ST2B1_HUMAN
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 03-AUG-2022, entry version 186.
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}.
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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; 75.
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; O00204; -.
DR PeptideAtlas; O00204; -.
DR PRIDE; O00204; -.
DR ProteomicsDB; 47777; -. [O00204-1]
DR ProteomicsDB; 47778; -. [O00204-2]
DR Antibodypedia; 31732; 263 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 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; 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; DPYEKNI; -.
DR OrthoDB; 780670at2759; -.
DR PhylomeDB; O00204; -.
DR TreeFam; TF321745; -.
DR BioCyc; MetaCyc:HS01587-MON; -.
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 1073 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 145 other tissues.
DR Genevisible; O00204; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
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:0004027; F:alcohol sulfotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0015485; F:cholesterol binding; IDA:CAFA.
DR GO; GO:0003676; F:nucleic acid binding; IMP:CAFA.
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; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
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; unknown pathological
FT significance; 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; unknown pathological
FT significance; 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
