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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

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • catalytic activity Source: InterPro
  • 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
Complete GO annotation...

Keywords - Biological processi

Carbohydrate metabolism, Transcription, Transcription regulation

Keywords - Ligandi

ATP-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

GO - Cellular componenti

  • cytoplasm Source: SGD
  • nuclear envelope lumen Source: SGD
  • nucleotide-activated protein kinase complex Source: SGD
  • nucleus Source: SGD
  • plasma membrane Source: SGD
Complete GO annotation...

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi63 – 631V → Q: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. 1 Publication
Mutagenesisi136 – 1361C → Y: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. 1 Publication
Mutagenesisi145 – 1451G → E: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. 1 Publication
Mutagenesisi146 – 1461R → A or Q: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. 1 Publication
Mutagenesisi166 – 1661T → N: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. 1 Publication
Mutagenesisi177 – 1771N → A or Y: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. 1 Publication
Mutagenesisi242 – 2421L → E: Decreases SNF1-activation efficiency; when associated with A-291 and E-293. 1 Publication
Mutagenesisi251 – 2511N → I: Leads to resistance to 2-deoxyglucose. 1 Publication
Mutagenesisi291 – 2911R → A: Decreases SNF1-activation efficiency; when associated with E-242 and E-293. 1 Publication
Mutagenesisi293 – 2931H → A: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. 2 Publications
Mutagenesisi293 – 2931H → E: Decreases SNF1-activation efficiency; when associated with E-242 and A-291. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3223225'-AMP-activated protein kinase subunit gammaPRO_0000204389Add
BLAST

Proteomic databases

MaxQBiP12904.

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

WithEntry#Exp.IntActNotes
GAL83Q047394EBI-17537,EBI-7244
SIP1P325784EBI-17537,EBI-17179
SIP2P341646EBI-17537,EBI-17187
SNF1P0678216EBI-17537,EBI-17516
YCL046WP255753EBI-17537,EBI-21748

Protein-protein interaction databases

BioGridi33136. 321 interactions.
DIPiDIP-592N.
IntActiP12904. 33 interactions.
MINTiMINT-364345.

Structurei

Secondary structure

1
322
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 2821Combined sources
Helixi31 – 344Combined sources
Beta strandi37 – 459Combined sources
Helixi50 – 5910Combined sources
Beta strandi65 – 695Combined sources
Turni70 – 734Combined sources
Beta strandi74 – 796Combined sources
Helixi81 – 9313Combined sources
Helixi95 – 1039Combined sources
Helixi106 – 11510Combined sources
Helixi132 – 14211Combined sources
Beta strandi145 – 1528Combined sources
Turni154 – 1563Combined sources
Beta strandi159 – 1668Combined sources
Helixi167 – 17711Combined sources
Helixi179 – 1813Combined sources
Helixi182 – 1854Combined sources
Helixi188 – 1903Combined sources
Helixi208 – 21811Combined sources
Beta strandi221 – 2266Combined sources
Beta strandi231 – 2377Combined sources
Helixi238 – 2469Combined sources
Helixi249 – 2524Combined sources
Helixi257 – 2637Combined sources
Beta strandi272 – 2743Combined sources
Helixi280 – 29011Combined sources
Beta strandi293 – 2986Combined sources
Beta strandi302 – 3098Combined sources
Helixi310 – 31910Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 6-321.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12904.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini37 – 9761CBS 1PROSITE-ProRule annotationAdd
BLAST
Domaini118 – 18164CBS 2PROSITE-ProRule annotationAdd
BLAST
Domaini194 – 25360CBS 3PROSITE-ProRule annotationAdd
BLAST
Domaini262 – 32261CBS 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 4 CBS domains.PROSITE-ProRule annotation

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

GeneTreeiENSGT00390000009849.
HOGENOMiHOG000176880.
OMAiASIHPFK.
OrthoDBiEOG092C39BT.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000644. 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.

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 6-321.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33136. 321 interactions.
DIPiDIP-592N.
IntActiP12904. 33 interactions.
MINTiMINT-364345.

PTM databases

iPTMnetiP12904.

Proteomic databases

MaxQBiP12904.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YGL115W.
SGDiS000003083. SNF4.

Phylogenomic databases

GeneTreeiENSGT00390000009849.
HOGENOMiHOG000176880.
OMAiASIHPFK.
OrthoDBiEOG092C39BT.

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.

Miscellaneous databases

EvolutionaryTraceiP12904.
PROiP12904.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000644. 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 nameiAAKG_YEAST
AccessioniPrimary (citable) accession number: P12904
Secondary accession number(s): D6VU32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: September 7, 2016
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

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

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.