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O54950 (AAKG1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. 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 gamma-1

Short name=AMPK gamma1
Short name=AMPK subunit gamma-1
Short name=AMPKg
Gene names
Name:Prkag1
Synonyms:Prkaac
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

AMP/ATP-binding 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. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive 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 AMPK pseudosubstrate motif resembles the sequence around sites phosphorylated on target proteins of AMPK, except the presence of a non-phosphorylatable residue in place of Ser. In the absence of AMP this pseudosubstrate sequence may bind to the active site groove on the alpha subunit (PRKAA1 or PRKAA2), preventing phosphorylation by the upstream activating kinase STK11/LKB1 By similarity.

The CBS domains mediate binding to AMP, ADP and ATP. 2 sites bind either AMP or ATP, whereas a third site contains a tightly bound AMP that does not exchange. Under physiological conditions AMPK mainly exists in its inactive form in complex with ATP, which is much more abundant than AMP By similarity.

Post-translational modification

Phosphorylated by ULK1 and ULK2; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1, ULK2 and AMPK. Ref.3

Sequence similarities

Belongs to the 5'-AMP-activated protein kinase gamma subunit family.

Contains 4 CBS domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3303305'-AMP-activated protein kinase subunit gamma-1
PRO_0000204378

Regions

Domain42 – 10261CBS 1
Domain124 – 18663CBS 2
Domain197 – 25963CBS 3
Domain271 – 32858CBS 4
Motif137 – 15822AMPK pseudosubstrate

Sites

Binding site691AMP 1 By similarity
Binding site691ATP 1 By similarity
Binding site1501AMP 2 By similarity
Binding site1501AMP 3 By similarity
Binding site1501ATP 2 By similarity
Binding site1511ATP 1 By similarity
Binding site1511ATP 2 By similarity
Binding site1691AMP 1 By similarity
Binding site1691ATP 1 By similarity
Binding site2971AMP 3 By similarity
Binding site2981AMP 1 By similarity
Binding site2981ATP 1 By similarity

Amino acid modifications

Modified residue2601Phosphoserine; by ULK1 By similarity
Modified residue2621Phosphothreonine; by ULK1 By similarity
Modified residue2691Phosphoserine; by ULK1 By similarity

Experimental info

Sequence conflict801S → C in AAB95475. Ref.1
Sequence conflict1371L → S in AAB95475. Ref.1
Sequence conflict1801T → I in AAB95475. Ref.1
Sequence conflict3201A → D in AAB95475. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O54950 [UniParc].

Last modified September 13, 2005. Version 2.
Checksum: 539F70EC8819C34D

FASTA33037,520
        10         20         30         40         50         60 
MESVAAESSP ALENEHFQET PESNNSVYTS FMKSHRCYDL IPTSSKLVVF DTSLQVKKAF 

        70         80         90        100        110        120 
FALVTNGVRA APLWDSKKQS FVGMLTITDF INILHRYYKS ALVQIYELEE HKIETWREVY 

       130        140        150        160        170        180 
LQDSFKPLVC ISPNASLFDA VSSLIRNKIH RLPVIDPESG NTLYILTHKR ILKFLKLFIT 

       190        200        210        220        230        240 
EFPKPEFMSK SLQELQIGTY ANIAMVRTTT PVYVALGIFV QHRVSALPVV DEKGRVVDIY 

       250        260        270        280        290        300 
SKFDVINLAA EKTYNNLDVS VTKALQHRSH YFEGVLKCYL HETLETIINR LVEAEVHRLV 

       310        320        330 
VVDEHDVVKG IVSLSDILQA LVLTGGEKKP 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, organisation, chromosomal localization and expression analysis of the mouse Prkag1 gene."
Shamsadin R., Jantsan K., Adham I.M., Engel W.
Cytogenet. Cell Genet. 92:134-138(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[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].
Strain: C57BL/6.
Tissue: Eye.
[3]"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 AND ULK2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF036535 mRNA. Translation: AAB95475.1.
BC086660 mRNA. Translation: AAH86660.1.
CCDSCCDS49724.1.
RefSeqNP_058061.2. NM_016781.2.
UniGeneMm.6670.

3D structure databases

ProteinModelPortalO54950.
SMRO54950. Positions 26-324.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202364. 2 interactions.
IntActO54950. 3 interactions.
MINTMINT-4583597.

PTM databases

PhosphoSiteO54950.

Proteomic databases

MaxQBO54950.
PaxDbO54950.
PRIDEO54950.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000168846; ENSMUSP00000132499; ENSMUSG00000067713.
GeneID19082.
KEGGmmu:19082.
UCSCuc007xoa.1. mouse.

Organism-specific databases

CTD5571.
MGIMGI:108411. Prkag1.

Phylogenomic databases

eggNOGCOG0517.
HOGENOMHOG000176880.
HOVERGENHBG050431.
InParanoidO54950.
KOK07200.
OMAALGIFVE.
OrthoDBEOG74FF0W.
PhylomeDBO54950.
TreeFamTF313247.

Enzyme and pathway databases

ReactomeREACT_147847. Translocation of Glut4 to the Plasma Membrane.
REACT_209837. Membrane Trafficking.
REACT_224594. Organelle biogenesis and maintenance.

Gene expression databases

BgeeO54950.
GenevestigatorO54950.

Family and domain databases

InterProIPR000644. CBS_dom.
[Graphical view]
PfamPF00571. CBS. 4 hits.
[Graphical view]
SMARTSM00116. CBS. 4 hits.
[Graphical view]
PROSITEPS51371. CBS. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio295618.
PROO54950.
SOURCESearch...

Entry information

Entry nameAAKG1_MOUSE
AccessionPrimary (citable) accession number: O54950
Secondary accession number(s): Q5PRE8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: September 13, 2005
Last modified: July 9, 2014
This is version 104 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