Prkab1

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
Traceable author statementⁱ
- 10098881
protein kinase activity Source: MGI
protein kinase binding Source: Ensembl

Complete GO annotation...

GO - Biological processⁱ

fatty acid biosynthetic process Source: UniProtKB-KW
membrane organization Source: Reactome
nail development
Source: MGI
Inferred from mutant phenotypeⁱ
- 25340873
positive regulation of gene expression Source: MGI
protein heterooligomerization Source: Ensembl
protein phosphorylation Source: MGI
regulation of protein kinase activity Source: InterPro
signal transduction Source: InterPro

Complete GO annotation...

Keywordsⁱ

Biological process	Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Biological process

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

Reactomeⁱ	R-MMU-1445148. Translocation of GLUT4 to the plasma membrane. 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.

Reactomeⁱ

R-MMU-1445148. Translocation of GLUT4 to the plasma membrane.
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-1 Short name: AMPK subunit beta-1 Short name: AMPKb
Gene namesⁱ	Name:Prkab1
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Chromosome 5

Organism-specific databases

MGIⁱ	MGI:1336167. Prkab1.

Subcellular locationⁱ

GO - Cellular componentⁱ

cytosol Source: Reactome
nucleotide-activated protein kinase complex Source: Ensembl
nucleus
Source: MGI
Inferred from direct assayⁱ
- 10098881

Complete GO annotation...

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	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 sources	1
Modified residueⁱ	148	PhosphothreonineBy similarity	1
Modified residueⁱ	170	PhosphoserineBy 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, Phosphoprotein

Proteomic databases

EPDⁱ	Q9R078.
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q9R078.
PaxDbⁱ	Q9R078.
PRIDEⁱ	Q9R078.

PTM databases

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

Complete GO annotation...

Protein-protein interaction databases

BioGridⁱ	202363. 4 interactors.
IntActⁱ	Q9R078. 10 interactors.
Molecular INTeraction database More...MINTⁱ	MINT-4086419.
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.
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000001416.
HOGENOMⁱ	HOG000230597.
HOVERGENⁱ	HBG050430.
InParanoidⁱ	Q9R078.
KEGG Orthology (KO) More...KOⁱ	K07199.
OMAⁱ	KCSDMSE.
Database of Orthologous Groups More...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. IPR030080. AMPK_beta-1. IPR006828. ASC_dom. IPR013783. Ig-like_fold. IPR014756. Ig_E-set.
PANTHERⁱ	PTHR10343:SF67. PTHR10343:SF67. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF16561. AMPK1_CBM. 1 hit. PF04739. AMPKBI. 1 hit.
SMARTⁱ	View protein in SMART SM01010. AMPKBI. 1 hit.
SUPFAMⁱ	SSF81296. SSF81296. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

Q9R078-1 [UniParc]FASTA Add to basket

« Hide

        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

Length:270

Mass (Da):30,308

Last modified:January 23, 2007 - v2

Checksum:ⁱ6B520A95A0A844E5

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF108215 mRNA. Translation: AAF14222.1. BC016398 mRNA. Translation: AAH16398.1.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS19598.1.
NCBI Reference Sequences More...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.
UCSC genome browser More...UCSCⁱ	uc008zew.1. mouse.

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF108215 mRNA. Translation: AAF14222.1. BC016398 mRNA. Translation: AAH16398.1.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS19598.1.
NCBI Reference Sequences More...RefSeqⁱ	NP_114075.1. NM_031869.2. XP_006530264.1. XM_006530201.1.
UniGeneⁱ	Mm.458152.

3D structure databases

ProteinModelPortalⁱ	Q9R078.
SMRⁱ	Q9R078.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	202363. 4 interactors.
IntActⁱ	Q9R078. 10 interactors.
Molecular INTeraction database More...MINTⁱ	MINT-4086419.
STRINGⁱ	10090.ENSMUSP00000031486.

PTM databases

iPTMnetⁱ	Q9R078.
PhosphoSitePlusⁱ	Q9R078.

Proteomic databases

EPDⁱ	Q9R078.
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q9R078.
PaxDbⁱ	Q9R078.
PRIDEⁱ	Q9R078.

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	19079.
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENSMUST00000031486; ENSMUSP00000031486; ENSMUSG00000029513. ENSMUST00000111999; ENSMUSP00000107630; ENSMUSG00000029513.
GeneIDⁱ	19079.
KEGGⁱ	mmu:19079.
UCSC genome browser More...UCSCⁱ	uc008zew.1. mouse.

Organism-specific databases

CTDⁱ	5564.
MGIⁱ	MGI:1336167. Prkab1.

Phylogenomic databases

eggNOGⁱ	KOG1616. Eukaryota. ENOG410XRB3. LUCA.
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000001416.
HOGENOMⁱ	HOG000230597.
HOVERGENⁱ	HBG050430.
InParanoidⁱ	Q9R078.
KEGG Orthology (KO) More...KOⁱ	K07199.
OMAⁱ	KCSDMSE.
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0DZR.
PhylomeDBⁱ	Q9R078.
TreeFamⁱ	TF313827.

Enzyme and pathway databases

Reactomeⁱ	R-MMU-1445148. Translocation of GLUT4 to the plasma membrane. 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.

Reactomeⁱ

R-MMU-1445148. Translocation of GLUT4 to the plasma membrane.
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.

Miscellaneous databases

ChiTaRSⁱ	Prkab1. mouse.
Protein Ontology More...PROⁱ	PR:Q9R078.
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSMUSG00000029513.
ExpressionAtlasⁱ	Q9R078. baseline and differential.
Genevisibleⁱ	Q9R078. MM.

Family and domain databases

Gene3Dⁱ	2.60.40.10. 1 hit.
InterProⁱ	View protein in InterPro IPR032640. AMPK1_CBM. IPR030080. AMPK_beta-1. IPR006828. ASC_dom. IPR013783. Ig-like_fold. IPR014756. Ig_E-set.
PANTHERⁱ	PTHR10343:SF67. PTHR10343:SF67. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF16561. AMPK1_CBM. 1 hit. PF04739. AMPKBI. 1 hit.
SMARTⁱ	View protein in SMART SM01010. AMPKBI. 1 hit.
SUPFAMⁱ	SSF81296. SSF81296. 1 hit.
ProtoNetⁱ	Search...

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:	June 7, 2017
	This is version 143 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

Documents

MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
SIMILARITY comments
Index of protein domains and families

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q9R078 (AAKB1_MOUSE)

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

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ