| 释义 |
- References
- Further reading
{{Infobox_gene}}Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthetase 2 is an enzyme that in humans is encoded by the PAPSS2 gene.[1][2]{{PBB_Summary
| section_title =
| summary_text = 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]
}}References1. ^{{cite journal | vauthors = 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 | title = Mutations in orthologous genes in human spondyloepimetaphyseal dysplasia and the brachymorphic mouse | journal = Nat Genet | volume = 20 | issue = 2 | pages = 157–62 |date=Oct 1998 | pmid = 9771708 | pmc = | doi = 10.1038/2458 }}
2. ^1 {{cite web | title = Entrez Gene: PAPSS2 3'-phosphoadenosine 5'-phosphosulfate synthase 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9060| accessdate = }}
Further reading{{refbegin | 2}}- {{cite journal |vauthors=Ewing RM, Chu P, Elisma F, etal |title=Large-scale mapping of human protein-protein interactions by mass spectrometry |journal=Mol. Syst. Biol. |volume=3 |issue= 1|pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 | pmc=1847948 }}
- {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
- {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
- {{cite journal | vauthors=Shimizu C, Fuda H, Lee YC, Strott CA |title=Transcriptional regulation of human 3'-phosphoadenosine 5'-phosphosulphate synthase 2 |journal=Biochem. J. |volume=363 |issue= Pt 2 |pages= 263–71 |year= 2002 |pmid= 11931653 |doi=10.1042/0264-6021:3630263 | pmc=1222474 }}
- {{cite journal |vauthors=Fuda H, Shimizu C, Lee YC, etal |title=Characterization and expression of human bifunctional 3'-phosphoadenosine 5'-phosphosulphate synthase isoforms |journal=Biochem. J. |volume=365 |issue= Pt 2 |pages= 497–504 |year= 2002 |pmid= 11931637 |doi= 10.1042/BJ20020044 | pmc=1222679 }}
- {{cite journal |vauthors=Xu ZH, Freimuth RR, Eckloff B, etal |title=Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 2 (PAPSS2) pharmacogenetics: gene resequencing, genetic polymorphisms and functional characterization of variant allozymes |journal=Pharmacogenetics |volume=12 |issue= 1 |pages= 11–21 |year= 2002 |pmid= 11773860 |doi=10.1097/00008571-200201000-00003 }}
- {{cite journal | vauthors=Xu Z, Wood TC, Adjei AA, Weinshilboum RM |title=Human 3'-phosphoadenosine 5'-phosphosulfate synthetase: radiochemical enzymatic assay, biochemical properties, and hepatic variation |journal=Drug Metab. Dispos. |volume=29 |issue= 2 |pages= 172–8 |year= 2001 |pmid= 11159808 |doi= }}
- {{cite journal |vauthors=Xu ZH, Otterness DM, Freimuth RR, etal |title=Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and PAPSS2: gene cloning, characterization and chromosomal localization |journal=Biochem. Biophys. Res. Commun. |volume=268 |issue= 2 |pages= 437–44 |year= 2000 |pmid= 10679223 |doi= 10.1006/bbrc.2000.2123 }}
- {{cite journal | vauthors=Besset S, Vincourt JB, Amalric F, Girard JP |title=Nuclear localization of PAPS synthetase 1: a sulfate activation pathway in the nucleus of eukaryotic cells |journal=FASEB J. |volume=14 |issue= 2 |pages= 345–54 |year= 2000 |pmid= 10657990 |doi= }}
- {{cite journal | vauthors=Kurima K, Singh B, Schwartz NB |title=Genomic organization of the mouse and human genes encoding the ATP sulfurylase/adenosine 5'-phosphosulfate kinase isoform SK2 |journal=J. Biol. Chem. |volume=274 |issue= 47 |pages= 33306–12 |year= 1999 |pmid= 10559207 |doi=10.1074/jbc.274.47.33306 }}
- {{cite journal |vauthors=Ahmad M, Haque MF, Ahmad W, etal |title=Distinct, autosomal recessive form of spondyloepimetaphyseal dysplasia segregating in an inbred Pakistani kindred |journal=Am. J. Med. Genet. |volume=78 |issue= 5 |pages= 468–73 |year= 1998 |pmid= 9714015 |doi=10.1002/(SICI)1096-8628(19980806)78:5<468::AID-AJMG13>3.0.CO;2-D }}
- {{cite journal |vauthors=Kurima K, Warman ML, Krishnan S, etal |title=A member of a family of sulfate-activating enzymes causes murine brachymorphism |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 15 |pages= 8681–5 |year= 1998 |pmid= 9671738 |doi=10.1073/pnas.95.15.8681 | pmc=21136 }}
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