Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00515
Entry Name
UniProt Accession
Theoretical PI
5.99
Molecular Weight
30302.22
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
5'-AMP-activated protein kinase subunit beta-2
Protein Synonyms/Alias
AMPK subunit beta-2;
Gene Name
PRKAB2
Gene Synonyms/Alias
Created Date
15-DEC-1998
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGNTTSDRV
[1]
N-Myristoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Oakhill JS, Chen ZP, Scott JW, Steel R, Castelli LA, Ling N, Macaulay SL, KempBE. β-Subunit myristoylation is the gatekeeper for initiating metabolic stresssensing by AMP-activated protein kinase (AMPK). Proc Natl Acad Sci U S A. 2010Nov 9;107(45):19237-41. doi: 10.1073/pnas.1009705107. Epub 2010 Oct 25. PubMedPMID: 20974912; PubMed Central PMCID: PMC2984171.[PMID:20974912]
Functional 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).
Sequence Annotation
Modified residue: 39 39 Phosphoserine; by ULK1.
Modified residue: 40 40 Phosphothreonine; by ULK1.
Modified residue: 69 69 Phosphoserine; by ULK1.
Modified residue: 108 108 Phosphoserine.
Modified residue: 174 174 Phosphoserine.
Modified residue: 184 184 Phosphoserine.
Protein Length
272 AA.
Protein Sequence
(Canonical)
MGNTTSDRVS GERHGAKAAR SEGAGGHAPG KEHKIMVGST DDPSVFSLPD SKLPGDKEFV  60
SWQQDLEDSV KPTQQARPTV IRWSEGGKEV FISGSFNNWS TKIPLIKSHN DFVAILDLPE  120
GEHQYKFFVD GQWVHDPSEP VVTSQLGTIN NLIHVKKSDF EVFDALKLDS MESSETSCRD  180
LSSSPPGPYG QEMYAFRSEE RFKSPPILPP HLLQVILNKD TNISCDPALL PEPNHVMLNH  240
LYALSIKDSV MVLSATHRYK KKYVTTLLYK PI                                272
FASTA
(Canonical)
>LipidDB-9606-00515|O43741
MGNTTSDRVSGERHGAKAARSEGAGGHAPGKEHKIMVGSTDDPSVFSLPDSKLPGDKEFV
SWQQDLEDSVKPTQQARPTVIRWSEGGKEVFISGSFNNWSTKIPLIKSHNDFVAILDLPE
GEHQYKFFVDGQWVHDPSEPVVTSQLGTINNLIHVKKSDFEVFDALKLDSMESSETSCRD
LSSSPPGPYGQEMYAFRSEERFKSPPILPPHLLQVILNKDTNISCDPALLPEPNHVMLNH
LYALSIKDSVMVLSATHRYKKKYVTTLLYKPI
Gene Ontology
GO:0031588; C:AMP-activated protein kinase complex; IDA:UniProtKB
GO:0005829; C:cytosol; TAS:Reactome
GO:0005654; C:nucleoplasm; TAS:Reactome
GO:0042802; F:identical protein binding; IPI:IntAct
GO:0006853; P:carnitine shuttle; TAS:Reactome
GO:0007050; P:cell cycle arrest; TAS:Reactome
GO:0044255; P:cellular lipid metabolic process; TAS:Reactome
GO:0006112; P:energy reserve metabolic process; TAS:Reactome
GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW
GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome
GO:0061024; P:membrane organization; TAS:Reactome
GO:0006468; P:protein phosphorylation; IDA:GOC
GO:0042304; P:regulation of fatty acid biosynthetic process; TAS:Reactome
GO:0007165; P:signal transduction; TAS:ProtInc
GO:0044281; P:small molecule metabolic process; TAS:Reactome
Interpro
InterPro; IPR006828; AMP_prot_kin_bsu_interact-dom
InterPro; IPR014756; Ig_E-set
Pfam
Pfam; PF04739; AMPKBI;
SMART
SMART; SM01010; AMPKBI;
PROSITE
PRINTS