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Protein

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

Gene

Prkag1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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.2 Publications

Sites

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

GO - Molecular functioni

  • ADP binding Source: UniProtKB
  • AMP binding Source: UniProtKB
  • ATP binding Source: UniProtKB
  • protein kinase binding Source: RGD

GO - Biological processi

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

BRENDAi2.7.11.31. 5301.
ReactomeiR-RNO-163680. AMPK inhibits chREBP transcriptional activation activity.
R-RNO-201722. Formation of the beta-catenin:TCF transactivating complex.
R-RNO-3214841. PKMTs methylate histone lysines.
R-RNO-3769402. Deactivation of the beta-catenin transactivating complex.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi3388. Prkag1.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: Reactome
  • nucleotide-activated protein kinase complex Source: UniProtKB
  • protein complex Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3303305'-AMP-activated protein kinase subunit gamma-1PRO_0000204380Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei260 – 2601Phosphoserine; by ULK11 Publication
Modified residuei262 – 2621Phosphothreonine; by ULK11 Publication
Modified residuei269 – 2691Phosphoserine; by ULK11 Publication

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. There is some ambiguity for a phosphosite: Ser-260/Thr-262.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP80385.
PRIDEiP80385.

PTM databases

iPTMnetiP80385.
PhosphoSiteiP80385.

Expressioni

Tissue specificityi

Highly expressed in heart and brain, also found in kidney, white adipose tissue, lung and spleen.

Gene expression databases

BgeeiENSRNOG00000014813.
GenevisibleiP80385. RN.

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 FNIP2.2 Publications

GO - Molecular functioni

  • protein kinase binding Source: RGD

Protein-protein interaction databases

DIPiDIP-37278N.
IntActiP80385. 1 interaction.
MINTiMINT-4566137.
STRINGi10116.ENSRNOP00000020093.

Structurei

Secondary structure

1
330
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 263Combined sources
Helixi27 – 348Combined sources
Helixi37 – 404Combined sources
Beta strandi43 – 519Combined sources
Helixi56 – 6611Combined sources
Beta strandi69 – 757Combined sources
Turni76 – 794Combined sources
Beta strandi80 – 867Combined sources
Helixi87 – 10115Combined sources
Turni102 – 1043Combined sources
Helixi108 – 1103Combined sources
Helixi113 – 1208Combined sources
Beta strandi121 – 1244Combined sources
Helixi137 – 14711Combined sources
Beta strandi152 – 1554Combined sources
Turni157 – 1593Combined sources
Beta strandi162 – 1665Combined sources
Helixi168 – 17811Combined sources
Beta strandi181 – 1833Combined sources
Helixi186 – 1894Combined sources
Helixi192 – 1954Combined sources
Beta strandi206 – 2094Combined sources
Helixi212 – 22211Combined sources
Beta strandi225 – 2306Combined sources
Beta strandi234 – 2418Combined sources
Helixi242 – 2443Combined sources
Helixi246 – 2505Combined sources
Beta strandi258 – 2603Combined sources
Helixi261 – 2644Combined sources
Helixi265 – 2673Combined sources
Beta strandi269 – 2713Combined sources
Beta strandi277 – 2793Combined sources
Beta strandi280 – 2834Combined sources
Helixi284 – 29411Combined sources
Beta strandi297 – 3026Combined sources
Beta strandi306 – 3138Combined sources
Helixi314 – 3229Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V8QX-ray2.10E1-330[»]
2V92X-ray2.40E1-330[»]
2V9JX-ray2.53E1-330[»]
2Y8LX-ray2.50E1-330[»]
2Y8QX-ray2.80E1-330[»]
2YA3X-ray2.51E1-330[»]
4CFHX-ray3.24E1-330[»]
4EAGX-ray2.70C1-330[»]
4EAIX-ray2.28C1-330[»]
4EAJX-ray2.61C1-330[»]
4EAKX-ray2.50C1-330[»]
4EALX-ray2.51C1-330[»]
4QFGX-ray3.46C1-330[»]
4QFRX-ray3.34C1-330[»]
4QFSX-ray3.55C1-330[»]
ProteinModelPortaliP80385.
SMRiP80385. Positions 23-326.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP80385.

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.2 Publications

Sequence similaritiesi

Contains 4 CBS domains.PROSITE-ProRule annotation

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiKOG1764. Eukaryota.
COG0517. LUCA.
GeneTreeiENSGT00760000119228.
HOGENOMiHOG000176880.
HOVERGENiHBG050431.
InParanoidiP80385.
KOiK07200.
PhylomeDBiP80385.
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]

Sequencei

Sequence statusi: Complete.

P80385-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESVAAESAP APENEHSQET PESNSSVYTT 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 SLEELQIGTY
210 220 230 240 250
ANIAMVRTTT PVYVALGIFV QHRVSALPVV DEKGRVVDIY SKFDVINLAA
260 270 280 290 300
EKTYNNLDVS VTKALQHRSH YFEGVLKCYL HETLEAIINR LVEAEVHRLV
310 320 330
VVDEHDVVKG IVSLSDILQA LVLTGGEKKP
Length:330
Mass (Da):37,386
Last modified:November 1, 1997 - v3
Checksum:i36031E526C1F1E97
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti114 – 1141E → Q AA sequence (PubMed:7961907).Curated
Sequence conflicti201 – 2011A → P AA sequence (PubMed:7961907).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95578 mRNA. Translation: CAA64831.1.
BC097940 mRNA. Translation: AAH97940.1.
U42413 mRNA. Translation: AAC52580.1.
PIRiT10759.
RefSeqiNP_037142.1. NM_013010.2.
UniGeneiRn.11089.

Genome annotation databases

EnsembliENSRNOT00000083354; ENSRNOP00000070458; ENSRNOG00000061499.
GeneIDi25520.
KEGGirno:25520.
UCSCiRGD:3388. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95578 mRNA. Translation: CAA64831.1.
BC097940 mRNA. Translation: AAH97940.1.
U42413 mRNA. Translation: AAC52580.1.
PIRiT10759.
RefSeqiNP_037142.1. NM_013010.2.
UniGeneiRn.11089.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V8QX-ray2.10E1-330[»]
2V92X-ray2.40E1-330[»]
2V9JX-ray2.53E1-330[»]
2Y8LX-ray2.50E1-330[»]
2Y8QX-ray2.80E1-330[»]
2YA3X-ray2.51E1-330[»]
4CFHX-ray3.24E1-330[»]
4EAGX-ray2.70C1-330[»]
4EAIX-ray2.28C1-330[»]
4EAJX-ray2.61C1-330[»]
4EAKX-ray2.50C1-330[»]
4EALX-ray2.51C1-330[»]
4QFGX-ray3.46C1-330[»]
4QFRX-ray3.34C1-330[»]
4QFSX-ray3.55C1-330[»]
ProteinModelPortaliP80385.
SMRiP80385. Positions 23-326.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-37278N.
IntActiP80385. 1 interaction.
MINTiMINT-4566137.
STRINGi10116.ENSRNOP00000020093.

PTM databases

iPTMnetiP80385.
PhosphoSiteiP80385.

Proteomic databases

PaxDbiP80385.
PRIDEiP80385.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000083354; ENSRNOP00000070458; ENSRNOG00000061499.
GeneIDi25520.
KEGGirno:25520.
UCSCiRGD:3388. rat.

Organism-specific databases

CTDi5571.
RGDi3388. Prkag1.

Phylogenomic databases

eggNOGiKOG1764. Eukaryota.
COG0517. LUCA.
GeneTreeiENSGT00760000119228.
HOGENOMiHOG000176880.
HOVERGENiHBG050431.
InParanoidiP80385.
KOiK07200.
PhylomeDBiP80385.
TreeFamiTF313247.

Enzyme and pathway databases

BRENDAi2.7.11.31. 5301.
ReactomeiR-RNO-163680. AMPK inhibits chREBP transcriptional activation activity.
R-RNO-201722. Formation of the beta-catenin:TCF transactivating complex.
R-RNO-3214841. PKMTs methylate histone lysines.
R-RNO-3769402. Deactivation of the beta-catenin transactivating complex.

Miscellaneous databases

EvolutionaryTraceiP80385.
PROiP80385.

Gene expression databases

BgeeiENSRNOG00000014813.
GenevisibleiP80385. RN.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiAAKG1_RAT
AccessioniPrimary (citable) accession number: P80385
Secondary accession number(s): Q4QQW6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 1, 1997
Last modified: September 7, 2016
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.