PRKAB2: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
m (Bot: HTTP→HTTPS)
imported>Contributor8472
m (Added links)
 
Line 5: Line 5:
{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = The protein encoded by this gene is a regulatory subunit of the [[AMP-activated protein kinase]] (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. This subunit may be a positive regulator of AMPK activity. It is highly expressed in skeletal muscle and thus may have tissue-specific roles.<ref name="entrez"/>
| summary_text = The protein encoded by this gene is a regulatory subunit of the [[AMP-activated protein kinase]] (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus [[phosphorylation|phosphorylates]] and inactivates [[acetyl-CoA carboxylase]] (ACC) and [[HMG-CoA reductase|beta-hydroxy beta-methylglutaryl-CoA reductase]] (HMGCR), key enzymes involved in regulating de novo biosynthesis of [[fatty acid]] and [[cholesterol]]. This subunit may be a positive regulator of AMPK activity. It is highly expressed in skeletal muscle and thus may have tissue-specific roles.<ref name="entrez"/>
}}
}}


Line 15: Line 15:
PRKAB2 has been shown to [[Protein-protein interaction|interact]] with [[PRKAG2]]<ref name=pmid10698692>{{cite journal |last=Cheung |first=P C |authorlink= |author2=Salt I P |author3=Davies S P |author4=Hardie D G |author5=Carling D  |date=March 2000  |title=Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding |journal=Biochem. J. |volume=346 |issue= 3|pages=659–69 |publisher= |location = ENGLAND| issn = 0264-6021| pmid = 10698692 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=1220898 | doi=10.1042/0264-6021:3460659}}</ref> and [[PRKAG1]].<ref name=pmid10698692/>
PRKAB2 has been shown to [[Protein-protein interaction|interact]] with [[PRKAG2]]<ref name=pmid10698692>{{cite journal |last=Cheung |first=P C |authorlink= |author2=Salt I P |author3=Davies S P |author4=Hardie D G |author5=Carling D  |date=March 2000  |title=Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding |journal=Biochem. J. |volume=346 |issue= 3|pages=659–69 |publisher= |location = ENGLAND| issn = 0264-6021| pmid = 10698692 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=1220898 | doi=10.1042/0264-6021:3460659}}</ref> and [[PRKAG1]].<ref name=pmid10698692/>


Research on the genes [[CHD1L]] and PRKAB2 within [[lymphoblast]] cells<ref name="pmid21824431">{{cite journal |vauthors=Harvard C, Strong E, Mercier E, Colnaghi R, Alcantara D, Chow E, Martell S, Tyson C, Hrynchak M, McGillivray B, Hamilton S, Marles S, Mhanni A, Dawson AJ, Pavlidis P, Qiao Y, Holden JJ, Lewis SM, O'Driscoll M, Rajcan-Separovic E | title = Understanding the impact of 1q21.1 copy number variant | journal = Orphanet J Rare Dis | volume = 6 | issue = | pages = 54 | year = 2011 | pmid = 21824431 | pmc = 3180300 | doi = 10.1186/1750-1172-6-54 }}</ref> lead to the conclusion that anomalies appear with the [[1q21.1-deletionsyndrome]]:  
Research on the genes [[CHD1L]] and PRKAB2 within [[lymphoblast]] cells<ref name="pmid21824431">{{cite journal |vauthors=Harvard C, Strong E, Mercier E, Colnaghi R, Alcantara D, Chow E, Martell S, Tyson C, Hrynchak M, McGillivray B, Hamilton S, Marles S, Mhanni A, Dawson AJ, Pavlidis P, Qiao Y, Holden JJ, Lewis SM, O'Driscoll M, Rajcan-Separovic E | title = Understanding the impact of 1q21.1 copy number variant | journal = Orphanet J Rare Dis | volume = 6 | issue = | pages = 54 | year = 2011 | pmid = 21824431 | pmc = 3180300 | doi = 10.1186/1750-1172-6-54 }}</ref> lead to the conclusion that anomalies appear with the [[1q21.1 deletion syndrome]]:  
* [[CHD1L]] is an enzyme which is involved in untangling the [[chromatid]]es and the DNA repair system. With 1q21.1 deletion syndrome a disturbance occurs, which leads to increased DNA breaks. The role of CHD1L is similar to that of [[helicase]] with the [[Werner syndrome]]
* [[CHD1L]] is an enzyme which is involved in untangling the [[chromatid]]s and the DNA repair system. With 1q21.1 deletion syndrome a disturbance occurs, which leads to increased DNA breaks. The role of CHD1L is similar to that of [[helicase]] with the [[Werner syndrome]]
* PRKAB2 is involved in maintaining the energy level of cells. With 1q21.1-deletion syndrome this function was attenuated.
* PRKAB2 is involved in maintaining the energy level of cells. With 1q21.1-deletion syndrome this function was attenuated.


Line 32: Line 32:
*{{cite journal  |vauthors=Thornton C, Snowden MA, Carling D |title=Identification of a novel AMP-activated protein kinase beta subunit isoform that is highly expressed in skeletal muscle |journal=J. Biol. Chem. |volume=273 |issue= 20 |pages= 12443–50 |year= 1998 |pmid= 9575201 |doi=10.1074/jbc.273.20.12443  }}
*{{cite journal  |vauthors=Thornton C, Snowden MA, Carling D |title=Identification of a novel AMP-activated protein kinase beta subunit isoform that is highly expressed in skeletal muscle |journal=J. Biol. Chem. |volume=273 |issue= 20 |pages= 12443–50 |year= 1998 |pmid= 9575201 |doi=10.1074/jbc.273.20.12443  }}
*{{cite journal  |vauthors=Cheung PC, Salt IP, Davies SP, etal |title=Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding |journal=Biochem. J. |volume=346 |issue=  3|pages= 659–69 |year= 2000 |pmid= 10698692 |doi=10.1042/0264-6021:3460659  | pmc=1220898  }}
*{{cite journal  |vauthors=Cheung PC, Salt IP, Davies SP, etal |title=Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding |journal=Biochem. J. |volume=346 |issue=  3|pages= 659–69 |year= 2000 |pmid= 10698692 |doi=10.1042/0264-6021:3460659  | pmc=1220898  }}
*{{cite journal  |vauthors=Xu XR, Huang J, Xu ZG, etal |title=Insight into hepatocellular carcinogenesis at transcriptome level by comparing gene expression profiles of hepatocellular carcinoma with those of corresponding noncancerous liver |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 26 |pages= 15089–94 |year= 2002 |pmid= 11752456 |doi= 10.1073/pnas.241522398  | pmc=64988 }}
*{{cite journal  |vauthors=Xu XR, Huang J, Xu ZG, etal |title=Insight into hepatocellular carcinogenesis at transcriptome level by comparing gene expression profiles of hepatocellular carcinoma with those of corresponding noncancerous liver |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 26 |pages= 15089–94 |year= 2002 |pmid= 11752456 |doi= 10.1073/pnas.241522398  | pmc=64988 |bibcode=2001PNAS...9815089X }}
*{{cite journal  |vauthors=Park SH, Paulsen SR, Gammon SR, etal |title=Effects of thyroid state on AMP-activated protein kinase and acetyl-CoA carboxylase expression in muscle |journal=J. Appl. Physiol. |volume=93 |issue= 6 |pages= 2081–8 |year= 2003 |pmid= 12433937 |doi= 10.1152/japplphysiol.00504.2002 }}
*{{cite journal  |vauthors=Park SH, Paulsen SR, Gammon SR, etal |title=Effects of thyroid state on AMP-activated protein kinase and acetyl-CoA carboxylase expression in muscle |journal=J. Appl. Physiol. |volume=93 |issue= 6 |pages= 2081–8 |year= 2003 |pmid= 12433937 |doi= 10.1152/japplphysiol.00504.2002 }}
*{{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=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 |bibcode=2002PNAS...9916899M }}
*{{cite journal  |vauthors=Prochazka M, Farook VS, Ossowski V, etal |title=Variant screening of PRKAB2, a type 2 diabetes mellitus susceptibility candidate gene on 1q in Pima Indians |journal=Mol. Cell. Probes |volume=16 |issue= 6 |pages= 421–7 |year= 2003 |pmid= 12490143 |doi=10.1006/mcpr.2002.0439  }}
*{{cite journal  |vauthors=Prochazka M, Farook VS, Ossowski V, etal |title=Variant screening of PRKAB2, a type 2 diabetes mellitus susceptibility candidate gene on 1q in Pima Indians |journal=Mol. Cell. Probes |volume=16 |issue= 6 |pages= 421–7 |year= 2003 |pmid= 12490143 |doi=10.1006/mcpr.2002.0439  }}
*{{cite journal  |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  |vauthors=Minokoshi Y, Alquier T, Furukawa N, etal |title=AMP-kinase regulates food intake by responding to hormonal and nutrient signals in the hypothalamus |journal=Nature |volume=428 |issue= 6982 |pages= 569–74 |year= 2004 |pmid= 15058305 |doi= 10.1038/nature02440 }}
*{{cite journal  |vauthors=Minokoshi Y, Alquier T, Furukawa N, etal |title=AMP-kinase regulates food intake by responding to hormonal and nutrient signals in the hypothalamus |journal=Nature |volume=428 |issue= 6982 |pages= 569–74 |year= 2004 |pmid= 15058305 |doi= 10.1038/nature02440 |bibcode=2004Natur.428..569M }}
*{{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=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=Kimura K, Wakamatsu A, Suzuki Y, etal |title=Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406  | pmc=1356129 }}
*{{cite journal  |vauthors=Kimura K, Wakamatsu A, Suzuki Y, etal |title=Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes |journal=Genome Res. |volume=16 |issue= 1 |pages= 55–65 |year= 2006 |pmid= 16344560 |doi= 10.1101/gr.4039406  | pmc=1356129 }}
*{{cite journal  |vauthors=Gregory SG, Barlow KF, McLay KE, etal |title=The DNA sequence and biological annotation of human chromosome 1 |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 }}
*{{cite journal  |vauthors=Gregory SG, Barlow KF, McLay KE, etal |title=The DNA sequence and biological annotation of human chromosome 1 |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 |bibcode=2006Natur.441..315G }}
*{{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=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 }}
}}
}}

Latest revision as of 01:41, 28 June 2018

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

5'-AMP-activated protein kinase subunit beta-2 is an enzyme that in humans is encoded by the PRKAB2 gene.[1][2]

The protein encoded by this gene is a regulatory subunit of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status. In response to cellular metabolic stresses, AMPK is activated, and thus phosphorylates and inactivates acetyl-CoA carboxylase (ACC) and beta-hydroxy beta-methylglutaryl-CoA reductase (HMGCR), key enzymes involved in regulating de novo biosynthesis of fatty acid and cholesterol. This subunit may be a positive regulator of AMPK activity. It is highly expressed in skeletal muscle and thus may have tissue-specific roles.[2]

Related gene problems

Interactions

PRKAB2 has been shown to interact with PRKAG2[3] and PRKAG1.[3]

Research on the genes CHD1L and PRKAB2 within lymphoblast cells[4] lead to the conclusion that anomalies appear with the 1q21.1 deletion syndrome:

  • CHD1L is an enzyme which is involved in untangling the chromatids and the DNA repair system. With 1q21.1 deletion syndrome a disturbance occurs, which leads to increased DNA breaks. The role of CHD1L is similar to that of helicase with the Werner syndrome
  • PRKAB2 is involved in maintaining the energy level of cells. With 1q21.1-deletion syndrome this function was attenuated.

References

  1. ↑ Stapleton D, Mitchelhill KI, Gao G, Widmer J, Michell BJ, Teh T, House CM, Fernandez CS, Cox T, Witters LA, Kemp BE (February 1996). "Mammalian AMP-activated protein kinase subfamily". J Biol Chem. 271 (2): 611–4. doi:10.1074/jbc.271.2.611. PMID 8557660.
  2. ↑ 2.0 2.1 "Entrez Gene: PRKAB2 protein kinase, AMP-activated, beta 2 non-catalytic subunit".
  3. ↑ 3.0 3.1 Cheung, P C; Salt I P; Davies S P; Hardie D G; Carling D (March 2000). "Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding". Biochem. J. ENGLAND. 346 (3): 659–69. doi:10.1042/0264-6021:3460659. ISSN 0264-6021. PMC 1220898. PMID 10698692.
  4. ↑ Harvard C, Strong E, Mercier E, Colnaghi R, Alcantara D, Chow E, Martell S, Tyson C, Hrynchak M, McGillivray B, Hamilton S, Marles S, Mhanni A, Dawson AJ, Pavlidis P, Qiao Y, Holden JJ, Lewis SM, O'Driscoll M, Rajcan-Separovic E (2011). "Understanding the impact of 1q21.1 copy number variant". Orphanet J Rare Dis. 6: 54. doi:10.1186/1750-1172-6-54. PMC 3180300. PMID 21824431.

Further reading


Retrieved from "https://www.wikidoc.org/index.php?title=PRKAB2&oldid=1530971"