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Protein

5'-AMP-activated protein kinase subunit gamma

Gene

SNF4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Adenine nucleotides-binding subunit gamma 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. 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 (SNF1) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits.18 Publications

Miscellaneous

Present with 11700 molecules/cell in log phase SD medium.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei146ADP 1By similarity1
Binding sitei195AMP, ADP or ATP 21 Publication1
Binding sitei200AMP, ADP or ATP 2; via amide nitrogen and carbonyl oxygen1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi166 – 169ADP 1By similarity4
Nucleotide bindingi221 – 222AMP, ADP or ATP 21 Publication2
Nucleotide bindingi291 – 293ADP 1By similarity3
Nucleotide bindingi309 – 312AMP, ADP or ATP 21 Publication4

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • protein serine/threonine kinase activator activity Source: SGD

GO - Biological processi

  • carbohydrate metabolic process Source: UniProtKB-KW
  • peroxisome organization Source: SGD
  • positive regulation of gluconeogenesis Source: SGD
  • protein phosphorylation Source: SGD
  • regulation of transcription from RNA polymerase II promoter Source: SGD
  • replicative cell aging Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Biological processCarbohydrate metabolism, Transcription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30613-MONOMER.
ReactomeiR-SCE-163680. AMPK inhibits chREBP transcriptional activation activity.
R-SCE-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-SCE-380972. Energy dependent regulation of mTOR by LKB1-AMPK.

Names & Taxonomyi

Protein namesi
Recommended name:
5'-AMP-activated protein kinase subunit gamma
Short name:
AMPK gamma
Short name:
AMPK subunit gamma
Alternative name(s):
Regulatory protein CAT3
Sucrose non-fermenting protein 4
Gene namesi
Name:SNF4
Synonyms:CAT3, SCI1
Ordered Locus Names:YGL115W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL115W.
SGDiS000003083. SNF4.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Leads to a decrease in the length of G1 with respect to the wild-type strain along with a smaller difference in the cell cycle length of parent and daughter cells.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi63V → Q: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. 1 Publication1
Mutagenesisi136C → Y: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. 1 Publication1
Mutagenesisi145G → E: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. 1 Publication1
Mutagenesisi146R → A or Q: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. 1 Publication1
Mutagenesisi166T → N: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. 1 Publication1
Mutagenesisi177N → A or Y: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. 1 Publication1
Mutagenesisi242L → E: Decreases SNF1-activation efficiency; when associated with A-291 and E-293. 1 Publication1
Mutagenesisi251N → I: Leads to resistance to 2-deoxyglucose. 1 Publication1
Mutagenesisi291R → A: Decreases SNF1-activation efficiency; when associated with E-242 and E-293. 1 Publication1
Mutagenesisi293H → A: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. 2 Publications1
Mutagenesisi293H → E: Decreases SNF1-activation efficiency; when associated with E-242 and A-291. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002043891 – 3225'-AMP-activated protein kinase subunit gammaAdd BLAST322

Proteomic databases

MaxQBiP12904.
PRIDEiP12904.

PTM databases

iPTMnetiP12904.

Interactioni

Subunit structurei

AMPK is a heterotrimer of an alpha catalytic subunit (SNF1), a beta (SIP1, SIP2 or GAL83) and a gamma non-catalytic subunits (SNF4). Note=Interaction between SNF1 and SNF4 is inhibited by high levels of glucose.3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi33136. 638 interactors.
DIPiDIP-592N.
IntActiP12904. 43 interactors.
MINTiMINT-364345.
STRINGi4932.YGL115W.

Structurei

Secondary structure

1322
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 28Combined sources21
Helixi31 – 34Combined sources4
Beta strandi37 – 45Combined sources9
Helixi50 – 59Combined sources10
Beta strandi65 – 69Combined sources5
Turni70 – 73Combined sources4
Beta strandi74 – 79Combined sources6
Helixi81 – 93Combined sources13
Helixi95 – 103Combined sources9
Helixi106 – 115Combined sources10
Helixi132 – 142Combined sources11
Beta strandi145 – 152Combined sources8
Turni154 – 156Combined sources3
Beta strandi159 – 166Combined sources8
Helixi167 – 177Combined sources11
Helixi179 – 181Combined sources3
Helixi182 – 185Combined sources4
Helixi188 – 190Combined sources3
Helixi208 – 218Combined sources11
Beta strandi221 – 226Combined sources6
Beta strandi231 – 237Combined sources7
Helixi238 – 246Combined sources9
Helixi249 – 252Combined sources4
Helixi257 – 263Combined sources7
Beta strandi272 – 274Combined sources3
Helixi280 – 290Combined sources11
Beta strandi293 – 298Combined sources6
Beta strandi302 – 309Combined sources8
Helixi310 – 319Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2NYCX-ray1.90A179-322[»]
2NYEX-ray2.50A/B179-322[»]
2QLVX-ray2.60C/F7-321[»]
3T4NX-ray2.30C2-322[»]
3TDHX-ray2.30C2-322[»]
3TE5X-ray2.50C2-322[»]
ProteinModelPortaliP12904.
SMRiP12904.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12904.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini37 – 97CBS 1Add BLAST61
Domaini118 – 181CBS 2Add BLAST64
Domaini194 – 253CBS 3Add BLAST60
Domaini262 – 322CBS 4Add BLAST61

Domaini

The 4 CBS domains mediate binding to nucleotides. Of the 4 potential nucleotide-binding sites, 2 are occupied, designated as sites 2 and 3 based on the CBS modules that provide the acidic residue for coordination with the 2'- and 3'-hydroxyl groups of the ribose of AMP. Site 3 can bind either AMP, ADP or ATP (AMP, ADP or ATP 2). Site 2 binds specifically ADP (ADP 1) and 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 ADP (PubMed:22019086).1 Publication

Sequence similaritiesi

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

GeneTreeiENSGT00390000009849.
HOGENOMiHOG000176880.
KOiK07200.
OMAiFPGVVIC.
OrthoDBiEOG092C39BT.

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.

P12904-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPTQDSQEK VSIEQQLAVE SIRKFLNSKT SYDVLPVSYR LIVLDTSLLV
60 70 80 90 100
KKSLNVLLQN SIVSAPLWDS KTSRFAGLLT TTDFINVIQY YFSNPDKFEL
110 120 130 140 150
VDKLQLDGLK DIERALGVDQ LDTASIHPSR PLFEACLKML ESRSGRIPLI
160 170 180 190 200
DQDEETHREI VVSVLTQYRI LKFVALNCRE THFLKIPIGD LNIITQDNMK
210 220 230 240 250
SCQMTTPVID VIQMLTQGRV SSVPIIDENG YLINVYEAYD VLGLIKGGIY
260 270 280 290 300
NDLSLSVGEA LMRRSDDFEG VYTCTKNDKL STIMDNIRKA RVHRFFVVDD
310 320
VGRLVGVLTL SDILKYILLG SN
Length:322
Mass (Da):36,401
Last modified:October 1, 1989 - v1
Checksum:i51B387E346EE9561
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21760 Genomic DNA. Translation: AAA34472.1.
M30470 Genomic DNA. Translation: AAA35061.1.
Z72637 Genomic DNA. Translation: CAA96823.1.
D16506 Genomic DNA. Translation: BAA03958.1.
BK006941 Genomic DNA. Translation: DAA07993.1.
PIRiA38906. RGBYC3.
RefSeqiNP_011400.1. NM_001180980.1.

Genome annotation databases

EnsemblFungiiYGL115W; YGL115W; YGL115W.
GeneIDi852763.
KEGGisce:YGL115W.

Similar proteinsi

Entry informationi

Entry nameiAAKG_YEAST
AccessioniPrimary (citable) accession number: P12904
Secondary accession number(s): D6VU32
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: November 22, 2017
This is version 162 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names