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O43704

- ST1B1_HUMAN

UniProt

O43704 - ST1B1_HUMAN

Protein

Sulfotransferase family cytosolic 1B member 1

Gene

SULT1B1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 2 (04 Jan 2005)
      Previous versions | rss
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    Functioni

    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 dopamine, small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3'-diiodothyronine, triidothyronine, reverse triiodothyronine and thyroxine.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei109 – 1091Proton acceptorBy similarity
    Binding sitei131 – 1311PAPS
    Binding sitei139 – 1391PAPS
    Binding sitei194 – 1941PAPS

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi48 – 536PAPS
    Nucleotide bindingi228 – 2336PAPS
    Nucleotide bindingi258 – 2603PAPS

    GO - Molecular functioni

    1. aryl sulfotransferase activity Source: Ensembl
    2. sulfotransferase activity Source: UniProtKB

    GO - Biological processi

    1. 3'-phosphoadenosine 5'-phosphosulfate metabolic process Source: Reactome
    2. cellular biogenic amine metabolic process Source: ProtInc
    3. epithelial cell differentiation Source: UniProt
    4. flavonoid metabolic process Source: BHF-UCL
    5. phenol-containing compound metabolic process Source: UniProtKB
    6. small molecule metabolic process Source: Reactome
    7. steroid metabolic process Source: UniProtKB-KW
    8. sulfation Source: BHF-UCL
    9. thyroid hormone metabolic process Source: UniProtKB
    10. xenobiotic metabolic process Source: BHF-UCL

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Lipid metabolism, Steroid metabolism

    Enzyme and pathway databases

    BRENDAi2.8.2.1. 2681.
    ReactomeiREACT_6913. Cytosolic sulfonation of small molecules.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sulfotransferase family cytosolic 1B member 1 (EC:2.8.2.-)
    Short name:
    ST1B1
    Short name:
    Sulfotransferase 1B1
    Alternative name(s):
    Sulfotransferase 1B2
    Short name:
    ST1B2
    Thyroid hormone sulfotransferase
    Gene namesi
    Name:SULT1B1
    Synonyms:ST1B2, SULT1B2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:17845. SULT1B1.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA415.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 296296Sulfotransferase family cytosolic 1B member 1PRO_0000085161Add
    BLAST

    Proteomic databases

    MaxQBiO43704.
    PaxDbiO43704.
    PRIDEiO43704.

    PTM databases

    PhosphoSiteiO43704.

    Expressioni

    Tissue specificityi

    Highly expressed in the liver, peripheral blood leukocytes, colon (mucosal lining), small intestine (jejunum) and spleen. A lesser expression was observed in the lung, placenta and thymus.1 Publication

    Gene expression databases

    ArrayExpressiO43704.
    BgeeiO43704.
    CleanExiHS_SULT1B1.
    GenevestigatoriO43704.

    Organism-specific databases

    HPAiHPA002107.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    BioGridi118108. 1 interaction.

    Structurei

    Secondary structure

    1
    296
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni5 – 95
    Beta strandi13 – 153
    Beta strandi18 – 203
    Helixi22 – 254
    Helixi29 – 324
    Beta strandi41 – 466
    Helixi51 – 6212
    Turni63 – 653
    Helixi67 – 704
    Helixi75 – 784
    Turni87 – 893
    Helixi93 – 997
    Beta strandi105 – 1084
    Turni112 – 1143
    Helixi117 – 1215
    Beta strandi125 – 1306
    Helixi133 – 14614
    Helixi156 – 16510
    Helixi173 – 18210
    Turni183 – 1864
    Beta strandi189 – 1935
    Helixi194 – 1996
    Helixi201 – 21111
    Helixi218 – 22710
    Helixi230 – 2345
    Turni237 – 2393
    Turni246 – 2483
    Turni251 – 2533
    Helixi264 – 2674
    Helixi271 – 28515

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Z5FX-ray2.10A/B1-296[»]
    3CKLX-ray2.00A/B1-296[»]
    ProteinModelPortaliO43704.
    SMRiO43704. Positions 1-296.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43704.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni107 – 1093Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the sulfotransferase 1 family.Curated

    Phylogenomic databases

    eggNOGiNOG260792.
    HOGENOMiHOG000037209.
    HOVERGENiHBG001195.
    InParanoidiO43704.
    KOiK01025.
    OMAiKNLKMVH.
    OrthoDBiEOG7V49ZK.
    PhylomeDBiO43704.
    TreeFamiTF321745.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR000863. Sulfotransferase_dom.
    [Graphical view]
    PfamiPF00685. Sulfotransfer_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O43704-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSPKDILRK DLKLVHGYPM TCAFASNWEK IEQFHSRPDD IVIATYPKSG    50
    TTWVSEIIDM ILNDGDIEKC KRGFITEKVP MLEMTLPGLR TSGIEQLEKN 100
    PSPRIVKTHL PTDLLPKSFW ENNCKMIYLA RNAKDVSVSY YHFDLMNNLQ 150
    PFPGTWEEYL EKFLTGKVAY GSWFTHVKNW WKKKEEHPIL FLYYEDMKEN 200
    PKEEIKKIIR FLEKNLNDEI LDRIIHHTSF EVMKDNPLVN YTHLPTTVMD 250
    HSKSPFMRKG TAGDWKNYFT VAQNEKFDAI YETEMSKTAL QFRTEI 296
    Length:296
    Mass (Da):34,899
    Last modified:January 4, 2005 - v2
    Checksum:iAFEB61B21DBD782C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti183 – 1831K → R in AAH10895. (PubMed:15489334)Curated
    Sequence conflicti186 – 1861E → G in BAA24547. (PubMed:9443824)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D89479 mRNA. Translation: BAA24547.1.
    U95726 mRNA. Translation: AAB65154.1.
    BC010895 mRNA. Translation: AAH10895.1.
    AF184894 Genomic DNA. Translation: AAF05917.1.
    CCDSiCCDS3530.1.
    PIRiJC5885.
    RefSeqiNP_055280.2. NM_014465.3.
    XP_005265734.1. XM_005265677.1.
    UniGeneiHs.129742.

    Genome annotation databases

    EnsembliENST00000310613; ENSP00000308770; ENSG00000173597.
    GeneIDi27284.
    KEGGihsa:27284.
    UCSCiuc003hen.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D89479 mRNA. Translation: BAA24547.1 .
    U95726 mRNA. Translation: AAB65154.1 .
    BC010895 mRNA. Translation: AAH10895.1 .
    AF184894 Genomic DNA. Translation: AAF05917.1 .
    CCDSi CCDS3530.1.
    PIRi JC5885.
    RefSeqi NP_055280.2. NM_014465.3.
    XP_005265734.1. XM_005265677.1.
    UniGenei Hs.129742.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Z5F X-ray 2.10 A/B 1-296 [» ]
    3CKL X-ray 2.00 A/B 1-296 [» ]
    ProteinModelPortali O43704.
    SMRi O43704. Positions 1-296.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118108. 1 interaction.

    Chemistry

    ChEMBLi CHEMBL1743294.

    PTM databases

    PhosphoSitei O43704.

    Proteomic databases

    MaxQBi O43704.
    PaxDbi O43704.
    PRIDEi O43704.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000310613 ; ENSP00000308770 ; ENSG00000173597 .
    GeneIDi 27284.
    KEGGi hsa:27284.
    UCSCi uc003hen.3. human.

    Organism-specific databases

    CTDi 27284.
    GeneCardsi GC04M070641.
    HGNCi HGNC:17845. SULT1B1.
    HPAi HPA002107.
    MIMi 608436. gene.
    neXtProti NX_O43704.
    PharmGKBi PA415.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG260792.
    HOGENOMi HOG000037209.
    HOVERGENi HBG001195.
    InParanoidi O43704.
    KOi K01025.
    OMAi KNLKMVH.
    OrthoDBi EOG7V49ZK.
    PhylomeDBi O43704.
    TreeFami TF321745.

    Enzyme and pathway databases

    BRENDAi 2.8.2.1. 2681.
    Reactomei REACT_6913. Cytosolic sulfonation of small molecules.

    Miscellaneous databases

    EvolutionaryTracei O43704.
    GeneWikii SULT1B1.
    GenomeRNAii 27284.
    NextBioi 50216.
    PROi O43704.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43704.
    Bgeei O43704.
    CleanExi HS_SULT1B1.
    Genevestigatori O43704.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR000863. Sulfotransferase_dom.
    [Graphical view ]
    Pfami PF00685. Sulfotransfer_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of rat ST1B1 and human ST1B2 cDNAs, encoding thyroid hormone sulfotransferases."
      Fujita K., Nagata K., Ozawa S., Sasano H., Yamazoe Y.
      J. Biochem. 122:1052-1061(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
      Tissue: Liver.
    2. "Expression and characterization of a novel thyroid hormone-sulfating form of cytosolic sulfotransferase from human liver."
      Wang J., Falany J.L., Falany C.N.
      Mol. Pharmacol. 53:274-282(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: Liver.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Bone marrow.
    4. "Mapping of the SULT1B2 gene to human chromosome 4q11-13."
      Falany C.N., Wang J.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-73.
    5. "Crystal structures of human sulfotransferases SULT1B1 and SULT1C1 complexed with the cofactor product adenosine-3'- 5'-diphosphate (PAP)."
      Dombrovski L., Dong A., Bochkarev A., Plotnikov A.N.
      Proteins 64:1091-1094(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ADENOSINE-3'-5'-DIPHOSPHATE.
    6. "Crystal structure of human cytosolic sulfotransferase SULT1B1 in complex with PAP and resveratrol."
      Structural genomics consortium (SGC)
      Submitted (APR-2008) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ADENOSINE-3'-5'-DIPHOSPHATE AND RESVERATROL.

    Entry informationi

    Entry nameiST1B1_HUMAN
    AccessioniPrimary (citable) accession number: O43704
    Secondary accession number(s): O15497, Q96FI1, Q9UK34
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 4, 2005
    Last sequence update: January 4, 2005
    Last modified: October 1, 2014
    This is version 117 of the entry and version 2 of the sequence. [Complete history]
    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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3