PAPSS2

PAPSS2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2AX4
Identifiers
Aliases	PAPSS2, ATPSK2, BCYM4, SK2, 3'-phosphoadenosine 5'-phosphosulfate synthase 2
External IDs	OMIM: 603005; MGI: 1330223; HomoloGene: 55840; GeneCards: PAPSS2; OMA:PAPSS2 - orthologs
Gene location (Human) Chr. Chromosome 10 (human)[1] Band 10q23.2-q23.31 Start 87,659,613 bp[1] End 87,747,705 bp[1]
Gene location (Mouse) Chr. Chromosome 19 (mouse)[2] Band 19 C1|19 27.46 cM Start 32,573,190 bp[2] End 32,644,587 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in tibia mucosa of sigmoid colon lower lobe of lung cartilage tissue beta cell visceral pleura adrenal cortex right adrenal gland right adrenal cortex jejunal mucosa Top expressed in duodenum lacrimal gland pyloric antrum occiput occipital bone epithelium of stomach islet of Langerhans mucous cell of stomach finger lateral part of occipital bone More reference expression data BioGPS More reference expression data
Gene ontology Molecular function ATP binding nucleotidyltransferase activity kinase activity catalytic activity nucleotide binding transferase activity sulfate adenylyltransferase (ATP) activity adenylylsulfate kinase activity Cellular component cytosol Biological process blood coagulation skeletal system development bone development phosphorylation metabolism sulfate assimilation 3'-phosphoadenosine 5'-phosphosulfate biosynthetic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9060 23972 Ensembl ENSG00000198682 ENSMUSG00000024899 UniProt O95340 Q5TB52 O88428 RefSeq (mRNA) NM_004670 NM_001015880 NM_001201470 NM_011864 NM_001360403 RefSeq (protein) NP_001015880 NP_004661 NP_004661.2 NP_001188399 NP_035994 NP_001347332 Location (UCSC) Chr 10: 87.66 – 87.75 Mb Chr 19: 32.57 – 32.64 Mb PubMed search [3] [4]
Wikidata
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Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 2 is an enzyme that in humans is encoded by the PAPSS2 gene.^[5][6]

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.^[6]

• 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.
• 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.
• 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.
• 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.
• 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.
• 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. doi:10.1096/fasebj.14.2.345. PMID 10657990. S2CID 9024784.
• 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. Bibcode:1998PNAS...95.8681K. doi:10.1073/pnas.95.15.8681. PMC 21136. PMID 9671738.

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