PAPSS2

3'-phosphoadenosine 5'-phosphosulfate synthase 2
PDB rendering based on 2ax4.
Available structures PDB 2ax4
Identifiers
Symbols	PAPSS2; ATPSK2; SK2
External IDs	OMIM: 603005 MGI: 1330223 HomoloGene: 55840 GeneCards: PAPSS2 Gene
Gene Ontology Molecular function • nucleotide binding • adenylylsulfate kinase activity • sulfate adenylyltransferase (ATP) activity • sulfate adenylyltransferase (ATP) activity • protein binding • ATP binding • nucleotidyltransferase activity Cellular component • cytosol Biological process • sulfate assimilation • skeletal system development • xenobiotic metabolic process • 3'-phosphoadenosine 5'-phosphosulfate metabolic process • 3'-phosphoadenosine 5'-phosphosulfate biosynthetic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	9060	23972
Ensembl	ENSG00000198682	ENSMUSG00000024899
UniProt	O95340	Q5BKP4
RefSeq (mRNA)	NM_001015880.1	XM_993984
RefSeq (protein)	NP_001015880.1	XP_999078
Location (UCSC)	Chr 10: 89.42 – 89.51 Mb	Chr 19: 32.69 – 32.74 Mb
PubMed search	[1]	[2]

Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 2 is an enzyme that in humans is encoded by the PAPSS2 gene.^[1][2]

Sulfation is a common modification of endogenous (lipids, proteins, and carbohydrates) and exogenous (xenobiotics and drugs) compounds. In mammals, the sulfate source is 3'-phosphoadenosine 5'-phosphosulfate (PAPS), created from ATP and inorganic sulfate. Two different tissue isoforms encoded by different genes synthesize PAPS. This gene encodes one of the two PAPS synthetases. Defects in this gene cause the Pakistani type of spondyloepimetaphyseal dysplasia. Two alternatively spliced transcript variants that encode different isoforms have been described for this gene.^[2]

References

1. ^ ul Haque MF, King LM, Krakow D, Cantor RM, Rusiniak ME, Swank RT, Superti-Furga A, Haque S, Abbas H, Ahmad W, Ahmad M, Cohn DH (Oct 1998). "Mutations in orthologous genes in human spondyloepimetaphyseal dysplasia and the brachymorphic mouse". Nat Genet 20 (2): 157–62. doi:10.1038/2458. PMID 9771708. 
2. ^ ^{a b} "Entrez Gene: PAPSS2 3'-phosphoadenosine 5'-phosphosulfate synthase 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9060. 

Further reading

• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928. 
• 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Shimizu C, Fuda H, Lee YC, Strott CA (2002). "Transcriptional regulation of human 3'-phosphoadenosine 5'-phosphosulphate synthase 2". Biochem. J. 363 (Pt 2): 263–71. doi:10.1042/0264-6021:3630263. PMC 1222474. PMID 11931653. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222474. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222679. 
• Xu ZH, Freimuth RR, Eckloff B, et al. (2002). "Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 2 (PAPSS2) pharmacogenetics: gene resequencing, genetic polymorphisms and functional characterization of variant allozymes". Pharmacogenetics 12 (1): 11–21. doi:10.1097/00008571-200201000-00003. PMID 11773860. 
• Xu Z, Wood TC, Adjei AA, Weinshilboum RM (2001). "Human 3'-phosphoadenosine 5'-phosphosulfate synthetase: radiochemical enzymatic assay, biochemical properties, and hepatic variation". Drug Metab. Dispos. 29 (2): 172–8. PMID 11159808. 
• 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. 
• 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. PMID 10657990. 
• Kurima K, Singh B, Schwartz NB (1999). "Genomic organization of the mouse and human genes encoding the ATP sulfurylase/adenosine 5'-phosphosulfate kinase isoform SK2". J. Biol. Chem. 274 (47): 33306–12. doi:10.1074/jbc.274.47.33306. PMID 10559207. 
• Ahmad M, Haque MF, Ahmad W, et al. (1998). "Distinct, autosomal recessive form of spondyloepimetaphyseal dysplasia segregating in an inbred Pakistani kindred". Am. J. Med. Genet. 78 (5): 468–73. doi:10.1002/(SICI)1096-8628(19980806)78:5<468::AID-AJMG13>3.0.CO;2-D. PMID 9714015. 
• 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. doi:10.1073/pnas.95.15.8681. PMC 21136. PMID 9671738. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=21136.