Details for: PAPSS1

Gene ID: 9061

Symbol: PAPSS1

Ensembl ID: ENSG00000138801

Description: 3'-phosphoadenosine 5'-phosphosulfate synthase 1

Associated with

Other Information

Genular Protein ID: 21557776

Symbol: PAPS1_HUMAN

Name: Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 9576487

Title: Sulfation in high endothelial venules: cloning and expression of the human PAPS synthetase.

PubMed ID: 9576487

DOI: 10.1096/fasebj.12.7.603

PubMed ID: 9668121

Title: Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains.

PubMed ID: 9668121

DOI: 10.1074/jbc.273.30.19311

PubMed ID: 9648242

Title: cDNA cloning, expression, and characterization of the human bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase enzyme.

PubMed ID: 9648242

DOI: 10.1271/bbb.62.1037

PubMed ID: 10679223

Title: Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and PAPSS2: gene cloning, characterization and chromosomal localization.

PubMed ID: 10679223

DOI: 10.1006/bbrc.2000.2123

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 9915785

Title: Site-selected mutagenesis of a conserved nucleotide binding HXGH motif located in the ATP sulfurylase domain of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase.

PubMed ID: 9915785

DOI: 10.1074/jbc.274.5.2601

PubMed ID: 14747722

Title: Expression, purification and crystallization of human 3'-phosphoadenosine-5'-phosphosulfate synthetase 1.

PubMed ID: 14747722

DOI: 10.1107/s0907444903027628

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 22223895

Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

PubMed ID: 22223895

DOI: 10.1074/mcp.m111.015131

PubMed ID: 15755455

Title: The crystal structure of human PAPS synthetase 1 reveals asymmetry in substrate binding.

PubMed ID: 15755455

DOI: 10.1016/j.jmb.2005.01.005

PubMed ID: 17540769

Title: Structural mechanism for substrate inhibition of the adenosine 5'-phosphosulfate kinase domain of human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 and its ramifications for enzyme regulation.

PubMed ID: 17540769

DOI: 10.1074/jbc.m701713200

PubMed ID: 17276460

Title: Elucidation of the active conformation of the APS-kinase domain of human PAPS synthetase 1.

PubMed ID: 17276460

DOI: 10.1016/j.jmb.2007.01.025

Sequence Information:

  • Length: 624
  • Mass: 70833
  • Checksum: A3DC9B943E68CDD6
  • Sequence:
  • MEIPGSLCKK VKLSNNAQNW GMQRATNVTY QAHHVSRNKR GQVVGTRGGF RGCTVWLTGL 
    SGAGKTTVSM ALEEYLVCHG IPCYTLDGDN IRQGLNKNLG FSPEDREENV RRIAEVAKLF 
    ADAGLVCITS FISPYTQDRN NARQIHEGAS LPFFEVFVDA PLHVCEQRDV KGLYKKARAG 
    EIKGFTGIDS EYEKPEAPEL VLKTDSCDVN DCVQQVVELL QERDIVPVDA SYEVKELYVP 
    ENKLHLAKTD AETLPALKIN KVDMQWVQVL AEGWATPLNG FMREREYLQC LHFDCLLDGG 
    VINLSVPIVL TATHEDKERL DGCTAFALMY EGRRVAILRN PEFFEHRKEE RCARQWGTTC 
    KNHPYIKMVM EQGDWLIGGD LQVLDRVYWN DGLDQYRLTP TELKQKFKDM NADAVFAFQL 
    RNPVHNGHAL LMQDTHKQLL ERGYRRPVLL LHPLGGWTKD DDVPLMWRMK QHAAVLEEGV 
    LNPETTVVAI FPSPMMYAGP TEVQWHCRAR MVAGANFYIV GRDPAGMPHP ETGKDLYEPS 
    HGAKVLTMAP GLITLEIVPF RVAAYNKKKK RMDYYDSEHH EDFEFISGTR MRKLAREGQK 
    PPEGFMAPKA WTVLTEYYKS LEKA

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.