LipidDB ID

LipidDB-9606-00117

Entry Name

UniProt Accession

Q9Y478; Q9UBV0; Q9UE20; Q9UEX2; Q9Y6V8;

Theoretical PI

5.94

Molecular Weight

30382.32

Genbank Protein ID

CAA12024.1; CAA73146.1; AAD09237.1; AAD00625.1; AAD00625.1; AAD00625.1; AAD00625.1; AAD00625.1; AAD00625.1; AAC98897.1; AAB71326.1; AAH01007.1; AAH01056.1; AAH01823.1; AAH17671.1;

Genbank Nucleotide ID

AJ224515; Y12556; U83994; U87276; U87271; U87272; U87273; U87274; U87275; AF022116; AC002563; BC001007; BC001056; BC001823; BC017671;

Protein Name

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

Protein Synonyms/Alias

AMPK subunit beta-1; AMPKb;

Gene Name

PRKAB1

Gene Synonyms/Alias

AMPK;

Created Date

01-JUN-2001

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]
[2] Oakhill JS, Steel R, Chen ZP, Scott JW, Ling N, Tam S, Kemp BE. AMPK is adirect adenylate charge-regulated protein kinase. Science. 2011 Jun17;332(6036):1433-5. doi: 10.1126/science.1200094.[PMID:21680840]

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

Region: 68 163 Glycogen-binding domain.
Modified residue: 4 4 Phosphothreonine.
Modified residue: 5 5 Phosphoserine.
Modified residue: 6 6 Phosphoserine.
Modified residue: 19 19 Phosphothreonine.
Modified residue: 24 24 Phosphoserine; by autocatalysis.
Modified residue: 25 25 Phosphoserine; by autocatalysis.
Modified residue: 40 40 Phosphoserine.
Modified residue: 96 96 Phosphoserine.
Modified residue: 101 101 Phosphoserine.
Modified residue: 108 108 Phosphoserine.
Modified residue: 148 148 Phosphothreonine.
Modified residue: 182 182 Phosphoserine.

Protein Length

270 AA.

Protein Sequence
(Canonical)

FASTA
(Canonical)

Gene Ontology

GO:0031588; C:AMP-activated protein kinase complex; IEA:Ensembl
GO:0005829; C:cytosol; TAS:Reactome
GO:0005634; C:nucleus; IEA:Ensembl
GO:0004672; F:protein kinase activity; IDA:UniProtKB
GO:0007050; P:cell cycle arrest; 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:0010628; P:positive regulation of gene expression; IDA:UniProtKB
GO:0051291; P:protein heterooligomerization; IEA:Ensembl
GO:0006468; P:protein phosphorylation; IDA:UniProtKB
GO:0050790; P:regulation of catalytic activity; IEA:Ensembl
GO:0007165; P:signal transduction; TAS:ProtInc

Interpro

InterPro; IPR006828; AMP_prot_kin_bsu_interact-dom
InterPro; IPR014756; Ig_E-set

Pfam

Pfam; PF04739; AMPKBI;

SMART

SMART; SM01010; AMPKBI;

PROSITE

PRINTS