UniProtKB - Q9R078 (AAKB1_MOUSE)
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Protein
5'-AMP-activated protein kinase subunit beta-1
Gene
Prkab1
Organism
Mus musculus (Mouse)
Status
Functioni
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).By similarity
GO - Molecular functioni
- AMP-activated protein kinase activity Source: MGI
- protein kinase activity Source: MGI
- protein kinase binding Source: Ensembl
GO - Biological processi
- fatty acid biosynthetic process Source: UniProtKB-KW
- nail development Source: MGI
- positive regulation of gene expression Source: MGI
- protein heterooligomerization Source: Ensembl
- protein phosphorylation Source: MGI
- regulation of catalytic activity Source: Ensembl
Keywordsi
Biological process | Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism |
Enzyme and pathway databases
Reactomei | R-MMU-1632852. Macroautophagy. R-MMU-380972. Energy dependent regulation of mTOR by LKB1-AMPK. R-MMU-5628897. TP53 Regulates Metabolic Genes. R-MMU-6804756. Regulation of TP53 Activity through Phosphorylation. |
Names & Taxonomyi
Protein namesi | Recommended name: 5'-AMP-activated protein kinase subunit beta-1Short name: AMPK subunit beta-1 Short name: AMPKb |
Gene namesi | Name:Prkab1 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:1336167. Prkab1. |
Subcellular locationi
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedBy similarity | |||
ChainiPRO_0000204364 | 2 – 270 | 5'-AMP-activated protein kinase subunit beta-1Add BLAST | 269 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Lipidationi | 2 | N-myristoyl glycineBy similarity | 1 | |
Modified residuei | 4 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 5 | PhosphoserineBy similarity | 1 | |
Modified residuei | 6 | PhosphoserineBy similarity | 1 | |
Modified residuei | 19 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 24 | Phosphoserine; by autocatalysisBy similarity | 1 | |
Modified residuei | 25 | Phosphoserine; by autocatalysisBy similarity | 1 | |
Modified residuei | 40 | PhosphoserineBy similarity | 1 | |
Modified residuei | 96 | PhosphoserineCombined sources | 1 | |
Modified residuei | 101 | PhosphoserineBy similarity | 1 | |
Modified residuei | 108 | Phosphoserine; by autocatalysisCombined sources1 Publication | 1 | |
Modified residuei | 148 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 182 | PhosphoserineCombined sources | 1 | |
Modified residuei | 201 | N6-succinyllysineCombined sources | 1 |
Post-translational modificationi
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.1 Publication
Keywords - PTMi
Lipoprotein, Myristate, PhosphoproteinProteomic databases
EPDi | Q9R078. |
MaxQBi | Q9R078. |
PaxDbi | Q9R078. |
PRIDEi | Q9R078. |
PTM databases
CarbonylDBi | Q9R078. |
iPTMneti | Q9R078. |
PhosphoSitePlusi | Q9R078. |
Expressioni
Gene expression databases
Bgeei | ENSMUSG00000029513. |
ExpressionAtlasi | Q9R078. baseline and differential. |
Genevisiblei | Q9R078. MM. |
Interactioni
Subunit structurei
AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with FNIP1 and FNIP2 (By similarity).By similarity
GO - Molecular functioni
- protein kinase binding Source: Ensembl
Protein-protein interaction databases
BioGridi | 202363. 4 interactors. |
IntActi | Q9R078. 10 interactors. |
MINTi | Q9R078. |
STRINGi | 10090.ENSMUSP00000031486. |
Structurei
3D structure databases
ProteinModelPortali | Q9R078. |
SMRi | Q9R078. |
ModBasei | Search... |
MobiDBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 68 – 163 | Glycogen-binding domainBy similarityAdd BLAST | 96 |
Domaini
The glycogen-binding domain may target AMPK to glycogen so that other factors like glycogen-bound debranching enzyme or protein phosphatases can directly affect AMPK activity.By similarity
Sequence similaritiesi
Belongs to the 5'-AMP-activated protein kinase beta subunit family.Curated
Phylogenomic databases
eggNOGi | KOG1616. Eukaryota. ENOG410XRB3. LUCA. |
GeneTreei | ENSGT00390000001416. |
HOGENOMi | HOG000230597. |
HOVERGENi | HBG050430. |
InParanoidi | Q9R078. |
KOi | K07199. |
OMAi | KCSDMSE. |
OrthoDBi | EOG091G0DZR. |
PhylomeDBi | Q9R078. |
TreeFami | TF313827. |
Family and domain databases
Gene3Di | 2.60.40.10. 1 hit. |
InterProi | View protein in InterPro IPR032640. AMPK1_CBM. IPR006828. ASC_dom. IPR037256. ASC_dom_sf. IPR013783. Ig-like_fold. IPR014756. Ig_E-set. |
Pfami | View protein in Pfam PF16561. AMPK1_CBM. 1 hit. PF04739. AMPKBI. 1 hit. |
SMARTi | View protein in SMART SM01010. AMPKBI. 1 hit. |
SUPFAMi | SSF160219. SSF160219. 1 hit. SSF81296. SSF81296. 1 hit. |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
Q9R078-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MGNTSSERAA LERQAGHKTP RRDSSGGAKD GDRPKILMDS PEDADIFHSE
60 70 80 90 100
EIKAPEKEEF LAWQHDLEAN DKAPAQARPT VFRWTGGGKE VYLSGSFNNW
110 120 130 140 150
SKLPLTRSQN NFVAILDLPE GEHQYKFFVD GQWTHDPSEP IVTSQLGTVN
160 170 180 190 200
NIIQVKKTDF EVFDALMVDS QKCSDVSELS SSPPGPYHQE PYMSKPEERF
210 220 230 240 250
KAPPILPPHL LQVILNKDTG ISCDPALLPE PNHVMLNHLY ALSIKDGVMV
260 270
LSATHRYKKK YVTTLLYKPI
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF108215 mRNA. Translation: AAF14222.1. BC016398 mRNA. Translation: AAH16398.1. |
CCDSi | CCDS19598.1. |
RefSeqi | NP_114075.1. NM_031869.2. XP_006530264.1. XM_006530201.1. |
UniGenei | Mm.458152. |
Genome annotation databases
Ensembli | ENSMUST00000031486; ENSMUSP00000031486; ENSMUSG00000029513. ENSMUST00000111999; ENSMUSP00000107630; ENSMUSG00000029513. |
GeneIDi | 19079. |
KEGGi | mmu:19079. |
UCSCi | uc008zew.1. mouse. |
Similar proteinsi
Entry informationi
Entry namei | AAKB1_MOUSE | |
Accessioni | Q9R078Primary (citable) accession number: Q9R078 Secondary accession number(s): Q91YN6 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 1, 2001 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 28, 2018 | |
This is version 148 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |