STS_HUMAN - dbPTM
STS_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STS_HUMAN
UniProt AC P08842
Protein Name Steryl-sulfatase
Gene Name STS
Organism Homo sapiens (Human).
Sequence Length 583
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein.
Protein Description Conversion of sulfated steroid precursors to estrogens during pregnancy..
Protein Sequence MPLRKMKIPFLLLFFLWEAESHAASRPNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMASWSRTGVFLFTASSGGLPTDEITFAKLLKDQGYSTALIGKWHLGMSCHSKTDFCHHPLHHGFNYFYGISLTNLRDCKPGEGSVFTTGFKRLVFLPLQIVGVTLLTLAALNCLGLLHVPLGVFFSLLFLAALILTLFLGFLHYFRPLNCFMMRNYEIIQQPMSYDNLTQRLTVEAAQFIQRNTETPFLLVLSYLHVHTALFSSKDFAGKSQHGVYGDAVEEMDWSVGQILNLLDELRLANDTLIYFTSDQGAHVEEVSSKGEIHGGSNGIYKGGKANNWEGGIRVPGILRWPRVIQAGQKIDEPTSNMDIFPTVAKLAGAPLPEDRIIDGRDLMPLLEGKSQRSDHEFLFHYCNAYLNAVRWHPQNSTSIWKAFFFTPNFNPVGSNGCFATHVCFCFGSYVTHHDPPLLFDISKDPRERNPLTPASEPRFYEILKVMQEAADRHTQTLPEVPDQFSWNNFLWKPWLQLCCPSTGLSCQCDREKQDKRLSR
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
47N-linked_GlycosylationGDPGCYGNKTIRTPN
CCCCCCCCCCCCCCC
16.3012657638
753-oxoalanine (Cys)HLAASPLCTPSRAAF
HHHCCCCCCCCHHHH
6.29-
75OxidationHLAASPLCTPSRAAF
HHHCCCCCCCCHHHH
6.2912657638
123UbiquitinationITFAKLLKDQGYSTA
HHHHHHHHHCCCCEE
59.44-
259N-linked_GlycosylationQQPMSYDNLTQRLTV
CCCCCCCCHHHHHHH
36.4312657638
368MalonylationNGIYKGGKANNWEGG
CCCCCCCCCCCCCCC
57.5226320211
393UbiquitinationRVIQAGQKIDEPTSN
HHCCCCCCCCCCCCC
51.73-
409UbiquitinationDIFPTVAKLAGAPLP
CCHHHHHHHCCCCCC
34.24-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of STS_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STS_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of STS_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RETR2_HUMANFAM134Aphysical
28514442
SUMF1_HUMANSUMF1physical
28514442
JAG2_HUMANJAG2physical
28514442
ALG9_HUMANALG9physical
28514442
ZDHC6_HUMANZDHHC6physical
28514442
ZNT1_HUMANSLC30A1physical
28514442
LRC8A_HUMANLRRC8Aphysical
28514442
CISD2_HUMANCISD2physical
28514442
CKAP4_HUMANCKAP4physical
28514442
AT11C_HUMANATP11Cphysical
28514442
CXA1_HUMANGJA1physical
28514442
TM214_HUMANTMEM214physical
28514442
ABCB8_HUMANABCB8physical
28514442
LMBR1_HUMANLMBR1physical
28514442
MBOA7_HUMANMBOAT7physical
28514442
GOGA5_HUMANGOLGA5physical
28514442
SIDT2_HUMANSIDT2physical
28514442
GEPH_HUMANGPHNphysical
28514442

Drug and Disease Associations
Kegg Disease
H00134 X-linked ichthyosis (XLI)
OMIM Disease
308100Ichthyosis, X-linked (IXL)
Kegg Drug
D09915 Irosustat (USAN/INN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STS_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structure of human estrone sulfatase suggests functional roles ofmembrane association.";
Hernandez-Guzman F.G., Higashiyama T., Pangborn W., Osawa Y.,Ghosh D.;
J. Biol. Chem. 278:22989-22997(2003).
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS,COFACTOR, TRANSMEMBRANE TOPOLOGY, ACTIVE SITE, AND GLYCOSYLATION ATASN-47 AND ASN-259.
"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).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION ATASN-47 AND ASN-259, AND LACK OF GLYCOSYLATION AT ASN-333 AND ASN-459.

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