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P08842

- STS_HUMAN

UniProt

P08842 - STS_HUMAN

Protein

Steryl-sulfatase

Gene

STS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 2 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Conversion of sulfated steroid precursors to estrogens during pregnancy.

    Catalytic activityi

    3-beta-hydroxyandrost-5-en-17-one 3-sulfate + H2O = 3-beta-hydroxyandrost-5-en-17-one + sulfate.

    Cofactori

    Binds 1 calcium ion per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi35 – 351Calcium
    Metal bindingi36 – 361Calcium
    Metal bindingi75 – 751Calcium; via 3-oxoalanine
    Active sitei136 – 13611 Publication
    Sitei333 – 3331Not glycosylated
    Metal bindingi342 – 3421Calcium
    Metal bindingi343 – 3431Calcium
    Sitei459 – 4591Not glycosylated

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. steryl-sulfatase activity Source: Reactome
    3. sulfuric ester hydrolase activity Source: MGI

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. epidermis development Source: ProtInc
    3. female pregnancy Source: UniProtKB-KW
    4. glycosphingolipid metabolic process Source: Reactome
    5. post-translational protein modification Source: Reactome
    6. small molecule metabolic process Source: Reactome
    7. sphingolipid metabolic process Source: Reactome
    8. steroid catabolic process Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid metabolism, Pregnancy, Steroid metabolism

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_116105. Glycosphingolipid metabolism.
    REACT_121036. The activation of arylsulfatases.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Steryl-sulfatase (EC:3.1.6.2)
    Alternative name(s):
    Arylsulfatase C
    Short name:
    ASC
    Steroid sulfatase
    Steryl-sulfate sulfohydrolase
    Gene namesi
    Name:STS
    Synonyms:ARSC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:11425. STS.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum Source: ProtInc
    2. endoplasmic reticulum lumen Source: Reactome
    3. endoplasmic reticulum membrane Source: Reactome
    4. endosome Source: ProtInc
    5. Golgi apparatus Source: ProtInc
    6. integral component of membrane Source: UniProtKB-KW
    7. intracellular membrane-bounded organelle Source: ProtInc
    8. lysosome Source: ProtInc
    9. membrane Source: ProtInc
    10. plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Ichthyosis, X-linked (IXL) [MIM:308100]: A keratinization disorder manifesting with mild erythroderma and generalized exfoliation of the skin within a few weeks after birth. Affected boys later develop large, polygonal, dark brown scales, especially on the neck, extremities, trunk, and buttocks.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti341 – 3411S → L in IXL; loss of activity. 2 Publications
    VAR_007240
    Natural varianti372 – 3721W → R in IXL; loss of activity. 2 Publications
    VAR_007241
    Natural varianti372 – 3721W → S in IXL; loss of activity. 1 Publication
    VAR_014020
    Natural varianti380 – 3801G → R in IXL. 1 Publication
    VAR_014021
    Natural varianti444 – 4441H → R in IXL; loss of activity. 1 Publication
    VAR_014022
    Natural varianti446 – 4461C → Y in IXL; loss of activity. 2 Publications
    VAR_007242
    Natural varianti560 – 5601Q → P in IXL. 1 Publication
    VAR_014023

    Keywords - Diseasei

    Disease mutation, Ichthyosis

    Organism-specific databases

    MIMi308100. phenotype.
    Orphaneti461. Recessive X-linked ichthyosis.
    281090. Syndromic X-linked ichthyosis.
    PharmGKBiPA36225.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 21211 PublicationAdd
    BLAST
    Chaini22 – 583562Steryl-sulfatasePRO_0000033414Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi47 – 471N-linked (GlcNAc...)2 Publications
    Modified residuei75 – 7513-oxoalanine (Cys)
    Disulfide bondi141 ↔ 148
    Disulfide bondi170 ↔ 242
    Glycosylationi259 – 2591N-linked (GlcNAc...)2 Publications
    Disulfide bondi446 ↔ 489
    Disulfide bondi481 ↔ 487
    Disulfide bondi562 ↔ 570
    Disulfide bondi563 ↔ 572

    Post-translational modificationi

    The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP08842.
    PaxDbiP08842.
    PRIDEiP08842.

    PTM databases

    PhosphoSiteiP08842.

    Expressioni

    Gene expression databases

    BgeeiP08842.
    CleanExiHS_STS.
    GenevestigatoriP08842.

    Organism-specific databases

    HPAiHPA002904.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    IntActiP08842. 1 interaction.
    MINTiMINT-1177440.
    STRINGi9606.ENSP00000217961.

    Structurei

    Secondary structure

    1
    583
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 369
    Helixi43 – 453
    Beta strandi48 – 503
    Helixi53 – 564
    Turni57 – 615
    Beta strandi62 – 698
    Helixi77 – 848
    Helixi88 – 914
    Beta strandi96 – 983
    Helixi118 – 1247
    Beta strandi128 – 1347
    Beta strandi141 – 1433
    Turni144 – 1463
    Helixi151 – 1533
    Beta strandi157 – 1648
    Helixi168 – 1703
    Helixi179 – 1857
    Helixi187 – 20519
    Helixi213 – 24129
    Beta strandi244 – 2463
    Beta strandi249 – 2546
    Helixi260 – 27314
    Turni274 – 2774
    Beta strandi280 – 2856
    Beta strandi290 – 2923
    Turni297 – 2993
    Beta strandi304 – 3063
    Helixi307 – 32822
    Helixi332 – 3343
    Beta strandi335 – 3439
    Beta strandi352 – 3543
    Beta strandi370 – 3723
    Helixi373 – 3764
    Beta strandi380 – 3834
    Turni385 – 3873
    Helixi400 – 4023
    Helixi403 – 4119
    Beta strandi417 – 4193
    Helixi427 – 4304
    Beta strandi440 – 4467
    Beta strandi449 – 4557
    Beta strandi464 – 4685
    Turni482 – 4843
    Beta strandi489 – 4913
    Beta strandi501 – 5033
    Turni505 – 5073
    Turni518 – 5214
    Helixi523 – 53715
    Helixi550 – 5534
    Helixi557 – 5593
    Beta strandi563 – 5686

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P49X-ray2.60A22-583[»]
    ProteinModelPortaliP08842.
    SMRiP08842. Positions 23-575.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08842.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini22 – 184163LumenalAdd
    BLAST
    Topological domaini209 – 2124Cytoplasmic
    Topological domaini235 – 583349LumenalAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei185 – 20824HelicalAdd
    BLAST
    Transmembranei213 – 23422HelicalAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the sulfatase family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG3119.
    HOGENOMiHOG000135352.
    HOVERGENiHBG004283.
    InParanoidiP08842.
    KOiK01131.
    OMAiGLSCQCD.
    OrthoDBiEOG7QZG9J.
    PhylomeDBiP08842.
    TreeFamiTF314186.

    Family and domain databases

    Gene3Di3.40.720.10. 2 hits.
    InterProiIPR017849. Alkaline_Pase-like_a/b/a.
    IPR017850. Alkaline_phosphatase_core.
    IPR000917. Sulfatase.
    IPR024607. Sulfatase_CS.
    [Graphical view]
    PfamiPF00884. Sulfatase. 1 hit.
    [Graphical view]
    SUPFAMiSSF53649. SSF53649. 1 hit.
    PROSITEiPS00523. SULFATASE_1. 1 hit.
    PS00149. SULFATASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P08842-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPLRKMKIPF LLLFFLWEAE SHAASRPNII LVMADDLGIG DPGCYGNKTI    50
    RTPNIDRLAS GGVKLTQHLA ASPLCTPSRA AFMTGRYPVR SGMASWSRTG 100
    VFLFTASSGG LPTDEITFAK LLKDQGYSTA LIGKWHLGMS CHSKTDFCHH 150
    PLHHGFNYFY GISLTNLRDC KPGEGSVFTT GFKRLVFLPL QIVGVTLLTL 200
    AALNCLGLLH VPLGVFFSLL FLAALILTLF LGFLHYFRPL NCFMMRNYEI 250
    IQQPMSYDNL TQRLTVEAAQ FIQRNTETPF LLVLSYLHVH TALFSSKDFA 300
    GKSQHGVYGD AVEEMDWSVG QILNLLDELR LANDTLIYFT SDQGAHVEEV 350
    SSKGEIHGGS NGIYKGGKAN NWEGGIRVPG ILRWPRVIQA GQKIDEPTSN 400
    MDIFPTVAKL AGAPLPEDRI IDGRDLMPLL EGKSQRSDHE FLFHYCNAYL 450
    NAVRWHPQNS TSIWKAFFFT PNFNPVGSNG CFATHVCFCF GSYVTHHDPP 500
    LLFDISKDPR ERNPLTPASE PRFYEILKVM QEAADRHTQT LPEVPDQFSW 550
    NNFLWKPWLQ LCCPSTGLSC QCDREKQDKR LSR 583
    Length:583
    Mass (Da):65,492
    Last modified:April 1, 1990 - v2
    Checksum:i74746AFA9D21A0A6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231A → E in AAA60596. (PubMed:3032454)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti341 – 3411S → L in IXL; loss of activity. 2 Publications
    VAR_007240
    Natural varianti372 – 3721W → R in IXL; loss of activity. 2 Publications
    VAR_007241
    Natural varianti372 – 3721W → S in IXL; loss of activity. 1 Publication
    VAR_014020
    Natural varianti380 – 3801G → R in IXL. 1 Publication
    VAR_014021
    Natural varianti444 – 4441H → R in IXL; loss of activity. 1 Publication
    VAR_014022
    Natural varianti446 – 4461C → Y in IXL; loss of activity. 2 Publications
    VAR_007242
    Natural varianti560 – 5601Q → P in IXL. 1 Publication
    VAR_014023

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04964 mRNA. Translation: AAA60597.1.
    M16505 mRNA. Translation: AAA60596.1.
    AK314034 mRNA. Translation: BAG36744.1.
    BC075030 mRNA. Translation: AAH75030.1.
    M23945 Genomic DNA. Translation: AAA60598.1.
    M23556 Genomic DNA. Translation: AAA60599.1.
    CCDSiCCDS14127.1.
    PIRiA32641. KJHUAC.
    RefSeqiNP_000342.2. NM_000351.4.
    UniGeneiHs.522578.
    Hs.700558.
    Hs.700559.
    Hs.740067.

    Genome annotation databases

    EnsembliENST00000217961; ENSP00000217961; ENSG00000101846.
    GeneIDi412.
    KEGGihsa:412.
    UCSCiuc004cry.4. human.

    Polymorphism databases

    DMDMi135006.

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Steroid sulfatase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04964 mRNA. Translation: AAA60597.1 .
    M16505 mRNA. Translation: AAA60596.1 .
    AK314034 mRNA. Translation: BAG36744.1 .
    BC075030 mRNA. Translation: AAH75030.1 .
    M23945 Genomic DNA. Translation: AAA60598.1 .
    M23556 Genomic DNA. Translation: AAA60599.1 .
    CCDSi CCDS14127.1.
    PIRi A32641. KJHUAC.
    RefSeqi NP_000342.2. NM_000351.4.
    UniGenei Hs.522578.
    Hs.700558.
    Hs.700559.
    Hs.740067.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1P49 X-ray 2.60 A 22-583 [» ]
    ProteinModelPortali P08842.
    SMRi P08842. Positions 23-575.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P08842. 1 interaction.
    MINTi MINT-1177440.
    STRINGi 9606.ENSP00000217961.

    Chemistry

    BindingDBi P08842.
    ChEMBLi CHEMBL3559.
    DrugBanki DB00655. Estrone.

    PTM databases

    PhosphoSitei P08842.

    Polymorphism databases

    DMDMi 135006.

    Proteomic databases

    MaxQBi P08842.
    PaxDbi P08842.
    PRIDEi P08842.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000217961 ; ENSP00000217961 ; ENSG00000101846 .
    GeneIDi 412.
    KEGGi hsa:412.
    UCSCi uc004cry.4. human.

    Organism-specific databases

    CTDi 412.
    GeneCardsi GC0XP007147.
    HGNCi HGNC:11425. STS.
    HPAi HPA002904.
    MIMi 300747. gene.
    308100. phenotype.
    neXtProti NX_P08842.
    Orphaneti 461. Recessive X-linked ichthyosis.
    281090. Syndromic X-linked ichthyosis.
    PharmGKBi PA36225.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3119.
    HOGENOMi HOG000135352.
    HOVERGENi HBG004283.
    InParanoidi P08842.
    KOi K01131.
    OMAi GLSCQCD.
    OrthoDBi EOG7QZG9J.
    PhylomeDBi P08842.
    TreeFami TF314186.

    Enzyme and pathway databases

    Reactomei REACT_116105. Glycosphingolipid metabolism.
    REACT_121036. The activation of arylsulfatases.

    Miscellaneous databases

    EvolutionaryTracei P08842.
    GeneWikii Steroid_sulfatase.
    GenomeRNAii 412.
    NextBioi 1743.
    PROi P08842.
    SOURCEi Search...

    Gene expression databases

    Bgeei P08842.
    CleanExi HS_STS.
    Genevestigatori P08842.

    Family and domain databases

    Gene3Di 3.40.720.10. 2 hits.
    InterProi IPR017849. Alkaline_Pase-like_a/b/a.
    IPR017850. Alkaline_phosphatase_core.
    IPR000917. Sulfatase.
    IPR024607. Sulfatase_CS.
    [Graphical view ]
    Pfami PF00884. Sulfatase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53649. SSF53649. 1 hit.
    PROSITEi PS00523. SULFATASE_1. 1 hit.
    PS00149. SULFATASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of human steroid-sulfatase. Membrane topology, glycosylation, and subcellular distribution in BHK-21 cells."
      Stein C., Hille A., Seidel J., Rijnbout S., Waheed A., Schmidt B., Geuze H., von Figura K.
      J. Biol. Chem. 264:13865-13872(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-47 AND ASN-259, LACK OF GLYCOSYLATION AT ASN-333 AND ASN-459.
    2. "Cloning and expression of steroid sulfatase cDNA and the frequent occurrence of deletions in STS deficiency: implications for X-Y interchange."
      Yen P.H., Allen E., Marsh B., Mohandas T., Wang N., Taggart R.T., Shapiro L.J.
      Cell 49:443-454(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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].
      Tissue: Placenta.
    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].
    5. "The human X-linked steroid sulfatase gene and a Y-encoded pseudogene: evidence for an inversion of the Y chromosome during primate evolution."
      Yen P.H., Marsh B., Allen E., Tsai S.P., Ellison J., Connolly L., Neiswanger K., Shapiro L.J.
      Cell 55:1123-1135(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-174 AND 461-583.
    6. Cited for: PROTEIN SEQUENCE OF 22-45.
      Tissue: Liver.
    7. "Structure of human estrone sulfatase suggests functional roles of membrane association."
      Hernandez-Guzman F.G., Higashiyama T., Pangborn W., Osawa Y., Ghosh D.
      J. Biol. Chem. 278:22989-22997(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, COFACTOR, TRANSMEMBRANE TOPOLOGY, ACTIVE SITE, GLYCOSYLATION AT ASN-47 AND ASN-259.
    8. "Identification of point mutations in the steroid sulfatase gene of three patients with X-linked ichthyosis."
      Basler E., Grompe M., Parenti G., Yates J., Ballabio A.
      Am. J. Hum. Genet. 50:483-491(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS IXL LEU-341; ARG-372 AND TYR-446.
    9. "Characterization of point mutations in patients with X-linked ichthyosis. Effects on the structure and function of the steroid sulfatase protein."
      Alperin E.S., Shapiro L.J.
      J. Biol. Chem. 272:20756-20763(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS IXL LEU-341; ARG-372; SER-372; ARG-444 AND TYR-446.
    10. "PCR diagnosis of X-linked ichthyosis: identification of a novel mutation (E560P) of the steroid sulfatase gene."
      Sugawara T., Shimizu H., Hoshi N., Fujimoto Y., Nakajima A., Fujimoto S.
      Hum. Mutat. 15:296-296(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT IXL PRO-560.
    11. "Novel point mutations in the steroid sulfatase gene in patients with X-linked ichthyosis: transfection analysis using the mutated genes."
      Oyama N., Satoh M., Iwatsuki K., Kaneko F.
      J. Invest. Dermatol. 114:1195-1199(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT IXL ARG-380.

    Entry informationi

    Entry nameiSTS_HUMAN
    AccessioniPrimary (citable) accession number: P08842
    Secondary accession number(s): B2RA47
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 154 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3