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P50225

- ST1A1_HUMAN

UniProt

P50225 - ST1A1_HUMAN

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Protein

Sulfotransferase 1A1

Gene

SULT1A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP50225.
CleanExiHS_SULT1A1.
ExpressionAtlasiP50225. baseline and differential.
GenevestigatoriP50225.

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

BioGridi112686. 40 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 – 153Combined sources
Beta strandi18 – 203Combined sources
Helixi22 – 3110Combined sources
Beta strandi41 – 466Combined sources
Helixi51 – 6212Combined sources
Turni63 – 653Combined sources
Helixi67 – 704Combined sources
Helixi75 – 784Combined sources
Beta strandi87 – 893Combined sources
Helixi92 – 976Combined sources
Beta strandi104 – 1074Combined sources
Turni111 – 1133Combined sources
Helixi116 – 1205Combined sources
Beta strandi124 – 1296Combined sources
Helixi132 – 14514Combined sources
Helixi155 – 16410Combined sources
Helixi172 – 18211Combined sources
Turni183 – 1853Combined sources
Beta strandi188 – 1925Combined sources
Helixi193 – 1986Combined sources
Helixi200 – 21112Combined sources
Helixi217 – 22610Combined sources
Helixi229 – 2346Combined sources
Turni236 – 2383Combined sources
Turni245 – 2473Combined sources
Turni250 – 2523Combined sources
Helixi263 – 2664Combined sources
Helixi270 – 28314Combined sources
Turni284 – 2863Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118932.
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

        10         20         30         40         50
MELIQDTSRP PLEYVKGVPL IKYFAEALGP LQSFQARPDD LLISTYPKSG
60 70 80 90 100
TTWVSQILDM IYQGGDLEKC HRAPIFMRVP FLEFKAPGIP SGMETLKDTP
110 120 130 140 150
APRLLKTHLP LALLPQTLLD QKVKVVYVAR NAKDVAVSYY HFYHMAKVHP
160 170 180 190 200
EPGTWDSFLE KFMVGEVSYG SWYQHVQEWW ELSRTHPVLY LFYEDMKENP
210 220 230 240 250
KREIQKILEF VGRSLPEETV DFVVQHTSFK EMKKNPMTNY TTVPQEFMDH
260 270 280 290
SISPFMRKGM AGDWKTTFTV AQNERFDADY AEKMAGCSLS FRSEL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 40 interactions.
IntActi P50225. 3 interactions.
STRINGi 9606.ENSP00000321988.

Chemistry

ChEMBLi CHEMBL1743291.
DrugBanki DB00316. Acetaminophen.
DB00675. Tamoxifen.

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.
GeneTreei ENSGT00760000118932.
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

Bgeei P50225.
CleanExi HS_SULT1A1.
ExpressionAtlasi P50225. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 149 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