SULT2B1
entrez
6820
canonical
uniprot
O00204
canonical
ensembl
ENSG00000088002
resolver
ensp
ENSP00000201586
resolver
ensp
ENSP00000312880
resolver
genesymbol
SULT2B1
resolver
genesymbol_syn
HSST2
resolver
hgnc
HGNC:11459
resolver
uniprot
O00205
resolver
uniprot
O75814
resolver
uniprot_entry
ST2B1_HUMAN
resolver
uniprot_sec
O00205
resolver
uniprot_sec
O75814
resolver
amino_acid_sequence
MDGPAEPQIPGLWDTYEDDISEISQKLPGEYFRYKGVPFPVGLYSLESISLAENTQDVRDDDIFIITYPKSGTTWMIEIICLILKEGDPSWIRSVPIWERAPWCETIVGAFSLPDQYSPRLMSSHLPIQIFTKAFFSSKAKVIYMGRNPRDVVVSLYHYSKIAGQLKDPGTPDQFLRDFLKGEVQFGSWFDHIKGWLRMKGKDNFLFITYEELQQDLQGSVERICGFLGRPLGKEALGSVVAHSTFSAMKANTMSNYTLLPPSLLDHRRGAFLRKGVCGDWKNHFTVAQSEAFDRAYRKQMRGMPTFPWDEDPEEDGSPDPEPSPEPEPKPSLEPNTSLEREPRPNSSPSPSPGQASETPHPRPS
uniprot
proteins
disease_involvement
DISEASE: Ichthyosis, congenital, autosomal recessive 14 (ARCI14) [MIM:617571]: A form of autosomal recessive congenital ichthyosis, a disorder of keratinization with abnormal differentiation and desquamation of the epidermis, resulting in abnormal skin scaling over the whole body. The main skin phenotypes are lamellar ichthyosis (LI) and non-bullous congenital ichthyosiform erythroderma (NCIE), although phenotypic overlap within the same patient or among patients from the same family can occur. Lamellar ichthyosis is a condition often associated with an embedment in a collodion-like membrane at birth; skin scales later develop, covering the entire body surface. Non-bullous congenital ichthyosiform erythroderma characterized by fine whitish scaling on an erythrodermal background; larger brownish scales are present on the buttocks, neck and legs. {ECO:0000269|PubMed:28575648}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.8.2.2
uniprot
proteins
function
FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation. Responsible for the sulfation of cholesterol (PubMed:12145317, PubMed:19589875). Catalyzes sulfation of the 3beta-hydroxyl groups of steroids, such as, pregnenolone and dehydroepiandrosterone (DHEA) (PubMed:12145317, PubMed:16855051, PubMed:21855633, PubMed:9799594). Preferentially sulfonates cholesterol, while it also has significant activity with pregnenolone and DHEA (PubMed:12145317, PubMed:21855633). Plays a role in epidermal cholesterol metabolism and in the regulation of epidermal proliferation and differentiation (PubMed:28575648). {ECO:0000269|PubMed:12145317, ECO:0000269|PubMed:16855051, ECO:0000269|PubMed:19589875, ECO:0000269|PubMed:21855633, ECO:0000269|PubMed:28575648, ECO:0000269|PubMed:9799594}.; FUNCTION: [Isoform 2]: Sulfonates pregnenolone but not cholesterol. {ECO:0000269|PubMed:12145317}.
uniprot
proteins
mass_dalton
41308
uniprot
proteins
mutagenesis
MUTAGEN 1..23; /note="Missing: Loss of the cholesterol sulfotransferase activity."; /evidence="ECO:0000269|PubMed:12145317"; MUTAGEN 1..18; /note="Missing: Increases the cholesterol sulfotransferase activity."; /evidence="ECO:0000269|PubMed:12145317"; MUTAGEN 19; /note="D->A: Increases the cholesterol sulfotransferase activity."; /evidence="ECO:0000269|PubMed:12145317"; MUTAGEN 20; /note="I->A: Loss of the cholesterol sulfotransferase activity."; /evidence="ECO:0000269|PubMed:12145317"; MUTAGEN 21; /note="S->A: Increases the cholesterol sulfotransferase activity."; /evidence="ECO:0000269|PubMed:12145317"; MUTAGEN 22; /note="E->A: Increases the cholesterol sulfotransferase activity."; /evidence="ECO:0000269|PubMed:12145317"; MUTAGEN 23; /note="I->A: Loss of the cholesterol sulfotransferase activity."; /evidence="ECO:0000269|PubMed:12145317"; MUTAGEN 347; /note="S->A: No change in subcellular localization."; /evidence="ECO:0000269|PubMed:21855633"; MUTAGEN 348; /note="S->D: 10-fold increase in specific activity for DHEA sulfation. 10-fold increase in substrate affinity for DHEA and pregnenolone. No effect on substrate affinity for PAPS. Increases enzyme stability."; /evidence="ECO:0000269|PubMed:21855633"; MUTAGEN 348; /note="S->G: Abolishes nuclear localization."; /evidence="ECO:0000269|PubMed:21855633"; MUTAGEN 352; /note="S->G: No change in subcellular localization."; /evidence="ECO:0000269|PubMed:21855633"; MUTAGEN 357; /note="S->G: No change in subcellular localization."; /evidence="ECO:0000269|PubMed:21855633
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. {ECO:0000269|PubMed:16855051}.
uniprot
proteins
protein_family
Sulfotransferase 1 family
uniprot
proteins
pubmed
12145317
uniprot
proteins
pubmed
12923182
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16855051
uniprot
proteins
pubmed
19589875
uniprot
proteins
pubmed
21855633
uniprot
proteins
pubmed
28575648
uniprot
proteins
pubmed
9799594
uniprot
proteins
sequence_length
365
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12923182, ECO:0000269|PubMed:16855051, ECO:0000269|PubMed:21855633, ECO:0000269|PubMed:28575648}. Microsome {ECO:0000269|PubMed:16855051, ECO:0000269|PubMed:21855633}. Nucleus {ECO:0000269|PubMed:16855051, ECO:0000269|PubMed:21855633}. Note=Phosphorylation of Ser-348 is required for translocation to the nucleus. {ECO:0000269|PubMed:21855633}.
uniprot
proteins