PASK

PASK
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1LL8, 3DLS
Identifiers
Aliases	PASK, PASKIN, STK37, PAS domain containing serine/threonine kinase
External IDs	OMIM: 607505 MGI: 2155936 HomoloGene: 9038 GeneCards: PASK
Gene location (Human)
Chr.	Chromosome 2 (human)[1]
End	241,150,264 bp[1]
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)[2]
End	93,343,482 bp[2]
RNA expression pattern
	; ;
	More reference expression data
Gene ontology
Molecular function	• kinase activity; • transferase activity; • nucleotide binding; • protein kinase activity; • GO:0001948 protein binding; • ATP binding; • phosphatidylinositol binding; • lipid binding; • protein serine/threonine kinase activity;
Cellular component	• cell nucleus; • cytosol; • cytoplasm;
Biological process	• regulation of respiratory gaseous exchange; • autophosphorylation; • negative regulation of glycogen biosynthetic process; • positive regulation of translation; • regulation of glucagon secretion; • phosphorylation; • protein phosphorylation; • energy homeostasis; • GO:0007243 intracellular signal transduction;
	Sources:Amigo / QuickGO
Orthologs
	23178
	269224
	ENSG00000115687
	ENSMUSG00000026274
	Q96RG2
	Q8CEE6
	NM_001252119; NM_001252120; NM_001252122; NM_001252124; NM_015148
	NM_080850
	NP_001239048; NP_001239049; NP_001239051; NP_001239053; NP_055963
	NP_543126
	Wikidata
View/Edit Human	View/Edit Mouse

PAS domain-containing serine/threonine-protein kinase is an enzyme that in humans is encoded by the PASK gene.[5][6][7][8]

PAS domains regulate the function of many intracellular signaling pathways in response to both extrinsic and intrinsic stimuli. PASK is an evolutionarily conserved protein present in yeast, flies, and mammals.[supplied by OMIM][8]

References

GRCh38: Ensembl release 89: ENSG00000115687 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000026274 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Hofer T, Spielmann P, Stengel P, Stier B, Katschinski DM, Desbaillets I, Gassmann M, Wenger RH (Nov 2001). "Mammalian PASKIN, a PAS-serine/threonine kinase related to bacterial oxygen sensors" (PDF). Biochem Biophys Res Commun. 288 (4): 757–64. doi:10.1006/bbrc.2001.5840. PMID 11688972.
Rutter J, Michnoff CH, Harper SM, Gardner KH, McKnight SL (Aug 2001). "PAS kinase: an evolutionarily conserved PAS domain-regulated serine/threonine kinase". Proc Natl Acad Sci U S A. 98 (16): 8991–6. doi:10.1073/pnas.161284798. PMC 55361. PMID 11459942.
da Silva Xavier G, Rutter J, Rutter GA (Jun 2004). "Involvement of Per-Arnt-Sim (PAS) kinase in the stimulation of preproinsulin and pancreatic duodenum homeobox 1 gene expression by glucose". Proc Natl Acad Sci U S A. 101 (22): 8319–24. doi:10.1073/pnas.0307737101. PMC 420392. PMID 15148392.
"Entrez Gene: PASK PAS domain containing serine/threonine kinase".

Nakajima D, Okazaki N, Yamakawa H, et al. (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Res. 9 (3): 99–106. doi:10.1093/dnares/9.3.99. PMID 12168954.
Nagase T, Seki N, Tanaka A, et al. (1996). "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1". DNA Res. 2 (4): 167–74, 199–210. doi:10.1093/dnares/2.4.167. PMID 8590280.
Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
Ceulemans H, Van Eynde A, Pérez-Callejón E, et al. (1999). "Structure and splice products of the human gene encoding sds22, a putative mitotic regulator of protein phosphatase-1". Eur. J. Biochem. 262 (1): 36–42. doi:10.1046/j.1432-1327.1999.00344.x. PMID 10231361.
Amezcua CA, Harper SM, Rutter J, Gardner KH (2003). "Structure and interactions of PAS kinase N-terminal PAS domain: model for intramolecular kinase regulation". Structure. 10 (10): 1349–61. doi:10.1016/S0969-2126(02)00857-2. PMID 12377121.
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.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
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.
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.
Eckhardt K, Troger J, Reissmann J, et al. (2007). "Male germ cell expression of the PAS domain kinase PASKIN and its novel target eukaryotic translation elongation factor eEF1A1". Cell. Physiol. Biochem. 20 (1–4): 227–40. doi:10.1159/000104169. PMID 17595531.
Kikani CK, Antonysamy SA, Bonanno JB, et al. (2010). "Structural bases of PAS domain-regulated kinase (PASK) activation in the absence of activation loop phosphorylation". J. Biol. Chem. 285 (52): 41034–43. doi:10.1074/jbc.M110.157594. PMC 3003402. PMID 20943661.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000115687 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000026274 - 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.

[pmid11688972-5] Hofer T, Spielmann P, Stengel P, Stier B, Katschinski DM, Desbaillets I, Gassmann M, Wenger RH (Nov 2001). "Mammalian PASKIN, a PAS-serine/threonine kinase related to bacterial oxygen sensors" (PDF). Biochem Biophys Res Commun. 288 (4): 757–64. doi:10.1006/bbrc.2001.5840. PMID 11688972.

[pmid11459942-6] Rutter J, Michnoff CH, Harper SM, Gardner KH, McKnight SL (Aug 2001). "PAS kinase: an evolutionarily conserved PAS domain-regulated serine/threonine kinase". Proc Natl Acad Sci U S A. 98 (16): 8991–6. doi:10.1073/pnas.161284798. PMC 55361. PMID 11459942.

[pmid15148392-7] Silva Xavier G, Rutter J, Rutter GA (Jun 2004). "Involvement of Per-Arnt-Sim (PAS) kinase in the stimulation of preproinsulin and pancreatic duodenum homeobox 1 gene expression by glucose". Proc Natl Acad Sci U S A. 101 (22): 8319–24. doi:10.1073/pnas.0307737101. PMC 420392. PMID 15148392.

[entrez-8] "Entrez Gene: PASK PAS domain containing serine/threonine kinase".

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

PASK

References

Further reading