Q9R078 (AAKB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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

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 › 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	1	1	Removed By similarity
	Chain	2 – 270	269	5'-AMP-activated protein kinase subunit beta-1		PRO_0000204364
Regions
	Region	68 – 163	96	Glycogen-binding domain By similarity
Amino acid modifications
	Modified residue	4	1	Phosphothreonine By similarity
	Modified residue	5	1	Phosphoserine By similarity
	Modified residue	6	1	Phosphoserine By similarity
	Modified residue	19	1	Phosphothreonine By similarity
	Modified residue	24	1	Phosphoserine; by autocatalysis By similarity
	Modified residue	25	1	Phosphoserine; by autocatalysis By similarity
	Modified residue	40	1	Phosphoserine By similarity
	Modified residue	96	1	Phosphoserine By similarity
	Modified residue	101	1	Phosphoserine By similarity
	Modified residue	108	1	Phosphoserine; by autocatalysis Ref.3 Ref.4
	Modified residue	148	1	Phosphothreonine By similarity
	Modified residue	182	1	Phosphoserine By similarity
	Modified residue	201	1	N6-succinyllysine Ref.6
	Lipidation	2	1	N-myristoyl glycine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9R078 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 6B520A95A0A844E5	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

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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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.
[6]	"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways." Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y. Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract] Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-201, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic fibroblast.
+	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. XP_006530264.1. XM_006530201.1.
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.
PhylomeDB	Q9R078.
TreeFam	TF313827.
Enzyme and pathway databases
Reactome	REACT_147847. Translocation of Glut4 to the Plasma Membrane.
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:	April 16, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program