P51688 (SPHM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N-sulphoglucosamine sulphohydrolase
EC=3.10.1.1

Alternative name(s):
Sulfoglucosamine sulfamidase
Sulphamidase

Gene names

Name:	SGSH
Synonyms:	HSS

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	502 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Lysosome
Coding sequence diversity	Polymorphism
Disease	Disease mutation Mucopolysaccharidosis
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Traceable author statement. Source: Reactome glycosaminoglycan catabolic process Traceable author statement. Source: Reactome proteoglycan metabolic process Traceable author statement Ref.1. Source: ProtInc small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	lysosomal lumen Traceable author statement. Source: Reactome
Molecular_function	N-sulfoglucosamine sulfohydrolase activity Inferred from electronic annotation. Source: EC catalytic activity Traceable author statement Ref.1. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW sulfuric ester hydrolase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Ref.1
	Chain	21 – 502	482	N-sulphoglucosamine sulphohydrolase		PRO_0000033433
Regions
	Compositional bias	26 – 29	4	Poly-Leu
Sites
	Metal binding	31	1	Calcium By similarity
	Metal binding	32	1	Calcium By similarity
	Metal binding	70	1	Calcium; via 3-oxoalanine By similarity
	Metal binding	273	1	Calcium By similarity
	Metal binding	274	1	Calcium By similarity
Amino acid modifications
	Modified residue	70	1	3-oxoalanine (Cys) By similarity
	Glycosylation	41	1	N-linked (GlcNAc...) Ref.5 Ref.6
	Glycosylation	142	1	N-linked (GlcNAc...) Potential
	Glycosylation	151	1	N-linked (GlcNAc...) Potential
	Glycosylation	264	1	N-linked (GlcNAc...) Ref.5
	Glycosylation	413	1	N-linked (GlcNAc...) Ref.6
Natural variations
	Natural variant	32	1	D → E in MPS3A. Ref.21		VAR_054670
	Natural variant	32	1	D → G in MPS3A. Ref.12		VAR_054671
	Natural variant	40	1	Y → N in MPS3A; intermediate. Ref.10		VAR_007388
	Natural variant	42	1	N → 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 variant	44	1	A → T in MPS3A; severe. Ref.10		VAR_007389
	Natural variant	66	1	S → W in MPS3A; intermediate/severe; common mutation in Italy. Ref.10 Ref.12 Ref.22		VAR_007390
	Natural variant	74	1	R → 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 variant	74	1	R → H in MPS3A.		VAR_007392
	Natural variant	79	1	T → P in MPS3A; severe. Ref.12		VAR_007393
	Natural variant	84 – 85	2	Missing in MPS3A.		VAR_007394
	Natural variant	84	1	H → Y in MPS3A. Ref.12		VAR_054673
	Natural variant	85	1	Q → R in MPS3A. Ref.11		VAR_007395
	Natural variant	88	1	M → T in MPS3A. Ref.20		VAR_054674
	Natural variant	90	1	G → R in MPS3A.		VAR_007396
	Natural variant	106	1	S → 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 variant	122	1	G → R in MPS3A; intermediate. Ref.10 Ref.12		VAR_007397
	Natural variant	128	1	P → L in MPS3A; intermediate. Ref.10 Ref.15		VAR_007398
	Natural variant	131	1	V → M in MPS3A.		VAR_007399
	Natural variant	139	1	T → M in MPS3A.		VAR_007400
	Natural variant	146	1	L → P in MPS3A; severe. Ref.10		VAR_007401
	Natural variant	150	1	R → Q in MPS3A; severe. Ref.10		VAR_007402
	Natural variant	150	1	R → W in MPS3A. Ref.12		VAR_054676
	Natural variant	163	1	L → 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 variant	179	1	D → N in MPS3A; severe. Ref.10		VAR_007403
	Natural variant	182	1	R → C in MPS3A; intermediate. Ref.10		VAR_007404
	Natural variant	191	1	G → 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 variant	193	1	F → L in MPS3A.		VAR_007405
	Natural variant	206	1	R → P in MPS3A; the mutant enzyme retains 8% residual activity. Ref.11 Ref.17		VAR_007406
	Natural variant	226	1	V → A. Ref.10		VAR_007407
	Natural variant	227	1	P → R in MPS3A; severe. Ref.10		VAR_007408
	Natural variant	234	1	A → G in MPS3A.		VAR_007409
	Natural variant	235	1	D → 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 variant	235	1	D → V in MPS3A.		VAR_007410
	Natural variant	245	1	R → H in MPS3A; severe; common mutation in Western Europe and Australia. Ref.12 Ref.21 Ref.22		VAR_007411
	Natural variant	251	1	G → A in MPS3A. Ref.21 Ref.22		VAR_054680
	Natural variant	273	1	D → N in MPS3A. Ref.12		VAR_054681
	Natural variant	288	1	P → S in MPS3A. Ref.14		VAR_054682
	Natural variant	293	1	P → 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 variant	293	1	P → T in MPS3A. Ref.19		VAR_054684
	Natural variant	298	1	S → 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		VAR_007412
	Natural variant	300	1	E → V in MPS3A. Ref.18		VAR_054685
	Natural variant	304	1	R → L. Ref.19		VAR_054686
	Natural variant	307	1	Q → P in MPS3A. Ref.18		VAR_054687
	Natural variant	321	1	T → A in MPS3A.		VAR_007413
	Natural variant	322	1	I → S in MPS3A. Ref.12		VAR_054688
	Natural variant	354	1	A → P in MPS3A. Ref.11		VAR_007414
	Natural variant	355	1	E → K in MPS3A. Ref.12		VAR_054689
	Natural variant	361	1	V → I. Corresponds to variant rs9894254 [ dbSNP | Ensembl ].		VAR_007415
	Natural variant	364	1	S → R in MPS3A.		VAR_007416
	Natural variant	369	1	E → K in MPS3A; intermediate. Ref.10 Ref.15		VAR_007417
	Natural variant	372	1	M → I. Corresponds to variant rs58786455 [ dbSNP | Ensembl ].		VAR_061884
	Natural variant	374	1	Y → H in MPS3A. Ref.12		VAR_054690
	Natural variant	377	1	R → 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 variant	377	1	R → H in MPS3A.		VAR_007419
	Natural variant	380	1	Q → R in MPS3A.		VAR_007420
	Natural variant	381	1	H → HQR in MPS3A.		VAR_054691
	Natural variant	386	1	L → R in MPS3A. Ref.11		VAR_007421
	Natural variant	387	1	V → M. Ref.19		VAR_054692
	Natural variant	389	1	N → K in MPS3A.		VAR_007422
	Natural variant	394	1	M → I. Corresponds to variant rs34297805 [ dbSNP | Ensembl ].		VAR_052517
	Natural variant	403	1	Missing 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 variant	432 – 435	4	YRAR → W in MPS3A.		VAR_054694
	Natural variant	433	1	R → Q in MPS3A; severe. Ref.15		VAR_054695
	Natural variant	433	1	R → 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 variant	436 – 438	3	Missing in MPS3A.		VAR_054697
	Natural variant	447	1	E → K in MPS3A.		VAR_007423
	Natural variant	456	1	R → 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 variant	486	1	V → F in MPS3A. Ref.12		VAR_054698

Sequences

	Sequence		Length	Mass (Da)
	P51688 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 90C5CDAB4DCC3808	FASTA	502	56,695
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00019988.
RefSeq	NP_000190.1. NM_000199.3.
UniGene	Hs.31074.
3D structure databases
ProteinModelPortal	P51688.
ModBase	Search...
Protein-protein interaction databases
IntAct	P51688. 1 interaction.
STRING	9606.ENSP00000314606.
PTM databases
PhosphoSite	P51688.
Polymorphism databases
DMDM	1711493.
Proteomic databases
PaxDb	P51688.
PRIDE	P51688.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000326317; ENSP00000314606; ENSG00000181523.
GeneID	6448.
KEGG	hsa:6448.
UCSC	uc002jxz.4. human.
Organism-specific databases
CTD	6448.
GeneCards	GC17M078183.
HGNC	HGNC:10818. SGSH.
HPA	HPA023436. HPA023451.
MIM	252900. phenotype. 605270. gene.
neXtProt	NX_P51688.
Orphanet	79269. Sanfilippo syndrome type A.
PharmGKB	PA35726.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG3119.
HOGENOM	HOG000234731.
HOVERGEN	HBG012598.
InParanoid	P51688.
KO	K01565.
OMA	RDPHETQ.
OrthoDB	EOG4RXZ01.
PhylomeDB	P51688.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism. REACT_116125. Disease.
Gene expression databases
ArrayExpress	P51688.
Bgee	P51688.
CleanEx	HS_SGSH.
Genevestigator	P51688.
GermOnline	ENSG00000181523. Homo sapiens.
Family and domain databases
Gene3D	3.40.720.10. 1 hit.
InterPro	IPR017849. Alkaline_Pase-like_a/b/a. IPR017850. Alkaline_phosphatase_core. IPR000917. Sulfatase. IPR024607. Sulfatase_CS. [Graphical view]
Pfam	PF00884. Sulfatase. 1 hit. [Graphical view]
SUPFAM	SSF53649. Alkaline_phosphatase_core. 1 hit.
PROSITE	PS00523. SULFATASE_1. 1 hit. PS00149. SULFATASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SGSH. human.
GenomeRNAi	6448.
NextBio	25061.
SOURCE	Search...

Entry information

Entry name

SPHM_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.