PAPSS2

3'-phosphoadenosine 5'-phosphosulfate synthase 2

PDB rendering based on 2ax4.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
2AX4

Identifiers

Symbols

PAPSS2 ; ATPSK2; BCYM4; SK2

External IDs

OMIM: 603005 MGI: 1330223 HomoloGene: 55840 GeneCards: PAPSS2 Gene

EC number

2.7.1.25, 2.7.7.4

Gene ontology
Molecular function	• adenylylsulfate kinase activity • sulfate adenylyltransferase (ATP) activity • ATP binding • nucleotidyltransferase activity
Cellular component	• cytosol
Biological process	• sulfate assimilation • skeletal system development • carbohydrate metabolic process • xenobiotic metabolic process • blood coagulation • phosphorylation • glycosaminoglycan metabolic process • small molecule metabolic process • 3'-phosphoadenosine 5'-phosphosulfate metabolic process • 3'-phosphoadenosine 5'-phosphosulfate biosynthetic process • bone development
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 10:
87.66 – 87.75 Mb

Chr 19:
32.62 – 32.67 Mb

PubMed search

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

↑ 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.
1 2 "Entrez Gene: PAPSS2 3'-phosphoadenosine 5'-phosphosulfate synthase 2".

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. 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. 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.

PDB gallery

2ax4: Crystal structure of the kinase domain of human 3'-phosphoadenosine 5'-phosphosulphate synthetase 2

Transferases: phosphorus-containing groups (EC 2.7)

2.7.1-2.7.4:
phosphotransferase/kinase
(PO₄)

2.7.1: OH acceptor	Hexo- Gluco- Fructo- Hepatic Galacto- Phosphofructo- 1 Liver Muscle Platelet 2 Riboflavin Shikimate Thymidine ADP-thymidine NAD⁺ Glycerol Pantothenate Mevalonate Pyruvate Deoxycytidine PFP Diacylglycerol Phosphoinositide 3 Class I PI 3 Class II PI 3 Sphingosine Glucose-1,6-bisphosphate synthase

2.7.2: COOH acceptor	Phosphoglycerate Aspartate kinase

2.7.3: N acceptor	Creatine

2.7.4: PO₄ acceptor	Phosphomevalonate Adenylate Nucleoside-diphosphate Uridylate Guanylate Thiamine-diphosphate

2.7.6: diphosphotransferase
(P₂O₇)

2.7.7: nucleotidyltransferase
(PO₄-nucleoside)

Polymerase

DNA polymerase	DNA-directed DNA polymerase I II III IV V RNA-directed DNA polymerase Reverse transcriptase Telomerase DNA nucleotidylexotransferase/Terminal deoxynucleotidyl transferase

RNA nucleotidyltransferase	RNA polymerase/DNA-directed RNA polymerase RNA polymerase I RNA polymerase II RNA polymerase III RNA polymerase IV Primase RNA-dependent RNA polymerase PNPase

Phosphorolytic
3' to 5' exoribonuclease

Nucleotidyltransferase

Guanylyltransferase

mRNA capping enzyme

Other

2.7.8: miscellaneous

Phosphatidyltransferases	CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase CDP-diacylglycerol—serine O-phosphatidyltransferase CDP-diacylglycerol—inositol 3-phosphatidyltransferase CDP-diacylglycerol—choline O-phosphatidyltransferase

Glycosyl-1-phosphotransferase	N-acetylglucosamine-1-phosphate transferase

2.7.10-2.7.13: protein kinase
(PO₄; protein acceptor)

2.7.10: protein-tyrosine	see tyrosine kinases

2.7.11: protein-serine/threonine	see serine/threonine-specific protein kinases

2.7.12: protein-dual-specificity	see serine/threonine-specific protein kinases

2.7.13: protein-histidine	Protein-histidine pros-kinase Protein-histidine tele-kinase Histidine kinase

glycosaminoglycan anabolism

Heparan sulfate: EXT1; EXT2

Chondroitin sulfate: PAPSS1; PAPSS2

glycosaminoglycan catabolism

Hunter, Hurler	Iduronate-2-sulfatase Iduronidase

Sanfilippo, Sly	Heparan sulfamidase N-acetyltransferase Alpha-N-acetylglucosaminidase Glucuronidase N-acetylglucosamine-6-sulfatase

Morquio/Maroteaux-Lamy	Arylsulfatase B Galactosamine-6 sulfatase Beta-galactosidase (GLB1)

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PAPSS2

References

Further reading