PAPSS1

PAPSS1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1X6V, 1XJQ, 1XNJ, 2OFW, 2OFX, 2PEY, 2PEZ, 2QJF
Identifiers
Aliases	PAPSS1, ATPSK1, PAPSS, SK1, 3'-phosphoadenosine 5'-phosphosulfate synthase 1
External IDs	OMIM: 603262; MGI: 1330587; HomoloGene: 81740; GeneCards: PAPSS1; OMA:PAPSS1 - orthologs
Gene location (Human) Chr. Chromosome 4 (human) Band 4q25 Start 107,590,276 bp End 107,720,234 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3 G3|3 61.05 cM Start 131,270,529 bp End 131,349,432 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in inferior ganglion of vagus nerve secondary oocyte Pons bronchial epithelial cell subthalamic nucleus pylorus corpus callosum endometrium superior vestibular nucleus Brodmann area 46 Top expressed in vestibular membrane of cochlear duct left colon submandibular gland vestibular sensory epithelium lacrimal gland migratory enteric neural crest cell medullary collecting duct ileum human fetus utricle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity nucleotide binding nucleotidyltransferase activity catalytic activity ATP binding kinase activity sulfate adenylyltransferase (ATP) activity protein homodimerization activity adenylylsulfate kinase activity Cellular component cytosol Biological process skeletal system development metabolism phosphorylation sulfate assimilation 3'-phosphoadenosine 5'-phosphosulfate biosynthetic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9061 23971 Ensembl ENSG00000138801 ENSMUSG00000028032 UniProt O43252 Q60967 RefSeq (mRNA) NM_005443 NM_001289477 NM_001289478 NM_001289479 NM_011863 RefSeq (protein) NP_005434 NP_001276406 NP_001276407 NP_001276408 NP_035993 Location (UCSC) Chr 4: 107.59 – 107.72 Mb Chr 3: 131.27 – 131.35 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 is an enzyme that in humans is encoded by the PAPSS1 gene.

Three-prime-phosphoadenosine 5-prime-phosphosulfate (PAPS) is the sulfate donor cosubstrate for all sulfotransferase (SULT) enzymes (Xu et al., 2000). 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]

Further reading

• Venkatachalam KV (2004). "Human 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase: biochemistry, molecular biology and genetic deficiency". IUBMB Life. 55 (1): 1–11. doi:10.1080/1521654031000072148. PMID 12716056. S2CID 37733913.
• Yanagisawa K, Sakakibara Y, Suiko M, et al. (1998). "cDNA cloning, expression, and characterization of the human bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase enzyme". Biosci. Biotechnol. Biochem. 62 (5): 1037–40. doi:10.1271/bbb.62.1037. PMID 9648242.
• Venkatachalam KV, Akita H, Strott CA (1998). "Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains". J. Biol. Chem. 273 (30): 19311–20. doi:10.1074/jbc.273.30.19311. PMID 9668121.
• Kurima K, Warman ML, Krishnan S, et al. (1998). "A member of a family of sulfate-activating enzymes causes murine brachymorphism". Proc. Natl. Acad. Sci. U.S.A. 95 (15): 8681–5. Bibcode:1998PNAS...95.8681K. doi:10.1073/pnas.95.15.8681. PMC 21136. PMID 9671738.
• Venkatachalam KV, Fuda H, Koonin EV, Strott CA (1999). "Site-selected mutagenesis of a conserved nucleotide binding HXGH motif located in the ATP sulfurylase domain of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase". J. Biol. Chem. 274 (5): 2601–4. doi:10.1074/jbc.274.5.2601. PMID 9915785.
• Besset S, Vincourt JB, Amalric F, Girard JP (2000). "Nuclear localization of PAPS synthetase 1: a sulfate activation pathway in the nucleus of eukaryotic cells". FASEB J. 14 (2): 345–54. doi:10.1096/fasebj.14.2.345. PMID 10657990. S2CID 9024784.
• Xu ZH, Otterness DM, Freimuth RR, et al. (2000). "Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and PAPSS2: gene cloning, characterization and chromosomal localization". Biochem. Biophys. Res. Commun. 268 (2): 437–44. doi:10.1006/bbrc.2000.2123. PMID 10679223.
• Fuda H, Shimizu C, Lee YC, et al. (2002). "Characterization and expression of human bifunctional 3'-phosphoadenosine 5'-phosphosulphate synthase isoforms". Biochem. J. 365 (Pt 2): 497–504. doi:10.1042/BJ20020044. PMC 1222679. PMID 11931637.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Harjes S, Scheidig A, Bayer P (2004). "Expression, purification and crystallization of human 3'-phosphoadenosine-5'-phosphosulfate synthetase 1". Acta Crystallogr. D. 60 (Pt 2): 350–2. doi:10.1107/S0907444903027628. PMID 14747722.
• Lansdon EB, Fisher AJ, Segel IH (2004). "Human 3'-phosphoadenosine 5'-phosphosulfate synthetase (isoform 1, brain): kinetic properties of the adenosine triphosphate sulfurylase and adenosine 5'-phosphosulfate kinase domains". Biochemistry. 43 (14): 4356–65. doi:10.1021/bi049827m. PMID 15065880.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Harjes S, Bayer P, Scheidig AJ (2005). "The crystal structure of human PAPS synthetase 1 reveals asymmetry in substrate binding". J. Mol. Biol. 347 (3): 623–35. doi:10.1016/j.jmb.2005.01.005. PMID 15755455.
• Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Sekulic N, Konrad M, Lavie A (2007). "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". J. Biol. Chem. 282 (30): 22112–21. doi:10.1074/jbc.M701713200. hdl:11858/00-001M-0000-0012-E08D-D. PMID 17540769.