Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  5'-AMP-activated protein kinase subunit beta-1  

UniProtKB / Swiss-Prot ID :  AAKB1_RAT

Gene Name (Synonyms) : 
Prkab1  

Species :  Rattus norvegicus (Rat). 

Subcellular Localization :   

Protein Function :  Non-catalytic subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Beta non-catalytic subunit acts as a scaffold on which the AMPK complex assembles, via its C-terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits (PRKAG1, PRKAG2 or PRKAG3). 

Protein Sequence MGNTSSERAALERQAGHKTPRRDSSGGTKDGDRPKILMDSPEDADIFHTEEMKAPEKEEFLAWQHDLEVN...
Predicted Secondary Structure CCCCCCHHHHHHHHCCCCCCCCCCCCCCCCCCCCCEECCCCCCCCCCCCCHHCCCHHHHHHHHHHCCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-myristoyl glycine.---MGNTSS
---CCCCCC
46.23UniProtKB
Link-
24PhosphoserinePRRDSSGGT
CCCCCCCCC
29.13Phosphositeplus
Link-
24Phosphoserine (AMPK_group)PRRDSSGGT
CCCCCCCCC
29.13PhosphoELM
Link-
24Phosphoserine; by autocatalysis.PRRDSSGGT
CCCCCCCCC
29.13UniProtKB
Link-
25PhosphoserineRRDSSGGTK
CCCCCCCCC
45.60Phosphositeplus
Link-
25Phosphoserine (AMPK_group)RRDSSGGTK
CCCCCCCCC
45.60PhosphoELM
Link-
25Phosphoserine; by autocatalysis.RRDSSGGTK
CCCCCCCCC
45.60UniProtKB
Link-
96PhosphoserineYLSGSFNNW
EEEEEECCE
22.79Phosphositeplus
Link
96Phosphoserine.YLSGSFNNW
EEEEEECCE
22.79UniProtKB
Link
101PhosphoserineFNNWSKLPL
ECCEEECCC
26.83Phosphositeplus
Link
101Phosphoserine.FNNWSKLPL
ECCEEECCC
26.83UniProtKB
Link
108PhosphoserinePLTRSQNNF
CCCCCCCCE
31.83Phosphositeplus
Link
108Phosphoserine (AMPK_group)PLTRSQNNF
CCCCCCCCE
31.83PhosphoELM
Link
108Phosphoserine; by autocatalysis.PLTRSQNNF
CCCCCCCCE
31.83UniProtKB
Link
182PhosphoserineELSSSPPGP
CCCCCCCCC
31.57Phosphositeplus
Link-
182Phosphoserine.ELSSSPPGP
CCCCCCCCC
31.57UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Myristoylation
ReferencePubMed
"Posttranslational modifications of the 5'-AMP-activated proteinkinase beta1 subunit.";
Mitchelhill K.I., Michell B.J., House C.M., Stapleton D., Dyck J.,Gamble J., Ullrich C., Witters L.A., Kemp B.E.;
J. Biol. Chem. 272:24475-24479(1997).
Cited for: PARTIAL PROTEIN SEQUENCE, MYRISTOYLATION AT GLY-2, AND PHOSPHORYLATIONAT SER-24; SER-25; SER-108 AND SER-182.
"Post-translational modifications of the beta-1 subunit of AMP-activated protein kinase affect enzyme activity and cellularlocalization.";
Warden S.M., Richardson C., O'Donnell J. Jr., Stapleton D., Kemp B.E.,Witters L.A.;
Biochem. J. 354:275-283(2001).
Cited for: MUTAGENESIS, MYRISTOYLATION AT GLY-2, AND PHOSPHORYLATION AT SER-24;SER-25; SER-108 AND SER-182.
Phosphorylation
ReferencePubMed
"Posttranslational modifications of the 5'-AMP-activated proteinkinase beta1 subunit.";
Mitchelhill K.I., Michell B.J., House C.M., Stapleton D., Dyck J.,Gamble J., Ullrich C., Witters L.A., Kemp B.E.;
J. Biol. Chem. 272:24475-24479(1997).
Cited for: PARTIAL PROTEIN SEQUENCE, MYRISTOYLATION AT GLY-2, AND PHOSPHORYLATIONAT SER-24; SER-25; SER-108 AND SER-182.
"Post-translational modifications of the beta-1 subunit of AMP-activated protein kinase affect enzyme activity and cellularlocalization.";
Warden S.M., Richardson C., O'Donnell J. Jr., Stapleton D., Kemp B.E.,Witters L.A.;
Biochem. J. 354:275-283(2001).
Cited for: MUTAGENESIS, MYRISTOYLATION AT GLY-2, AND PHOSPHORYLATION AT SER-24;SER-25; SER-108 AND SER-182.
"Identification of phosphorylation sites in AMP-activated proteinkinase (AMPK) for upstream AMPK kinases and study of their roles bysite-directed mutagenesis.";
Woods A., Vertommen D., Neumann D., Turk R., Bayliss J.,Schlattner U., Wallimann T., Carling D., Rider M.H.;
J. Biol. Chem. 278:28434-28442(2003).
Cited for: PHOSPHORYLATION AT SER-96; SER-101 AND SER-108.
"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS.";
Moser K., White F.M.;
J. Proteome Res. 5:98-104(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures