Primary Information
BoMiProt ID	Bomi3534
Protein Name	5'-AMP-activated protein kinase subunit beta-1
Organism	Bos taurus
Uniprot ID	Q5BIS9
Milk Fraction	Exosomes
Ref Sequence ID	NP_001019729.1
Aminoacid Length	270
Molecular Weight	30287
FASTA Sequence	Download
Gene Name	PRKAB1
Gene ID	534107
Protein Existence Status	Reviewed
Secondary Information
Presence in other biological fluids/tissue/cells	prostate gland
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.It is an essential enzyme for regulating energy homeostasis . It is able to activate fatty acid β-oxidation, glycolysis and glucose transport while inhibiting lipid synthesis.
Biochemical Properties	AMPK is a heterotrimer that consists of a catalytic α and regulatory β− and γ-subunits. Each subunit exists in different isoforms, with two α (α1 and α2), two β (β1 and β2), and three γ (γ1, γ2, γ3) isoforms differentially expressed in various tissues in up to 12 different isoenzymes. The kinase activity of AMPK is regulated by phosphorylation of the conserved threonine in the catalytic domain of the α-subunit by adenine nucleotide binding to the γ-subunit and by glycogen binding to a conserved mid-molecule carbohydrate-binding module (CBM) located in the β-subunits.
PTMs	Lipoylation, Myristoylation, Phosphorylation at Ser
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation	>sp|Q5BIS9|AAKB1_BOVIN 5'-AMP-activated protein kinase subunit beta-1 OS=Bos taurus OX=9913 GN=PRKAB1 PE=2 SV=3 MGNT*4 S*5 S*6ERAALDRQGGHKT*19PRRDS*24S*25GGSKDGDRPKILMDS*40PEDADLFHSEEIKAPEKEEFLAWQHDLEVNDKAPAQARPTVFRWTGGGKEVYLSGS*96FNNWS*101KLPLTRS*108HNNFVAILDLPEGEHQYKFFVDGQWTHDPSEPVVTSQLGT*148VNNVIQVKKTDFEVFDALMVDSQKCSDVSELS SS*182PPGPYHQEPYISKPEERFKAPPILPPHLLQVILNKDTGISCDPALLPEPNHVMLNHLY ALSIKDGVMVLSATHRYKKKYVTTLLYKPI
Predicted Disorder Regions	1-79, 172-202
DisProt Annotation
TM Helix Prediction	No TM helices
Significance of PTMs	Phosphorylated when associated with the catalytic subunit (PRKAA1 or PRKAA2). Phosphorylated by ULK1; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1 and AMPK
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