AAKB1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AAKB1_MOUSE
• UniProt AC: Q9R078
• Protein Name: 5'-AMP-activated protein kinase subunit beta-1
• Gene Name: Prkab1
• Organism: Mus musculus (Mouse).
• Sequence Length: 270
• 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) (By similarity)..
• Protein Sequence: MGNTSSERAALERQAGHKTPRRDSSGGAKDGDRPKILMDSPEDADIFHSEEIKAPEKEEFLAWQHDLEANDKAPAQARPTVFRWTGGGKEVYLSGSFNNWSKLPLTRSQNNFVAILDLPEGEHQYKFFVDGQWTHDPSEPIVTSQLGTVNNIIQVKKTDFEVFDALMVDSQKCSDVSELSSSPPGPYHQEPYMSKPEERFKAPPILPPHLLQVILNKDTGISCDPALLPEPNHVMLNHLYALSIKDGVMVLSATHRYKKKYVTTLLYKPI

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
2	Myristoylation	------MGNTSSERA ------CCCCHHHHH	46.23	-
4	Phosphorylation	----MGNTSSERAAL ----CCCCHHHHHHH	28.09	-
5	Phosphorylation	---MGNTSSERAALE ---CCCCHHHHHHHH	33.91	-
6	Phosphorylation	--MGNTSSERAALER --CCCCHHHHHHHHH	29.12	-
19	Phosphorylation	ERQAGHKTPRRDSSG HHHCCCCCCCCCCCC	19.16	27149854
24	Phosphorylation	HKTPRRDSSGGAKDG CCCCCCCCCCCCCCC	29.13	27087446
25	Phosphorylation	KTPRRDSSGGAKDGD CCCCCCCCCCCCCCC	45.60	27087446
40	Phosphorylation	RPKILMDSPEDADIF CCCCCCCCHHHCCCC	19.07	24925903
49	Phosphorylation	EDADIFHSEEIKAPE HHCCCCCCCCCCCCC	26.61	24925903
72	Ubiquitination	HDLEANDKAPAQARP CCHHCCCCCCCCCCC	56.95	-
92	Phosphorylation	TGGGKEVYLSGSFNN CCCCCEEEEECCCCC	9.02	29472430
94	Phosphorylation	GGKEVYLSGSFNNWS CCCEEEEECCCCCCC	18.07	23984901
96	Phosphorylation	KEVYLSGSFNNWSKL CEEEEECCCCCCCCC	22.79	25521595
101	Phosphorylation	SGSFNNWSKLPLTRS ECCCCCCCCCCCCCC	26.83	22817900
106	Phosphorylation	NWSKLPLTRSQNNFV CCCCCCCCCCCCCEE	26.74	21082442
108	Phosphorylation	SKLPLTRSQNNFVAI CCCCCCCCCCCEEEE	31.83	24925903
125	Phosphorylation	LPEGEHQYKFFVDGQ CCCCCCEEEEEECCE	16.21	25619855
144	Phosphorylation	PSEPIVTSQLGTVNN CCCCEEEEECCCCCC	16.71	46163113
148	Phosphorylation	IVTSQLGTVNNIIQV EEEEECCCCCCEEEE	28.75	30352176
170	Phosphorylation	FDALMVDSQKCSDVS CCCEEECCCCCCCHH	21.82	29899451
174	Phosphorylation	MVDSQKCSDVSELSS EECCCCCCCHHHHCC	48.35	20139300
177	Phosphorylation	SQKCSDVSELSSSPP CCCCCCHHHHCCCCC	37.50	26239621
180	Phosphorylation	CSDVSELSSSPPGPY CCCHHHHCCCCCCCC	25.39	27742792
181	Phosphorylation	SDVSELSSSPPGPYH CCHHHHCCCCCCCCC	60.53	6457323
182	Phosphorylation	DVSELSSSPPGPYHQ CHHHHCCCCCCCCCC	31.57	27087446
187	Phosphorylation	SSSPPGPYHQEPYMS CCCCCCCCCCCCCCC	23.27	25521595
192	Phosphorylation	GPYHQEPYMSKPEER CCCCCCCCCCCHHHH	17.17	26160508
194	Phosphorylation	YHQEPYMSKPEERFK CCCCCCCCCHHHHHC	38.93	26160508
201	Succinylation	SKPEERFKAPPILPP CCHHHHHCCCCCCCH	67.23	-
201	Succinylation	SKPEERFKAPPILPP CCHHHHHCCCCCCCH	67.23	23806337
201	Acetylation	SKPEERFKAPPILPP CCHHHHHCCCCCCCH	67.23	23806337
240	Phosphorylation	HVMLNHLYALSIKDG EECCEEEEEEEECCC	9.65	72591
261	Phosphorylation	THRYKKKYVTTLLYK CCCCCCCEEEEEEEC	16.35	22499769
263	Phosphorylation	RYKKKYVTTLLYKPI CCCCCEEEEEEECCC	14.50	22499769
264	Phosphorylation	YKKKYVTTLLYKPI- CCCCEEEEEEECCC-	12.53	22499769
267	Phosphorylation	KYVTTLLYKPI---- CEEEEEEECCC----	20.17	22499769

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
108	S	Phosphorylation	Kinase	PRKAB1	-	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AAKB1_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 AAKB1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CIDEA_MOUSE	Cidea	physical	18480843
AAPK1_MOUSE	Prkaa1	physical	18480843
AAKG1_MOUSE	Prkag1	physical	18480843

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND MASSSPECTROMETRY.
PubMed: 19131326

"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND MASSSPECTROMETRY.
PubMed: 19144319

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND MASSSPECTROMETRY.
PubMed: 19367708