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UniProtKB - Q06520 (ST2A1_HUMAN)

Entry version 200 (02 Jun 2021)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
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Protein

Sulfotransferase 2A1

Gene

SULT2A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of steroids and bile acids in the liver and adrenal glands. Mediates the sulfation of a wide range of steroids and sterols, including pregnenolone, androsterone, DHEA, bile acids, cholesterol and as well many xenobiotics that contain alcohol and phenol functional groups (PubMed:7678732, PubMed:2268288, PubMed:14573603, PubMed:18042734, PubMed:19589875, PubMed:21187059, PubMed:29671343, PubMed:7854148).

Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites. Plays an important role in maintening steroid and lipid homeostasis (PubMed:21187059, PubMed:19589875, PubMed:14573603).

Plays a key role in bile acid metabolism (PubMed:2268288).

In addition, catalyzes the metabolic activation of potent carcinogenic polycyclic arylmethanols (By similarity).

By similarity8 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Subject to substrate inhibition. Alternate orientations for binding of steroid substrates to SULT2A1 may play a role in substrate inhibition.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.8 µM for DHEA1 Publication
  2. KM=3.1 µM for DHEA1 Publication
  3. KM=1.6 µM for DHEA1 Publication
  4. KM=0.1 µM for (24S)-hydroxycholesterol 24-sulfate1 Publication
  5. KM=3.7 µM for (24S)-hydroxycholesterol1 Publication
  6. KM=1.5 µM for lithocholic acid1 Publication
  7. KM=4.2 µM for taurolithocholate1 Publication
  8. KM=2.1 µM for 3alpha-hydroxy-5alpha-androstan-17-one,1 Publication
  9. KM=1.4 µM for androsterone1 Publication
  10. KM=24.88 µM for PAPS1 Publication
  1. Vmax=227 nmol/min/mg enzyme with DHEA1 Publication
  2. Vmax=22.55 nmol/min/mg enzyme with DHEA1 Publication
  3. Vmax=54.3 µmol/min/mg enzyme with lithocholic acid1 Publication
  4. Vmax=203 nmol/min/mg enzyme with androsterone as substrate1 Publication
  5. Vmax=245 nmol/min/mg enzyme with DHEA1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei99Proton acceptor2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei121PAPS1 Publication1
Binding sitei129PAPS1 Publication1
Binding sitei184PAPS1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi44 – 49PAPS1 Publication6
Nucleotide bindingi218 – 223PAPS1 Publication6
Nucleotide bindingi247 – 249PAPS1 Publication3

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTransferase
Biological processBile acid catabolism, Lipid degradation, Lipid metabolism, Steroid metabolism

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:HS02732-MONOMER

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q06520

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-156584, Cytosolic sulfonation of small molecules
R-HSA-1989781, PPARA activates gene expression

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		Q06520

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000001650

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Sulfotransferase 2A1 (EC:2.8.2.27 Publications)
Short name:
ST2A1
Alternative name(s):
Bile salt sulfotransferase (EC:2.8.2.142 Publications)
Dehydroepiandrosterone sulfotransferase1 Publication
Short name:
DHEA-ST1 Publication
Short name:
DHEA-ST81 Publication
Hydroxysteroid Sulfotransferase
Short name:
HST
ST2
SULT2A31 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:SULT2A1
Synonyms:HST, STD
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 19

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:11458, SULT2A1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		125263, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q06520

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000105398.3

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi137M → I: Strongly reduces substrate inhibition when ADT or DHEA are used as substrates. 1 Publication1
Mutagenesisi137M → W: Substrate inhibition is completly eliminated for DHEA; when associated with A-238. 1 Publication1
Mutagenesisi238Y → A: Completely eliminates the substrate inhibition when ADT is used as substrate. Partially eliminates substrate inhibition when DHEA is used as substrate. Completely eliminates the substrate inhibition for DHEA, when associated with I-137. 1 Publication1
Mutagenesisi238Y → F: Strongly reduces substrate inhibition when ADT or DHEA are used as substrates. 1 Publication1
Mutagenesisi238Y → W: Strongly reduces substrate inhibition when ADT or DHEA are used as substrates. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		6822

Open Targets

More...OpenTargetsi		ENSG00000105398

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA346

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q06520, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2077

Drug and drug target database

More...DrugBanki		DB05812, Abiraterone
DB01812, Adenosine 3',5'-diphosphate
DB02854, Aetiocholanolone
DB04445, Mercuric iodide
DB09073, Palbociclib
DB01708, Prasterone
DB09288, Propacetamol
DB00675, Tamoxifen

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		SULT2A1

Domain mapping of disease mutations (DMDM)

More...DMDMi		1711591

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000851411 – 285Sulfotransferase 2A1Add BLAST285

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei251PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q06520

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q06520

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q06520

PeptideAtlas

More...PeptideAtlasi		Q06520

PRoteomics IDEntifications database

More...PRIDEi		Q06520

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		58456

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q06520

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q06520

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Liver, adrenal and at lower level in the kidney. Is present in human fetus in higher level in the adrenal than the liver and the kidney.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000105398, Expressed in metanephros and 94 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q06520, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q06520, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000105398, Tissue enriched (liver)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		112691, 6 interactors

Protein interaction database and analysis system

More...IntActi		Q06520, 6 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000222002

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q06520

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q06520, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1285
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q06520

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q06520

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the sulfotransferase 1 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1584, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000154432

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_027239_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q06520

Identification of Orthologs from Complete Genome Data

More...OMAi		HAMKENK

Database of Orthologous Groups

More...OrthoDBi		780670at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q06520

TreeFam database of animal gene trees

More...TreeFami		TF321745

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR027417, P-loop_NTPase
IPR000863, Sulfotransferase_dom

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00685, Sulfotransfer_1, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52540, SSF52540, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q06520-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSDDFLWFEG IAFPTMGFRS ETLRKVRDEF VIRDEDVIIL TYPKSGTNWL 
        60         70         80         90        100
AEILCLMHSK GDAKWIQSVP IWERSPWVES EIGYTALSET ESPRLFSSHL 
       110        120        130        140        150
PIQLFPKSFF SSKAKVIYLM RNPRDVLVSG YFFWKNMKFI KKPKSWEEYF 
       160        170        180        190        200
EWFCQGTVLY GSWFDHIHGW MPMREEKNFL LLSYEELKQD TGRTIEKICQ 
       210        220        230        240        250
FLGKTLEPEE LNLILKNSSF QSMKENKMSN YSLLSVDYVV DKAQLLRKGV 
       260        270        280 
SGDWKNHFTV AQAEDFDKLF QEKMADLPRE LFPWE
Length:285
Mass (Da):33,780
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i06DFF2006B284A08
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti90T → S in AAA35758 (PubMed:7678732).Curated1
Sequence conflicti90T → S in CAA49755 (PubMed:7678732).Curated1
Sequence conflicti119L → D AA sequence (PubMed:7678732).Curated1
Sequence conflicti159L → V in AAB23169 (PubMed:1520333).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_08388144K → E Sulfating activity toward both DHEA and pregnenolone is completely abolished. 1 PublicationCorresponds to variant dbSNP:rs772897551Ensembl.1
Natural variantiVAR_05252063A → P1 PublicationCorresponds to variant dbSNP:rs11569681EnsemblClinVar.1
Natural variantiVAR_08388276P → T Decreases of the sulfotransferase activity toward DHEA; decreases of the sulfotransferase activity toward pregnenolone. 1 PublicationCorresponds to variant dbSNP:rs775030275Ensembl.1
Natural variantiVAR_083883147E → K Decreases of the sulfotransferase activity toward DHEA; no effect on the sulfotransferase activity toward pregnenolone. 1 PublicationCorresponds to variant dbSNP:rs751309613Ensembl.1
Natural variantiVAR_083884148E → K Decreases of the sulfotransferase activity toward DHEA; decreases of the sulfotransferase activity toward pregnenolone. 1 PublicationCorresponds to variant dbSNP:rs368067020Ensembl.1
Natural variantiVAR_083885246L → P Decreases of the sulfotransferase activity toward DHEA; decreases of the sulfotransferase activity toward pregnenolone. 1 PublicationCorresponds to variant dbSNP:rs757338859Ensembl.1
Natural variantiVAR_083886258F → L Decreases of the sulfotransferase activity toward DHEA; decreases of the sulfotransferase activity toward pregnenolone. 1 PublicationCorresponds to variants dbSNP:rs746239667 and dbSNP:rs779218418EnsemblEnsembl.1
Natural variantiVAR_052521261A → T. Corresponds to variant dbSNP:rs11569679Ensembl.1
Natural variantiVAR_083887262Q → E Decreases of the sulfotransferase activity toward DHEA; no effect on the sulfotransferase activity toward pregnenolone. 1 PublicationCorresponds to variant dbSNP:rs753928755Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
L20000 mRNA Translation: AAA35758.1
X70222 mRNA Translation: CAA49755.1
U08024 mRNA Translation: AAA17749.1
U08025 mRNA Translation: AAA17750.1
X84816 mRNA Translation: CAA59274.1
L36196 L36195 Genomic DNA Translation: AAA75491.1
U13061 U13060 Genomic DNA Translation: AAC51353.1
S43859 mRNA Translation: AAB23169.2
BC020755 mRNA Translation: AAH20755.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS12707.1

Protein sequence database of the Protein Information Resource

More...PIRi		I53037, I38548

NCBI Reference Sequences

More...RefSeqi		NP_003158.2, NM_003167.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000222002; ENSP00000222002; ENSG00000105398

Database of genes from NCBI RefSeq genomes

More...GeneIDi		6822

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:6822

UCSC genome browser

More...UCSCi		uc002phr.2, human

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L20000 mRNA Translation: AAA35758.1
X70222 mRNA Translation: CAA49755.1
U08024 mRNA Translation: AAA17749.1
U08025 mRNA Translation: AAA17750.1
X84816 mRNA Translation: CAA59274.1
L36196 L36195 Genomic DNA Translation: AAA75491.1
U13061 U13060 Genomic DNA Translation: AAC51353.1
S43859 mRNA Translation: AAB23169.2
BC020755 mRNA Translation: AAH20755.1
CCDSiCCDS12707.1
PIRiI53037, I38548
RefSeqiNP_003158.2, NM_003167.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EFHX-ray2.40A/B1-281[»]
1J99X-ray1.99A2-285[»]
1OV4X-ray2.70A2-285[»]
2QP3X-ray2.60A2-285[»]
2QP4X-ray3.00A2-285[»]
3F3YX-ray2.20A/B/C/D1-285[»]
4IFBX-ray2.30A/B1-285[»]
SMRiQ06520
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi112691, 6 interactors
IntActiQ06520, 6 interactors
STRINGi9606.ENSP00000222002

Chemistry databases

BindingDBiQ06520
ChEMBLiCHEMBL2077
DrugBankiDB05812, Abiraterone
DB01812, Adenosine 3',5'-diphosphate
DB02854, Aetiocholanolone
DB04445, Mercuric iodide
DB09073, Palbociclib
DB01708, Prasterone
DB09288, Propacetamol
DB00675, Tamoxifen
SwissLipidsiSLP:000001650

PTM databases

iPTMnetiQ06520
PhosphoSitePlusiQ06520

Genetic variation databases

BioMutaiSULT2A1
DMDMi1711591

Proteomic databases

MassIVEiQ06520
MaxQBiQ06520
PaxDbiQ06520
PeptideAtlasiQ06520
PRIDEiQ06520
ProteomicsDBi58456

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		4362, 465 antibodies

The DNASU plasmid repository

More...DNASUi		6822

Genome annotation databases

EnsembliENST00000222002; ENSP00000222002; ENSG00000105398
GeneIDi6822
KEGGihsa:6822
UCSCiuc002phr.2, human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		6822
DisGeNETi6822

GeneCards: human genes, protein and diseases

More...GeneCardsi		SULT2A1
HGNCiHGNC:11458, SULT2A1
HPAiENSG00000105398, Tissue enriched (liver)
MIMi125263, gene
neXtProtiNX_Q06520
OpenTargetsiENSG00000105398
PharmGKBiPA346
VEuPathDBiHostDB:ENSG00000105398.3

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1584, Eukaryota
GeneTreeiENSGT00940000154432
HOGENOMiCLU_027239_1_0_1
InParanoidiQ06520
OMAiHAMKENK
OrthoDBi780670at2759
PhylomeDBiQ06520
TreeFamiTF321745

Enzyme and pathway databases

BioCyciMetaCyc:HS02732-MONOMER
PathwayCommonsiQ06520
ReactomeiR-HSA-156584, Cytosolic sulfonation of small molecules
R-HSA-1989781, PPARA activates gene expression
SABIO-RKiQ06520

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		6822, 3 hits in 984 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		SULT2A1, human
EvolutionaryTraceiQ06520

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Bile_salt_sulfotransferase

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		6822
PharosiQ06520, Tbio

Protein Ontology

More...PROi		PR:Q06520
RNActiQ06520, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000105398, Expressed in metanephros and 94 other tissues
ExpressionAtlasiQ06520, baseline and differential
GenevisibleiQ06520, HS

Family and domain databases

InterProiView protein in InterPro
IPR027417, P-loop_NTPase
IPR000863, Sulfotransferase_dom
PfamiView protein in Pfam
PF00685, Sulfotransfer_1, 1 hit
SUPFAMiSSF52540, SSF52540, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiST2A1_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q06520
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: June 2, 2021
This is version 200 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families
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