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Protein

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

Gene

PRKAG1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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)DescriptionActionsGraphical viewLength
Binding sitei70AMP, ADP or ATP 2By similarity1
Binding sitei130AMP, ADP or ATP 1; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei151AMP 3By similarity1
Binding sitei170AMP, ADP or ATP 2By similarity1
Binding sitei200AMP 3By similarity1
Binding sitei205AMP 3; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei269AMP, ADP or ATP 2By similarity1
Binding sitei277AMP, ADP or ATP 2; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei298AMP 3By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi87 – 90AMP, ADP or ATP 1By similarity4
Nucleotide bindingi151 – 152AMP, ADP or ATP 1By similarity2
Nucleotide bindingi226 – 227AMP 3By similarity2
Nucleotide bindingi242 – 245AMP, ADP or ATP 2By similarity4
Nucleotide bindingi298 – 299AMP, ADP or ATP 2By similarity2
Nucleotide bindingi314 – 317AMP 3By similarity4

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandATP-binding, Nucleotide-binding

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002043761 – 3305'-AMP-activated protein kinase subunit gamma-1Add BLAST330

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei261Phosphoserine; by ULK1By similarity1
Modified residuei263Phosphothreonine; by ULK1By similarity1
Modified residuei270Phosphoserine; by ULK1By similarity1

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.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP58108.
PRIDEiP58108.

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

STRINGi9913.ENSBTAP00000043459.

Structurei

3D structure databases

ProteinModelPortaliP58108.
SMRiP58108.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini43 – 103CBS 1PROSITE-ProRule annotationAdd BLAST61
Domaini125 – 187CBS 2PROSITE-ProRule annotationAdd BLAST63
Domaini198 – 260CBS 3PROSITE-ProRule annotationAdd BLAST63
Domaini272 – 329CBS 4PROSITE-ProRule annotationAdd BLAST58

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi138 – 159AMPK pseudosubstrateAdd BLAST22

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 4 CBS domains mediate binding to nucleotides. Of the 4 potential nucleotide-binding sites, 3 are occupied, designated as sites 1, 3, and 4 based on the CBS modules that provide the acidic residue for coordination with the 2'- and 3'-hydroxyl groups of the ribose of AMP. Of these, site 4 appears to be a structural site that retains a tightly held AMP molecule (AMP 3). The 2 remaining sites, 1 and 3, can bind either AMP, ADP or ATP. Site 1 (AMP, ADP or ATP 1) is the high-affinity binding site and likely accommodates AMP or ADP. Site 3 (AMP, ADP or ATP 2) is the weakest nucleotide-binding site on the gamma subunit, yet it is exquisitely sensitive to changes in nucleotide levels and this allows AMPK to respond rapidly to changes in cellular energy status. Site 3 is likely to be responsible for protection of a conserved threonine in the activation loop of the alpha catalytic subunit through conformational changes induced by binding of AMP or ADP.By similarity

Sequence similaritiesi

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiKOG1764. Eukaryota.
COG0517. LUCA.
HOGENOMiHOG000176880.
HOVERGENiHBG050431.
InParanoidiP58108.
KOiK07200.

Family and domain databases

InterProiView protein in InterPro
IPR000644. CBS_dom.
PfamiView protein in Pfam
PF00571. CBS. 3 hits.
SMARTiView protein in SMART
SM00116. CBS. 4 hits.
PROSITEiView protein in PROSITE
PS51371. CBS. 4 hits.

Sequencei

Sequence statusi: Complete.

P58108-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAVPSSDSY PAVENEHLQE TPESNNSVYT SFMKSHRCYD LIPTSSKLVV
60 70 80 90 100
FDTSLQVKKA FFALVTNGVR AAPLWDSKKQ SFVGMLTITD FINILHRYYK
110 120 130 140 150
SALVQIYELE EHKIETWREV YLQDSFKPLV CISPNASLFD AVSSLIRNKI
160 170 180 190 200
HRLPVIDPES GNTLYILTHK RILKFLKLFI TEFPKPEFMS KSLEELQIGT
210 220 230 240 250
YANIAMVRTT TPVYVALGIF VQHRVSALPV VDEKGRVVDI YSKFDVINLA
260 270 280 290 300
AEKTYNNLDV SVTKALQHRS HYFEGVLKCY LHETLETIIN RLVEAEVHRL
310 320 330
VVVDENDVVK GIVSLSDILQ ALVLTGGEKP
Length:330
Mass (Da):37,497
Last modified:June 13, 2006 - v2
Checksum:i40C9C8D5B1798FDA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti121Y → F in AAK19307 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF329081 Genomic DNA. Translation: AAK19307.1.
BT025456 mRNA. Translation: ABF57412.1.
BC113296 mRNA. Translation: AAI13297.1.
RefSeqiNP_777011.2. NM_174586.2.
UniGeneiBt.5588.

Genome annotation databases

GeneIDi282324.
KEGGibta:282324.

Similar proteinsi

Entry informationi

Entry nameiAAKG1_BOVIN
AccessioniPrimary (citable) accession number: P58108
Secondary accession number(s): Q29RZ6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: June 13, 2006
Last modified: August 30, 2017
This is version 83 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families