LOCUS       NP_005434                624 aa            linear   PRI 19-SEP-2024
DEFINITION  bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1 [Homo
            sapiens].
ACCESSION   NP_005434
VERSION     NP_005434.4
DBSOURCE    REFSEQ: accession NM_005443.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 624)
  AUTHORS   Zhu,X., Zhu,P., Chen,X., Zhang,L., Wu,C., Zhang,H., Shen,X., Qi,Y.,
            Chen,M., Wang,S. and Yi,X.
  TITLE     Correlation of 3'-phosphoadenosine-5'-phosphosulfate synthase 1
            (PAPSS1) expression with clinical parameters and prognosis in
            esophageal squamous cell carcinoma
  JOURNAL   Histol Histopathol 38 (11), 1327-1335 (2023)
   PUBMED   36734141
  REMARK    GeneRIF: Correlation of 3'-phosphoadenosine-5'-phosphosulfate
            synthase 1 (PAPSS1) expression with clinical parameters and
            prognosis in esophageal squamous cell carcinoma.
REFERENCE   2  (residues 1 to 624)
  AUTHORS   Sun,L., Ji,W.X., Li,Y., Li,Z.L., Duan,C.C., Xia,B.R. and Xiao,L.
  TITLE     The PAPSS1 gene is a modulator of response to cisplatin by
            regulating estrogen receptor alpha signaling activity in ovarian
            cancer cells
  JOURNAL   J Ovarian Res 16 (1), 187 (2023)
   PUBMED   37684671
  REMARK    GeneRIF: The PAPSS1 gene is a modulator of response to cisplatin by
            regulating estrogen receptor alpha signaling activity in ovarian
            cancer cells.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 624)
  AUTHORS   Huttlin,E.L., Bruckner,R.J., Navarrete-Perea,J., Cannon,J.R.,
            Baltier,K., Gebreab,F., Gygi,M.P., Thornock,A., Zarraga,G., Tam,S.,
            Szpyt,J., Gassaway,B.M., Panov,A., Parzen,H., Fu,S., Golbazi,A.,
            Maenpaa,E., Stricker,K., Guha Thakurta,S., Zhang,T., Rad,R.,
            Pan,J., Nusinow,D.P., Paulo,J.A., Schweppe,D.K., Vaites,L.P.,
            Harper,J.W. and Gygi,S.P.
  TITLE     Dual proteome-scale networks reveal cell-specific remodeling of the
            human interactome
  JOURNAL   Cell 184 (11), 3022-3040 (2021)
   PUBMED   33961781
REFERENCE   4  (residues 1 to 624)
  AUTHORS   Leung,A.W.Y., Veinotte,C.J., Melong,N., Oh,M.H., Chen,K.,
            Enfield,K.S.S., Backstrom,I., Warburton,C., Yapp,D., Berman,J.N.,
            Bally,M.B. and Lockwood,W.W.
  TITLE     In Vivo Validation of PAPSS1 (3'-phosphoadenosine 5'-phosphosulfate
            synthase 1) as a Cisplatin-sensitizing Therapeutic Target
  JOURNAL   Clin Cancer Res 23 (21), 6555-6566 (2017)
   PUBMED   28790117
  REMARK    GeneRIF: These results suggest that PAPSS1 inhibition enhances
            cisplatin activity in multiple preclinical model systems and that
            low PAPSS1 expression may serve as a biomarker for platin
            sensitivity in cancer patients. Developing strategies to target
            PAPSS1 activity in conjunction with platinum-based chemotherapy may
            offer an approach to improving treatment outcomes
REFERENCE   5  (residues 1 to 624)
  AUTHORS   Zhu,W., Gliddon,B.L., Jarman,K.E., Moretti,P.A.B., Tin,T.,
            Parise,L.V., Woodcock,J.M., Powell,J.A., Ruszkiewicz,A.,
            Pitman,M.R. and Pitson,S.M.
  TITLE     CIB1 contributes to oncogenic signalling by Ras via modulating the
            subcellular localisation of sphingosine kinase 1
  JOURNAL   Oncogene 36 (18), 2619-2627 (2017)
   PUBMED   27941888
  REMARK    GeneRIF: we found that ectopic expression of oncogenic KRas and
            HRas in cells resulted in elevated CIB1 expression. We previously
            described the Ca(2+)-myristoyl switch function of CIB1, and its
            ability to facilitate agonist-induced plasma membrane localisation
            of sphingosine kinase 1 (SK1), a location where SK1 is known to
            elicit oncogenic signalling.
REFERENCE   6  (residues 1 to 624)
  AUTHORS   Faiyaz ul Haque,M., King,L.M., Krakow,D., Cantor,R.M.,
            Rusiniak,M.E., Swank,R.T., Superti-Furga,A., Haque,S., Abbas,H.,
            Ahmad,W., Ahmad,M. and Cohn,D.H.
  TITLE     Mutations in orthologous genes in human spondyloepimetaphyseal
            dysplasia and the brachymorphic mouse
  JOURNAL   Nat Genet 20 (2), 157-162 (1998)
   PUBMED   9771708
REFERENCE   7  (residues 1 to 624)
  AUTHORS   Venkatachalam,K.V., Akita,H. and Strott,C.A.
  TITLE     Molecular cloning, expression, and characterization of human
            bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its
            functional domains
  JOURNAL   J Biol Chem 273 (30), 19311-19320 (1998)
   PUBMED   9668121
REFERENCE   8  (residues 1 to 624)
  AUTHORS   Kurima,K., Warman,M.L., Krishnan,S., Domowicz,M., Krueger,R.C. Jr.,
            Deyrup,A. and Schwartz,N.B.
  TITLE     A member of a family of sulfate-activating enzymes causes murine
            brachymorphism
  JOURNAL   Proc Natl Acad Sci U S A 95 (15), 8681-8685 (1998)
   PUBMED   9671738
  REMARK    Erratum:[Proc Natl Acad Sci U S A 1998 Sep 29;95(20):12071]
REFERENCE   9  (residues 1 to 624)
  AUTHORS   Yanagisawa,K., Sakakibara,Y., Suiko,M., Takami,Y., Nakayama,T.,
            Nakajima,H., Takayanagi,K., Natori,Y. and Liu,M.C.
  TITLE     cDNA cloning, expression, and characterization of the human
            bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase
            enzyme
  JOURNAL   Biosci Biotechnol Biochem 62 (5), 1037-1040 (1998)
   PUBMED   9648242
REFERENCE   10 (residues 1 to 624)
  AUTHORS   Girard,J.P., Baekkevold,E.S. and Amalric,F.
  TITLE     Sulfation in high endothelial venules: cloning and expression of
            the human PAPS synthetase
  JOURNAL   FASEB J 12 (7), 603-612 (1998)
   PUBMED   9576487
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AU132232.1, BQ437924.1 and BC011392.1.
            
            On Apr 2, 2004 this sequence version replaced NP_005434.3.
            
            Summary: Three-prime-phosphoadenosine 5-prime-phosphosulfate (PAPS)
            is the sulfate donor cosubstrate for all sulfotransferase (SULT)
            enzymes (Xu et al., 2000 [PubMed 10679223]). SULTs catalyze the
            sulfate conjugation of many endogenous and exogenous compounds,
            including drugs and other xenobiotics. In humans, PAPS is
            synthesized from adenosine 5-prime triphosphate (ATP) and inorganic
            sulfate by 2 isoforms, PAPSS1 and PAPSS2 (MIM 603005).[supplied by
            OMIM, Mar 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AF105227.1, SRR3476690.94533.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265174.5/ ENSP00000265174.4
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..624
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="4"
                     /map="4q25"
     Protein         1..624
                     /product="bifunctional 3'-phosphoadenosine
                     5'-phosphosulfate synthase 1"
                     /EC_number="2.7.1.25"
                     /EC_number="2.7.7.4"
                     /note="3-prime-phosphoadenosine 5-prime-phosphosulfate
                     synthase 1; SK 1; PAPSS 1; PAPS synthase 1; sulfurylase
                     kinase 1; adenylyl-sulfate kinase; sulfate
                     adenylyltransferase"
                     /calculated_mol_wt=70702
     Region          1..225
                     /region_name="Adenylyl-sulfate kinase.
                     /evidence=ECO:0000305|PubMed:15755455,
                     ECO:0000305|PubMed:17276460, ECO:0000305|PubMed:17540769"
                     /note="propagated from UniProtKB/Swiss-Prot (O43252.2)"
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0007744|PubMed:22223895; propagated from
                     UniProtKB/Swiss-Prot (O43252.2)"
     Site            12
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0000250|UniProtKB:Q60967; propagated from
                     UniProtKB/Swiss-Prot (O43252.2)"
     Region          33..227
                     /region_name="CysC"
                     /note="Adenylylsulfate kinase or related kinase [Inorganic
                     ion transport and metabolism]; COG0529"
                     /db_xref="CDD:440295"
     Region          234..624
                     /region_name="Sulfate adenylyltransferase.
                     /evidence=ECO:0000305|PubMed:15755455"
                     /note="propagated from UniProtKB/Swiss-Prot (O43252.2)"
     Region          254..617
                     /region_name="ATPS"
                     /note="ATP-sulfurylase; cd00517"
                     /db_xref="CDD:173895"
     Site            order(418..422,428,431,495,520..522,524..525,561..563)
                     /site_type="active"
                     /db_xref="CDD:173895"
     Site            425..428
                     /site_type="other"
                     /note="HXXH motif"
                     /db_xref="CDD:173895"
     Site            456..466
                     /site_type="other"
                     /note="flexible loop"
                     /db_xref="CDD:173895"
     CDS             1..624
                     /gene="PAPSS1"
                     /gene_synonym="ATPSK1; PAPSS; SK1"
                     /coded_by="NM_005443.5:56..1930"
                     /db_xref="CCDS:CCDS3676.1"
                     /db_xref="GeneID:9061"
                     /db_xref="HGNC:HGNC:8603"
                     /db_xref="MIM:603262"
ORIGIN      
        1 meipgslckk vklsnnaqnw gmqratnvty qahhvsrnkr gqvvgtrggf rgctvwltgl
       61 sgagkttvsm aleeylvchg ipcytldgdn irqglnknlg fspedreenv rriaevaklf
      121 adaglvcits fispytqdrn narqihegas lpffevfvda plhvceqrdv kglykkarag
      181 eikgftgids eyekpeapel vlktdscdvn dcvqqvvell qerdivpvda syevkelyvp
      241 enklhlaktd aetlpalkin kvdmqwvqvl aegwatplng fmrereylqc lhfdclldgg
      301 vinlsvpivl tathedkerl dgctafalmy egrrvailrn peffehrkee rcarqwgttc
      361 knhpyikmvm eqgdwliggd lqvldrvywn dgldqyrltp telkqkfkdm nadavfafql
      421 rnpvhnghal lmqdthkqll ergyrrpvll lhplggwtkd ddvplmwrmk qhaavleegv
      481 lnpettvvai fpspmmyagp tevqwhcrar mvaganfyiv grdpagmphp etgkdlyeps
      541 hgakvltmap glitleivpf rvaaynkkkk rmdyydsehh edfefisgtr mrklaregqk
      601 ppegfmapka wtvlteyyks leka
//
