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

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O54950 (AAKG1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 92. 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 gamma-1
Short name=AMPK gamma1
Short name=AMPK subunit gamma-1
Short name=AMPKg

Gene names

Name:	Prkag1
Synonyms:	Prkaac

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	330 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism
Domain	CBS domain Repeat
Ligand	ATP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW protein heterooligomerization Inferred from electronic annotation. Source: Compara regulation of catalytic activity Inferred from electronic annotation. Source: Compara response to stress Traceable author statement PubMed 10098881. Source: MGI
Cellular_component	AMP-activated protein kinase complex Inferred from sequence or structural similarity. Source: UniProtKB cytosol Traceable author statement. Source: Reactome nucleus Inferred from direct assay PubMed 10098881. Source: MGI
Molecular_function	ADP binding Inferred from sequence or structural similarity. Source: UniProtKB AMP binding Inferred from sequence or structural similarity. Source: UniProtKB AMP-activated protein kinase activity Traceable author statement PubMed 10098881. Source: MGI ATP binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 330

330

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

PRO_0000204378

Regions

Domain

42 – 102

CBS 1

Domain

124 – 186

CBS 2

Domain

197 – 259

CBS 3

Domain

271 – 328

CBS 4

Motif

137 – 158

AMPK pseudosubstrate

Sites

Binding site

AMP 1 By similarity

Binding site

ATP 1 By similarity

Binding site

150

AMP 2 By similarity

Binding site

150

AMP 3 By similarity

Binding site

150

ATP 2 By similarity

Binding site

151

ATP 1 By similarity

Binding site

151

ATP 2 By similarity

Binding site

169

AMP 1 By similarity

Binding site

169

ATP 1 By similarity

Binding site

297

AMP 3 By similarity

Binding site

298

AMP 1 By similarity

Binding site

298

ATP 1 By similarity

Amino acid modifications

Modified residue

260

Phosphoserine; by ULK1 By similarity

Modified residue

262

Phosphothreonine; by ULK1 By similarity

Modified residue

269

Phosphoserine; by ULK1 By similarity

Experimental info

Sequence conflict

S → C in AAB95475. Ref.1

Sequence conflict

137

L → S in AAB95475. Ref.1

Sequence conflict

180

T → I in AAB95475. Ref.1

Sequence conflict

320

A → D in AAB95475. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

O54950 [UniParc].

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

330

37,520

        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' referencesShow '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.
IPI	IPI00119930.
RefSeq	NP_058061.2. NM_016781.2.
UniGene	Mm.6670.
3D structure databases
ProteinModelPortal	O54950.
SMR	O54950. Positions 23-326.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4583597.
PTM databases
PhosphoSite	O54950.
Proteomic databases
PaxDb	O54950.
PRIDE	O54950.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000168846; ENSMUSP00000132499; ENSMUSG00000067713.
GeneID	19082.
KEGG	mmu:19082.
UCSC	uc007xoa.1. mouse.
Organism-specific databases
CTD	5571.
MGI	MGI:108411. Prkag1.
Phylogenomic databases
eggNOG	COG0517.
HOGENOM	HOG000176880.
HOVERGEN	HBG050431.
InParanoid	O54950.
KO	K07200.
OMA	ALGIFVE.
OrthoDB	EOG45DWPQ.
Enzyme and pathway databases
Reactome	REACT_147847. Translocation of Glut4 to the Plasma Membrane. REACT_88307. Membrane Trafficking.
Gene expression databases
ArrayExpress	O54950.
Bgee	O54950.
Genevestigator	O54950.
GermOnline	ENSMUSG00000067713. Mus musculus.
Family and domain databases
InterPro	IPR000644. Cysta_beta_synth_core. [Graphical view]
Pfam	PF00571. CBS. 3 hits. [Graphical view]
SMART	SM00116. CBS. 4 hits. [Graphical view]
PROSITE	PS51371. CBS. 4 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	295618.
SOURCE	Search...

Entry information

Entry name

AAKG1_MOUSE

Accession

Primary (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:	May 29, 2013
This is version 92 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

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

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

Sites

Amino acid modifications

Experimental info

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