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P08842

- STS_HUMAN

UniProt

P08842 - STS_HUMAN

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Protein

Steryl-sulfatase

Gene

STS

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

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 – 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 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
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 – 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.
GeneTreeiENSGT00760000119062.
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

        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:
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 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 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

« 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.

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 29, 2014
This is version 155 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