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

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Q9R078 (AAKB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 112. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
5'-AMP-activated protein kinase subunit beta-1
Short name=AMPK subunit beta-1
Short name=AMPKb

Gene names

Name:

Prkab1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	270 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	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.
Domain	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.
Post-translational modification	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. Ref.5
Sequence similarities	Belongs to the 5'-AMP-activated protein kinase beta subunit family.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
PTM	Lipoprotein Myristate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of gene expression Inferred from electronic annotation. Source: Ensembl protein heterooligomerization Inferred from electronic annotation. Source: Ensembl regulation of catalytic activity Inferred from electronic annotation. Source: Ensembl
Cellular_component	AMP-activated protein kinase complex Inferred from electronic annotation. Source: Ensembl cytosol Traceable author statement. Source: Reactome nucleus Inferred from direct assay PubMed 10098881. Source: MGI
Molecular_function	AMP-activated protein kinase activity Traceable author statement PubMed 10098881. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 270

269

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

PRO_0000204364

Regions

Region

68 – 163

Glycogen-binding domain By similarity

Amino acid modifications

Modified residue

Phosphothreonine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphothreonine By similarity

Modified residue

Phosphoserine; by autocatalysis By similarity

Modified residue

Phosphoserine; by autocatalysis By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

101

Phosphoserine By similarity

Modified residue

108

Phosphoserine; by autocatalysis Ref.3 Ref.4

Modified residue

148

Phosphothreonine By similarity

Modified residue

182

Phosphoserine By similarity

Lipidation

N-myristoyl glycine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q9R078 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 6B520A95A0A844E5
Show »

FASTA

270

30,308

        10         20         30         40         50         60 
MGNTSSERAA LERQAGHKTP RRDSSGGAKD GDRPKILMDS PEDADIFHSE EIKAPEKEEF 

        70         80         90        100        110        120 
LAWQHDLEAN DKAPAQARPT VFRWTGGGKE VYLSGSFNNW SKLPLTRSQN NFVAILDLPE 

       130        140        150        160        170        180 
GEHQYKFFVD GQWTHDPSEP IVTSQLGTVN NIIQVKKTDF EVFDALMVDS QKCSDVSELS 

       190        200        210        220        230        240 
SSPPGPYHQE PYMSKPEERF KAPPILPPHL LQVILNKDTG ISCDPALLPE PNHVMLNHLY 

       250        260        270 
ALSIKDGVMV LSATHRYKKK YVTTLLYKPI

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"5'-AMP-activated protein kinase subunit beta interacts with the p42 subunit of translation initiation factor eIF3." Valentijn L.J., Hoff E.I., Baas F. Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: CD-1.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, MASS SPECTROMETRY.
[4]	"Large scale localization of protein phosphorylation by use of electron 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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[5]	"Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory feedback loop." Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M., Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B. Autophagy 7:696-706(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY ULK1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF108215 mRNA. Translation: AAF14222.1. BC016398 mRNA. Translation: AAH16398.1.
RefSeq	NP_114075.1. NM_031869.2.
UniGene	Mm.458152.
3D structure databases
ProteinModelPortal	Q9R078.
SMR	Q9R078. Positions 77-270.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	202363. 1 interaction.
IntAct	Q9R078. 10 interactions.
MINT	MINT-4086419.
PTM databases
PhosphoSite	Q9R078.
Proteomic databases
PaxDb	Q9R078.
PRIDE	Q9R078.
Protocols and materials databases
DNASU	19079.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000031486; ENSMUSP00000031486; ENSMUSG00000029513. ENSMUST00000111999; ENSMUSP00000107630; ENSMUSG00000029513.
GeneID	19079.
KEGG	mmu:19079.
UCSC	uc008zew.1. mouse.
Organism-specific databases
CTD	5564.
MGI	MGI:1336167. Prkab1.
Phylogenomic databases
eggNOG	NOG238368.
GeneTree	ENSGT00390000001416.
HOGENOM	HOG000230597.
HOVERGEN	HBG050430.
InParanoid	Q9R078.
KO	K07199.
OMA	DADIFHG.
OrthoDB	EOG7SXW3Z.
TreeFam	TF313827.
Enzyme and pathway databases
Reactome	REACT_147847. Translocation of Glut4 to the Plasma Membrane. REACT_88307. Membrane Trafficking.
Gene expression databases
ArrayExpress	Q9R078.
Bgee	Q9R078.
Genevestigator	Q9R078.
Family and domain databases
InterPro	IPR006828. AMP_prot_kin_bsu_interact-dom. IPR014756. Ig_E-set. [Graphical view]
Pfam	PF04739. AMPKBI. 1 hit. [Graphical view]
SMART	SM01010. AMPKBI. 1 hit. [Graphical view]
SUPFAM	SSF81296. SSF81296. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	PRKAB1. mouse.
NextBio	295614.
PRO	Q9R078.
SOURCE	Search...

Entry information

Entry name

AAKB1_MOUSE

Accession

Primary (citable) accession number: Q9R078
Secondary accession number(s): Q91YN6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	January 23, 2007
Last modified:	February 19, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

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

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents