UniProt ID | ST2B1_HUMAN | |
---|---|---|
UniProt AC | O00204 | |
Protein Name | Sulfotransferase family cytosolic 2B member 1 | |
Gene Name | SULT2B1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 365 | |
Subcellular Localization | Cytoplasm. Microsome. Nucleus. Cytoplasm, cytosol . Phosphorylation of Ser-348 is required for translocation to the nucleus. | |
Protein Description | Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of many hormones, neurotransmitters, drugs and xenobiotic compounds. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Sulfates hydroxysteroids like DHEA. Isoform 1 preferentially sulfonates cholesterol, and isoform 2 avidly sulfonates pregnenolone but not cholesterol. Plays a role in epidermal cholesterol metabolism and in the regulation of epidermal proliferation and differentiation. [PubMed: 28575648] | |
Protein Sequence | MDGPAEPQIPGLWDTYEDDISEISQKLPGEYFRYKGVPFPVGLYSLESISLAENTQDVRDDDIFIITYPKSGTTWMIEIICLILKEGDPSWIRSVPIWERAPWCETIVGAFSLPDQYSPRLMSSHLPIQIFTKAFFSSKAKVIYMGRNPRDVVVSLYHYSKIAGQLKDPGTPDQFLRDFLKGEVQFGSWFDHIKGWLRMKGKDNFLFITYEELQQDLQGSVERICGFLGRPLGKEALGSVVAHSTFSAMKANTMSNYTLLPPSLLDHRRGAFLRKGVCGDWKNHFTVAQSEAFDRAYRKQMRGMPTFPWDEDPEEDGSPDPEPSPEPEPKPSLEPNTSLEREPRPNSSPSPSPGQASETPHPRPS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
3 (in isoform 2) | Phosphorylation | - | 23.24 | 29507054 | |
9 (in isoform 2) | Phosphorylation | - | 4.23 | 29507054 | |
15 | Phosphorylation | QIPGLWDTYEDDISE CCCCCHHCCCCCHHH | 19.75 | 22210691 | |
16 | Phosphorylation | IPGLWDTYEDDISEI CCCCHHCCCCCHHHH | 18.19 | 22210691 | |
31 | Phosphorylation | SQKLPGEYFRYKGVP HHHCCCCCCEECCCC | 10.16 | 22210691 | |
44 | Phosphorylation | VPFPVGLYSLESISL CCCCCEEEEHHCCCC | 12.79 | 27174698 | |
45 | Phosphorylation | PFPVGLYSLESISLA CCCCEEEEHHCCCCC | 30.61 | 27174698 | |
48 | Phosphorylation | VGLYSLESISLAENT CEEEEHHCCCCCCCC | 23.83 | 27174698 | |
50 | Phosphorylation | LYSLESISLAENTQD EEEHHCCCCCCCCCC | 30.70 | 27174698 | |
55 | Phosphorylation | SISLAENTQDVRDDD CCCCCCCCCCCCCCC | 20.04 | 27174698 | |
123 | Phosphorylation | QYSPRLMSSHLPIQI CCCHHHHHCCCCHHH | 21.14 | 20068231 | |
124 | Phosphorylation | YSPRLMSSHLPIQIF CCHHHHHCCCCHHHH | 18.31 | 20068231 | |
132 | Phosphorylation | HLPIQIFTKAFFSSK CCCHHHHHHHHHCCC | 24.08 | 20068231 | |
137 | Phosphorylation | IFTKAFFSSKAKVIY HHHHHHHCCCCEEEE | 25.19 | 25106551 | |
138 | Phosphorylation | FTKAFFSSKAKVIYM HHHHHHCCCCEEEEC | 31.32 | 28060719 | |
155 | Phosphorylation | NPRDVVVSLYHYSKI CHHHHEEEEECHHHH | 16.17 | 24719451 | |
157 | Phosphorylation | RDVVVSLYHYSKIAG HHHEEEEECHHHHHC | 7.39 | 24719451 | |
159 | Phosphorylation | VVVSLYHYSKIAGQL HEEEEECHHHHHCCC | 9.71 | 24719451 | |
253 | Phosphorylation | FSAMKANTMSNYTLL HHHHHCCCCCCCEEC | 27.17 | - | |
318 | Phosphorylation | EDPEEDGSPDPEPSP CCCCCCCCCCCCCCC | 38.15 | 26657352 | |
324 | Phosphorylation | GSPDPEPSPEPEPKP CCCCCCCCCCCCCCC | 39.99 | 25849741 | |
347 | Phosphorylation | EREPRPNSSPSPSPG CCCCCCCCCCCCCCC | 46.43 | 30278072 | |
348 | Phosphorylation | REPRPNSSPSPSPGQ CCCCCCCCCCCCCCC | 35.72 | 30278072 | |
350 | Phosphorylation | PRPNSSPSPSPGQAS CCCCCCCCCCCCCCC | 39.70 | 30278072 | |
352 | Phosphorylation | PNSSPSPSPGQASET CCCCCCCCCCCCCCC | 46.10 | 25849741 | |
357 | Phosphorylation | SPSPGQASETPHPRP CCCCCCCCCCCCCCC | 33.83 | 26330541 | |
359 | Phosphorylation | SPGQASETPHPRPS- CCCCCCCCCCCCCC- | 25.13 | 26330541 | |
365 | Phosphorylation | ETPHPRPS------- CCCCCCCC------- | 54.88 | 26330541 |
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 ST2B1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ST2B1_HUMAN !! |
* 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 ST2B1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
AL2SB_HUMAN | ALS2CR12 | physical | 16189514 | |
ST2B1_HUMAN | SULT2B1 | physical | 25416956 | |
ST1B1_HUMAN | SULT1B1 | physical | 25416956 | |
AL2SB_HUMAN | ALS2CR12 | physical | 25416956 |
Kegg Disease | ||||||
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There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Site-directed mutagenesis of human cytosolic sulfotransferase (SULT)2B1b to phospho-mimetic Ser348Asp results in an isoform with increasedcatalytic activity."; Salman E.D., He D., Runge-Morris M., Kocarek T.A., Falany C.N.; J. Steroid Biochem. Mol. Biol. 127:315-323(2011). Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, PHOSPHORYLATIONAT SER-348, AND MUTAGENESIS OF SER-347; SER-348; SER-352 AND SER-357. |