Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P08842

- STS_HUMAN

UniProt

P08842 - STS_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Steryl-sulfatase

Gene

STS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequence
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

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

Ca2+1 PublicationNote: Binds 1 Ca2+ ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi35 – 351Calcium1 Publication
Metal bindingi36 – 361Calcium1 Publication
Metal bindingi75 – 751Calcium; via 3-oxoalanine1 Publication
Active sitei136 – 13611 Publication
Sitei333 – 3331Not glycosylated
Metal bindingi342 – 3421Calcium1 Publication
Metal bindingi343 – 3431Calcium1 Publication
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
Complete GO annotation...

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:11425. STS.

Subcellular locationi

Endoplasmic reticulum membrane; Multi-pass membrane protein

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 184163LumenalAdd
BLAST
Transmembranei185 – 20824HelicalAdd
BLAST
Topological domaini209 – 2124Cytoplasmic
Transmembranei213 – 23422HelicalAdd
BLAST
Topological domaini235 – 583349LumenalAdd
BLAST

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
Complete GO annotation...

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)1 Publication
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.1 Publication

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP08842.

Family & Domainsi

Sequence similaritiesi

Belongs to the sulfatase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3119.
GeneTreeiENSGT00760000119062.
HOGENOMiHOG000135352.
HOVERGENiHBG004283.
InParanoidiP08842.
KOiK01131.
OMAiVFIPLQI.
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

        10         20         30         40         50
MPLRKMKIPF LLLFFLWEAE SHAASRPNII LVMADDLGIG DPGCYGNKTI 
        60         70         80         90        100
RTPNIDRLAS GGVKLTQHLA ASPLCTPSRA AFMTGRYPVR SGMASWSRTG 
       110        120        130        140        150
VFLFTASSGG LPTDEITFAK LLKDQGYSTA LIGKWHLGMS CHSKTDFCHH 
       160        170        180        190        200
PLHHGFNYFY GISLTNLRDC KPGEGSVFTT GFKRLVFLPL QIVGVTLLTL 
       210        220        230        240        250
AALNCLGLLH VPLGVFFSLL FLAALILTLF LGFLHYFRPL NCFMMRNYEI 
       260        270        280        290        300
IQQPMSYDNL TQRLTVEAAQ FIQRNTETPF LLVLSYLHVH TALFSSKDFA 
       310        320        330        340        350
GKSQHGVYGD AVEEMDWSVG QILNLLDELR LANDTLIYFT SDQGAHVEEV 
       360        370        380        390        400
SSKGEIHGGS NGIYKGGKAN NWEGGIRVPG ILRWPRVIQA GQKIDEPTSN 
       410        420        430        440        450
MDIFPTVAKL AGAPLPEDRI IDGRDLMPLL EGKSQRSDHE FLFHYCNAYL 
       460        470        480        490        500
NAVRWHPQNS TSIWKAFFFT PNFNPVGSNG CFATHVCFCF GSYVTHHDPP 
       510        520        530        540        550
LLFDISKDPR ERNPLTPASE PRFYEILKVM QEAADRHTQT LPEVPDQFSW 
       560        570        580 
NNFLWKPWLQ LCCPSTGLSC QCDREKQDKR LSR
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 DB06713. Norelgestromin.

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.
GeneTreei ENSGT00760000119062.
HOGENOMi HOG000135352.
HOVERGENi HBG004283.
InParanoidi P08842.
KOi K01131.
OMAi VFIPLQI.
OrthoDBi EOG7QZG9J.
PhylomeDBi P08842.
TreeFami TF314186.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSi STS. human.
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

« Hide 'large scale' publications
  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, OXOALANINE AT CYS-75, 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.
+Additional computationally mapped references.

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: January 7, 2015
This is version 157 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.
© 2002– 2015 UniProt Consortium | License & Disclaimer