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{{Infobox_gene}}
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'''5'-AMP-activated protein kinase subunit beta-1''' is an [[enzyme]] that in humans is encoded by the ''PRKAB1'' [[gene]].<ref name="pmid8557660">{{cite journal |vauthors=Stapleton D, Mitchelhill KI, Gao G, Widmer J, Michell BJ, Teh T, House CM, Fernandez CS, Cox T, Witters LA, Kemp BE | title = Mammalian AMP-activated protein kinase subfamily | journal = J Biol Chem | volume = 271 | issue = 2 | pages = 611–4 |date=February 1996 | pmid = 8557660 | pmc =  | doi =10.1074/jbc.271.2.611 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PRKAB1 protein kinase, AMP-activated, beta 1 non-catalytic subunit| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5564| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
 
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PRKAB1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1z0m.
| PDB = {{PDB2|1z0m}}, {{PDB2|1z0n}}
| Name = Protein kinase, AMP-activated, beta 1 non-catalytic subunit
| HGNCid = 9378
| Symbol = PRKAB1
| AltSymbols =; AMPK; HAMPKb; MGC17785
| OMIM = 602740
| ECnumber =
| Homologene = 38160
| MGIid = 1336167
  | GeneAtlas_image1 = PBB_GE_PRKAB1_201835_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PRKAB1_201834_at_tn.png
| Function = {{GNF_GO|id=GO:0004553 |text = hydrolase activity, hydrolyzing O-glycosyl compounds}}
  | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}  
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0006633 |text = fatty acid biosynthetic process}} {{GNF_GO|id=GO:0007165 |text = signal transduction}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5564
    | Hs_Ensembl = ENSG00000111725
    | Hs_RefseqProtein = NP_006244
    | Hs_RefseqmRNA = NM_006253
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 118590144
    | Hs_GenLoc_end = 118603799
    | Hs_Uniprot = Q9Y478
    | Mm_EntrezGene = 19079
    | Mm_Ensembl = ENSMUSG00000029513
    | Mm_RefseqmRNA = NM_031869
    | Mm_RefseqProtein = NP_114075
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 116274585
    | Mm_GenLoc_end = 116285427
    | Mm_Uniprot = Q3U5I9
  }}
}}
'''Protein kinase, AMP-activated, beta 1 non-catalytic subunit''', also known as '''PRKAB1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRKAB1 protein kinase, AMP-activated, beta 1 non-catalytic subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5564| accessdate = }}</ref>


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{{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. The myristoylation and phosphorylation of this subunit have been shown to affect the enzyme activity and cellular localization of AMPK. This subunit may also serve as an adaptor molecule mediating the association of the AMPK complex.<ref name="entrez">{{cite web | title = Entrez Gene: PRKAB1 protein kinase, AMP-activated, beta 1 non-catalytic subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5564| accessdate = }}</ref>
| 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. The myristoylation and phosphorylation of this subunit have been shown to affect the enzyme activity and cellular localization of AMPK. This subunit may also serve as an adaptor molecule mediating the association of the AMPK complex.<ref name="entrez"/>
}}
 
==Model organisms==
{| class="wikitable sortable collapsible collapsed" border="1" cellpadding="2" style="float: right;" |
|+ ''Prkab1'' knockout mouse phenotype
|-
! Characteristic!! Phenotype
|-
| [[Homozygote]] viability || bgcolor="#488ED3"|Normal
|-
| [[Recessive]] lethal study || bgcolor="#488ED3"|Normal
|-
| Fertility || bgcolor="#488ED3"|Normal
|-
| Body weight || bgcolor="#488ED3"|Normal
|-
| [[Open Field (animal test)|Anxiety]] || bgcolor="#488ED3"|Normal
|-
| Neurological assessment || bgcolor="#488ED3"|Normal
|-
| Grip strength || bgcolor="#488ED3"|Normal
|-
| [[Hot plate test|Hot plate]] || bgcolor="#488ED3"|Normal
|-
| [[Dysmorphology]] || bgcolor="#488ED3"|Normal
|-
| [[Indirect calorimetry]] || bgcolor="#488ED3"|Normal
|-
| [[Glucose tolerance test]] || bgcolor="#C40000"|Abnormal<ref name="Glucose tolerance test">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MAVE/glucose-tolerance-ip/ |title=Glucose tolerance test data for Prkab1 |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| [[Auditory brainstem response]] || bgcolor="#488ED3"|Normal
|-
| [[Dual-energy X-ray absorptiometry|DEXA]] || bgcolor="#488ED3"|Normal
|-
| [[Radiography]] || bgcolor="#488ED3"|Normal
|-
| Body temperature || bgcolor="#488ED3"|Normal
|-
| Eye morphology || bgcolor="#488ED3"|Normal
|-
| [[Clinical chemistry]] || bgcolor="#C40000"|Abnormal<ref name="Clinical chemistry">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MAVE/plasma-chemistry/ |title=Clinical chemistry data for Prkab1 |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| [[Blood plasma|Plasma]] [[immunoglobulin]]s || bgcolor="#C40000"|Abnormal
|-
| [[Haematology]] || bgcolor="#C40000"|Abnormal<ref name="Haematology">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MAVE/haematology-cbc/ |title=Haematology data for Prkab1 |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| [[Peripheral blood lymphocyte]]s || bgcolor="#488ED3"|Normal
|-
| [[Micronucleus test]] || bgcolor="#488ED3"|Normal
|-
| Heart weight || bgcolor="#488ED3"|Normal
|-
| Eye Histopathology || bgcolor="#488ED3"|Normal
|-
| ''[[Salmonella]]'' infection || bgcolor="#488ED3"|Normal<ref name="''Salmonella'' infection">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MAVE/salmonella-challenge/ |title=''Salmonella'' infection data for Prkab1 |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| ''[[Citrobacter]]'' infection || bgcolor="#488ED3"|Normal<ref name="''Citrobacter'' infection">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MAVE/citrobacter-challenge/ |title=''Citrobacter'' infection data for Prkab1 |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| colspan=2; style="text-align: center;" | All tests and analysis from<ref name="mgp_reference">{{cite journal | doi = 10.1111/j.1755-3768.2010.4142.x | title = The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice | year = 2010 | author = Gerdin AK | journal = Acta Ophthalmologica | volume = 88 | pages =  925–7 }}</ref><ref>[http://www.sanger.ac.uk/mouseportal/ Mouse Resources Portal], Wellcome Trust Sanger Institute.</ref>
|}
[[Model organism]]s have been used in the study of PRKAB1 function. A conditional [[knockout mouse]] line, called ''Prkab1<sup>tm1a(KOMP)Wtsi</sup>''<ref name="allele_ref">{{cite web |url=http://www.knockoutmouse.org/martsearch/search?query=Prkab1 |title=International Knockout Mouse Consortium}}</ref><ref name="mgi_allele_ref">{{cite web |url=http://www.informatics.jax.org/searchtool/Search.do?query=MGI:4362414 |title=Mouse Genome Informatics}}</ref> was generated as part of the [[International Knockout Mouse Consortium]] program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.<ref name="pmid21677750">{{Cite journal
| last1 = Skarnes |first1 =W. C.
| doi = 10.1038/nature10163
| last2 = Rosen | first2 = B.
| last3 = West | first3 = A. P.
| last4 = Koutsourakis | first4 = M.
| last5 = Bushell | first5 = W.
| last6 = Iyer | first6 = V.
| last7 = Mujica | first7 = A. O.
| last8 = Thomas | first8 = M.
| last9 = Harrow | first9 = J.
| last10 = Cox | first10 = T.
| last11 = Jackson | first11 = D.
| last12 = Severin | first12 = J.
| last13 = Biggs | first13 = P.
| last14 = Fu | first14 = J.
| last15 = Nefedov | first15 = M.
| last16 = De Jong | first16 = P. J.
| last17 = Stewart | first17 = A. F.
| last18 = Bradley | first18 = A.
| title = A conditional knockout resource for the genome-wide study of mouse gene function
| journal = Nature
| volume = 474
| issue = 7351
| pages = 337–342
| year = 2011
| pmid = 21677750
| pmc =3572410
}}</ref><ref name="mouse_library">{{cite journal | doi = 10.1038/474262a | title = Mouse library set to be knockout | year = 2011 | author = Dolgin E | journal = Nature | volume = 474 | issue = 7351 | pages = 262–3 | pmid = 21677718 }}</ref><ref name="mouse_for_all_reasons">{{cite journal | doi = 10.1016/j.cell.2006.12.018 | title = A Mouse for All Reasons | year = 2007 | journal = Cell | volume = 128 | pages = 9–13 | pmid = 17218247 |vauthors=Collins FS, Rossant J, Wurst W | issue = 1 }}</ref>
 
Male and female animals underwent a standardized [[phenotypic screen]] to determine the effects of deletion.<ref name="mgp_reference" /><ref name="pmid21722353">{{cite journal|vauthors=van der Weyden L, White JK, Adams DJ, Logan DW | title=The mouse genetics toolkit: revealing function and mechanism. | journal=Genome Biol | year= 2011 | volume= 12 | issue= 6 | pages= 224 | pmid=21722353 | doi=10.1186/gb-2011-12-6-224  | pmc=3218837}}</ref> Twenty five tests were carried out on [[mutant]] mice and four significant abnormalities were observed.<ref name="mgp_reference" /> Homozygous mutant males displayed [[impaired glucose tolerance]]. Animals of both sex had increased circulating [[bilirubin]] levels, increased IgG3 levels, and a number of atypical [[haematology]] parameters.<ref name="mgp_reference" />
 
==Interactions==
PRKAB1 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/>
 
The 5'-AMP-activated protein kinase beta subunit interaction domain (AMPKBI) is a conserved domain found in the beta subunit of the 5-AMP-activated protein kinase complex, and its [[Saccharomyces cerevisiae|yeast]] [[Homology (biology)|homologues]] Sip1, Sip2 and Gal83, which are found in the SNF1 kinase [[Protein complex|complex]].<ref name="pmid8621499">{{cite journal |vauthors=Gao G, Fernandez CS, Stapleton D, Auster AS, Widmer J, Dyck JR, Kemp BE, Witters LA | title = Non-catalytic beta- and gamma-subunit isoforms of the 5'-AMP-activated protein kinase | journal = J. Biol. Chem. | volume = 271 | issue = 15 | pages = 8675–81 |date=April 1996 | pmid = 8621499 | doi = 10.1074/jbc.271.15.8675| url = }}</ref> This region is sufficient for interaction of this subunit with the kinase complex, but is not solely responsible for the interaction, and the interaction partner is not known.<ref name="pmid7813428">{{cite journal |vauthors=Yang X, Jiang R, Carlson M | title = A family of proteins containing a conserved domain that mediates interaction with the yeast SNF1 protein kinase complex | journal = EMBO J. | volume = 13 | issue = 24 | pages = 5878–86 |date=December 1994 | pmid = 7813428 | pmc = 395563 | doi = | url = }}</ref>
 
{{Infobox protein family
| Symbol = AMPKBI
| Name = AMPKBI
| image =
| width =
| caption = crystal structure of the adenylate sensor from amp-activated protein kinase complexed with atp
| Pfam = PF04739
| Pfam_clan = 
| InterPro = IPR006828
| SMART =
| PROSITE =
| MEROPS =
| SCOP =
| TCDB =
| OPM family =
| OPM protein =
| CAZy =
| CDD =
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist|33em}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin |33em}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Carling D |title=The AMP-activated protein kinase cascade--a unifying system for energy control. |journal=Trends Biochem. Sci. |volume=29 |issue= 1 |pages= 18-24 |year= 2004 |pmid= 14729328 |doi=  }}
*{{cite journal  | author=Carling D |title=The AMP-activated protein kinase cascade--a unifying system for energy control |journal=Trends Biochem. Sci. |volume=29 |issue= 1 |pages= 18–24 |year= 2004 |pmid= 14729328 |doi=10.1016/j.tibs.2003.11.005 }}
*{{cite journal | author=Stapleton D, Mitchelhill KI, Gao G, ''et al.'' |title=Mammalian AMP-activated protein kinase subfamily. |journal=J. Biol. Chem. |volume=271 |issue= 2 |pages= 611-4 |year= 1996 |pmid= 8557660 |doi= }}
*{{cite journal   |vauthors=Gao G, Fernandez CS, Stapleton D, etal |title=Non-catalytic beta- and gamma-subunit isoforms of the 5'-AMP-activated protein kinase |journal=J. Biol. Chem. |volume=271 |issue= 15 |pages= 8675–81 |year= 1996 |pmid= 8621499 |doi=10.1074/jbc.271.15.8675 }}
*{{cite journal | author=Gao G, Fernandez CS, Stapleton D, ''et al.'' |title=Non-catalytic beta- and gamma-subunit isoforms of the 5'-AMP-activated protein kinase. |journal=J. Biol. Chem. |volume=271 |issue= 15 |pages= 8675-81 |year= 1996 |pmid= 8621499 |doi=  }}
*{{cite journal   |vauthors=Woods A, Cheung PC, Smith FC, etal |title=Characterization of AMP-activated protein kinase beta and gamma subunits. Assembly of the heterotrimeric complex in vitro |journal=J. Biol. Chem. |volume=271 |issue= 17 |pages= 10282–90 |year= 1996 |pmid= 8626596 |doi=  10.1074/jbc.271.48.30517}}
*{{cite journal | author=Woods A, Cheung PC, Smith FC, ''et al.'' |title=Characterization of AMP-activated protein kinase beta and gamma subunits. Assembly of the heterotrimeric complex in vitro. |journal=J. Biol. Chem. |volume=271 |issue= 17 |pages= 10282-90 |year= 1996 |pmid= 8626596 |doi= }}
*{{cite journal   |vauthors=Dyck JR, Gao G, Widmer J, etal |title=Regulation of 5'-AMP-activated protein kinase activity by the noncatalytic beta and gamma subunits |journal=J. Biol. Chem. |volume=271 |issue= 30 |pages= 17798–803 |year= 1996 |pmid= 8663446 |doi=10.1074/jbc.271.30.17798  }}
*{{cite journal | author=Dyck JR, Gao G, Widmer J, ''et al.'' |title=Regulation of 5'-AMP-activated protein kinase activity by the noncatalytic beta and gamma subunits. |journal=J. Biol. Chem. |volume=271 |issue= 30 |pages= 17798-803 |year= 1996 |pmid= 8663446 |doi=  }}
*{{cite journal   |vauthors=Stapleton D, Woollatt E, Mitchelhill KI, etal |title=AMP-activated protein kinase isoenzyme family: subunit structure and chromosomal location |journal=FEBS Lett. |volume=409 |issue= 3 |pages= 452–6 |year= 1997 |pmid= 9224708 |doi=10.1016/S0014-5793(97)00569-3 }}
*{{cite journal | author=Stapleton D, Woollatt E, Mitchelhill KI, ''et al.'' |title=AMP-activated protein kinase isoenzyme family: subunit structure and chromosomal location. |journal=FEBS Lett. |volume=409 |issue= 3 |pages= 452-6 |year= 1997 |pmid= 9224708 |doi= }}
*{{cite journal   |vauthors=Mitchelhill KI, Michell BJ, House CM, etal |title=Posttranslational modifications of the 5'-AMP-activated protein kinase beta1 subunit |journal=J. Biol. Chem. |volume=272 |issue= 39 |pages= 24475–9 |year= 1997 |pmid= 9305909 |doi=10.1074/jbc.272.39.24475  }}
*{{cite journal  | author=Mitchelhill KI, Michell BJ, House CM, ''et al.'' |title=Posttranslational modifications of the 5'-AMP-activated protein kinase beta1 subunit. |journal=J. Biol. Chem. |volume=272 |issue= 39 |pages= 24475-9 |year= 1997 |pmid= 9305909 |doi=  }}
*{{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 | author=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=  }}
*{{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 | author=Cheung PC, Salt IP, Davies SP, ''et al.'' |title=Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding. |journal=Biochem. J. |volume=346 Pt 3 |issue= |pages= 659-69 |year= 2000 |pmid= 10698692 |doi= }}
*{{cite journal   |vauthors=da Silva Xavier G, Leclerc I, Salt IP, etal |title=Role of AMP-activated protein kinase in the regulation by glucose of islet beta cell gene expression |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 8 |pages= 4023–8 |year= 2000 |pmid= 10760274 |doi=10.1073/pnas.97.8.4023  | pmc=18135  }}
*{{cite journal | author=da Silva Xavier G, Leclerc I, Salt IP, ''et al.'' |title=Role of AMP-activated protein kinase in the regulation by glucose of islet beta cell gene expression. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 8 |pages= 4023-8 |year= 2000 |pmid= 10760274 |doi=  }}
*{{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  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |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 }}
*{{cite journal  |vauthors=Lemieux K, Konrad D, Klip A, Marette A |title=The AMP-activated protein kinase activator AICAR does not induce GLUT4 translocation to transverse tubules but stimulates glucose uptake and p38 mitogen-activated protein kinases alpha and beta in skeletal muscle |journal=FASEB J. |volume=17 |issue= 12 |pages= 1658–65 |year= 2003 |pmid= 12958172 |doi= 10.1096/fj.02-1125com }}
*{{cite journal | author=Lemieux K, Konrad D, Klip A, Marette A |title=The AMP-activated protein kinase activator AICAR does not induce GLUT4 translocation to transverse tubules but stimulates glucose uptake and p38 mitogen-activated protein kinases alpha and beta in skeletal muscle. |journal=FASEB J. |volume=17 |issue= 12 |pages= 1658-65 |year= 2003 |pmid= 12958172 |doi= 10.1096/fj.02-1125com }}
*{{cite journal   |vauthors=Landree LE, Hanlon AL, Strong DW, etal |title=C75, a fatty acid synthase inhibitor, modulates AMP-activated protein kinase to alter neuronal energy metabolism |journal=J. Biol. Chem. |volume=279 |issue= 5 |pages= 3817–27 |year= 2004 |pmid= 14615481 |doi= 10.1074/jbc.M310991200 }}
*{{cite journal  | author=Landree LE, Hanlon AL, Strong DW, ''et al.'' |title=C75, a fatty acid synthase inhibitor, modulates AMP-activated protein kinase to alter neuronal energy metabolism. |journal=J. Biol. Chem. |volume=279 |issue= 5 |pages= 3817-27 |year= 2004 |pmid= 14615481 |doi= 10.1074/jbc.M310991200 }}
*{{cite journal  |vauthors=Inoki K, Zhu T, Guan KL |title=TSC2 mediates cellular energy response to control cell growth and survival |journal=Cell |volume=115 |issue= 5 |pages= 577–90 |year= 2004 |pmid= 14651849 |doi=10.1016/S0092-8674(03)00929-2  }}
*{{cite journal | author=Inoki K, Zhu T, Guan KL |title=TSC2 mediates cellular energy response to control cell growth and survival. |journal=Cell |volume=115 |issue= 5 |pages= 577-90 |year= 2004 |pmid= 14651849 |doi= }}
*{{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 | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |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=Andersson U, Filipsson K, Abbott CR, etal |title=AMP-activated protein kinase plays a role in the control of food intake |journal=J. Biol. Chem. |volume=279 |issue= 13 |pages= 12005–8 |year= 2004 |pmid= 14742438 |doi= 10.1074/jbc.C300557200 }}
*{{cite journal  | author=Andersson U, Filipsson K, Abbott CR, ''et al.'' |title=AMP-activated protein kinase plays a role in the control of food intake. |journal=J. Biol. Chem. |volume=279 |issue= 13 |pages= 12005-8 |year= 2004 |pmid= 14742438 |doi= 10.1074/jbc.C300557200 }}
*{{cite journal  |vauthors=Pilon G, Dallaire P, Marette A |title=Inhibition of inducible nitric-oxide synthase by activators of AMP-activated protein kinase: a new mechanism of action of insulin-sensitizing drugs |journal=J. Biol. Chem. |volume=279 |issue= 20 |pages= 20767–74 |year= 2004 |pmid= 14985344 |doi= 10.1074/jbc.M401390200 }}
*{{cite journal | author=Pilon G, Dallaire P, Marette A |title=Inhibition of inducible nitric-oxide synthase by activators of AMP-activated protein kinase: a new mechanism of action of insulin-sensitizing drugs. |journal=J. Biol. Chem. |volume=279 |issue= 20 |pages= 20767-74 |year= 2004 |pmid= 14985344 |doi= 10.1074/jbc.M401390200 }}
*{{cite journal   |vauthors=Shaw RJ, Kosmatka M, Bardeesy N, etal |title=The tumor suppressor LKB1 kinase directly activates AMP-activated kinase and regulates apoptosis in response to energy stress |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 10 |pages= 3329–35 |year= 2004 |pmid= 14985505 |doi= 10.1073/pnas.0308061100 | pmc=373461 }}
*{{cite journal | author=Shaw RJ, Kosmatka M, Bardeesy N, ''et al.'' |title=The tumor suppressor LKB1 kinase directly activates AMP-activated kinase and regulates apoptosis in response to energy stress. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 10 |pages= 3329-35 |year= 2004 |pmid= 14985505 |doi= 10.1073/pnas.0308061100 }}
*{{cite journal   |vauthors=Kim EK, Miller I, Aja S, etal |title=C75, a fatty acid synthase inhibitor, reduces food intake via hypothalamic AMP-activated protein kinase |journal=J. Biol. Chem. |volume=279 |issue= 19 |pages= 19970–6 |year= 2004 |pmid= 15028725 |doi= 10.1074/jbc.M402165200 }}
*{{cite journal | author=Kim EK, Miller I, Aja S, ''et al.'' |title=C75, a fatty acid synthase inhibitor, reduces food intake via hypothalamic AMP-activated protein kinase. |journal=J. Biol. Chem. |volume=279 |issue= 19 |pages= 19970-6 |year= 2004 |pmid= 15028725 |doi= 10.1074/jbc.M402165200 }}
}}
}}
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{{InterPro content|IPR006828}}
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[[Category:Genes mutated in mice]]
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[[Category:EC 2.7.11]]

Revision as of 18:40, 7 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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n/a

RefSeq (protein)

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Location (UCSC)n/an/a
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View/Edit Human

5'-AMP-activated protein kinase subunit beta-1 is an enzyme that in humans is encoded by the PRKAB1 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. The myristoylation and phosphorylation of this subunit have been shown to affect the enzyme activity and cellular localization of AMPK. This subunit may also serve as an adaptor molecule mediating the association of the AMPK complex.[2]

Model organisms

Model organisms have been used in the study of PRKAB1 function. A conditional knockout mouse line, called Prkab1tm1a(KOMP)Wtsi[10][11] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[12][13][14]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[8][15] Twenty five tests were carried out on mutant mice and four significant abnormalities were observed.[8] Homozygous mutant males displayed impaired glucose tolerance. Animals of both sex had increased circulating bilirubin levels, increased IgG3 levels, and a number of atypical haematology parameters.[8]

Interactions

PRKAB1 has been shown to interact with PRKAG2[16] and PRKAG1.[16]

The 5'-AMP-activated protein kinase beta subunit interaction domain (AMPKBI) is a conserved domain found in the beta subunit of the 5-AMP-activated protein kinase complex, and its yeast homologues Sip1, Sip2 and Gal83, which are found in the SNF1 kinase complex.[17] This region is sufficient for interaction of this subunit with the kinase complex, but is not solely responsible for the interaction, and the interaction partner is not known.[18]

AMPKBI
Identifiers
SymbolAMPKBI
PfamPF04739
InterProIPR006828

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: PRKAB1 protein kinase, AMP-activated, beta 1 non-catalytic subunit".
  3. "Glucose tolerance test data for Prkab1". Wellcome Trust Sanger Institute.
  4. "Clinical chemistry data for Prkab1". Wellcome Trust Sanger Institute.
  5. "Haematology data for Prkab1". Wellcome Trust Sanger Institute.
  6. "Salmonella infection data for Prkab1". Wellcome Trust Sanger Institute.
  7. "Citrobacter infection data for Prkab1". Wellcome Trust Sanger Institute.
  8. 8.0 8.1 8.2 8.3 Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
  9. Mouse Resources Portal, Wellcome Trust Sanger Institute.
  10. "International Knockout Mouse Consortium".
  11. "Mouse Genome Informatics".
  12. Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M.; Harrow, J.; Cox, T.; Jackson, D.; Severin, J.; Biggs, P.; Fu, J.; Nefedov, M.; De Jong, P. J.; Stewart, A. F.; Bradley, A. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  13. Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  14. Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
  15. van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biol. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
  16. 16.0 16.1 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.
  17. Gao G, Fernandez CS, Stapleton D, Auster AS, Widmer J, Dyck JR, Kemp BE, Witters LA (April 1996). "Non-catalytic beta- and gamma-subunit isoforms of the 5'-AMP-activated protein kinase". J. Biol. Chem. 271 (15): 8675–81. doi:10.1074/jbc.271.15.8675. PMID 8621499.
  18. Yang X, Jiang R, Carlson M (December 1994). "A family of proteins containing a conserved domain that mediates interaction with the yeast SNF1 protein kinase complex". EMBO J. 13 (24): 5878–86. PMC 395563. PMID 7813428.

Further reading

This article incorporates text from the public domain Pfam and InterPro: IPR006828