P22304 (IDS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Iduronate 2-sulfatase
EC=3.1.6.13

Alternative name(s):
Alpha-L-iduronate sulfate sulfatase
Short name=Idursulfase

Cleaved into the following 2 chains:

1. Iduronate 2-sulfatase 42 kDa chain
2. Iduronate 2-sulfatase 14 kDa chain

Gene names

Name:	IDS
Synonyms:	SIDS

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	550 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)

Function	Required for the lysosomal degradation of heparan sulfate and dermatan sulfate.
Catalytic activity	Hydrolysis of the 2-sulfate groups of the L-iduronate 2-sulfate units of dermatan sulfate, heparan sulfate and heparin.
Cofactor	Binds 1 calcium ion per subunit By similarity.
Subunit structure	Liver iduronate 2-sulfatase is composed of two major forms (A and B) which contain both a 42 kDa and a 14 kDa polypeptides.
Subcellular location	Lysosome.
Tissue specificity	Liver, kidney, lung, and placenta.
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 2 (MPS2) [MIM:309900]: An X-linked lysosomal storage disease characterized by intracellular accumulation of heparan sulfate and dermatan sulfate and their excretion in urine. Most children with MPS2 have a severe form with early somatic abnormalities including skeletal deformities, hepatosplenomegaly, and progressive cardiopulmonary deterioration. A prominent feature is neurological damage that presents as developmental delay and hyperactivity but progresses to mental retardation and dementia. They die before 15 years of age, usually as a result of obstructive airway disease or cardiac failure. In contrast, those with a mild form of MPS2 may survive into adulthood, with attenuated somatic complications and often without mental retardation. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44
Sequence similarities	Belongs to the sulfatase family.

Ontologies

Keywords
Cellular component	Lysosome
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Mucopolysaccharidosis
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Glycoprotein Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Traceable author statement. Source: Reactome chondroitin sulfate catabolic process Traceable author statement. Source: Reactome
Cellular_component	lysosomal lumen Traceable author statement. Source: Reactome
Molecular_function	iduronate-2-sulfatase activity Traceable author statement. Source: Reactome metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P22304-1)

Also known as: Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P22304-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     337-343: WALGEHG → FLMRTNT
     344-550: Missing.

Isoform 3 (identifier: P22304-3)

The sequence of this isoform differs from the canonical sequence as follows:
     294-312: RKIRQSYFASVSYLDTQVG → EDQSSTGFRLKTSSTRKYK
     313-550: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 25	25	Potential
	Propeptide	26 – 33	8			PRO_0000033428
	Chain	34 – 455	422	Iduronate 2-sulfatase 42 kDa chain		PRO_0000033429
	Chain	456 – 550	95	Iduronate 2-sulfatase 14 kDa chain		PRO_0000033430
Sites
	Metal binding	45	1	Calcium By similarity
	Metal binding	46	1	Calcium By similarity
	Metal binding	84	1	Calcium; via 3-oxoalanine By similarity
	Metal binding	334	1	Calcium By similarity
	Metal binding	335	1	Calcium By similarity
Amino acid modifications
	Modified residue	84	1	3-oxoalanine (Cys) By similarity
	Glycosylation	115	1	N-linked (GlcNAc...) Ref.10
	Glycosylation	144	1	N-linked (GlcNAc...) Potential
	Glycosylation	246	1	N-linked (GlcNAc...) Potential
	Glycosylation	280	1	N-linked (GlcNAc...) Potential
	Glycosylation	325	1	N-linked (GlcNAc...) Potential
	Glycosylation	513	1	N-linked (GlcNAc...) Potential
	Glycosylation	537	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	294 – 312	19	RKIRQ…DTQVG → EDQSSTGFRLKTSSTRKYK in isoform 3.		VSP_039116
	Alternative sequence	313 – 550	238	Missing in isoform 3.		VSP_039117
	Alternative sequence	337 – 343	7	WALGEHG → FLMRTNT in isoform 2.		VSP_006301
	Alternative sequence	344 – 550	207	Missing in isoform 2.		VSP_006302
	Natural variant	41	1	L → P in MPS2; mild form; increase in enzyme activity observed in transfected cells. Ref.39		VAR_026915
	Natural variant	41	1	Missing in MPS2; intermediate form. Ref.43		VAR_026914
	Natural variant	45	1	D → N in MPS2. Ref.27		VAR_007313
	Natural variant	48	1	R → P in MPS2; mild form. Ref.18 Ref.33		VAR_007314
	Natural variant	54	1	Y → D in MPS2; severe form. Ref.29		VAR_007315
	Natural variant	63	1	N → D in MPS2; mild/intermediate form. Ref.20 Ref.22 Ref.24 Ref.29		VAR_007316
	Natural variant	68	1	A → E in MPS2; severe. Ref.14		VAR_007317
	Natural variant	71	1	S → N in MPS2; mild form. Ref.28		VAR_026916
	Natural variant	71	1	S → R in MPS2; severe form. Ref.37		VAR_008998
	Natural variant	73	1	L → F in MPS2; severe form. Ref.26		VAR_026917
	Natural variant	79	1	A → E in MPS2; mild form. Ref.29		VAR_007318
	Natural variant	82	1	A → E in MPS2. Ref.37		VAR_008999
	Natural variant	82	1	A → V in MPS2; no significant enzyme activity. Ref.44		VAR_026918
	Natural variant	85	1	A → S in MPS2; severe form. Ref.28		VAR_026919
	Natural variant	85	1	A → T in MPS2; mild to severe forms. Ref.20 Ref.28 Ref.31 Ref.33 Ref.37		VAR_007319
	Natural variant	86	1	P → L in MPS2; intermediate to severe forms. Ref.17 Ref.28 Ref.30 Ref.33		VAR_007320
	Natural variant	86	1	P → Q in MPS2. Ref.20		VAR_007321
	Natural variant	86	1	P → R in MPS2; severe form. Ref.13 Ref.22		VAR_007322
	Natural variant	87	1	S → N in MPS2; mild form. Ref.17		VAR_007323
	Natural variant	88	1	R → C in MPS2; severe form. Ref.20 Ref.29 Ref.37 Ref.41		VAR_007324
	Natural variant	88	1	R → G in MPS2; severe form. Ref.28		VAR_026920
	Natural variant	88	1	R → H in MPS2; intermediate/severe form; higher affinity for the artificial substrate; poor transport to lysosomes. Ref.20 Ref.28 Ref.29 Ref.30 Ref.31 Ref.38		VAR_007325
	Natural variant	88	1	R → L in MPS2; severe form. Ref.29		VAR_007326
	Natural variant	88	1	R → P in MPS2; severe form; total absence of residual activity; poor transport to lysosomes. Ref.30 Ref.38		VAR_007327
	Natural variant	89	1	V → F in MPS2. Ref.28		VAR_026921
	Natural variant	92	1	L → P in MPS2; severe form. Ref.17		VAR_007328
	Natural variant	94	1	G → D in MPS2; mild form. Ref.13		VAR_007329
	Natural variant	95	1	R → G in MPS2; intermediate form. Ref.22		VAR_026922
	Natural variant	95	1	R → T in MPS2; mild form. Ref.41		VAR_026923
	Natural variant	95	1	Missing in MPS2; severe form. Ref.37		VAR_009000
	Natural variant	102	1	L → R in MPS2; mild form. Ref.29		VAR_007330
	Natural variant	108	1	Y → C in MPS2; mild form. Ref.20		VAR_007331
	Natural variant	108	1	Y → S in MPS2; mild form. Ref.28		VAR_026924
	Natural variant	115	1	N → Y in MPS2. Ref.27		VAR_007332
	Natural variant	117	1	S → Y in MPS2; severe form. Ref.43		VAR_026926
	Natural variant	117	1	Missing in MPS2; severe form; deleterious mutation; results in an inactive enzyme. Ref.18 Ref.20 Ref.28 Ref.40		VAR_026925
	Natural variant	118	1	T → I in MPS2; mild to severe forms; greatly reduced activity; poor transport to lysosomes. Ref.28 Ref.30 Ref.38		VAR_007333
	Natural variant	118	1	Missing in MPS2; severe form. Ref.26		VAR_026927
	Natural variant	120	1	P → H in MPS2; mild form.		VAR_007334
	Natural variant	120	1	P → R in MPS2; severe form. Ref.13		VAR_007335
	Natural variant	121	1	Q → H in MPS2; severe form. Ref.26		VAR_026928
	Natural variant	121	1	Q → R in MPS2; severe form. Ref.28		VAR_026929
	Natural variant	125	1	E → V in MPS2; mild form. Ref.20		VAR_007336
	Natural variant	132	1	S → W in MPS2; severe form. Ref.16 Ref.26		VAR_007337
	Natural variant	134	1	G → R in MPS2; severe form. Ref.20		VAR_007338
	Natural variant	135	1	K → N in MPS2; intermediate form. Ref.17		VAR_007339
	Natural variant	135	1	K → R in MPS2; intermediate form. Ref.11 Corresponds to variant rs28937311 [ dbSNP | Ensembl ].		VAR_007340
	Natural variant	138	1	H → D in MPS2; mild/intermediate form. Ref.28		VAR_026930
	Natural variant	140	1	G → V in MPS2; no significant enzyme activity. Ref.44		VAR_026931
	Natural variant	143	1	S → F in MPS2. Ref.32 Ref.35		VAR_007341
	Natural variant	148	1	D → H in MPS2; intermediate form. Ref.28		VAR_026932
	Natural variant	159	1	H → P in MPS2; severe form. Ref.29		VAR_007342
	Natural variant	159	1	Missing in MPS2; intermediate form.		VAR_007343
	Natural variant	160	1	P → R in MPS2.		VAR_007344
	Natural variant	181	1	N → I in MPS2; mild form. Ref.41		VAR_026933
	Natural variant	182	1	L → P in MPS2; intermediate form. Ref.33		VAR_026934
	Natural variant	184	1	C → F in MPS2; mild/intermediate form. Ref.20		VAR_007345
	Natural variant	184	1	C → W in MPS2. Ref.32		VAR_007346
	Natural variant	196	1	L → S in MPS2; mild/intermediate form. Ref.29 Ref.33		VAR_007347
	Natural variant	198	1	D → G in MPS2; mild form. Ref.29		VAR_007348
	Natural variant	205	1	A → P in MPS2; intermediate form. Ref.22		VAR_026935
	Natural variant	221	1	L → P in MPS2; intermediate form. Ref.13		VAR_007349
	Natural variant	224	1	G → E in MPS2; severe form. Ref.29		VAR_007350
	Natural variant	225	1	Y → D in MPS2; intermediate form. Ref.33		VAR_007351
	Natural variant	227	1	K → M in MPS2; intermediate form. Ref.33		VAR_026936
	Natural variant	227	1	K → Q in MPS2; severe form.		VAR_007352
	Natural variant	228	1	P → L in MPS2. Ref.27		VAR_007353
	Natural variant	228	1	P → T in MPS2; severe form. Ref.34		VAR_026937
	Natural variant	229	1	H → R in MPS2; intermediate/severe form. Ref.28 Ref.34		VAR_026938
	Natural variant	229	1	H → Y in MPS2; severe form. Ref.16		VAR_007354
	Natural variant	231	1	P → L in MPS2; mild form. Ref.34		VAR_026939
	Natural variant	252	1	D → N in MPS2. Ref.20		VAR_007355
	Natural variant	259	1	L → P in MPS2; severe form. Ref.43		VAR_026940
	Natural variant	264	1	Y → N in MPS2. Ref.36		VAR_009001
	Natural variant	265	1	N → I in MPS2; intermediate form; deleterious mutation; residual activity of 7.5% of the wild-type. Ref.40		VAR_026941
	Natural variant	266	1	P → H in MPS2; mild form. Ref.30		VAR_007356
	Natural variant	266	1	P → R in MPS2. Ref.27		VAR_007357
	Natural variant	269	1	D → V in MPS2. Ref.32		VAR_007358
	Natural variant	293	1	Q → H in MPS2; mild form. Ref.14		VAR_007359
	Natural variant	299	1	S → I in MPS2; mild form. Ref.43		VAR_026942
	Natural variant	308	1	D → E in MPS2; mild form. Ref.34		VAR_026943
	Natural variant	308	1	D → N in MPS2; intermediate form. Ref.33		VAR_026944
	Natural variant	309	1	T → A in MPS2; severe form. Ref.34		VAR_026945
	Natural variant	313	1	R → C in MPS2; unknown pathological significance. Ref.34		VAR_026946
	Natural variant	314	1	L → P in MPS2; severe form. Ref.33		VAR_026947
	Natural variant	333	1	S → L in MPS2; severe form. Ref.18 Ref.20 Ref.21 Ref.23 Ref.28 Ref.29 Ref.33		VAR_007360
	Natural variant	334	1	D → G in MPS2; severe form. Ref.23		VAR_009002
	Natural variant	334	1	D → N in MPS2; mild form. Ref.28		VAR_026948
	Natural variant	335	1	H → R in MPS2; intermediate form. Ref.28		VAR_026949
	Natural variant	336	1	G → E in MPS2; severe from. Ref.28		VAR_026950
	Natural variant	336	1	G → R in MPS2; severe form. Ref.26		VAR_026951
	Natural variant	337	1	W → R in MPS2; intermediate form. Ref.18 Ref.33		VAR_007361
	Natural variant	339	1	L → R in MPS2; severe form. Ref.28		VAR_026952
	Natural variant	340	1	G → D in MPS2; mild form. Ref.29		VAR_007362
	Natural variant	341	1	E → K in MPS2; severe form. Ref.26 Ref.35		VAR_008134
	Natural variant	342	1	H → Y in MPS2; mild form. Ref.35		VAR_008135
	Natural variant	345	1	W → C in MPS2; mild form. Ref.17		VAR_007363
	Natural variant	346	1	A → D in MPS2; mild/severe form. Ref.21		VAR_007364
	Natural variant	346	1	A → V in MPS2; mild/severe form. Ref.19		VAR_007365
	Natural variant	347	1	K → I in MPS2. Ref.20		VAR_007366
	Natural variant	347	1	K → Q in MPS2; severe form. Ref.26		VAR_026953
	Natural variant	347	1	K → T in MPS2; severe form; deleterious mutation confirmed. Ref.24 Ref.40		VAR_007367
	Natural variant	348	1	Y → H in MPS2. Ref.32		VAR_007368
	Natural variant	349	1	S → I in MPS2; severe form. Ref.31 Ref.33		VAR_007369
	Natural variant	358	1	P → R in MPS2; severe form. Ref.16		VAR_007370
	Natural variant	403	1	L → R in MPS2; intermediate form. Ref.20 Ref.28		VAR_007371
	Natural variant	410	1	L → P in MPS2. Ref.15		VAR_026954
	Natural variant	422	1	C → G in MPS2; mild form. Ref.11 Ref.13 Corresponds to variant rs28937310 [ dbSNP | Ensembl ].		VAR_007372
	Natural variant	422	1	C → R in MPS2; severe form. Ref.41		VAR_026955
	Natural variant	432	1	C → Y in MPS2; severe form. Ref.29		VAR_007373
	Natural variant	434	1	E → K in MPS2. Ref.27		VAR_007374
	Natural variant	465	1	Q → P in MPS2; severe form. Ref.36		VAR_009003
	Natural variant	467	1	P → L in MPS2; severe form. Ref.28 Ref.41		VAR_026956
	Natural variant	468	1	R → G in MPS2; mild to severe forms.		VAR_007375
	Natural variant	468	1	R → L in MPS2; mild to severe forms. Ref.18 Ref.24 Ref.33		VAR_007376
	Natural variant	468	1	R → Q in MPS2; severe/intermediate form; greatly reduced activity; poor transport to lysosomes. Ref.18 Ref.20 Ref.22 Ref.24 Ref.25 Ref.26 Ref.28 Ref.29 Ref.33 Ref.37 Ref.38 Ref.41		VAR_007377
	Natural variant	468	1	R → W in MPS2; mild to severe forms. Ref.12 Ref.17 Ref.22 Ref.26 Ref.28 Ref.33 Ref.36 Ref.37 Ref.41		VAR_007378
	Natural variant	469	1	P → H in MPS2; mild form. Ref.16		VAR_007379
	Natural variant	478	1	D → G in MPS2; mild form. Ref.14		VAR_007380
	Natural variant	478	1	D → Y in MPS2; severe form. Ref.29		VAR_007381
	Natural variant	480	1	P → L in MPS2; mild form. Ref.28		VAR_026957
	Natural variant	480	1	P → Q in MPS2; mild form. Ref.28		VAR_026958
	Natural variant	480	1	P → R in MPS2; severe form. Ref.28		VAR_026959
	Natural variant	485	1	I → K in MPS2. Ref.27		VAR_007382
	Natural variant	485	1	I → R in MPS2; severe form. Ref.14 Ref.29		VAR_007383
	Natural variant	488 – 489	2	MG → IA in MPS2; intermediate form; mutation A-489 confirmed as causative of MPS2.		VAR_026960
	Natural variant	490	1	Y → S in MPS2; intermediate form. Ref.28		VAR_026961
	Natural variant	491	1	S → F in MPS2; mild form. Ref.35		VAR_008136
	Natural variant	502	1	W → C in MPS2; severe form. Ref.27		VAR_007384
	Natural variant	502	1	W → S in MPS2.		VAR_007385
	Natural variant	521	1	E → K in MPS2; severe form. Ref.26		VAR_026962
	Natural variant	521	1	E → V in MPS2; severe form. Ref.26 Ref.31 Ref.37		VAR_007386
	Natural variant	523	1	Y → C in MPS2; mild form. Ref.16		VAR_007387

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified August 1, 1991. Version 1. Checksum: EA1B713417280413	FASTA	550	61,873
	10 20 30 40 50 60 MPPPRTGRGL LWLGLVLSSV CVALGSETQA NSTTDALNVL LIIVDDLRPS LGCYGDKLVR 70 80 90 100 110 120 SPNIDQLASH SLLFQNAFAQ QAVCAPSRVS FLTGRRPDTT RLYDFNSYWR VHAGNFSTIP 130 140 150 160 170 180 QYFKENGYVT MSVGKVFHPG ISSNHTDDSP YSWSFPPYHP SSEKYENTKT CRGPDGELHA 190 200 210 220 230 240 NLLCPVDVLD VPEGTLPDKQ STEQAIQLLE KMKTSASPFF LAVGYHKPHI PFRYPKEFQK 250 260 270 280 290 300 LYPLENITLA PDPEVPDGLP PVAYNPWMDI RQREDVQALN ISVPYGPIPV DFQRKIRQSY 310 320 330 340 350 360 FASVSYLDTQ VGRLLSALDD LQLANSTIIA FTSDHGWALG EHGEWAKYSN FDVATHVPLI 370 380 390 400 410 420 FYVPGRTASL PEAGEKLFPY LDPFDSASQL MEPGRQSMDL VELVSLFPTL AGLAGLQVPP 430 440 450 460 470 480 RCPVPSFHVE LCREGKNLLK HFRFRDLEED PYLPGNPREL IAYSQYPRPS DIPQWNSDKP 490 500 510 520 530 540 SLKDIKIMGY SIRTIDYRYT VWVGFNPDEF LANFSDIHAG ELYFVDSDPL QDHNMYNDSQ 550 GGDLFQLLMP
	Isoform 2 (Short) [UniParc]. Checksum: 3C8D59915F8E8DD0	FASTA	343	38,310
	10 20 30 40 50 60 MPPPRTGRGL LWLGLVLSSV CVALGSETQA NSTTDALNVL LIIVDDLRPS LGCYGDKLVR 70 80 90 100 110 120 SPNIDQLASH SLLFQNAFAQ QAVCAPSRVS FLTGRRPDTT RLYDFNSYWR VHAGNFSTIP 130 140 150 160 170 180 QYFKENGYVT MSVGKVFHPG ISSNHTDDSP YSWSFPPYHP SSEKYENTKT CRGPDGELHA 190 200 210 220 230 240 NLLCPVDVLD VPEGTLPDKQ STEQAIQLLE KMKTSASPFF LAVGYHKPHI PFRYPKEFQK 250 260 270 280 290 300 LYPLENITLA PDPEVPDGLP PVAYNPWMDI RQREDVQALN ISVPYGPIPV DFQRKIRQSY 310 320 330 340 FASVSYLDTQ VGRLLSALDD LQLANSTIIA FTSDHGFLMR TNT
	Isoform 3 [UniParc]. Checksum: 8084F40A273B575F	FASTA	312	34,893
	10 20 30 40 50 60 MPPPRTGRGL LWLGLVLSSV CVALGSETQA NSTTDALNVL LIIVDDLRPS LGCYGDKLVR 70 80 90 100 110 120 SPNIDQLASH SLLFQNAFAQ QAVCAPSRVS FLTGRRPDTT RLYDFNSYWR VHAGNFSTIP 130 140 150 160 170 180 QYFKENGYVT MSVGKVFHPG ISSNHTDDSP YSWSFPPYHP SSEKYENTKT CRGPDGELHA 190 200 210 220 230 240 NLLCPVDVLD VPEGTLPDKQ STEQAIQLLE KMKTSASPFF LAVGYHKPHI PFRYPKEFQK 250 260 270 280 290 300 LYPLENITLA PDPEVPDGLP PVAYNPWMDI RQREDVQALN ISVPYGPIPV DFQEDQSSTG 310 FRLKTSSTRK YK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Hunter syndrome: isolation of an iduronate-2-sulfatase cDNA clone and analysis of patient DNA." Wilson P.J., Morris C.P., Anson D.S., Occhiodoro T., Bielicki J., Clements P.R., Hopwood J.J. Proc. Natl. Acad. Sci. U.S.A. 87:8531-8535(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 34-58 AND 456-473. Tissue: Endothelial cell.
[2]	"Sequence of the human iduronate 2-sulfatase (IDS) gene." Wilson P.J., Meaney C.A., Hopwood J.J., Morris C.P. Genomics 17:773-775(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"130 kb of DNA sequence reveals two new genes and a regional duplication distal to the human iduronate-2-sulfate sulfatase locus." Timms K.M., Lu F., Shen Y., Pierson C.A., Muzny D.M., Gu Y., Nelson D.L., Gibbs R.A. Genome Res. 5:71-78(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Identification of an alternative transcript from the human iduronate-2-sulfatase (IDS) gene." Malmgren H., Carlberg B.M., Pettersson U., Bondeson M.L. Genomics 29:291-293(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Lymphocyte.
[5]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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] (ISOFORM 3). Tissue: Skin.
[8]	"Determination of the organisation of coding sequences within the iduronate sulphate sulphatase (IDS) gene." Flomen R.H., Green E.P., Green P.M., Bentley D.R., Giannelli F. Hum. Mol. Genet. 2:5-10(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-398.
[9]	"Molecular basis of mucopolysaccharidosis type II: mutations in the iduronate-2-sulphatase gene." Hopwood J.J., Bunge S., Morris C.P., Wilson P.J., Steglich C., Beck M., Schwinger E., Gal A. Hum. Mutat. 2:435-442(1993) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON MPS2 VARIANTS.
[10]	"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-115, MASS SPECTROMETRY. Tissue: Liver.
[11]	"Mutation analysis of the iduronate-2-sulfatase gene in patients with mucopolysaccharidosis type II (Hunter syndrome)." Bunge S., Steglich C., Beck M., Rosenkranz W., Schwinger E., Hopwood J.J., Gal A. Hum. Mol. Genet. 1:335-339(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 ARG-135 AND GLY-422.
[12]	"Mutation R468W of the iduronate-2-sulfatase gene in mild Hunter syndrome (mucopolysaccharidosis type II) confirmed by in vitro mutagenesis and expression." Crotti P.L., Bunge S., Anderson R.A., Whitley C.B. Hum. Mol. Genet. 1:755-757(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MPS2 TRP-468.
[13]	"Iduronate-2-sulfatase gene mutations in 16 patients with mucopolysaccharidosis type II (Hunter syndrome)." Bunge S., Steglich C., Zuther C., Beck M., Morris C.P., Schwinger E., Schinzel A., Hopwood J.J., Gal A. Hum. Mol. Genet. 2:1871-1875(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 ARG-86; ASP-94; ARG-120; PRO-221 AND GLY-422.
[14]	"Mutations of the iduronate-2-sulfatase (IDS) gene in patients with Hunter syndrome (mucopolysaccharidosis II)." Schroeder W., Wulff K., Wehnert M., Seidlitz G., Herrmann F.H. Hum. Mutat. 4:128-131(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 GLU-68; HIS-293; GLY-478 AND ARG-485.
[15]	"Mutation analysis of Jewish Hunter patients in Israel." Ben-Simon-Schiff E., Bach G., Hopwood J.J., Abeliovich D. Hum. Mutat. 4:263-270(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MPS2 PRO-410.
[16]	"Molecular diagnosis of mucopolysaccharidosis type II (Hunter syndrome) by automated sequencing and computer-assisted interpretation: toward mutation mapping of the iduronate-2-sulfatase gene." Jonsson J.J., Aronovich E.L., Braun S.E., Whitley C.B. Am. J. Hum. Genet. 56:597-607(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 TRP-132; TYR-229; ARG-358; HIS-469 AND CYS-523.
[17]	"Mutations of the iduronate-2-sulfatase gene in 12 Polish patients with mucopolysaccharidosis type II (Hunter syndrome)." Popowska E., Rathmann M., Tylki-Szymanska A., Bunge S., Steglich C., Schwinger E., Gal A. Hum. Mutat. 5:97-100(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 LEU-86; ASN-87; PRO-92; ASN-135; CYS-345 AND TRP-468.
[18]	"Mucopolysaccharidosis type II (Hunter disease): identification and characterization of eight point mutations in the iduronate-2-sulfatase gene in Japanese patients." Sukegawa K., Tomatsu S., Fukao T., Iwata H., Song X.-Q., Yamada Y., Fukuda S., Isogai K., Orii T. Hum. Mutat. 6:136-143(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 PRO-48; SER-117 DEL; LEU-333; ARG-337; LEU-468 AND GLN-468.
[19]	"Mutations of the iduronate-2-sulfatase gene on a T146T background in three patients with Hunter syndrome." Li P., Huffman P., Thompson J.N. Hum. Mutat. 5:272-274(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MPS2 VAL-346.
[20]	"Mucopolysaccharidosis type II (Hunter syndrome): mutation 'hot spots' in the iduronate-2-sulfatase gene." Rathmann M., Bunge S., Beck M., Kresse H., Tylki-Szymanska A., Gal A. Am. J. Hum. Genet. 59:1202-1209(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 ASP-63; THR-85; GLN-86; CYS-88; HIS-88; CYS-108; SER-117 DEL; VAL-125; ARG-134; PHE-184; ASN-252; LEU-333; ILE-347; ARG-403 AND GLN-468.
[21]	"Mutations in the iduronate-2-sulfatase gene in five Norwegians with Hunter syndrome." Olsen T.C., Eiken H.G., Knappskog P.M., Kase B.F., Mansson J.-E., Boman H., Apold J. Hum. Genet. 97:198-203(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 LEU-333 AND ASP-346.
[22]	"Mutation analysis in 20 patients with Hunter disease." Goldenfum S.L., Young E., Michelakakis H., Tsagarakis S., Winchester B. Hum. Mutat. 7:76-78(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 ASP-63; ARG-86; GLY-95; PRO-205; TRP-468 AND GLN-468.
[23]	"Detection of four novel mutations in the iduronate-2-sulphatase gene by single-strand conformation polymorphism analysis of genomic amplicons." Li P., Thompson J.N. J. Inherit. Metab. Dis. 19:93-94(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 LEU-333 AND GLY-334.
[24]	"Mucopolysaccharidosis type II: identification of six novel mutations in Italian patients." Villani G.R.D., Balzano N., Grosso M., Salvadore F., Izzo P., di Natale P. Hum. Mutat. 10:71-75(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 ASP-63; THR-347; GLN-468 AND LEU-468.
[25]	"Hunter disease in a girl caused by R468Q mutation in the iduronate-2-sulfatase gene and skewed inactivation of the X chromosome carrying the normal allele." Sukegawa K., Song X.-Q., Masuno M., Fukao T., Shimozawa N., Fukuda S., Isogai K., Nishio H., Matsuo M., Tomatsu S., Kondo N., Orii T. Hum. Mutat. 10:361-367(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MPS2 GLN-468.
[26]	"Molecular analysis in 23 Hunter disease families." Lissens W., Seneca S., Liebaers I. J. Inherit. Metab. Dis. 20:453-456(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 PHE-73; THR-118 DEL; HIS-121; TRP-132; ARG-336; LYS-341; GLN-347; TRP-468; GLN-468; LYS-521 AND VAL-521.
[27]	"Mutation analysis in 57 unrelated patients with MPS II." Vafiadaki E., Cooper A., Heptinstall L.E., Hatton C.E., Thornley M., Wraith J.E. Arch. Dis. Child. 79:237-241(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 ASN-45; TYR-115; LEU-228; ARG-266; LYS-434; LYS-485 AND CYS-502.
[28]	"Identification of iduronate sulfatase gene alterations in 70 unrelated Hunter patients." Froissart R., Maire I., Millat G., Cudry S., Birot A.-M., Bonnet V., Bouton O., Bozon D. Clin. Genet. 53:362-368(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 ASN-71; SER-85; THR-85; LEU-86; GLY-88; HIS-88; PHE-89; SER-108; SER-117 DEL; ILE-118; ARG-121; ASP-138; HIS-148; ARG-229; LEU-333; ASN-334; ARG-335; GLU-336; ARG-339; ARG-403; LEU-467; GLN-468; TRP-468; ARG-480; GLN-480; LEU-480 AND SER-490.
[29]	"Mutational spectrum of the iduronate-2-sulfatase (IDS) gene in 36 unrelated Russian MPS II patients." Karsten S., Voskoboeva E., Tishkanina S., Pettersson U., Krasnopolskaya X., Bondeson M.-L. Hum. Genet. 103:732-735(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 ASP-54; ASP-63; GLU-79; CYS-88; LEU-88; HIS-88; ARG-102; PRO-159; SER-196; GLY-198; GLU-224; LEU-333; ASP-340; TYR-432; GLN-468; TYR-478 AND ARG-485.
[30]	"Detection of four novel mutations in the iduronate-2-sulfatase gene." Balzano N., Villani G.R.D., Grosso M., Izzo P., di Natale P. Hum. Mutat. 11:333-333(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 LEU-86; HIS-88; PRO-88; ILE-118 AND HIS-266.
[31]	"Mutations in the iduronate-2-sulfatase gene in 12 Spanish patients with Hunter disease." Gort L., Coll M.J., Chabas A. Hum. Mutat. Suppl. 1:S66-S68(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 THR-85; HIS-88; ILE-349 AND VAL-521.
[32]	"Identification of 9 novel gene mutations in 19 unrelated Hunter syndrome (Mucopolysaccharidosis type II) patients." Karsten S.L., Voskoboeva E., Carlberg B.-M., Kleijer W.J., Toennesen T., Pettersson U., Bondeson M.-L. Hum. Mutat. 12:433-433(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 PHE-143; TRP-184; VAL-269 AND HIS-348.
[33]	"Mutation analysis in the iduronate-2-sulphatase gene in 43 Japanese patients with mucopolysaccharidosis type II (Hunter disease)." Isogai K., Sukegawa K., Tomatsu S., Fukao T., Song X.-Q., Yamada Y., Fukuda S., Orii T., Kondo N. J. Inherit. Metab. Dis. 21:60-70(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 PRO-48; THR-85; LEU-86; PRO-182; SER-196; ASP-225; MET-227; ASN-308; PRO-314; LEU-333; ARG-337; ILE-349; GLN-468; LEU-468 AND TRP-468.
[34]	"Hunter disease in the Spanish population: molecular analysis in 31 families." Gort L., Chabas A., Coll M.J. J. Inherit. Metab. Dis. 21:655-661(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 THR-228; ARG-229; LEU-231; GLU-308; ALA-309 AND CYS-313.
[35]	"Identification of 6 new mutations in the iduronate sulfatase gene." Vallance H.D., Bernard L., Rashed M., Chiu D., Le G., Toone J., Applegarth D.A., Coulter-Mackie M. Hum. Mutat. 13:338-338(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 PHE-143; LYS-341; TYR-342 AND PHE-491.
[36]	"Mutation analysis of iduronate-2-sulphatase gene in 24 patients with Hunter syndrome: characterisation of 6 novel mutations." Hartog C., Fryer A., Upadhyaya M. Hum. Mutat. 14:87-87(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 ASN-264; PRO-465 AND TRP-468.
[37]	"Molecular basis of iduronate-2-sulphatase gene mutations in patients with mucopolysaccharidosis type II (Hunter syndrome)." Li P., Bellows A.B., Thompson J.N. J. Med. Genet. 36:21-27(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 ARG-71; GLU-82; THR-85; CYS-88; ARG-95 DEL; GLN-468; TRP-468 AND VAL-521.
[38]	"Expression of five iduronate-2-sulfatase site-directed mutations." Villani G.R.D., Daniele A., Balzano N., Di Natale P. Biochim. Biophys. Acta 1501:71-80(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS MPS2 HIS-88; PRO-88; ILE-118 AND GLN-468.
[39]	"MPS II in females: molecular basis of two different cases." Cudry S., Tigaud I., Froissart R., Bonnet V., Maire I., Bozon D. J. Med. Genet. 37:E29-E29(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MPS2 PRO-41, CHARACTERIZATION OF VARIANT MPS2 PRO-41.
[40]	"The effect of four mutations on the expression of iduronate-2-sulfatase in mucopolysaccharidosis type II." Bonuccelli G., Di Natale P., Corsolini F., Villani G., Regis S., Filocamo M. Biochim. Biophys. Acta 1537:233-238(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 SER-117 DEL; ILE-265 AND THR-347, CHARACTERIZATION OF VARIANTS MPS2 SER-117 DEL; ILE-265 AND THR-347.
[41]	"Molecular basis of mucopolysaccharidosis type II in Portugal: identification of four novel mutations." Moreira da Silva I., Froissart R., Marques dos Santos H., Caseiro C., Maire I., Bozon D. Clin. Genet. 60:316-318(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 CYS-88; THR-95; ILE-181; ARG-422; LEU-467; GLN-468 AND TRP-468.
[42]	"Expression studies of two novel in CIS-mutations identified in an intermediate case of Hunter syndrome." Ricci V., Filocamo M., Regis S., Corsolini F., Stroppiano M., Di Duca M., Gatti R. Am. J. Med. Genet. A 120:84-87(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MPS2 488-ILE-ALA-489, CHARACTERIZATION OF VARIANT MPS2 488-ILE-ALA-489.
[43]	"Mutational spectrum of the iduronate 2 sulfatase gene in 25 unrelated Korean Hunter syndrome patients: identification of 13 novel mutations." Kim C.H., Hwang H.Z., Song S.M., Paik K.H., Kwon E.K., Moon K.B., Yoon J.H., Han C.K., Jin D.-K. Hum. Mutat. 21:449-450(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 LEU-41 DEL; TYR-117; PRO-259 AND ILE-299.
[44]	"Multiple cryptic splice sites can be activated by IDS point mutations generating misspliced transcripts." Lualdi S., Pittis M.G., Regis S., Parini R., Allegri A.E., Furlan F., Bembi B., Filocamo M. J. Mol. Med. 84:692-700(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MPS2 VAL-82 AND VAL-140, CHARACTERIZATION OF VARIANTS MPS2 VAL-82 AND VAL-140.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	M58342 mRNA. Translation: AAA63197.1. L13329 , L13321, L13322, L13323, L13324, L13325, L13326, L13327, L13328 Genomic DNA. Translation: AAA16877.1. L04586 , L04578, L04579, L04580, L04581, L04583, L04582, L04584, L04585 Genomic DNA. Translation: AAA59192.1. L40586 mRNA. Translation: AAA92014.1. AC233288 Genomic DNA. No translation available. CH471171 Genomic DNA. Translation: EAW61282.1. CH471171 Genomic DNA. Translation: EAW61281.1. CH471171 Genomic DNA. Translation: EAW61283.1. BC006170 mRNA. Translation: AAH06170.1. AF011889 Genomic DNA. Translation: AAC77828.1.
IPI	IPI00006121. IPI00013771. IPI00026104.
PIR	KJHUID. A47535.
RefSeq	NP_000193.1. NM_000202.5. NP_006114.1. NM_006123.4.
UniGene	Hs.460960.
3D structure databases
ProteinModelPortal	P22304.
ModBase	Search...
Protein-protein interaction databases
IntAct	P22304. 1 interaction.
STRING	9606.ENSP00000339801.
PTM databases
PhosphoSite	P22304.
Polymorphism databases
DMDM	124174.
Proteomic databases
PaxDb	P22304.
PRIDE	P22304.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000340855; ENSP00000339801; ENSG00000010404. ENST00000370441; ENSP00000359470; ENSG00000010404. ENST00000370443; ENSP00000359472; ENSG00000010404. ENST00000466323; ENSP00000418264; ENSG00000010404. ENST00000595787; ENSP00000471213; ENSG00000267816. ENST00000595885; ENSP00000469247; ENSG00000267816. ENST00000596155; ENSP00000470806; ENSG00000267816. ENST00000599152; ENSP00000470508; ENSG00000267816.
GeneID	3423.
KEGG	hsa:3423.
UCSC	uc004fcw.4. human. uc011mxh.2. human.
Organism-specific databases
CTD	3423.
GeneCards	GC0XM148558.
HGNC	HGNC:5389. IDS.
MIM	300823. gene. 309900. phenotype.
neXtProt	NX_P22304.
Orphanet	217085. Mucopolysaccharidosis type 2A. 217093. Mucopolysaccharidosis type 2B.
PharmGKB	PA29636.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG3119.
HOGENOM	HOG000014304.
HOVERGEN	HBG006120.
InParanoid	P22304.
KO	K01136.
OMA	CREGKNL.
OrthoDB	EOG49078W.
PhylomeDB	P22304.
Enzyme and pathway databases
BioCyc	MetaCyc:HS00286-MONOMER.
Reactome	REACT_111217. Metabolism. REACT_116125. Disease.
Gene expression databases
ArrayExpress	P22304.
Bgee	P22304.
CleanEx	HS_IDS.
Genevestigator	P22304.
GermOnline	ENSG00000010404. 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	IDS. human.
GenomeRNAi	3423.
NextBio	13500.
PMAP-CutDB	P22304.
SOURCE	Search...

Entry information

Entry name

IDS_HUMAN

Accession

Primary (citable) accession number: P22304
Secondary accession number(s): D3DWT4, Q14604, Q9BRM3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	May 1, 2013
This is version 136 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.