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Q9R078 (AAKB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
5'-AMP-activated protein kinase subunit beta-1

Short name=AMPK subunit beta-1
Short name=AMPKb
Gene names
Name:Prkab1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length270 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 2702695'-AMP-activated protein kinase subunit beta-1
PRO_0000204364

Regions

Region68 – 16396Glycogen-binding domain By similarity

Amino acid modifications

Modified residue41Phosphothreonine By similarity
Modified residue51Phosphoserine By similarity
Modified residue61Phosphoserine By similarity
Modified residue191Phosphothreonine By similarity
Modified residue241Phosphoserine; by autocatalysis By similarity
Modified residue251Phosphoserine; by autocatalysis By similarity
Modified residue401Phosphoserine By similarity
Modified residue961Phosphoserine By similarity
Modified residue1011Phosphoserine By similarity
Modified residue1081Phosphoserine; by autocatalysis Ref.3 Ref.4
Modified residue1481Phosphothreonine By similarity
Modified residue1821Phosphoserine By similarity
Modified residue2011N6-succinyllysine Ref.6
Lipidation21N-myristoyl glycine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9R078 [UniParc].

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

FASTA27030,308
        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' 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.
RefSeqNP_114075.1. NM_031869.2.
XP_006530264.1. XM_006530201.1.
UniGeneMm.458152.

3D structure databases

ProteinModelPortalQ9R078.
SMRQ9R078. Positions 77-270.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202363. 1 interaction.
IntActQ9R078. 10 interactions.
MINTMINT-4086419.

PTM databases

PhosphoSiteQ9R078.

Proteomic databases

PaxDbQ9R078.
PRIDEQ9R078.

Protocols and materials databases

DNASU19079.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031486; ENSMUSP00000031486; ENSMUSG00000029513.
ENSMUST00000111999; ENSMUSP00000107630; ENSMUSG00000029513.
GeneID19079.
KEGGmmu:19079.
UCSCuc008zew.1. mouse.

Organism-specific databases

CTD5564.
MGIMGI:1336167. Prkab1.

Phylogenomic databases

eggNOGNOG238368.
GeneTreeENSGT00390000001416.
HOGENOMHOG000230597.
HOVERGENHBG050430.
InParanoidQ9R078.
KOK07199.
OMADADIFHG.
OrthoDBEOG7SXW3Z.
PhylomeDBQ9R078.
TreeFamTF313827.

Enzyme and pathway databases

ReactomeREACT_147847. Translocation of Glut4 to the Plasma Membrane.

Gene expression databases

ArrayExpressQ9R078.
BgeeQ9R078.
GenevestigatorQ9R078.

Family and domain databases

InterProIPR006828. AMP_prot_kin_bsu_interact-dom.
IPR014756. Ig_E-set.
[Graphical view]
PfamPF04739. AMPKBI. 1 hit.
[Graphical view]
SMARTSM01010. AMPKBI. 1 hit.
[Graphical view]
SUPFAMSSF81296. SSF81296. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPRKAB1. mouse.
NextBio295614.
PROQ9R078.
SOURCESearch...

Entry information

Entry nameAAKB1_MOUSE
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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