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Q91WG5

- AAKG2_MOUSE

UniProt

Q91WG5 - AAKG2_MOUSE

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Protein
5'-AMP-activated protein kinase subunit gamma-2
Gene
Prkag2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei299 – 2991AMP 1 By similarity
Binding sitei299 – 2991ATP 1 By similarity
Binding sitei380 – 3801AMP 2 By similarity
Binding sitei380 – 3801AMP 3 By similarity
Binding sitei380 – 3801ATP 2 By similarity
Binding sitei381 – 3811ATP 1 By similarity
Binding sitei381 – 3811ATP 2 By similarity
Binding sitei399 – 3991AMP 1 By similarity
Binding sitei399 – 3991ATP 1 By similarity
Binding sitei527 – 5271AMP 3 By similarity
Binding sitei528 – 5281AMP 1 By similarity
Binding sitei528 – 5281ATP 1 By similarity

GO - Molecular functioni

  1. ADP binding Source: Ensembl
  2. AMP binding Source: Ensembl
  3. AMP-activated protein kinase activity Source: MGI
  4. ATP binding Source: UniProtKB-KW
  5. cAMP-dependent protein kinase inhibitor activity Source: Ensembl
  6. cAMP-dependent protein kinase regulator activity Source: Ensembl
  7. phosphorylase kinase regulator activity Source: Ensembl
  8. protein kinase activator activity Source: Ensembl

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
  2. glycogen metabolic process Source: Ensembl
  3. intracellular signal transduction Source: Ensembl
  4. positive regulation of peptidyl-threonine phosphorylation Source: Ensembl
  5. protein phosphorylation Source: GOC
  6. regulation of fatty acid metabolic process Source: Ensembl
  7. regulation of glycolytic process 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-2
Short name:
AMPK gamma2
Short name:
AMPK subunit gamma-2
Gene namesi
Name:Prkag2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1336153. Prkag2.

Subcellular locationi

GO - Cellular componenti

  1. AMP-activated protein kinase complex Source: Ensembl
  2. cytosol Source: Reactome
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5665665'-AMP-activated protein kinase subunit gamma-2
PRO_0000204382Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei65 – 651Phosphoserine1 Publication
Modified residuei71 – 711Phosphoserine1 Publication
Modified residuei73 – 731Phosphoserine1 Publication
Modified residuei90 – 901Phosphoserine1 Publication
Modified residuei138 – 1381Phosphoserine1 Publication
Modified residuei143 – 1431Phosphoserine1 Publication
Modified residuei158 – 1581Phosphoserine1 Publication
Modified residuei161 – 1611Phosphoserine1 Publication
Modified residuei196 – 1961Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by ULK1; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1 and AMPK.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ91WG5.
PaxDbiQ91WG5.
PRIDEiQ91WG5.

PTM databases

PhosphoSiteiQ91WG5.

Expressioni

Gene expression databases

ArrayExpressiQ91WG5.
BgeeiQ91WG5.
GenevestigatoriQ91WG5.

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.

Protein-protein interaction databases

BioGridi223832. 1 interaction.
IntActiQ91WG5. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ91WG5.
SMRiQ91WG5. Positions 257-554.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini272 – 33261CBS 1
Add
BLAST
Domaini354 – 41259CBS 2
Add
BLAST
Domaini427 – 48963CBS 3
Add
BLAST
Domaini501 – 55959CBS 4
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi367 – 38822AMPK pseudosubstrate
Add
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.
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.

Sequence similaritiesi

Contains 4 CBS domains.

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiCOG0517.
GeneTreeiENSGT00390000009849.
HOGENOMiHOG000176880.
HOVERGENiHBG050431.
InParanoidiQ91WG5.
KOiK07200.
OMAiGAKQKEN.
OrthoDBiEOG74FF0W.
TreeFamiTF313247.

Family and domain databases

InterProiIPR000644. CBS_dom.
[Graphical view]
PfamiPF00571. CBS. 3 hits.
[Graphical view]
SMARTiSM00116. CBS. 4 hits.
[Graphical view]
PROSITEiPS51371. CBS. 4 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform A (identifier: Q91WG5-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MGSAAMDTKK KKEVSSPGGS SGKKNPSLKR RSLRVHIPDL SSFAMPLLDG    50
DVENSEKHSS RKVDSPFSSG SPSRGLFSRG PQPRPSSPVS APVRPKTSPG 100
SPKTVFPFSY QESPPRSPRR MSFSGIFRSS SKESSPNSNP STSPGGIRFF 150
SRSRKTSSVS SSPSTPTQVT KQHPFPLESY KQEPERPESR IYASSSPPDT 200
GQRFCLAFQS PARPPLASPT YHAPLRTAVL AAAPGPAEAG MLEKLEFQEE 250
EDSESGVYMR FMRSHKCYDI VPTSSKLVVF DTTLQVKKAF FALVANGVRA 300
APLWESKKQS FVGMLTITDF INILHRYYKS PMVQIYELEE HKIETWRELY 350
LQETFKPLVN ISPDASLFDA VYSLIKNKIH RLPVIDPISG NALYILTHKR 400
ILKFLQLFMS DMPKPAFMKQ NLDELGIGTY HNIAFIHPDT PIIKALNIFV 450
ERRISALPVV DESGKVVDIY SKFDVINLAA EKTYNNLDIT VTQALQHRSQ 500
YFEGVVKCSK LETLETIVDR IVRAEVHRLV VVNEADSIVG IISLSDILQA 550
LILTPAGAKQ KETETE 566
Length:566
Mass (Da):62,949
Last modified:July 27, 2011 - v2
Checksum:iD112BFD69D1C5ACB
GO
Isoform B (identifier: Q91WG5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-240: Missing.

Show »
Length:326
Mass (Da):37,312
Checksum:iFEA2EEAB9550999A
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 240240Missing in isoform B.
VSP_015586Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti257 – 2571V → F in AAH15283. 1 Publication
Sequence conflicti516 – 5161T → N in AAQ55224. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY348864 mRNA. Translation: AAQ55224.1.
AC116151 Genomic DNA. No translation available.
AC125270 Genomic DNA. No translation available.
BC015283 mRNA. Translation: AAH15283.1.
CCDSiCCDS19130.1. [Q91WG5-1]
CCDS51437.1. [Q91WG5-2]
RefSeqiNP_001164027.1. NM_001170556.1. [Q91WG5-2]
NP_663376.2. NM_145401.2. [Q91WG5-1]
UniGeneiMm.33649.

Genome annotation databases

EnsembliENSMUST00000030784; ENSMUSP00000030784; ENSMUSG00000028944. [Q91WG5-1]
ENSMUST00000114975; ENSMUSP00000110626; ENSMUSG00000028944. [Q91WG5-2]
GeneIDi108099.
KEGGimmu:108099.
UCSCiuc008wsk.2. mouse. [Q91WG5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY348864 mRNA. Translation: AAQ55224.1 .
AC116151 Genomic DNA. No translation available.
AC125270 Genomic DNA. No translation available.
BC015283 mRNA. Translation: AAH15283.1 .
CCDSi CCDS19130.1. [Q91WG5-1 ]
CCDS51437.1. [Q91WG5-2 ]
RefSeqi NP_001164027.1. NM_001170556.1. [Q91WG5-2 ]
NP_663376.2. NM_145401.2. [Q91WG5-1 ]
UniGenei Mm.33649.

3D structure databases

ProteinModelPortali Q91WG5.
SMRi Q91WG5. Positions 257-554.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 223832. 1 interaction.
IntActi Q91WG5. 1 interaction.

PTM databases

PhosphoSitei Q91WG5.

Proteomic databases

MaxQBi Q91WG5.
PaxDbi Q91WG5.
PRIDEi Q91WG5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000030784 ; ENSMUSP00000030784 ; ENSMUSG00000028944 . [Q91WG5-1 ]
ENSMUST00000114975 ; ENSMUSP00000110626 ; ENSMUSG00000028944 . [Q91WG5-2 ]
GeneIDi 108099.
KEGGi mmu:108099.
UCSCi uc008wsk.2. mouse. [Q91WG5-1 ]

Organism-specific databases

CTDi 51422.
MGIi MGI:1336153. Prkag2.

Phylogenomic databases

eggNOGi COG0517.
GeneTreei ENSGT00390000009849.
HOGENOMi HOG000176880.
HOVERGENi HBG050431.
InParanoidi Q91WG5.
KOi K07200.
OMAi GAKQKEN.
OrthoDBi EOG74FF0W.
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

ChiTaRSi PRKAG2. mouse.
NextBioi 360062.
PROi Q91WG5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q91WG5.
Bgeei Q91WG5.
Genevestigatori Q91WG5.

Family and domain databases

InterProi IPR000644. CBS_dom.
[Graphical view ]
Pfami PF00571. CBS. 3 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 of mouse protein kinase, AMP-activated, gamma 2 non-catalytic subunit."
    Zhou G., Jiang D., Zhang Y.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
    Strain: C57BL/6J.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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] (ISOFORM A).
    Strain: FVB/N.
    Tissue: Kidney.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-71; SER-73; SER-90; SER-138; SER-143; SER-158; SER-161 AND SER-196, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  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.

Entry informationi

Entry nameiAAKG2_MOUSE
AccessioniPrimary (citable) accession number: Q91WG5
Secondary accession number(s): E9QK80, Q6V7V5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 98 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

Similar proteinsi