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O54950

- AAKG1_MOUSE

UniProt

O54950 - AAKG1_MOUSE

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Protein

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

Gene

Prkag1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei69 – 691AMP 1By similarity
Binding sitei69 – 691ATP 1By similarity
Binding sitei150 – 1501AMP 2By similarity
Binding sitei150 – 1501AMP 3By similarity
Binding sitei150 – 1501ATP 2By similarity
Binding sitei151 – 1511ATP 1By similarity
Binding sitei151 – 1511ATP 2By similarity
Binding sitei169 – 1691AMP 1By similarity
Binding sitei169 – 1691ATP 1By similarity
Binding sitei297 – 2971AMP 3By similarity
Binding sitei298 – 2981AMP 1By similarity
Binding sitei298 – 2981ATP 1By similarity

GO - Molecular functioni

  1. ADP binding Source: UniProtKB
  2. AMP-activated protein kinase activity Source: MGI
  3. AMP binding Source: UniProtKB
  4. ATP binding Source: UniProtKB

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
  2. positive regulation of gene expression Source: Ensembl
  3. protein heterooligomerization Source: Ensembl
  4. regulation of catalytic activity Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_199054. Translocation of GLUT4 to the plasma membrane.
REACT_205688. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_220701. Regulation of AMPK activity via LKB1.

Names & Taxonomyi

Protein namesi
Recommended name:
5'-AMP-activated protein kinase subunit gamma-1
Short name:
AMPK gamma1
Short name:
AMPK subunit gamma-1
Short name:
AMPKg
Gene namesi
Name:Prkag1
Synonyms:Prkaac
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:108411. Prkag1.

Subcellular locationi

GO - Cellular componenti

  1. AMP-activated protein kinase complex Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: Ensembl
  4. nucleus Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3303305'-AMP-activated protein kinase subunit gamma-1PRO_0000204378Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei260 – 2601Phosphoserine; by ULK1By similarity
Modified residuei262 – 2621Phosphothreonine; by ULK1By similarity
Modified residuei269 – 2691Phosphoserine; by ULK1By similarity

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO54950.
PaxDbiO54950.
PRIDEiO54950.

PTM databases

PhosphoSiteiO54950.

Expressioni

Gene expression databases

BgeeiO54950.
ExpressionAtlasiO54950. baseline and differential.
GenevestigatoriO54950.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi202364. 2 interactions.
IntActiO54950. 3 interactions.
MINTiMINT-4583597.

Structurei

3D structure databases

ProteinModelPortaliO54950.
SMRiO54950. Positions 26-324.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 10261CBS 1PROSITE-ProRule annotationAdd
BLAST
Domaini124 – 18663CBS 2PROSITE-ProRule annotationAdd
BLAST
Domaini197 – 25963CBS 3PROSITE-ProRule annotationAdd
BLAST
Domaini271 – 32858CBS 4PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi137 – 15822AMPK pseudosubstrateAdd
BLAST

Domaini

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).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).By similarity

Sequence similaritiesi

Contains 4 CBS domains.PROSITE-ProRule annotation

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiCOG0517.
HOGENOMiHOG000176880.
HOVERGENiHBG050431.
InParanoidiO54950.
KOiK07200.
OMAiALGIFVE.
OrthoDBiEOG74FF0W.
PhylomeDBiO54950.
TreeFamiTF313247.

Family and domain databases

InterProiIPR000644. CBS_dom.
[Graphical view]
PfamiPF00571. CBS. 4 hits.
[Graphical view]
SMARTiSM00116. CBS. 4 hits.
[Graphical view]
PROSITEiPS51371. CBS. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O54950-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MESVAAESSP ALENEHFQET PESNNSVYTS FMKSHRCYDL IPTSSKLVVF
60 70 80 90 100
DTSLQVKKAF FALVTNGVRA APLWDSKKQS FVGMLTITDF INILHRYYKS
110 120 130 140 150
ALVQIYELEE HKIETWREVY LQDSFKPLVC ISPNASLFDA VSSLIRNKIH
160 170 180 190 200
RLPVIDPESG NTLYILTHKR ILKFLKLFIT EFPKPEFMSK SLQELQIGTY
210 220 230 240 250
ANIAMVRTTT PVYVALGIFV QHRVSALPVV DEKGRVVDIY SKFDVINLAA
260 270 280 290 300
EKTYNNLDVS VTKALQHRSH YFEGVLKCYL HETLETIINR LVEAEVHRLV
310 320 330
VVDEHDVVKG IVSLSDILQA LVLTGGEKKP
Length:330
Mass (Da):37,520
Last modified:September 13, 2005 - v2
Checksum:i539F70EC8819C34D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 801S → C in AAB95475. (PubMed:11306812)Curated
Sequence conflicti137 – 1371L → S in AAB95475. (PubMed:11306812)Curated
Sequence conflicti180 – 1801T → I in AAB95475. (PubMed:11306812)Curated
Sequence conflicti320 – 3201A → D in AAB95475. (PubMed:11306812)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF036535 mRNA. Translation: AAB95475.1.
BC086660 mRNA. Translation: AAH86660.1.
CCDSiCCDS49724.1.
RefSeqiNP_058061.2. NM_016781.2.
UniGeneiMm.6670.

Genome annotation databases

EnsembliENSMUST00000168846; ENSMUSP00000132499; ENSMUSG00000067713.
GeneIDi19082.
KEGGimmu:19082.
UCSCiuc007xoa.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF036535 mRNA. Translation: AAB95475.1 .
BC086660 mRNA. Translation: AAH86660.1 .
CCDSi CCDS49724.1.
RefSeqi NP_058061.2. NM_016781.2.
UniGenei Mm.6670.

3D structure databases

ProteinModelPortali O54950.
SMRi O54950. Positions 26-324.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202364. 2 interactions.
IntActi O54950. 3 interactions.
MINTi MINT-4583597.

PTM databases

PhosphoSitei O54950.

Proteomic databases

MaxQBi O54950.
PaxDbi O54950.
PRIDEi O54950.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000168846 ; ENSMUSP00000132499 ; ENSMUSG00000067713 .
GeneIDi 19082.
KEGGi mmu:19082.
UCSCi uc007xoa.1. mouse.

Organism-specific databases

CTDi 5571.
MGIi MGI:108411. Prkag1.

Phylogenomic databases

eggNOGi COG0517.
HOGENOMi HOG000176880.
HOVERGENi HBG050431.
InParanoidi O54950.
KOi K07200.
OMAi ALGIFVE.
OrthoDBi EOG74FF0W.
PhylomeDBi O54950.
TreeFami TF313247.

Enzyme and pathway databases

Reactomei REACT_199054. Translocation of GLUT4 to the plasma membrane.
REACT_205688. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_220701. Regulation of AMPK activity via LKB1.

Miscellaneous databases

NextBioi 295618.
PROi O54950.
SOURCEi Search...

Gene expression databases

Bgeei O54950.
ExpressionAtlasi O54950. baseline and differential.
Genevestigatori O54950.

Family and domain databases

InterProi IPR000644. CBS_dom.
[Graphical view ]
Pfami PF00571. CBS. 4 hits.
[Graphical view ]
SMARTi SM00116. CBS. 4 hits.
[Graphical view ]
PROSITEi PS51371. CBS. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiAAKG1_MOUSE
AccessioniPrimary (citable) accession number: O54950
Secondary accession number(s): Q5PRE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: September 13, 2005
Last modified: October 29, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3