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Q8BGM7

- AAKG3_MOUSE

UniProt

Q8BGM7 - AAKG3_MOUSE

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Protein

5'-AMP-activated protein kinase subunit gamma-3

Gene

Prkag3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 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 sitei225 – 2251AMP 1By similarity
Binding sitei225 – 2251ATP 1By similarity
Binding sitei306 – 3061AMP 2By similarity
Binding sitei306 – 3061AMP 3By similarity
Binding sitei306 – 3061ATP 2By similarity
Binding sitei307 – 3071ATP 1By similarity
Binding sitei307 – 3071ATP 2By similarity
Binding sitei325 – 3251AMP 1By similarity
Binding sitei325 – 3251ATP 1By similarity
Binding sitei453 – 4531AMP 3By similarity
Binding sitei454 – 4541AMP 1By similarity
Binding sitei454 – 4541ATP 1By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
  2. glucose transport Source: MGI
  3. glycogen biosynthetic process Source: MGI
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.
REACT_257725. Regulation of Rheb GTPase activity by AMPK.

Names & Taxonomyi

Protein namesi
Recommended name:
5'-AMP-activated protein kinase subunit gamma-3
Short name:
AMPK gamma3
Short name:
AMPK subunit gamma-3
Gene namesi
Name:Prkag3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1891343. Prkag3.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4894895'-AMP-activated protein kinase subunit gamma-3PRO_0000204385Add
BLAST

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

PaxDbiQ8BGM7.
PRIDEiQ8BGM7.

PTM databases

PhosphoSiteiQ8BGM7.

Expressioni

Gene expression databases

BgeeiQ8BGM7.
ExpressionAtlasiQ8BGM7. baseline and differential.
GenevestigatoriQ8BGM7.

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

STRINGi10090.ENSMUSP00000080342.

Structurei

3D structure databases

ProteinModelPortaliQ8BGM7.
SMRiQ8BGM7. Positions 181-480.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini197 – 25862CBS 1PROSITE-ProRule annotationAdd
BLAST
Domaini280 – 34061CBS 2PROSITE-ProRule annotationAdd
BLAST
Domaini355 – 41561CBS 3PROSITE-ProRule annotationAdd
BLAST
Domaini427 – 48660CBS 4PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi293 – 31422AMPK 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.
GeneTreeiENSGT00390000009849.
HOGENOMiHOG000176880.
HOVERGENiHBG050431.
InParanoidiQ8BGM7.
KOiK07200.
OMAiAKASRWT.
OrthoDBiEOG74FF0W.
PhylomeDBiQ8BGM7.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8BGM7-1) [UniParc]FASTAAdd to Basket

Also known as: Long

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

        10         20         30         40         50
MEPELEHTLP GTLTWSHSGG PESQEMDFLE QGENSWPSPA VATSSERTCA
60 70 80 90 100
IRGVKASRWT RQEAVEEAEP PGLGEGAQSR PAAESTRQEA TFPKATPLAQ
110 120 130 140 150
AVPLAEAETS PTGWDLLLPD CAASAGGSST GDLELTIEFP APEAWDCELE
160 170 180 190 200
GLGKDRPRPG PSPQAPLLGL SWDDELQKPG AQVYMHFMQE HTCYDAMATS
210 220 230 240 250
SKLVIFDTTL EIKKAFFAMV ANGVRAAPLW DSKKQSFVGM LTITDFILVL
260 270 280 290 300
HRYYRSPLVQ IYEIEEHKIE TWREIYLQGC FKPLVSISPN DSLFEAVYAL
310 320 330 340 350
IKNRIHRLPV LDPVSGTVLY ILTHKRLLKF LHIFGALLPR PSFLCRTIQD
360 370 380 390 400
LGIGTFRDLA VVLETAPVLT ALDIFVDRRV SALPVVNESG QVVGLYSRFD
410 420 430 440 450
VIHLAAQQTY NHLDMSVGEA LRQRTLCLEG VLSCQPHESL GEVIDRIARE
460 470 480
QVHRLVLVDE TQHLLGVVSL SDILQALVLS PAGIDALSA
Length:489
Mass (Da):53,849
Last modified:March 1, 2003 - v1
Checksum:i85C9F71D8BDBDA5D
GO
Isoform 2 (identifier: Q8BGM7-2) [UniParc]FASTAAdd to Basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: Missing.

Show »
Length:464
Mass (Da):51,117
Checksum:iCEC324A5855C3F2E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti390 – 3901G → GS in AAP22981. (PubMed:14970697)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2525Missing in isoform 2. 2 PublicationsVSP_015588Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF525500 mRNA. Translation: AAN47137.1.
AF525501 mRNA. Translation: AAN47138.1.
AY263402 Genomic DNA. Translation: AAP22981.1.
AK036585 mRNA. Translation: BAC29492.1.
BC116749 mRNA. Translation: AAI16750.1.
BC116777 mRNA. Translation: AAI16778.1.
CCDSiCCDS15055.1. [Q8BGM7-1]
RefSeqiNP_714966.1. NM_153744.3. [Q8BGM7-1]
XP_006496051.1. XM_006495988.1. [Q8BGM7-1]
XP_006496052.1. XM_006495989.1. [Q8BGM7-1]
UniGeneiMm.166501.
Mm.453463.

Genome annotation databases

EnsembliENSMUST00000081636; ENSMUSP00000080342; ENSMUSG00000006542. [Q8BGM7-1]
ENSMUST00000113672; ENSMUSP00000109302; ENSMUSG00000006542. [Q8BGM7-2]
ENSMUST00000160732; ENSMUSP00000125344; ENSMUSG00000006542. [Q8BGM7-1]
ENSMUST00000188073; ENSMUSP00000139909; ENSMUSG00000006542. [Q8BGM7-1]
GeneIDi241113.
KEGGimmu:241113.
UCSCiuc007bnb.2. mouse. [Q8BGM7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF525500 mRNA. Translation: AAN47137.1 .
AF525501 mRNA. Translation: AAN47138.1 .
AY263402 Genomic DNA. Translation: AAP22981.1 .
AK036585 mRNA. Translation: BAC29492.1 .
BC116749 mRNA. Translation: AAI16750.1 .
BC116777 mRNA. Translation: AAI16778.1 .
CCDSi CCDS15055.1. [Q8BGM7-1 ]
RefSeqi NP_714966.1. NM_153744.3. [Q8BGM7-1 ]
XP_006496051.1. XM_006495988.1. [Q8BGM7-1 ]
XP_006496052.1. XM_006495989.1. [Q8BGM7-1 ]
UniGenei Mm.166501.
Mm.453463.

3D structure databases

ProteinModelPortali Q8BGM7.
SMRi Q8BGM7. Positions 181-480.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000080342.

PTM databases

PhosphoSitei Q8BGM7.

Proteomic databases

PaxDbi Q8BGM7.
PRIDEi Q8BGM7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000081636 ; ENSMUSP00000080342 ; ENSMUSG00000006542 . [Q8BGM7-1 ]
ENSMUST00000113672 ; ENSMUSP00000109302 ; ENSMUSG00000006542 . [Q8BGM7-2 ]
ENSMUST00000160732 ; ENSMUSP00000125344 ; ENSMUSG00000006542 . [Q8BGM7-1 ]
ENSMUST00000188073 ; ENSMUSP00000139909 ; ENSMUSG00000006542 . [Q8BGM7-1 ]
GeneIDi 241113.
KEGGi mmu:241113.
UCSCi uc007bnb.2. mouse. [Q8BGM7-1 ]

Organism-specific databases

CTDi 53632.
MGIi MGI:1891343. Prkag3.

Phylogenomic databases

eggNOGi COG0517.
GeneTreei ENSGT00390000009849.
HOGENOMi HOG000176880.
HOVERGENi HBG050431.
InParanoidi Q8BGM7.
KOi K07200.
OMAi AKASRWT.
OrthoDBi EOG74FF0W.
PhylomeDBi Q8BGM7.
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.
REACT_257725. Regulation of Rheb GTPase activity by AMPK.

Miscellaneous databases

NextBioi 384884.
PROi Q8BGM7.
SOURCEi Search...

Gene expression databases

Bgeei Q8BGM7.
ExpressionAtlasi Q8BGM7. baseline and differential.
Genevestigatori Q8BGM7.

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 and characterization of mouse 5'-AMP-activated protein kinase gamma3 subunit."
    Yu H., Fujii N., Hirshman M.F., Pomerleau J.M., Goodyear L.J.
    Am. J. Physiol. 286:C283-C292(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    Strain: BALB/c.
    Tissue: Skeletal muscle.
  2. "Comparative sequence analysis of the PRKAG3 region between human and pig: evolution of repetitive sequences and potential new exons."
    Amarger V., Erlandsson R., Pielberg G., Jeon J.-T., Andersson L.
    Cytogenet. Genome Res. 102:163-172(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Bone.
  4. "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 2).
    Tissue: Brain.
  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 nameiAAKG3_MOUSE
AccessioniPrimary (citable) accession number: Q8BGM7
Secondary accession number(s): Q0VG42, Q80WK8, Q8CJ41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: March 1, 2003
Last modified: November 26, 2014
This is version 85 of the entry and version 1 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