AAKG1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AAKG1_MOUSE
• UniProt AC: O54950
• Protein Name: 5'-AMP-activated protein kinase subunit gamma-1
• Gene Name: Prkag1
• Organism: Mus musculus (Mouse).
• Sequence Length: 330
• Protein Description: AMP/ATP-binding 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. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive (By similarity)..
• Protein Sequence: MESVAAESSPALENEHFQETPESNNSVYTSFMKSHRCYDLIPTSSKLVVFDTSLQVKKAFFALVTNGVRAAPLWDSKKQSFVGMLTITDFINILHRYYKSALVQIYELEEHKIETWREVYLQDSFKPLVCISPNASLFDAVSSLIRNKIHRLPVIDPESGNTLYILTHKRILKFLKLFITEFPKPEFMSKSLQELQIGTYANIAMVRTTTPVYVALGIFVQHRVSALPVVDEKGRVVDIYSKFDVINLAAEKTYNNLDVSVTKALQHRSHYFEGVLKCYLHETLETIINRLVEAEVHRLVVVDEHDVVKGIVSLSDILQALVLTGGEKKP

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
3	Phosphorylation	-----MESVAAESSP -----CCCCCCCCCH	18.76	26643407
8	Phosphorylation	MESVAAESSPALENE CCCCCCCCCHHHCCH	36.57	26643407
9	Phosphorylation	ESVAAESSPALENEH CCCCCCCCHHHCCHH	13.00	26643407
20	Phosphorylation	ENEHFQETPESNNSV CCHHHCCCCCCCCCH	22.90	26643407
254	Phosphorylation	NLAAEKTYNNLDVSV HHHHHHHCCCCCHHH	17.08	18779572
260	Phosphorylation	TYNNLDVSVTKALQH HCCCCCHHHHHHHHC	24.60	18779572
262	Phosphorylation	NNLDVSVTKALQHRS CCCCHHHHHHHHCCC	11.77	-
263	Ubiquitination	NLDVSVTKALQHRSH CCCHHHHHHHHCCCH	44.97	22790023
269	Phosphorylation	TKALQHRSHYFEGVL HHHHHCCCHHHHHHH	22.03	-
313	Phosphorylation	DVVKGIVSLSDILQA HHHCHHHCHHHHHHH	21.89	51459801
328	Ubiquitination	LVLTGGEKKP----- HHHCCCCCCC-----	73.88	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
260	S	Phosphorylation	Kinase	ULK1	O70405	Uniprot
262	T	Phosphorylation	Kinase	ULK1	O70405	Uniprot
269	S	Phosphorylation	Kinase	ULK1	O70405	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AAKG1_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of AAKG1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CIDEA_MOUSE	Cidea	physical	18480843
AAPK1_MOUSE	Prkaa1	physical	18480843
AAKB1_MOUSE	Prkab1	physical	18480843

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.