ID ST2B1_HUMAN Reviewed; 365 AA. AC O00204; O00205; O75814; DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot. DT 04-JAN-2005, sequence version 2. DT 24-JAN-2024, entry version 194. DE RecName: Full=Sulfotransferase 2B1; DE EC=2.8.2.2 {ECO:0000269|PubMed:12145317, ECO:0000269|PubMed:12923182, ECO:0000269|PubMed:16855051, ECO:0000269|PubMed:19589875, ECO:0000269|PubMed:21855633, ECO:0000269|PubMed:9799594}; DE AltName: Full=Alcohol sulfotransferase; DE AltName: Full=Hydroxysteroid sulfotransferase 2; DE AltName: Full=Sulfotransferase family 2B member 1; DE AltName: Full=Sulfotransferase family cytosolic 2B member 1; DE Short=ST2B1; GN Name=SULT2B1; Synonyms=HSST2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 RP AND 2), FUNCTION, TISSUE SPECIFICITY, AND CATALYTIC ACTIVITY. RC TISSUE=Placenta; RX PubMed=9799594; DOI=10.1006/geno.1998.5518; RA Her C., Wood T.C., Eichler E.E., Mohrenweiser H.W., Ramagli L.S., RA Siciliano M.J., Weinshilboum R.M.; RT "Human hydroxysteroid sulfotransferase SULT2B1: two enzymes encoded by a RT single chromosome 19 gene."; RL Genomics 53:284-295(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP FUNCTION (ISOFORMS 1 AND 2), MUTAGENESIS OF 1-MET--ASP-18; 1-MET--ILE-23; RP ASP-19; ILE-20; SER-21; GLU-22 AND ILE-23, CATALYTIC ACTIVITY, AND RP FUNCTION. RX PubMed=12145317; DOI=10.1074/jbc.m207165200; RA Fuda H., Lee Y.C., Shimizu C., Javitt N.B., Strott C.A.; RT "Mutational analysis of human hydroxysteroid sulfotransferase SULT2B1 RT isoforms reveals that exon 1B of the SULT2B1 gene produces cholesterol RT sulfotransferase, whereas exon 1A yields pregnenolone sulfotransferase."; RL J. Biol. Chem. 277:36161-36166(2002). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES, RP SUBCELLULAR LOCATION, PHOSPHORYLATION, CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=16855051; DOI=10.1124/dmd.106.011114; RA He D., Falany C.N.; RT "Characterization of proline-serine-rich carboxyl terminus in human RT sulfotransferase 2B1b: immunogenicity, subcellular localization, kinetic RT properties, and phosphorylation."; RL Drug Metab. Dispos. 34:1749-1755(2006). RN [6] RP CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=19589875; DOI=10.1124/dmd.108.025759; RA Cook I.T., Duniec-Dmuchowski Z., Kocarek T.A., Runge-Morris M., RA Falany C.N.; RT "24-hydroxycholesterol sulfation by human cytosolic sulfotransferases: RT formation of monosulfates and disulfates, molecular modeling, sulfatase RT sensitivity, and inhibition of liver x receptor activation."; RL Drug Metab. Dispos. 37:2069-2078(2009). RN [7] RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, PHOSPHORYLATION AT RP SER-348, MUTAGENESIS OF SER-347; SER-348; SER-352 AND SER-357, CATALYTIC RP ACTIVITY, AND FUNCTION. RX PubMed=21855633; DOI=10.1016/j.jsbmb.2011.07.010; RA Salman E.D., He D., Runge-Morris M., Kocarek T.A., Falany C.N.; RT "Site-directed mutagenesis of human cytosolic sulfotransferase (SULT) 2B1b RT to phospho-mimetic Ser348Asp results in an isoform with increased catalytic RT activity."; RL J. Steroid Biochem. Mol. Biol. 127:315-323(2011). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 19-312 IN COMPLEX WITH RP ADENOSINE-3'-5'-DIPHOSPHATE (PAP) AND PREGNENOLONE, CATALYTIC ACTIVITY, AND RP FUNCTION. RX PubMed=12923182; DOI=10.1074/jbc.m308312200; RA Lee K.A., Fuda H., Lee Y.C., Negishi M., Strott C.A., Pedersen L.C.; RT "Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the RT presence of pregnenolone and 3'-phosphoadenosine 5'-phosphate. Rationale RT for specificity differences between prototypical SULT2A1 and the SULT2BG1 RT isoforms."; RL J. Biol. Chem. 278:44593-44599(2003). RN [9] RP VARIANTS ARCI14 LEU-149 AND GLN-274, FUNCTION, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RX PubMed=28575648; DOI=10.1016/j.ajhg.2017.05.007; RA Heinz L., Kim G.J., Marrakchi S., Christiansen J., Turki H., RA Rauschendorf M.A., Lathrop M., Hausser I., Zimmer A.D., Fischer J.; RT "Mutations in SULT2B1 cause autosomal-recessive congenital ichthyosis in RT humans."; RL Am. J. Hum. Genet. 100:926-939(2017). CC -!- FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate CC (PAPS) as sulfonate donor to catalyze the sulfate conjugation. CC Responsible for the sulfation of cholesterol (PubMed:19589875, CC PubMed:12145317). Catalyzes sulfation of the 3beta-hydroxyl groups of CC steroids, such as, pregnenolone and dehydroepiandrosterone (DHEA) CC (PubMed:9799594, PubMed:12145317, PubMed:21855633, PubMed:16855051). CC Preferentially sulfonates cholesterol, while it has also significant CC activity with pregnenolone and DHEA (PubMed:12145317, PubMed:21855633). CC Plays a role in epidermal cholesterol metabolism and in the regulation CC of epidermal proliferation and differentiation (PubMed:28575648). CC {ECO:0000269|PubMed:12145317, ECO:0000269|PubMed:16855051, CC ECO:0000269|PubMed:19589875, ECO:0000269|PubMed:21855633, CC ECO:0000269|PubMed:28575648, ECO:0000269|PubMed:9799594}. CC -!- FUNCTION: [Isoform 2]: Sulfonates pregnenolone but not cholesterol. CC {ECO:0000269|PubMed:12145317}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'- CC bisphosphate + an alkyl sulfate + H(+); Xref=Rhea:RHEA:22552, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:58339, CC ChEBI:CHEBI:58343, ChEBI:CHEBI:83414; EC=2.8.2.2; CC Evidence={ECO:0000269|PubMed:12145317, ECO:0000269|PubMed:16855051, CC ECO:0000269|PubMed:19589875, ECO:0000269|PubMed:21855633, CC ECO:0000269|PubMed:9799594}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3'-phosphoadenylyl sulfate + 3beta-hydroxyandrost-5-en-17-one CC = adenosine 3',5'-bisphosphate + dehydroepiandrosterone 3-sulfate + CC H(+); Xref=Rhea:RHEA:51216, ChEBI:CHEBI:15378, ChEBI:CHEBI:28689, CC ChEBI:CHEBI:57905, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343; CC Evidence={ECO:0000269|PubMed:12145317, ECO:0000269|PubMed:16855051, CC ECO:0000269|PubMed:21855633, ECO:0000269|PubMed:9799594}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51217; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(24S)-hydroxycholesterol + 3'-phosphoadenylyl sulfate = (24S)- CC hydroxycholesterol 3-sulfate + adenosine 3',5'-bisphosphate + H(+); CC Xref=Rhea:RHEA:52348, ChEBI:CHEBI:15378, ChEBI:CHEBI:34310, CC ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:136567; CC Evidence={ECO:0000269|PubMed:19589875}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52349; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3'-phosphoadenylyl sulfate + cholesterol = adenosine 3',5'- CC bisphosphate + cholesterol sulfate + H(+); Xref=Rhea:RHEA:52368, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:58339, CC ChEBI:CHEBI:58343, ChEBI:CHEBI:136579; CC Evidence={ECO:0000269|PubMed:12145317, ECO:0000269|PubMed:12923182}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52369; CC Evidence={ECO:0000305}; CC -!- CATALYTIC ACTIVITY: CC Reaction=3'-phosphoadenylyl sulfate + pregnenolone = adenosine 3',5'- CC bisphosphate + H(+) + pregnenolone sulfate; Xref=Rhea:RHEA:52356, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16581, ChEBI:CHEBI:58339, CC ChEBI:CHEBI:58343, ChEBI:CHEBI:133000; CC Evidence={ECO:0000269|PubMed:12145317, ECO:0000269|PubMed:12923182, CC ECO:0000269|PubMed:21855633}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52357; CC Evidence={ECO:0000305}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=23.5 uM for (24S)-hydroxycholesterol CC {ECO:0000269|PubMed:19589875}; CC KM=10.9 uM for DHEA (at 37 degrees Celsius, in the presence of 1 mM CC MgCl2) {ECO:0000269|PubMed:21855633}; CC KM=3.8 uM for DHEA (at 37 degrees Celsius, in the presence of 10 mM CC MgCl2) {ECO:0000269|PubMed:16855051}; CC KM=11.8 uM for pregnenolone (at 37 degrees Celsius, in the presence CC of 1 mM MgCl2) {ECO:0000269|PubMed:21855633}; CC KM=0.6 uM for PAPS (at 37 degrees Celsius, in the presence of 1 mM CC MgCl2) {ECO:0000269|PubMed:21855633}; CC Vmax=1752 pmol/min/mg enzyme toward DHEA (at 37 degrees Celsius, in CC the presence of 10 mM MgCl2) {ECO:0000269|PubMed:16855051}; CC Temperature dependence: CC Optimum temperature is 37 degrees Celsius. Retains 70% and 20% of CC activity when incubated at 42 degrees Celsius for 45 and 120 minutes, CC respectively. Activity is lost after 200 minutes incubation at 42 CC degrees Celsius. {ECO:0000269|PubMed:16855051, CC ECO:0000269|PubMed:21855633}; CC -!- INTERACTION: CC O00204; P14621: ACYP2; NbExp=3; IntAct=EBI-749441, EBI-10198377; CC O00204; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-749441, EBI-742054; CC O00204; Q96Q35: FLACC1; NbExp=8; IntAct=EBI-749441, EBI-750451; CC O00204; Q96Q35-2: FLACC1; NbExp=8; IntAct=EBI-749441, EBI-11533409; CC O00204; Q9P2G9-2: KLHL8; NbExp=3; IntAct=EBI-749441, EBI-11959635; CC O00204; O43900: PRICKLE3; NbExp=3; IntAct=EBI-749441, EBI-1751761; CC O00204; Q04864-2: REL; NbExp=3; IntAct=EBI-749441, EBI-10829018; CC O00204; O76094: SRP72; NbExp=3; IntAct=EBI-749441, EBI-1058850; CC O00204; P50225: SULT1A1; NbExp=7; IntAct=EBI-749441, EBI-2814403; CC O00204; O43704: SULT1B1; NbExp=9; IntAct=EBI-749441, EBI-10179062; CC O00204; Q6IMI6: SULT1C3; NbExp=3; IntAct=EBI-749441, EBI-12837366; CC O00204; Q6ZNH5: ZNF497; NbExp=3; IntAct=EBI-749441, EBI-10486136; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12923182, CC ECO:0000269|PubMed:16855051, ECO:0000269|PubMed:21855633, CC ECO:0000269|PubMed:28575648}. Microsome {ECO:0000269|PubMed:16855051, CC ECO:0000269|PubMed:21855633}. Nucleus {ECO:0000269|PubMed:16855051, CC ECO:0000269|PubMed:21855633}. Note=Phosphorylation of Ser-348 is CC required for translocation to the nucleus. CC {ECO:0000269|PubMed:21855633}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=SULT2B1b, B; CC IsoId=O00204-1; Sequence=Displayed; CC Name=2; Synonyms=SULT2B1a, A; CC IsoId=O00204-2; Sequence=VSP_012510; CC -!- TISSUE SPECIFICITY: Expressed in the stratum granulosum-stratum corneum CC junction in the skin (at protein level) (PubMed:28575648). Expressed CC highly in placenta, prostate and trachea and lower expression in the CC small intestine and lung (PubMed:9799594). CC {ECO:0000269|PubMed:28575648, ECO:0000269|PubMed:9799594}. CC -!- DOMAIN: The C-terminus, which contains a proline/serine-rich region is CC involved in nuclear translocation and enzymatic thermostability. CC {ECO:0000269|PubMed:16855051}. CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:16855051}. CC -!- DISEASE: Ichthyosis, congenital, autosomal recessive 14 (ARCI14) CC [MIM:617571]: A form of autosomal recessive congenital ichthyosis, a CC disorder of keratinization with abnormal differentiation and CC desquamation of the epidermis, resulting in abnormal skin scaling over CC the whole body. The main skin phenotypes are lamellar ichthyosis (LI) CC and non-bullous congenital ichthyosiform erythroderma (NCIE), although CC phenotypic overlap within the same patient or among patients from the CC same family can occur. Lamellar ichthyosis is a condition often CC associated with an embedment in a collodion-like membrane at birth; CC skin scales later develop, covering the entire body surface. Non- CC bullous congenital ichthyosiform erythroderma characterized by fine CC whitish scaling on an erythrodermal background; larger brownish scales CC are present on the buttocks, neck and legs. CC {ECO:0000269|PubMed:28575648}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U92314; AAC78498.1; -; mRNA. DR EMBL; U92315; AAC78499.1; -; mRNA. DR EMBL; U92322; AAC78553.1; -; Genomic_DNA. DR EMBL; U92316; AAC78553.1; JOINED; Genomic_DNA. DR EMBL; U92318; AAC78553.1; JOINED; Genomic_DNA. DR EMBL; U92319; AAC78553.1; JOINED; Genomic_DNA. DR EMBL; U92320; AAC78553.1; JOINED; Genomic_DNA. DR EMBL; U92321; AAC78553.1; JOINED; Genomic_DNA. DR EMBL; U92322; AAC78554.1; -; Genomic_DNA. DR EMBL; U92316; AAC78554.1; JOINED; Genomic_DNA. DR EMBL; U92317; AAC78554.1; JOINED; Genomic_DNA. DR EMBL; U92318; AAC78554.1; JOINED; Genomic_DNA. DR EMBL; U92319; AAC78554.1; JOINED; Genomic_DNA. DR EMBL; U92320; AAC78554.1; JOINED; Genomic_DNA. DR EMBL; U92321; AAC78554.1; JOINED; Genomic_DNA. DR EMBL; AC008403; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC034694; AAH34694.1; -; mRNA. DR CCDS; CCDS12723.1; -. [O00204-1] DR CCDS; CCDS12724.1; -. [O00204-2] DR RefSeq; NP_004596.2; NM_004605.2. [O00204-2] DR RefSeq; NP_814444.1; NM_177973.1. [O00204-1] DR PDB; 1Q1Q; X-ray; 2.91 A; A=24-365. DR PDB; 1Q1Z; X-ray; 2.40 A; A=19-312. DR PDB; 1Q20; X-ray; 2.30 A; A=19-312. DR PDB; 1Q22; X-ray; 2.50 A; A=19-312. DR PDBsum; 1Q1Q; -. DR PDBsum; 1Q1Z; -. DR PDBsum; 1Q20; -. DR PDBsum; 1Q22; -. DR AlphaFoldDB; O00204; -. DR SMR; O00204; -. DR BioGRID; 112689; 83. DR IntAct; O00204; 17. DR STRING; 9606.ENSP00000201586; -. DR ChEMBL; CHEMBL1743297; -. DR DrugBank; DB01812; Adenosine 3',5'-diphosphate. DR DrugBank; DB03309; N-cyclohexyltaurine. DR DrugBank; DB01708; Prasterone. DR DrugBank; DB02789; Pregnenolone. DR SwissLipids; SLP:000001653; -. [O00204-1] DR SwissLipids; SLP:000001654; -. [O00204-2] DR MoonDB; O00204; Predicted. DR iPTMnet; O00204; -. DR PhosphoSitePlus; O00204; -. DR BioMuta; SULT2B1; -. DR EPD; O00204; -. DR jPOST; O00204; -. DR MassIVE; O00204; -. DR MaxQB; O00204; -. DR PaxDb; 9606-ENSP00000201586; -. DR PeptideAtlas; O00204; -. DR PRIDE; O00204; -. DR ProteomicsDB; 47777; -. [O00204-1] DR ProteomicsDB; 47778; -. [O00204-2] DR Antibodypedia; 31732; 303 antibodies from 28 providers. DR DNASU; 6820; -. DR Ensembl; ENST00000201586.7; ENSP00000201586.2; ENSG00000088002.12. [O00204-1] DR Ensembl; ENST00000323090.4; ENSP00000312880.3; ENSG00000088002.12. [O00204-2] DR GeneID; 6820; -. DR KEGG; hsa:6820; -. DR MANE-Select; ENST00000201586.7; ENSP00000201586.2; NM_177973.2; NP_814444.1. DR UCSC; uc002pjl.4; human. [O00204-1] DR AGR; HGNC:11459; -. DR CTD; 6820; -. DR DisGeNET; 6820; -. DR GeneCards; SULT2B1; -. DR HGNC; HGNC:11459; SULT2B1. DR HPA; ENSG00000088002; Tissue enhanced (esophagus, skin, vagina). DR MalaCards; SULT2B1; -. DR MIM; 604125; gene. DR MIM; 617571; phenotype. DR neXtProt; NX_O00204; -. DR OpenTargets; ENSG00000088002; -. DR Orphanet; 79394; Congenital ichthyosiform erythroderma. DR Orphanet; 313; Lamellar ichthyosis. DR PharmGKB; PA36249; -. DR VEuPathDB; HostDB:ENSG00000088002; -. DR eggNOG; KOG1584; Eukaryota. DR GeneTree; ENSGT00940000159269; -. DR HOGENOM; CLU_027239_1_0_1; -. DR InParanoid; O00204; -. DR OMA; LAYWKAY; -. DR OrthoDB; 3083090at2759; -. DR PhylomeDB; O00204; -. DR TreeFam; TF321745; -. DR BioCyc; MetaCyc:HS01587-MONOMER; -. DR PathwayCommons; O00204; -. DR Reactome; R-HSA-156584; Cytosolic sulfonation of small molecules. DR SABIO-RK; O00204; -. DR SignaLink; O00204; -. DR BioGRID-ORCS; 6820; 15 hits in 1151 CRISPR screens. DR ChiTaRS; SULT2B1; human. DR EvolutionaryTrace; O00204; -. DR GeneWiki; SULT2B1; -. DR GenomeRNAi; 6820; -. DR Pharos; O00204; Tbio. DR PRO; PR:O00204; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; O00204; Protein. DR Bgee; ENSG00000088002; Expressed in lower esophagus mucosa and 147 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0015485; F:cholesterol binding; IDA:CAFA. DR GO; GO:0051922; F:cholesterol sulfotransferase activity; IEA:RHEA. DR GO; GO:0003676; F:nucleic acid binding; IMP:CAFA. DR GO; GO:0036094; F:small molecule binding; EXP:DisProt. DR GO; GO:1990239; F:steroid hormone binding; IMP:CAFA. DR GO; GO:0050294; F:steroid sulfotransferase activity; IDA:UniProtKB. DR GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central. DR GO; GO:0050427; P:3'-phosphoadenosine 5'-phosphosulfate metabolic process; IDA:CAFA. DR GO; GO:0008203; P:cholesterol metabolic process; IMP:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB. DR GO; GO:0045606; P:positive regulation of epidermal cell differentiation; IMP:UniProtKB. DR GO; GO:0008202; P:steroid metabolic process; IDA:UniProtKB. DR GO; GO:0051923; P:sulfation; IBA:GO_Central. DR DisProt; DP00404; -. DR DisProt; DP01099; -. [O00204-2] DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000863; Sulfotransferase_dom. DR PANTHER; PTHR11783:SF9; SULFOTRANSFERASE 2B1; 1. DR PANTHER; PTHR11783; SULFOTRANSFERASE SULT; 1. DR Pfam; PF00685; Sulfotransfer_1; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR Genevisible; O00204; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Disease variant; KW Endoplasmic reticulum; Ichthyosis; Lipid metabolism; Microsome; Nucleus; KW Phosphoprotein; Reference proteome; Steroid metabolism; Transferase. FT CHAIN 1..365 FT /note="Sulfotransferase 2B1" FT /id="PRO_0000085149" FT REGION 303..365 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 346..365 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 125 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P49891" FT BINDING 70..75 FT /ligand="3'-phosphoadenylyl sulfate" FT /ligand_id="ChEBI:CHEBI:58339" FT /evidence="ECO:0000250|UniProtKB:P49891" FT BINDING 98 FT /ligand="substrate" FT BINDING 103 FT /ligand="substrate" FT BINDING 125 FT /ligand="substrate" FT BINDING 147 FT /ligand="3'-phosphoadenylyl sulfate" FT /ligand_id="ChEBI:CHEBI:58339" FT /evidence="ECO:0000250|UniProtKB:P49891" FT BINDING 155 FT /ligand="3'-phosphoadenylyl sulfate" FT /ligand_id="ChEBI:CHEBI:58339" FT /evidence="ECO:0000250|UniProtKB:P49891" FT BINDING 210 FT /ligand="3'-phosphoadenylyl sulfate" FT /ligand_id="ChEBI:CHEBI:58339" FT /evidence="ECO:0000250|UniProtKB:P49891" FT BINDING 244..249 FT /ligand="3'-phosphoadenylyl sulfate" FT /ligand_id="ChEBI:CHEBI:58339" FT /evidence="ECO:0000250|UniProtKB:P49891" FT BINDING 274..276 FT /ligand="3'-phosphoadenylyl sulfate" FT /ligand_id="ChEBI:CHEBI:58339" FT /evidence="ECO:0000250|UniProtKB:P49891" FT MOD_RES 348 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:21855633" FT VAR_SEQ 1..23 FT /note="MDGPAEPQIPGLWDTYEDDISEI -> MASPPPFH (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9799594" FT /id="VSP_012510" FT VARIANT 51 FT /note="L -> S (in dbSNP:rs16982149)" FT /id="VAR_020887" FT VARIANT 149 FT /note="P -> L (in ARCI14; uncertain significance; FT dbSNP:rs1114167424)" FT /evidence="ECO:0000269|PubMed:28575648" FT /id="VAR_079210" FT VARIANT 240 FT /note="V -> I (in dbSNP:rs2302947)" FT /id="VAR_021988" FT VARIANT 274 FT /note="R -> Q (in ARCI14; uncertain significance; FT dbSNP:rs762765702)" FT /evidence="ECO:0000269|PubMed:28575648" FT /id="VAR_079211" FT VARIANT 345 FT /note="P -> L (in dbSNP:rs17842463)" FT /id="VAR_020888" FT MUTAGEN 1..23 FT /note="Missing: Loss of the cholesterol sulfotransferase FT activity." FT /evidence="ECO:0000269|PubMed:12145317" FT MUTAGEN 1..18 FT /note="Missing: Increases the cholesterol sulfotransferase FT activity." FT /evidence="ECO:0000269|PubMed:12145317" FT MUTAGEN 19 FT /note="D->A: Increases the cholesterol sulfotransferase FT activity." FT /evidence="ECO:0000269|PubMed:12145317" FT MUTAGEN 20 FT /note="I->A: Loss of the cholesterol sulfotransferase FT activity." FT /evidence="ECO:0000269|PubMed:12145317" FT MUTAGEN 21 FT /note="S->A: Increases the cholesterol sulfotransferase FT activity." FT /evidence="ECO:0000269|PubMed:12145317" FT MUTAGEN 22 FT /note="E->A: Increases the cholesterol sulfotransferase FT activity." FT /evidence="ECO:0000269|PubMed:12145317" FT MUTAGEN 23 FT /note="I->A: Loss of the cholesterol sulfotransferase FT activity." FT /evidence="ECO:0000269|PubMed:12145317" FT MUTAGEN 347 FT /note="S->A: No change in subcellular localization." FT /evidence="ECO:0000269|PubMed:21855633" FT MUTAGEN 348 FT /note="S->D: 10-fold increase in specific activity for DHEA FT sulfation. 10-fold increase in substrate affinity for DHEA FT and pregnenolone. No effect on substrate affinity for PAPS. FT Increases enzyme stability." FT /evidence="ECO:0000269|PubMed:21855633" FT MUTAGEN 348 FT /note="S->G: Abolishes nuclear localization." FT /evidence="ECO:0000269|PubMed:21855633" FT MUTAGEN 352 FT /note="S->G: No change in subcellular localization." FT /evidence="ECO:0000269|PubMed:21855633" FT MUTAGEN 357 FT /note="S->G: No change in subcellular localization." FT /evidence="ECO:0000269|PubMed:21855633" FT CONFLICT 350 FT /note="S -> N (in Ref. 1; AAC78498)" FT /evidence="ECO:0000305" FT HELIX 19..25 FT /evidence="ECO:0007829|PDB:1Q20" FT STRAND 31..34 FT /evidence="ECO:0007829|PDB:1Q20" FT STRAND 37..41 FT /evidence="ECO:0007829|PDB:1Q20" FT HELIX 46..54 FT /evidence="ECO:0007829|PDB:1Q20" FT STRAND 63..68 FT /evidence="ECO:0007829|PDB:1Q20" FT HELIX 73..84 FT /evidence="ECO:0007829|PDB:1Q20" FT TURN 85..87 FT /evidence="ECO:0007829|PDB:1Q20" FT HELIX 90..94 FT /evidence="ECO:0007829|PDB:1Q20" FT HELIX 97..100 FT /evidence="ECO:0007829|PDB:1Q20" FT STRAND 103..106 FT /evidence="ECO:0007829|PDB:1Q20" FT HELIX 110..112 FT /evidence="ECO:0007829|PDB:1Q20" FT STRAND 121..124 FT /evidence="ECO:0007829|PDB:1Q20" FT TURN 128..130 FT /evidence="ECO:0007829|PDB:1Q20" FT HELIX 133..135 FT /evidence="ECO:0007829|PDB:1Q20" FT STRAND 141..146 FT /evidence="ECO:0007829|PDB:1Q20" FT HELIX 149..162 FT /evidence="ECO:0007829|PDB:1Q20" FT STRAND 163..166 FT /evidence="ECO:0007829|PDB:1Q1Z" FT HELIX 172..180 FT /evidence="ECO:0007829|PDB:1Q20" FT HELIX 189..196 FT /evidence="ECO:0007829|PDB:1Q20" FT HELIX 197..199 FT /evidence="ECO:0007829|PDB:1Q20" FT STRAND 205..209 FT /evidence="ECO:0007829|PDB:1Q20" FT HELIX 210..215 FT /evidence="ECO:0007829|PDB:1Q20" FT HELIX 217..228 FT /evidence="ECO:0007829|PDB:1Q20" FT HELIX 234..244 FT /evidence="ECO:0007829|PDB:1Q20" FT HELIX 246..250 FT /evidence="ECO:0007829|PDB:1Q20" FT TURN 253..255 FT /evidence="ECO:0007829|PDB:1Q20" FT TURN 256..259 FT /evidence="ECO:0007829|PDB:1Q1Z" FT TURN 262..264 FT /evidence="ECO:0007829|PDB:1Q20" FT TURN 267..269 FT /evidence="ECO:0007829|PDB:1Q20" FT HELIX 280..283 FT /evidence="ECO:0007829|PDB:1Q20" FT HELIX 287..300 FT /evidence="ECO:0007829|PDB:1Q20" FT TURN 301..303 FT /evidence="ECO:0007829|PDB:1Q20" SQ SEQUENCE 365 AA; 41308 MW; 13E95248DD40DF91 CRC64; MDGPAEPQIP GLWDTYEDDI SEISQKLPGE YFRYKGVPFP VGLYSLESIS LAENTQDVRD DDIFIITYPK SGTTWMIEII CLILKEGDPS WIRSVPIWER APWCETIVGA FSLPDQYSPR LMSSHLPIQI FTKAFFSSKA KVIYMGRNPR DVVVSLYHYS KIAGQLKDPG TPDQFLRDFL KGEVQFGSWF DHIKGWLRMK GKDNFLFITY EELQQDLQGS VERICGFLGR PLGKEALGSV VAHSTFSAMK ANTMSNYTLL PPSLLDHRRG AFLRKGVCGD WKNHFTVAQS EAFDRAYRKQ MRGMPTFPWD EDPEEDGSPD PEPSPEPEPK PSLEPNTSLE REPRPNSSPS PSPGQASETP HPRPS //