PRKAG3 ELISA Kit for Human(Homo sapiens) | EIAab.comPRKAG3 ELISA Kit for Human(Homo sapiens)

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Index > Protein center > PRKAG3(Gene name) > Human

PRKAG3 (Gene name),

5'-AMP-activated protein kinase subunit gamma-3 (Protein name ), AAKG3_HUMAN from NCBI database.

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General Annotation

Antigen Annotation

Predicted Eptitope

Vaild Sequence

Related Databases

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Gene name:

PRKAG3(AMPKG3);

Protein name:

5'-AMP-activated protein kinase subunit gamma-3(AMPK gamma3;AMPK subunit gamma-3);

Alternative:

Organism:

Human (Homo sapiens).

General Annotation

Sub Unit:

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.

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.

Subcellular Location:

N/A

Protein Attributes:

Sequence length:

489

Sequence:

50:

100:

150:

200:

250:

300:

350:

400:

450:

489:

QVHRLVLVDE | TQHLLGVVSL | SDILQALVLS | PAGIDALGA

3D Structure:

N/A

Predicted Eptitope:

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Vaild Sequence:

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Related Databases

UniGene:

Hs.591634

SMR:

Q9UGI9

STRING:

9606.ENSP00000233944

KEGG:

hsa:53632

MIM:

604976

String:

Q9UGI9

Pfam:

PF00571

Uniprot:

Q9UGI9

FOR

ELISA Kit for Human AMPK gamma3

CLIA Kit for Human AMPK gamma3

Polyclonal Antibody for Human AMPK gamma3

Monoclonal Antibody for Human AMPK gamma3

Protein for Human AMPK gamma3

R&D Technical Data

For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.

Precision

For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.

Recovery

For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.

Linearity

For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.

References

1.

"Characterization of AMP-activated protein kinase gamma-subunit isoforms and their role in AMP binding."
Cheung P.C.F. , Salt I.P. , Davies S.P. , Hardie D.G. , Carling D.
Biochem. J.346:659-669(2000) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)
2.

"A mutation in PRKAG3 associated with excess glycogen content in pig skeletal muscle."
Milan D. , Jeon J.-T. , Looft C. , Amarger V. , Robic A. , Thelander M. , Rogel-Gaillard C. , Paul S. , Iannuccelli N. , Rask L. , Ronne H. , Lundstroem K. , Reinsch N. , Gellin J. , Kalm E. , Le Roy P. , Chardon P. , Andersson L.
Science288:1248-1251(2000) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2)
tissue: Skeletal muscle.
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]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1);VARIANT ALA-71
4.

"CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations."
Scott J.W. , Hawley S.A. , Green K.A. , Anis M. , Stewart G. , Scullion G.A. , Norman D.G. , Hardie D.G.
J. Clin. Invest.113:274-284(2004) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: DOMAIN CBS;AMP-BINDING;ATP-BINDING;FUNCTION
5.

"Regulation of AMP-activated protein kinase by a pseudosubstrate sequence on the gamma subunit."
Scott J.W. , Ross F.A. , Liu J.K. , Hardie D.G.
EMBO J.26:806-815(2007) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: DOMAIN AMPK PSEUDOSUBSTRATE
6.

"AMP-activated protein kinase in metabolic control and insulin signaling."
Towler M.C. , Hardie D.G.
Circ. Res.100:328-341(2007) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: REVIEW ON FUNCTION
7.

"AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy."
Hardie D.G.
Nat. Rev. Mol. Cell Biol.8:774-785(2007) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: REVIEW ON FUNCTION
8.

"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.
Autophagy7:696-706(2011) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION BY ULK1
9.

"Gain-of-function R225W mutation in human AMPKgamma(3) causing increased glycogen and decreased triglyceride in skeletal muscle."
Costford S.R. , Kavaslar N. , Ahituv N. , Chaudhry S.N. , Schackwitz W.S. , Dent R. , Pennacchio L.A. , McPherson R. , Harper M.E.
PLoS ONE2:E903-E903(2007) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: VARIANTS ALA-71; GLN-76; GLY-103; VAL-113; VAL-153; PRO-161; SER-171; SER-180; THR-197; GLN-211; GLN-225; TRP-225; ARG-260; THR-269; CYS-307; GLN-340; TRP-340; MET-446; VAL-482 AND ASN-485;POLYMORPHISM

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