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P50225

- ST1A1_HUMAN

UniProt

P50225 - ST1A1_HUMAN

Protein

Sulfotransferase 1A1

Gene

SULT1A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 3 (30 Nov 2010)
      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 catecholamines, phenolic drugs and neurotransmitters. Has also estrogen sulfotransferase activity. responsible for the sulfonation and activation of minoxidil. Is Mediates the metabolic activation of carcinogenic N-hydroxyarylamines to DNA binding products and could so participate as modulating factor of cancer risk.2 Publications

    Catalytic activityi

    3'-phosphoadenylyl sulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei108 – 1081Proton acceptorBy similarity
    Binding sitei130 – 1301PAPS
    Binding sitei138 – 1381PAPS
    Binding sitei193 – 1931PAPS

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi48 – 536PAPS
    Nucleotide bindingi227 – 2326PAPS
    Nucleotide bindingi255 – 2595PAPS

    GO - Molecular functioni

    1. aryl sulfotransferase activity Source: UniProtKB
    2. flavonol 3-sulfotransferase activity Source: BHF-UCL
    3. steroid sulfotransferase activity Source: UniProtKB
    4. sulfotransferase activity Source: ProtInc

    GO - Biological processi

    1. 3'-phosphoadenosine 5'-phosphosulfate metabolic process Source: Reactome
    2. amine metabolic process Source: ProtInc
    3. catecholamine metabolic process Source: UniProtKB-KW
    4. estrogen metabolic process Source: UniProtKB
    5. flavonoid metabolic process Source: BHF-UCL
    6. small molecule metabolic process Source: Reactome
    7. sulfation Source: BHF-UCL
    8. xenobiotic metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Catecholamine metabolism, Lipid metabolism, Steroid metabolism

    Enzyme and pathway databases

    BioCyciMetaCyc:HS09898-MONOMER.
    BRENDAi2.8.2.1. 2681.
    ReactomeiREACT_6913. Cytosolic sulfonation of small molecules.
    SABIO-RKP50225.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sulfotransferase 1A1 (EC:2.8.2.1)
    Short name:
    ST1A1
    Alternative name(s):
    Aryl sulfotransferase 1
    HAST1/HAST2
    Phenol sulfotransferase 1
    Phenol-sulfating phenol sulfotransferase 1
    Short name:
    P-PST 1
    ST1A3
    Thermostable phenol sulfotransferase
    Short name:
    Ts-PST
    Gene namesi
    Name:SULT1A1
    Synonyms:STP, STP1
    ORF Names:OK/SW-cl.88
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:11453. SULT1A1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi70 – 701C → S: Increased sensitivity of enzyme activity to heat inactivation. 1 Publication

    Organism-specific databases

    PharmGKBiPA343.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 295295Sulfotransferase 1A1PRO_0000085127Add
    BLAST

    Proteomic databases

    MaxQBiP50225.
    PaxDbiP50225.
    PRIDEiP50225.

    2D gel databases

    OGPiP50225.

    PTM databases

    PhosphoSiteiP50225.

    Expressioni

    Tissue specificityi

    Liver, lung, adrenal, brain, platelets and skin.

    Gene expression databases

    ArrayExpressiP50225.
    BgeeiP50225.
    CleanExiHS_SULT1A1.
    GenevestigatoriP50225.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Protein-protein interaction databases

    BioGridi112686. 35 interactions.
    IntActiP50225. 3 interactions.
    STRINGi9606.ENSP00000321988.

    Structurei

    Secondary structure

    1
    295
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi13 – 153
    Beta strandi18 – 203
    Helixi22 – 3110
    Beta strandi41 – 466
    Helixi51 – 6212
    Turni63 – 653
    Helixi67 – 704
    Helixi75 – 784
    Beta strandi87 – 893
    Helixi92 – 976
    Beta strandi104 – 1074
    Turni111 – 1133
    Helixi116 – 1205
    Beta strandi124 – 1296
    Helixi132 – 14514
    Helixi155 – 16410
    Helixi172 – 18211
    Turni183 – 1853
    Beta strandi188 – 1925
    Helixi193 – 1986
    Helixi200 – 21112
    Helixi217 – 22610
    Helixi229 – 2346
    Turni236 – 2383
    Turni245 – 2473
    Turni250 – 2523
    Helixi263 – 2664
    Helixi270 – 28314
    Turni284 – 2863

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LS6X-ray1.90A1-295[»]
    1Z28X-ray2.30A1-295[»]
    2D06X-ray2.30A/B1-295[»]
    3QVUX-ray2.50A/B1-295[»]
    3QVVX-ray2.35A/B1-295[»]
    3U3JX-ray2.70A/B1-294[»]
    3U3KX-ray2.36A/B1-295[»]
    3U3MX-ray2.30A1-295[»]
    3U3OX-ray2.00A1-295[»]
    3U3RX-ray2.36A1-295[»]
    4GRAX-ray2.56A/B1-295[»]
    ProteinModelPortaliP50225.
    SMRiP50225. Positions 7-295.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP50225.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni106 – 1083Substrate binding

    Sequence similaritiesi

    Belongs to the sulfotransferase 1 family.Curated

    Phylogenomic databases

    eggNOGiNOG260792.
    HOGENOMiHOG000037209.
    HOVERGENiHBG001195.
    InParanoidiP50225.
    KOiK01014.
    OMAiVGLPINI.
    OrthoDBiEOG7V49ZK.
    PhylomeDBiP50225.
    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.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P50225-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MELIQDTSRP PLEYVKGVPL IKYFAEALGP LQSFQARPDD LLISTYPKSG    50
    TTWVSQILDM IYQGGDLEKC HRAPIFMRVP FLEFKAPGIP SGMETLKDTP 100
    APRLLKTHLP LALLPQTLLD QKVKVVYVAR NAKDVAVSYY HFYHMAKVHP 150
    EPGTWDSFLE KFMVGEVSYG SWYQHVQEWW ELSRTHPVLY LFYEDMKENP 200
    KREIQKILEF VGRSLPEETV DFVVQHTSFK EMKKNPMTNY TTVPQEFMDH 250
    SISPFMRKGM AGDWKTTFTV AQNERFDADY AEKMAGCSLS FRSEL 295
    Length:295
    Mass (Da):34,165
    Last modified:November 30, 2010 - v3
    Checksum:i7D4362A603A29176
    GO
    Isoform 2 (identifier: P50225-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-124: MELIQDTSRP...PQTLLDQKVK → MLAKLLCDQV...LKQKFWNTYM

    Note: No experimental confirmation available.

    Show »
    Length:217
    Mass (Da):25,388
    Checksum:i8A6A935E4DD11A6D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti90 – 901P → L in AAA67895. (PubMed:8423770)Curated
    Sequence conflicti146 – 1461A → T in CAA59147. (PubMed:7864863)Curated
    Sequence conflicti181 – 1811E → G in CAA59147. (PubMed:7864863)Curated
    Sequence conflicti243 – 2431V → A in AAA67895. (PubMed:8423770)Curated
    Sequence conflicti290 – 2901S → T in AAA99892. (PubMed:8423770)Curated
    Sequence conflicti290 – 2901S → T in AAC50480. (PubMed:8924211)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti37 – 371R → Q.1 Publication
    VAR_009302
    Natural varianti151 – 1511E → D.
    Corresponds to variant rs1042014 [ dbSNP | Ensembl ].
    VAR_028721
    Natural varianti151 – 1511E → Q.
    Corresponds to variant rs1042011 [ dbSNP | Ensembl ].
    VAR_057339
    Natural varianti213 – 2131R → H in allele SULT1A1*2; common polymorphism; has a lower activity. 4 Publications
    Corresponds to variant rs9282861 [ dbSNP | Ensembl ].
    VAR_007425
    Natural varianti223 – 2231V → M.15 Publications
    Corresponds to variant rs1801030 [ dbSNP | Ensembl ].
    VAR_009303
    Natural varianti235 – 2351N → T.
    Corresponds to variant rs35728980 [ dbSNP | Ensembl ].
    VAR_014889
    Natural varianti282 – 2821E → K.2 Publications
    Corresponds to variant rs36043491 [ dbSNP | Ensembl ].
    VAR_061886

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 124124MELIQ…DQKVK → MLAKLLCDQVVGAPIAVSAF YAGMSILQGKDDIFLDLKQK FWNTYM in isoform 2. 1 PublicationVSP_040101Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09031 mRNA. Translation: AAA18613.1.
    L19955 mRNA. Translation: AAA02935.1.
    L10819 mRNA. Translation: AAA35562.1.
    L19999 mRNA. Translation: AAA99892.1.
    U26309 mRNA. Translation: AAA67895.1.
    X84654 mRNA. Translation: CAA59147.1.
    X78283 mRNA. Translation: CAA55089.1.
    U71086 Genomic DNA. Translation: AAB09597.1.
    U54701 Genomic DNA. Translation: AAC50480.1.
    AJ007418 mRNA. Translation: CAA07495.1.
    U52852 Genomic DNA. Translation: AAC51816.1.
    AB062428 mRNA. Translation: BAB93491.1.
    BT007324 mRNA. Translation: AAP35988.1.
    CR608214 mRNA. No translation available.
    AC020765 Genomic DNA. No translation available.
    BC000923 mRNA. Translation: AAH00923.1.
    BC110887 mRNA. Translation: AAI10888.1.
    L15346 Genomic DNA. Translation: AAA60595.1.
    CCDSiCCDS10637.1. [P50225-2]
    CCDS32420.1. [P50225-1]
    PIRiI57945.
    JC2523.
    JC5248.
    S52399.
    S52794.
    RefSeqiNP_001046.2. NM_001055.3. [P50225-1]
    NP_803565.1. NM_177529.2. [P50225-1]
    NP_803566.1. NM_177530.2. [P50225-1]
    NP_803878.1. NM_177534.2. [P50225-1]
    NP_803880.1. NM_177536.3. [P50225-2]
    XP_005255579.1. XM_005255522.1. [P50225-1]
    UniGeneiHs.567342.
    Hs.736805.

    Genome annotation databases

    EnsembliENST00000314752; ENSP00000321988; ENSG00000196502. [P50225-1]
    ENST00000350842; ENSP00000329399; ENSG00000196502. [P50225-2]
    ENST00000395607; ENSP00000378971; ENSG00000196502. [P50225-1]
    ENST00000395609; ENSP00000378972; ENSG00000196502. [P50225-1]
    ENST00000569554; ENSP00000457912; ENSG00000196502. [P50225-1]
    GeneIDi6817.
    KEGGihsa:6817.
    UCSCiuc002dqi.3. human. [P50225-1]
    uc002dqm.3. human. [P50225-2]

    Polymorphism databases

    DMDMi313104286.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U09031 mRNA. Translation: AAA18613.1 .
    L19955 mRNA. Translation: AAA02935.1 .
    L10819 mRNA. Translation: AAA35562.1 .
    L19999 mRNA. Translation: AAA99892.1 .
    U26309 mRNA. Translation: AAA67895.1 .
    X84654 mRNA. Translation: CAA59147.1 .
    X78283 mRNA. Translation: CAA55089.1 .
    U71086 Genomic DNA. Translation: AAB09597.1 .
    U54701 Genomic DNA. Translation: AAC50480.1 .
    AJ007418 mRNA. Translation: CAA07495.1 .
    U52852 Genomic DNA. Translation: AAC51816.1 .
    AB062428 mRNA. Translation: BAB93491.1 .
    BT007324 mRNA. Translation: AAP35988.1 .
    CR608214 mRNA. No translation available.
    AC020765 Genomic DNA. No translation available.
    BC000923 mRNA. Translation: AAH00923.1 .
    BC110887 mRNA. Translation: AAI10888.1 .
    L15346 Genomic DNA. Translation: AAA60595.1 .
    CCDSi CCDS10637.1. [P50225-2 ]
    CCDS32420.1. [P50225-1 ]
    PIRi I57945.
    JC2523.
    JC5248.
    S52399.
    S52794.
    RefSeqi NP_001046.2. NM_001055.3. [P50225-1 ]
    NP_803565.1. NM_177529.2. [P50225-1 ]
    NP_803566.1. NM_177530.2. [P50225-1 ]
    NP_803878.1. NM_177534.2. [P50225-1 ]
    NP_803880.1. NM_177536.3. [P50225-2 ]
    XP_005255579.1. XM_005255522.1. [P50225-1 ]
    UniGenei Hs.567342.
    Hs.736805.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LS6 X-ray 1.90 A 1-295 [» ]
    1Z28 X-ray 2.30 A 1-295 [» ]
    2D06 X-ray 2.30 A/B 1-295 [» ]
    3QVU X-ray 2.50 A/B 1-295 [» ]
    3QVV X-ray 2.35 A/B 1-295 [» ]
    3U3J X-ray 2.70 A/B 1-294 [» ]
    3U3K X-ray 2.36 A/B 1-295 [» ]
    3U3M X-ray 2.30 A 1-295 [» ]
    3U3O X-ray 2.00 A 1-295 [» ]
    3U3R X-ray 2.36 A 1-295 [» ]
    4GRA X-ray 2.56 A/B 1-295 [» ]
    ProteinModelPortali P50225.
    SMRi P50225. Positions 7-295.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112686. 35 interactions.
    IntActi P50225. 3 interactions.
    STRINGi 9606.ENSP00000321988.

    Chemistry

    ChEMBLi CHEMBL1743291.

    PTM databases

    PhosphoSitei P50225.

    Polymorphism databases

    DMDMi 313104286.

    2D gel databases

    OGPi P50225.

    Proteomic databases

    MaxQBi P50225.
    PaxDbi P50225.
    PRIDEi P50225.

    Protocols and materials databases

    DNASUi 6817.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000314752 ; ENSP00000321988 ; ENSG00000196502 . [P50225-1 ]
    ENST00000350842 ; ENSP00000329399 ; ENSG00000196502 . [P50225-2 ]
    ENST00000395607 ; ENSP00000378971 ; ENSG00000196502 . [P50225-1 ]
    ENST00000395609 ; ENSP00000378972 ; ENSG00000196502 . [P50225-1 ]
    ENST00000569554 ; ENSP00000457912 ; ENSG00000196502 . [P50225-1 ]
    GeneIDi 6817.
    KEGGi hsa:6817.
    UCSCi uc002dqi.3. human. [P50225-1 ]
    uc002dqm.3. human. [P50225-2 ]

    Organism-specific databases

    CTDi 6817.
    GeneCardsi GC16M028616.
    H-InvDB HIX0017846.
    HGNCi HGNC:11453. SULT1A1.
    MIMi 171150. gene.
    neXtProti NX_P50225.
    PharmGKBi PA343.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG260792.
    HOGENOMi HOG000037209.
    HOVERGENi HBG001195.
    InParanoidi P50225.
    KOi K01014.
    OMAi VGLPINI.
    OrthoDBi EOG7V49ZK.
    PhylomeDBi P50225.
    TreeFami TF321745.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS09898-MONOMER.
    BRENDAi 2.8.2.1. 2681.
    Reactomei REACT_6913. Cytosolic sulfonation of small molecules.
    SABIO-RK P50225.

    Miscellaneous databases

    EvolutionaryTracei P50225.
    GeneWikii SULT1A1.
    GenomeRNAii 6817.
    NextBioi 26605.
    PROi P50225.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P50225.
    Bgeei P50225.
    CleanExi HS_SULT1A1.
    Genevestigatori P50225.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-223.
      Tissue: Brain.
    2. "Molecular characterisation of a human aryl sulfotransferase cDNA."
      Zhu X., Veronese M.E., Sansom L.N., McManus M.E.
      Biochem. Biophys. Res. Commun. 192:671-676(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-223.
      Tissue: Liver.
    3. "Sequence analysis and expression of the cDNA for the phenol-sulfating form of human liver phenol sulfotransferase."
      Wilborn T.W., Comer K.A., Dooley T.P., Reardon I.M., Heinrikson R.L., Falany C.N.
      Mol. Pharmacol. 43:70-77(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANTS MET-223 AND LYS-282.
      Tissue: Liver.
    4. "Structural similarity and diversity of sulfotransferases."
      Yamazoe Y., Nagata K., Ozawa S., Kato R.
      Chem. Biol. Interact. 92:107-117(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-223.
    5. "Molecular cloning of an isoform of phenol sulfotransferase from human brain hippocampus."
      Hwang S.-R., Kohn A.B., Hook V.Y.H.
      Biochem. Biophys. Res. Commun. 207:701-707(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-223.
      Tissue: Hippocampus.
    6. "Human platelet phenolsulfotransferases: cDNA cloning, stable expression in V79 cells and identification of a novel allelic variant of the phenol-sulfating form."
      Jones A.L., Hagen M., Coughtrie M.W.H., Roberts R.C., Glatt H.
      Biochem. Biophys. Res. Commun. 208:855-862(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-223.
      Tissue: Blood.
    7. "Primary structures and properties of two related forms of aryl sulfotransferases in human liver."
      Ozawa S., Nagata K., Shimada M., Ueda M., Tsuzuki T., Yamazoe Y., Kato R.
      Pharmacogenetics 5:S135-S140(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-223.
      Tissue: Liver.
    8. "Genomic organization and DNA sequences of two human phenol sulfotransferase genes (STP1 and STP2) on the short arm of chromosome 16."
      Dooley T.P., Huang Z.
      Biochem. Biophys. Res. Commun. 228:134-140(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT MET-223.
    9. "Human phenol sulfotransferase gene contains two alternative promoters: structure and expression of the gene."
      Bernier F., Soucy P., Luu-The V.
      DNA Cell Biol. 15:367-375(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS MET-223 AND LYS-282.
    10. "A single amino acid, Glu146, governs the substrate specificity of a human dopamine sulfotransferase, SULT1A3."
      Dajani R., Hood A.M., Coughtrie M.W.
      Mol. Pharmacol. 54:942-948(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-223.
      Tissue: Liver.
    11. Raftogianis R.B., Her C., Weinshilboum R.M.
      Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT MET-223.
    12. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
      Shichijo S., Itoh K.
      Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS HIS-213 AND MET-223.
      Tissue: Colon adenocarcinoma.
    13. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT HIS-213.
    14. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    15. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    16. "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] (ISOFORM 1), VARIANT MET-223.
      Tissue: Colon and Placenta.
    17. "Mapping of the phenol sulfotransferase gene (STP) to human chromosome 16p12.1-p11.2 and to mouse chromosome 7."
      Dooley T.P., Obermoeller R.D., Leiter E.H., Chapman H.D., Falany C.N., Deng Z., Siciliano M.J.
      Genomics 18:440-443(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-107 (ISOFORM 1).
    18. "Functional characterization of two human sulphotransferase cDNAs that encode monoamine- and phenol-sulphating forms of phenol sulphotransferase: substrate kinetics, thermal-stability and inhibitor-sensitivity studies."
      Veronese M.E., Burgess W., Zhu X., McManus M.E.
      Biochem. J. 302:497-502(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    19. "Characterization of expressed human phenol-sulfating phenol sulfotransferase: effect of mutating cys70 on activity and thermostability."
      Falany C.N., Zhuang W., Falany J.L.
      Chem. Biol. Interact. 92:57-66(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-70.
    20. "Structure of a human carcinogen-converting enzyme, SULT1A1. Structural and kinetic implications of substrate inhibition."
      Gamage N.U., Duggleby R.G., Barnett A.C., Tresillian M., Latham C.F., Liyou N.E., McManus M.E., Martin J.L.
      J. Biol. Chem. 278:7655-7662(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ADENOSINE-3'-5'-DIPHOSPHATE (PAP) AND P-NITROPHENOL, CATALYTIC ACTIVITY, FUNCTION.
    21. "The structure of human SULT1A1 crystallized with estradiol. An insight into active site plasticity and substrate inhibition with multi-ring substrates."
      Gamage N.U., Tsvetanov S., Duggleby R.G., McManus M.E., Martin J.L.
      J. Biol. Chem. 280:41482-41486(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH ADENOSINE-3'-5'-DIPHOSPHATE AND ESTRADIOL, CATALYTIC ACTIVITY, FUNCTION.
    22. "Crystal structures of SULT1A2 and SULT1A1 *3: insights into the substrate inhibition and the role of Tyr149 in SULT1A2."
      Lu J., Li H., Zhang J., Li M., Liu M.Y., An X., Liu M.C., Chang W.
      Biochem. Biophys. Res. Commun. 396:429-434(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH ADENOSINE-3'-5'-DIPHOSPHATE.
    23. "Directed evolution of sulfotransferases and paraoxonases by ancestral libraries."
      Alcolombri U., Elias M., Tawfik D.S.
      J. Mol. Biol. 411:837-853(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEXES WITH ADENOSINE-3'-5'-DIPHOSPHATE AND P-NITROPHENOL, CATALYTIC ACTIVITY.
    24. "The molecular basis for the broad substrate specificity of human sulfotransferase 1A1."
      Berger I., Guttman C., Amar D., Zarivach R., Aharoni A.
      PLoS ONE 6:E26794-E26794(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEXES WITH ADENOSINE-3'-5'-DIPHOSPHATE AND P-NITROPHENOL, CATALYTIC ACTIVITY.
    25. "Phenol sulfotransferase pharmacogenetics in humans: association of common SULT1A1 alleles with TS PST phenotype."
      Raftogianis R.B., Wood T.C., Otterness D.M., Van Loon J.A., Weinshilboum R.M.
      Biochem. Biophys. Res. Commun. 239:298-304(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GLN-37; HIS-213 AND MET-223.
    26. "Association between functional genetic polymorphisms of human sulfotransferases 1A1 and 1A2."
      Engelke C.E., Meinl W., Boeing H., Glatt H.
      Pharmacogenetics 10:163-169(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HIS-213.
    27. Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiST1A1_HUMAN
    AccessioniPrimary (citable) accession number: P50225
    Secondary accession number(s): Q2NL71
    , Q86U58, Q92818, Q9BVU6, Q9UGG7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 148 of the entry and version 3 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    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

    External Data

    Dasty 3