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P22304 (IDS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Iduronate 2-sulfatase

EC=3.1.6.13
Alternative name(s):
Alpha-L-iduronate sulfate sulfatase
Short name=Idursulfase
Gene names
Name:IDS
Synonyms:SIDS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length550 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Propeptide26 – 338
PRO_0000033428
Chain34 – 455422Iduronate 2-sulfatase 42 kDa chain
PRO_0000033429
Chain456 – 55095Iduronate 2-sulfatase 14 kDa chain
PRO_0000033430

Sites

Metal binding451Calcium By similarity
Metal binding461Calcium By similarity
Metal binding841Calcium; via 3-oxoalanine By similarity
Metal binding3341Calcium By similarity
Metal binding3351Calcium By similarity

Amino acid modifications

Modified residue8413-oxoalanine (Cys) By similarity
Glycosylation1151N-linked (GlcNAc...) Ref.10
Glycosylation1441N-linked (GlcNAc...) Potential
Glycosylation2461N-linked (GlcNAc...) Potential
Glycosylation2801N-linked (GlcNAc...) Potential
Glycosylation3251N-linked (GlcNAc...) Potential
Glycosylation5131N-linked (GlcNAc...) Potential
Glycosylation5371N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence294 – 31219RKIRQ…DTQVG → EDQSSTGFRLKTSSTRKYK in isoform 3.
VSP_039116
Alternative sequence313 – 550238Missing in isoform 3.
VSP_039117
Alternative sequence337 – 3437WALGEHG → FLMRTNT in isoform 2.
VSP_006301
Alternative sequence344 – 550207Missing in isoform 2.
VSP_006302
Natural variant411L → P in MPS2; mild form; increase in enzyme activity observed in transfected cells. Ref.39
VAR_026915
Natural variant411Missing in MPS2; intermediate form. Ref.43
VAR_026914
Natural variant451D → N in MPS2. Ref.27
VAR_007313
Natural variant481R → P in MPS2; mild form. Ref.18 Ref.33
VAR_007314
Natural variant541Y → D in MPS2; severe form. Ref.29
VAR_007315
Natural variant631N → D in MPS2; mild/intermediate form. Ref.20 Ref.22 Ref.24 Ref.29
VAR_007316
Natural variant681A → E in MPS2; severe. Ref.14
VAR_007317
Natural variant711S → N in MPS2; mild form. Ref.28
VAR_026916
Natural variant711S → R in MPS2; severe form. Ref.37
VAR_008998
Natural variant731L → F in MPS2; severe form. Ref.26
VAR_026917
Natural variant791A → E in MPS2; mild form. Ref.29
VAR_007318
Natural variant821A → E in MPS2. Ref.37
VAR_008999
Natural variant821A → V in MPS2; no significant enzyme activity. Ref.44
VAR_026918
Natural variant851A → S in MPS2; severe form. Ref.28
VAR_026919
Natural variant851A → T in MPS2; mild to severe forms. Ref.20 Ref.28 Ref.31 Ref.33 Ref.37
VAR_007319
Natural variant861P → L in MPS2; intermediate to severe forms. Ref.17 Ref.28 Ref.30 Ref.33
VAR_007320
Natural variant861P → Q in MPS2. Ref.20
VAR_007321
Natural variant861P → R in MPS2; severe form. Ref.13 Ref.22
VAR_007322
Natural variant871S → N in MPS2; mild form. Ref.17
VAR_007323
Natural variant881R → C in MPS2; severe form. Ref.20 Ref.29 Ref.37 Ref.41
VAR_007324
Natural variant881R → G in MPS2; severe form. Ref.28
VAR_026920
Natural variant881R → 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 variant881R → L in MPS2; severe form. Ref.29
VAR_007326
Natural variant881R → P in MPS2; severe form; total absence of residual activity; poor transport to lysosomes. Ref.30 Ref.38
VAR_007327
Natural variant891V → F in MPS2. Ref.28
VAR_026921
Natural variant921L → P in MPS2; severe form. Ref.17
VAR_007328
Natural variant941G → D in MPS2; mild form. Ref.13
VAR_007329
Natural variant951R → G in MPS2; intermediate form. Ref.22
VAR_026922
Natural variant951R → T in MPS2; mild form. Ref.41
VAR_026923
Natural variant951Missing in MPS2; severe form. Ref.37
VAR_009000
Natural variant1021L → R in MPS2; mild form. Ref.29
VAR_007330
Natural variant1081Y → C in MPS2; mild form. Ref.20
VAR_007331
Natural variant1081Y → S in MPS2; mild form. Ref.28
VAR_026924
Natural variant1151N → Y in MPS2. Ref.27
VAR_007332
Natural variant1171S → Y in MPS2; severe form. Ref.43
VAR_026926
Natural variant1171Missing in MPS2; severe form; deleterious mutation; results in an inactive enzyme. Ref.18 Ref.20 Ref.28 Ref.40
VAR_026925
Natural variant1181T → I in MPS2; mild to severe forms; greatly reduced activity; poor transport to lysosomes. Ref.28 Ref.30 Ref.38
VAR_007333
Natural variant1181Missing in MPS2; severe form. Ref.26
VAR_026927
Natural variant1201P → H in MPS2; mild form.
VAR_007334
Natural variant1201P → R in MPS2; severe form. Ref.13
VAR_007335
Natural variant1211Q → H in MPS2; severe form. Ref.26
VAR_026928
Natural variant1211Q → R in MPS2; severe form. Ref.28
VAR_026929
Natural variant1251E → V in MPS2; mild form. Ref.20
VAR_007336
Natural variant1321S → W in MPS2; severe form. Ref.16 Ref.26
VAR_007337
Natural variant1341G → R in MPS2; severe form. Ref.20
VAR_007338
Natural variant1351K → N in MPS2; intermediate form. Ref.17
VAR_007339
Natural variant1351K → R in MPS2; intermediate form. Ref.11
Corresponds to variant rs28937311 [ dbSNP | Ensembl ].
VAR_007340
Natural variant1381H → D in MPS2; mild/intermediate form. Ref.28
VAR_026930
Natural variant1401G → V in MPS2; no significant enzyme activity. Ref.44
VAR_026931
Natural variant1431S → F in MPS2. Ref.32 Ref.35
VAR_007341
Natural variant1481D → H in MPS2; intermediate form. Ref.28
VAR_026932
Natural variant1591H → P in MPS2; severe form. Ref.29
VAR_007342
Natural variant1591Missing in MPS2; intermediate form.
VAR_007343
Natural variant1601P → R in MPS2.
VAR_007344
Natural variant1811N → I in MPS2; mild form. Ref.41
VAR_026933
Natural variant1821L → P in MPS2; intermediate form. Ref.33
VAR_026934
Natural variant1841C → F in MPS2; mild/intermediate form. Ref.20
VAR_007345
Natural variant1841C → W in MPS2. Ref.32
VAR_007346
Natural variant1961L → S in MPS2; mild/intermediate form. Ref.29 Ref.33
VAR_007347
Natural variant1981D → G in MPS2; mild form. Ref.29
VAR_007348
Natural variant2051A → P in MPS2; intermediate form. Ref.22
VAR_026935
Natural variant2211L → P in MPS2; intermediate form. Ref.13
VAR_007349
Natural variant2241G → E in MPS2; severe form. Ref.29
VAR_007350
Natural variant2251Y → D in MPS2; intermediate form. Ref.33
VAR_007351
Natural variant2271K → M in MPS2; intermediate form. Ref.33
VAR_026936
Natural variant2271K → Q in MPS2; severe form.
VAR_007352
Natural variant2281P → L in MPS2. Ref.27
VAR_007353
Natural variant2281P → T in MPS2; severe form. Ref.34
VAR_026937
Natural variant2291H → R in MPS2; intermediate/severe form. Ref.28 Ref.34
VAR_026938
Natural variant2291H → Y in MPS2; severe form. Ref.16
VAR_007354
Natural variant2311P → L in MPS2; mild form. Ref.34
VAR_026939
Natural variant2521D → N in MPS2. Ref.20
Corresponds to variant rs146458524 [ dbSNP | Ensembl ].
VAR_007355
Natural variant2591L → P in MPS2; severe form. Ref.43
VAR_026940
Natural variant2641Y → N in MPS2. Ref.36
VAR_009001
Natural variant2651N → I in MPS2; intermediate form; deleterious mutation; residual activity of 7.5% of the wild-type. Ref.40
VAR_026941
Natural variant2661P → H in MPS2; mild form. Ref.30
VAR_007356
Natural variant2661P → R in MPS2. Ref.27
VAR_007357
Natural variant2691D → V in MPS2. Ref.32
VAR_007358
Natural variant2931Q → H in MPS2; mild form. Ref.14
VAR_007359
Natural variant2991S → I in MPS2; mild form. Ref.43
VAR_026942
Natural variant3081D → E in MPS2; mild form. Ref.34
VAR_026943
Natural variant3081D → N in MPS2; intermediate form. Ref.33
VAR_026944
Natural variant3091T → A in MPS2; severe form. Ref.34
Corresponds to variant rs145807417 [ dbSNP | Ensembl ].
VAR_026945
Natural variant3131R → C in MPS2; unknown pathological significance. Ref.34
Corresponds to variant rs201048643 [ dbSNP | Ensembl ].
VAR_026946
Natural variant3141L → P in MPS2; severe form. Ref.33
VAR_026947
Natural variant3331S → L in MPS2; severe form. Ref.18 Ref.20 Ref.21 Ref.23 Ref.28 Ref.29 Ref.33
VAR_007360
Natural variant3341D → G in MPS2; severe form. Ref.23
VAR_009002
Natural variant3341D → N in MPS2; mild form. Ref.28
VAR_026948
Natural variant3351H → R in MPS2; intermediate form. Ref.28
VAR_026949
Natural variant3361G → E in MPS2; severe from. Ref.28
VAR_026950
Natural variant3361G → R in MPS2; severe form. Ref.26
VAR_026951
Natural variant3371W → R in MPS2; intermediate form. Ref.18 Ref.33
VAR_007361
Natural variant3391L → R in MPS2; severe form. Ref.28
VAR_026952
Natural variant3401G → D in MPS2; mild form. Ref.29
VAR_007362
Natural variant3411E → K in MPS2; severe form. Ref.26 Ref.35
VAR_008134
Natural variant3421H → Y in MPS2; mild form. Ref.35
VAR_008135
Natural variant3451W → C in MPS2; mild form. Ref.17
VAR_007363
Natural variant3461A → D in MPS2; mild/severe form. Ref.21
VAR_007364
Natural variant3461A → V in MPS2; mild/severe form. Ref.19
VAR_007365
Natural variant3471K → I in MPS2. Ref.20
VAR_007366
Natural variant3471K → Q in MPS2; severe form. Ref.26
VAR_026953
Natural variant3471K → T in MPS2; severe form; deleterious mutation confirmed. Ref.24 Ref.40
VAR_007367
Natural variant3481Y → H in MPS2. Ref.32
VAR_007368
Natural variant3491S → I in MPS2; severe form. Ref.31 Ref.33
VAR_007369
Natural variant3581P → R in MPS2; severe form. Ref.16
VAR_007370
Natural variant4031L → R in MPS2; intermediate form. Ref.20 Ref.28
VAR_007371
Natural variant4101L → P in MPS2. Ref.15
VAR_026954
Natural variant4221C → G in MPS2; mild form. Ref.11 Ref.13
Corresponds to variant rs28937310 [ dbSNP | Ensembl ].
VAR_007372
Natural variant4221C → R in MPS2; severe form. Ref.41
VAR_026955
Natural variant4321C → Y in MPS2; severe form. Ref.29
VAR_007373
Natural variant4341E → K in MPS2. Ref.27
VAR_007374
Natural variant4651Q → P in MPS2; severe form. Ref.36
VAR_009003
Natural variant4671P → L in MPS2; severe form. Ref.28 Ref.41
VAR_026956
Natural variant4681R → G in MPS2; mild to severe forms.
VAR_007375
Natural variant4681R → L in MPS2; mild to severe forms. Ref.18 Ref.24 Ref.33
VAR_007376
Natural variant4681R → 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 variant4681R → 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 variant4691P → H in MPS2; mild form. Ref.16
VAR_007379
Natural variant4781D → G in MPS2; mild form. Ref.14
VAR_007380
Natural variant4781D → Y in MPS2; severe form. Ref.29
VAR_007381
Natural variant4801P → L in MPS2; mild form. Ref.28
VAR_026957
Natural variant4801P → Q in MPS2; mild form. Ref.28
VAR_026958
Natural variant4801P → R in MPS2; severe form. Ref.28
VAR_026959
Natural variant4851I → K in MPS2. Ref.27
VAR_007382
Natural variant4851I → R in MPS2; severe form. Ref.14 Ref.29
VAR_007383
Natural variant488 – 4892MG → IA in MPS2; intermediate form; mutation A-489 confirmed as causative of MPS2.
VAR_026960
Natural variant4901Y → S in MPS2; intermediate form. Ref.28
VAR_026961
Natural variant4911S → F in MPS2; mild form. Ref.35
VAR_008136
Natural variant5021W → C in MPS2; severe form. Ref.27
VAR_007384
Natural variant5021W → S in MPS2.
VAR_007385
Natural variant5211E → K in MPS2; severe form. Ref.26
VAR_026962
Natural variant5211E → V in MPS2; severe form. Ref.26 Ref.31 Ref.37
VAR_007386
Natural variant5231Y → C in MPS2; mild form. Ref.16
VAR_007387

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: EA1B713417280413

FASTA55061,873
        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 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: 3C8D59915F8E8DD0
Show »

FASTA34338,310
Isoform 3 [UniParc].

Checksum: 8084F40A273B575F
Show »

FASTA31234,893

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M58342 mRNA. Translation: AAA63197.1.
L13329 expand/collapse EMBL AC list , L13321, L13322, L13323, L13324, L13325, L13326, L13327, L13328 Genomic DNA. Translation: AAA16877.1.
L04586 expand/collapse EMBL AC list , 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.
CCDSCCDS14685.1. [P22304-1]
CCDS14686.1. [P22304-2]
PIRKJHUID. A47535.
RefSeqNP_000193.1. NM_000202.6. [P22304-1]
NP_001160022.1. NM_001166550.2.
NP_006114.1. NM_006123.4. [P22304-2]
UniGeneHs.460960.

3D structure databases

ProteinModelPortalP22304.
SMRP22304. Positions 29-450.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109649. 1 interaction.
IntActP22304. 2 interactions.
MINTMINT-4722325.
STRING9606.ENSP00000339801.

Protein family/group databases

Allergome9623. Hom s Idursulfase.

PTM databases

PhosphoSiteP22304.

Polymorphism databases

DMDM124174.

Proteomic databases

MaxQBP22304.
PaxDbP22304.
PRIDEP22304.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000340855; ENSP00000339801; ENSG00000010404. [P22304-1]
ENST00000370441; ENSP00000359470; ENSG00000010404. [P22304-2]
ENST00000370443; ENSP00000359472; ENSG00000010404. [P22304-3]
ENST00000466323; ENSP00000418264; ENSG00000010404. [P22304-3]
ENST00000595787; ENSP00000471213; ENSG00000267816. [P22304-1]
ENST00000595885; ENSP00000469247; ENSG00000267816. [P22304-3]
ENST00000596155; ENSP00000470806; ENSG00000267816. [P22304-3]
ENST00000599152; ENSP00000470508; ENSG00000267816. [P22304-2]
GeneID3423.
KEGGhsa:3423.
UCSCuc004fcw.4. human. [P22304-1]
uc011mxh.2. human. [P22304-2]

Organism-specific databases

CTD3423.
GeneCardsGC0XM148558.
HGNCHGNC:5389. IDS.
MIM300823. gene.
309900. phenotype.
neXtProtNX_P22304.
Orphanet217093. Mucopolysaccharidosis type 2, attenuated form.
217085. Mucopolysaccharidosis type 2, severe form.
PharmGKBPA29636.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3119.
HOGENOMHOG000014304.
HOVERGENHBG006120.
InParanoidP22304.
KOK01136.
OMADHNMYND.
PhylomeDBP22304.
TreeFamTF323156.

Enzyme and pathway databases

BioCycMetaCyc:HS00286-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

ArrayExpressP22304.
BgeeP22304.
CleanExHS_IDS.
GenevestigatorP22304.

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

ChiTaRSIDS. human.
GeneWikiIduronate-2-sulfatase.
GenomeRNAi3423.
NextBio13500.
PMAP-CutDBP22304.
PROP22304.
SOURCESearch...

Entry information

Entry nameIDS_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 150 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 X

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