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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).

References

1. ^ GRCh38: Ensembl release 89: ENSG00000138801 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000028032 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Girard JP, Baekkevold ES, Amalric F (May 1998). "Sulfation in high endothelial venules: cloning and expression of the human PAPS synthetase". FASEB Journal. 12 (7): 603–612. doi:10.1096/fasebj.12.7.603. PMID 9576487. S2CID 19530341.
6. Faiyaz ul Haque M, King LM, Krakow D, Cantor RM, Rusiniak ME, Swank RT, et al. (October 1998). "Mutations in orthologous genes in human spondyloepimetaphyseal dysplasia and the brachymorphic mouse". Nature Genetics. 20 (2): 157–162. doi:10.1038/2458. PMID 9771708. S2CID 13108930.
7. ^ "Entrez Gene: PAPSS1 3'-phosphoadenosine 5'-phosphosulfate synthase 1".

Further reading

• Venkatachalam KV (January 2003). "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, Takami Y, Nakayama T, Nakajima H, et al. (May 1998). "cDNA cloning, expression, and characterization of the human bifunctional ATP sulfurylase/adenosine 5'-phosphosulfate kinase enzyme". Bioscience, Biotechnology, and Biochemistry. 62 (5): 1037–1040. doi:10.1271/bbb.62.1037. PMID 9648242.
• Venkatachalam KV, Akita H, Strott CA (July 1998). "Molecular cloning, expression, and characterization of human bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase and its functional domains". The Journal of Biological Chemistry. 273 (30): 19311–19320. doi:10.1074/jbc.273.30.19311. PMID 9668121.
• Kurima K, Warman ML, Krishnan S, Domowicz M, Krueger RC, Deyrup A, Schwartz NB (July 1998). "A member of a family of sulfate-activating enzymes causes murine brachymorphism". Proceedings of the National Academy of Sciences of the United States of America. 95 (15): 8681–8685. Bibcode:1998PNAS...95.8681K. doi:10.1073/pnas.95.15.8681. PMC 21136. PMID 9671738.
• Venkatachalam KV, Fuda H, Koonin EV, Strott CA (January 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". The Journal of Biological Chemistry. 274 (5): 2601–2604. doi:10.1074/jbc.274.5.2601. PMID 9915785.
• Besset S, Vincourt JB, Amalric F, Girard JP (February 2000). "Nuclear localization of PAPS synthetase 1: a sulfate activation pathway in the nucleus of eukaryotic cells". FASEB Journal. 14 (2): 345–354. doi:10.1096/fasebj.14.2.345. PMID 10657990. S2CID 9024784.
• Xu ZH, Otterness DM, Freimuth RR, Carlini EJ, Wood TC, Mitchell S, et al. (February 2000). "Human 3'-phosphoadenosine 5'-phosphosulfate synthetase 1 (PAPSS1) and PAPSS2: gene cloning, characterization and chromosomal localization". Biochemical and Biophysical Research Communications. 268 (2): 437–444. doi:10.1006/bbrc.2000.2123. PMID 10679223.
• Fuda H, Shimizu C, Lee YC, Akita H, Strott CA (July 2002). "Characterization and expression of human bifunctional 3'-phosphoadenosine 5'-phosphosulphate synthase isoforms". The Biochemical Journal. 365 (Pt 2): 497–504. doi:10.1042/BJ20020044. PMC 1222679. PMID 11931637.
• Harjes S, Scheidig A, Bayer P (February 2004). "Expression, purification and crystallization of human 3'-phosphoadenosine-5'-phosphosulfate synthetase 1". Acta Crystallographica. Section D, Biological Crystallography. 60 (Pt 2): 350–352. doi:10.1107/S0907444903027628. PMID 14747722.
• Lansdon EB, Fisher AJ, Segel IH (April 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): 4356–4365. doi:10.1021/bi049827m. PMID 15065880.
• Harjes S, Bayer P, Scheidig AJ (April 2005). "The crystal structure of human PAPS synthetase 1 reveals asymmetry in substrate binding". Journal of Molecular Biology. 347 (3): 623–635. doi:10.1016/j.jmb.2005.01.005. PMID 15755455.
• Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, et al. (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–968. 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, Ota T, Nishikawa T, Yamashita R, et al. (January 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Sekulic N, Konrad M, Lavie A (July 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". The Journal of Biological Chemistry. 282 (30): 22112–22121. doi:10.1074/jbc.M701713200. hdl:11858/00-001M-0000-0012-E08D-D. PMID 17540769.

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