AAKB1_RAT - dbPTM
AAKB1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AAKB1_RAT
UniProt AC P80386
Protein Name 5'-AMP-activated protein kinase subunit beta-1
Gene Name Prkab1
Organism Rattus norvegicus (Rat).
Sequence Length 270
Subcellular Localization
Protein Description 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 MGNTSSERAALERQAGHKTPRRDSSGGTKDGDRPKILMDSPEDADIFHTEEMKAPEKEEFLAWQHDLEVNEKAPAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRSQNNFVAILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVKKTDFEVFDALMVDSQKCSDVSELSSSPPGPYHQEPYISKPEERFKAPPILPPHLLQVILNKDTGISCDPALLPEPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKPI
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2N-myristoyl glycine------MGNTSSERA
------CCCCCCHHH
46.2311171104
9305909
24PhosphoserineHKTPRRDSSGGTKDG
CCCCCCCCCCCCCCC
29.1311171104
9305909
25PhosphoserineKTPRRDSSGGTKDGD
CCCCCCCCCCCCCCC
45.6011171104
9305909
40PhosphoserineRPKILMDSPEDADIF
CCCEECCCCCCCCCC
19.0722673903
96PhosphoserineKEVYLSGSFNNWSKL
CEEEEEEEECCEEEC
22.7912764152
101PhosphoserineSGSFNNWSKLPLTRS
EEEECCEEECCCCCC
26.8312764152
106PhosphothreonineNWSKLPLTRSQNNFV
CEEECCCCCCCCCEE
26.7423984901
108PhosphoserineSKLPLTRSQNNFVAI
EECCCCCCCCCEEEE
31.8322673903
11171104
12764152
9305909
125PhosphotyrosineLPEGEHQYKFFVDGQ
CCCCCEEEEEEECCC
16.2123353032
144PhosphoserinePSEPIVTSQLGTVNN
CCCCCCHHCCCCEEE
16.7123984901
180PhosphoserineCSDVSELSSSPPGPY
CCCCCCCCCCCCCCC
25.3923712012
181PhosphoserineSDVSELSSSPPGPYH
CCCCCCCCCCCCCCC
60.536457321
182PhosphoserineDVSELSSSPPGPYHQ
CCCCCCCCCCCCCCC
31.5711171104
9305909

Disease-associated PTM Sites based on nsSNP

* Distance = the distance between SNP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SNP Related Disease Reference

Oops, there are no SNP-PTM records of AAKB1_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAF1_HUMANRAF1physical
9091312

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
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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