → K in MPS3A.
VAR_007422
Natural variant3941M → I.
Corresponds to variant rs34297805 [ dbSNP | Ensembl ].
VAR_052517
Natural variant4031Missing 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. Ref.16
VAR_054693
Natural variant432 – 4354YRAR → W in MPS3A.
VAR_054694
Natural variant4331R → Q in MPS3A; severe. Ref.15
VAR_054695
Natural variant4331R → 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. Ref.12 Ref.16
VAR_054696
Natural variant436 – 4383Missing in MPS3A.
VAR_054697
Natural variant4471E → K in MPS3A.
VAR_007423
Natural variant4561R → 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. Ref.7 Ref.10 Ref.12 Ref.13 Ref.15 Ref.17
Corresponds to variant rs7503034 [ dbSNP | Ensembl ].
VAR_007424
Natural variant4861V → F in MPS3A. Ref.12
VAR_054698

Sequences

Sequence LengthMass (Da)Tools
P51688 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 90C5CDAB4DCC3808

FASTA50256,695
        10         20         30         40         50         60 
MSCPVPACCA LLLVLGLCRA RPRNALLLLA DDGGFESGAY NNSAIATPHL DALARRSLLF 

        70         80         90        100        110        120 
RNAFTSVSSC SPSRASLLTG LPQHQNGMYG LHQDVHHFNS FDKVRSLPLL LSQAGVRTGI 

       130        140        150        160        170        180 
IGKKHVGPET VYPFDFAYTE ENGSVLQVGR NITRIKLLVR KFLQTQDDRP FFLYVAFHDP 

       190        200        210        220        230        240 
HRCGHSQPQY GTFCEKFGNG ESGMGRIPDW TPQAYDPLDV LVPYFVPNTP AARADLAAQY 

       250        260        270        280        290        300 
TTVGRMDQGV GLVLQELRDA GVLNDTLVIF TSDNGIPFPS GRTNLYWPGT AEPLLVSSPE 

       310        320        330        340        350        360 
HPKRWGQVSE AYVSLLDLTP TILDWFSIPY PSYAIFGSKT IHLTGRSLLP ALEAEPLWAT 

       370        380        390        400        410        420 
VFGSQSHHEV TMSYPMRSVQ HRHFRLVHNL NFKMPFPIDQ DFYVSPTFQD LLNRTTAGQP 

       430        440        450        460        470        480 
TGWYKDLRHY YYRARWELYD RSRDPHETQN LATDPRFAQL LEMLRDQLAK WQWETHDPWV 

       490        500 
CAPDGVLEEK LSPQCQPLHN EL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Molecular defects in Sanfilippo syndrome type A."
Blanch L., Weber B., Guo X.-H., Scott H.S., Hopwood J.J.
Hum. Mol. Genet. 6:787-791(1997) [PubMed] [Europe PMC] [Abstract]
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]"Analysis of Sanfilippo A gene mutations in a large pedigree."
Di Natale P., Villani G.R.D., Di Domenico C., Daniele A., Dionisi Vici C., Bartuli A.
Clin. Genet. 63:314-318(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U30894 mRNA. Translation: AAA86530.1.
U60111 expand/collapse EMBL AC list , U60107, U60108, U60109, U60110 Genomic DNA. Translation: AAB17952.1.
AK291257 mRNA. Translation: BAF83946.1.
BC047318 mRNA. Translation: AAH47318.1.
RefSeqNP_000190.1. NM_000199.3.
UniGeneHs.31074.

3D structure databases

ProteinModelPortalP51688.
SMRP51688. Positions 20-479.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112346. 8 interactions.
IntActP51688. 1 interaction.
STRING9606.ENSP00000314606.

PTM databases

PhosphoSiteP51688.

Proteomic databases

PaxDbP51688.
PRIDEP51688.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000326317; ENSP00000314606; ENSG00000181523.
GeneID6448.
KEGGhsa:6448.
UCSCuc002jxz.4. human.

Organism-specific databases

CTD6448.
GeneCardsGC17M078183.
HGNCHGNC:10818. SGSH.
HPAHPA023436.
HPA023451.
MIM252900. phenotype.
605270. gene.
neXtProtNX_P51688.
Orphanet79269. Sanfilippo syndrome type A.
PharmGKBPA35726.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3119.
HOGENOMHOG000234731.
HOVERGENHBG012598.
InParanoidP51688.
KOK01565.
OMARDPHETQ.
PhylomeDBP51688.
TreeFamTF323156.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

ArrayExpressP51688.
BgeeP51688.
CleanExHS_SGSH.
GenevestigatorP51688.

Family and domain databases

Gene3D3.40.720.10. 1 hit.
InterProIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR000917. Sulfatase.
IPR024607. Sulfatase_CS.
[Graphical view]
PfamPF00884. Sulfatase. 1 hit.
[Graphical view]
SUPFAMSSF53649. SSF53649. 2 hits.
PROSITEPS00523. SULFATASE_1. 1 hit.
PS00149. SULFATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSGSH. human.
GeneWikiSGSH.
GenomeRNAi6448.
NextBio25061.
PROP51688.
SOURCESearch...

Entry information

Entry nameSPHM_HUMAN
AccessionPrimary (citable) accession number: P51688
Secondary accession number(s): A8K5E2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM