CPLM-023808

Genbank Nucleotide ID

5'-AMP-activated protein kinase subunit beta-1

Protein Synonyms/Alias

AMPK subunit beta-1; AMPKb

Homo sapiens (Human)

Position	Peptide	Type	References
57	EEIKAPEKEEFLAWQ	ubiquitination	[1, 2]
89	FRWTGGGKEVYLSGS	ubiquitination	[3]
102	GSFNNWSKLPLTRSH	ubiquitination	[3, 4]
157	NNIIQVKKTDFEVFD	ubiquitination	[3]
195	HQEPYVCKPEERFRA	ubiquitination	[3, 5]
268	YVTTLLYKPI*****	ubiquitination	[3, 5]

[1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]

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).

REGION 68 163 Glycogen-binding domain (By similarity).
MOD_RES 4 4 Phosphothreonine.
MOD_RES 5 5 Phosphoserine.
MOD_RES 6 6 Phosphoserine.
MOD_RES 19 19 Phosphothreonine.
MOD_RES 24 24 Phosphoserine; by autocatalysis (By
MOD_RES 25 25 Phosphoserine; by autocatalysis (By
MOD_RES 40 40 Phosphoserine.
MOD_RES 96 96 Phosphoserine.
MOD_RES 101 101 Phosphoserine (By similarity).
MOD_RES 108 108 Phosphoserine.
MOD_RES 148 148 Phosphothreonine.
MOD_RES 182 182 Phosphoserine (By similarity).
LIPID 2 2 N-myristoyl glycine.

Complete proteome; Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Lipoprotein; Myristate; Phosphoprotein; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0031588; C:AMP-activated protein kinase complex; IEA:Compara.
GO:0005829; C:cytosol; TAS:Reactome.
GO:0005634; C:nucleus; IEA:Compara.
GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO:0007050; P:cell cycle arrest; TAS:Reactome.
GO:0016044; P:cellular membrane organization; TAS:Reactome.
GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO:0051291; P:protein heterooligomerization; IEA:Compara.
GO:0050790; P:regulation of catalytic activity; IEA:Compara.

IPR006828; AMP_prot_kin_bsu_interact-dom.