O60507 · TPST1_HUMAN

  • Protein
    Protein-tyrosine sulfotransferase 1
  • Gene
    TPST1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Catalyzes the O-sulfation of tyrosine residues within acidic motifs of polypeptides, using 3'-phosphoadenylyl sulfate (PAPS) as cosubstrate.

Catalytic activity

Features

Showing features for binding site, active site, site.

137050100150200250300350
TypeIDPosition(s)Description
Binding site79-833'-phosphoadenylyl sulfate (UniProtKB | ChEBI)
Active site100Proton donor/acceptor
Site159Transition state stabilizer
Binding site1843'-phosphoadenylyl sulfate (UniProtKB | ChEBI)
Binding site1923'-phosphoadenylyl sulfate (UniProtKB | ChEBI)
Binding site1963'-phosphoadenylyl sulfate (UniProtKB | ChEBI)
Binding site2393'-phosphoadenylyl sulfate (UniProtKB | ChEBI)
Site286Transition state stabilizer
Binding site286-2953'-phosphoadenylyl sulfate (UniProtKB | ChEBI)
Binding site3013'-phosphoadenylyl sulfate (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular ComponentGolgi apparatus
Cellular ComponentGolgi membrane
Cellular Componentmembrane
Molecular Functionprotein homodimerization activity
Molecular Functionprotein-tyrosine sulfotransferase activity
Biological Process3'-phosphoadenosine 5'-phosphosulfate metabolic process
Biological Processpost-translational protein modification

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein-tyrosine sulfotransferase 1
  • EC number
  • Alternative names
    • Tyrosylprotein sulfotransferase 1 (TPST-1)

Gene names

    • Name
      TPST1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    O60507
  • Secondary accessions
    • A4D2M0
    • Q6FGM7

Proteomes

Organism-specific databases

Subcellular Location

Golgi apparatus membrane
; Single-pass type II membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-8Cytoplasmic
Transmembrane9-25Helical; Signal-anchor for type II membrane protein
Topological domain26-370Lumenal

Keywords

Disease & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis60Loss of one glycosylation site. Loss of N-glycosylation; when associated with A-262.
Mutagenesis262Loss of one glycosylation site. Loss of N-glycosylation; when associated with A-60.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 355 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, glycosylation, disulfide bond, modified residue (large scale data).

TypeIDPosition(s)SourceDescription
ChainPRO_00001898261-370UniProtProtein-tyrosine sulfotransferase 1
Glycosylation60UniProtN-linked (GlcNAc...) asparagine
Disulfide bond97↔157UniProt
Disulfide bond226↔234UniProt
Glycosylation262UniProtN-linked (GlcNAc...) asparagine
Modified residue (large scale data)279PRIDEPhosphoserine

Post-translational modification

N-glycosylated.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Ubiquitous. Detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Homodimer (PubMed:16859706, PubMed:28821720).
Can also form heterodimers with TPST2 (PubMed:25660941).

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region102-106Interaction with peptide substrate

Sequence similarities

Belongs to the protein sulfotransferase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    370
  • Mass (Da)
    42,188
  • Last updated
    1998-08-01 v1
  • Checksum
    FB9EB341AFE36407
MVGKLKQNLLLACLVISSVTVFYLGQHAMECHHRIEERSQPVKLESTRTTVRTGLDLKANKTFAYHKDMPLIFIGGVPRSGTTLMRAMLDAHPDIRCGEETRVIPRILALKQMWSRSSKEKIRLDEAGVTDEVLDSAMQAFLLEIIVKHGEPAPYLCNKDPFALKSLTYLSRLFPNAKFLLMVRDGRASVHSMISRKVTIAGFDLNSYRDCLTKWNRAIETMYNQCMEVGYKKCMLVHYEQLVLHPERWMRTLLKFLQIPWNHSVLHHEEMIGKAGGVSLSKVERSTDQVIKPVNVGALSKWVGKIPPDVLQDMAVIAPMLAKLGYDPYANPPNYGKPDPKIIENTRRVYKGEFQLPDFLKEKPQTEQVE

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
C9J3I4C9J3I4_HUMANTPST1140
C9K0F3C9K0F3_HUMANTPST141

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF038009
EMBL· GenBank· DDBJ
AAC13552.1
EMBL· GenBank· DDBJ
mRNA
AK313098
EMBL· GenBank· DDBJ
BAG35922.1
EMBL· GenBank· DDBJ
mRNA
CR542060
EMBL· GenBank· DDBJ
CAG46857.1
EMBL· GenBank· DDBJ
mRNA
CR542080
EMBL· GenBank· DDBJ
CAG46877.1
EMBL· GenBank· DDBJ
mRNA
CH236961
EMBL· GenBank· DDBJ
EAL23739.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471140
EMBL· GenBank· DDBJ
EAX07937.1
EMBL· GenBank· DDBJ
Genomic DNA
BC013188
EMBL· GenBank· DDBJ
AAH13188.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any 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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp