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P12904

- AAKG_YEAST

UniProt

P12904 - AAKG_YEAST

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Protein

5'-AMP-activated protein kinase subunit gamma

Gene
SNF4, CAT3, SCI1, YGL115W
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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

  1. ATP binding Source: UniProtKB-KW
  2. catalytic activity Source: InterPro
  3. protein binding Source: IntAct
  4. protein serine/threonine kinase activator activity Source: SGD

GO - Biological processi

  1. carbohydrate metabolic process Source: UniProtKB-KW
  2. peroxisome organization Source: SGD
  3. positive regulation of gluconeogenesis Source: SGD
  4. positive regulation of protein serine/threonine kinase activity Source: GOC
  5. protein phosphorylation Source: SGD
  6. regulation of transcription from RNA polymerase II promoter Source: SGD
  7. replicative cell aging Source: SGD
  8. 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.
ReactomeiREACT_209479. Regulation of AMPK activity via LKB1.
REACT_212098. AMPK inhibits chREBP transcriptional activation activity.

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
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGL115w.
SGDiS000003083. SNF4.

Subcellular locationi

Nucleus. Cytoplasm 3 Publications

GO - Cellular componenti

  1. AMP-activated protein kinase complex Source: SGD
  2. cytoplasm Source: SGD
  3. nuclear envelope lumen Source: SGD
  4. nucleus Source: SGD
  5. 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.
PaxDbiP12904.
PeptideAtlasiP12904.

Expressioni

Gene expression databases

GenevestigatoriP12904.

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.2 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. 312 interactions.
DIPiDIP-592N.
IntActiP12904. 32 interactions.
MINTiMINT-364345.
STRINGi4932.YGL115W.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP12904.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 4 CBS domains.

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiCOG0517.
GeneTreeiENSGT00390000009849.
HOGENOMiHOG000176880.
OMAiLNCRETH.
OrthoDBiEOG73JM5R.

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

MKPTQDSQEK VSIEQQLAVE SIRKFLNSKT SYDVLPVSYR LIVLDTSLLV    50
KKSLNVLLQN SIVSAPLWDS KTSRFAGLLT TTDFINVIQY YFSNPDKFEL 100
VDKLQLDGLK DIERALGVDQ LDTASIHPSR PLFEACLKML ESRSGRIPLI 150
DQDEETHREI VVSVLTQYRI LKFVALNCRE THFLKIPIGD LNIITQDNMK 200
SCQMTTPVID VIQMLTQGRV SSVPIIDENG YLINVYEAYD VLGLIKGGIY 250
NDLSLSVGEA LMRRSDDFEG VYTCTKNDKL STIMDNIRKA RVHRFFVVDD 300
VGRLVGVLTL SDILKYILLG SN 322
Length:322
Mass (Da):36,401
Last modified:October 1, 1989 - v1
Checksum:i51B387E346EE9561
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi A38906. RGBYC3.
RefSeqi NP_011400.1. NM_001180980.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2NYC X-ray 1.90 A 179-322 [» ]
2NYE X-ray 2.50 A/B 179-322 [» ]
2QLV X-ray 2.60 C/F 7-321 [» ]
3T4N X-ray 2.30 C 2-322 [» ]
3TDH X-ray 2.30 C 2-322 [» ]
3TE5 X-ray 2.50 C 2-322 [» ]
ProteinModelPortali P12904.
SMRi P12904. Positions 6-321.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33136. 312 interactions.
DIPi DIP-592N.
IntActi P12904. 32 interactions.
MINTi MINT-364345.
STRINGi 4932.YGL115W.

Proteomic databases

MaxQBi P12904.
PaxDbi P12904.
PeptideAtlasi P12904.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGL115W ; YGL115W ; YGL115W .
GeneIDi 852763.
KEGGi sce:YGL115W.

Organism-specific databases

CYGDi YGL115w.
SGDi S000003083. SNF4.

Phylogenomic databases

eggNOGi COG0517.
GeneTreei ENSGT00390000009849.
HOGENOMi HOG000176880.
OMAi LNCRETH.
OrthoDBi EOG73JM5R.

Enzyme and pathway databases

BioCyci YEAST:G3O-30613-MONOMER.
Reactomei REACT_209479. Regulation of AMPK activity via LKB1.
REACT_212098. AMPK inhibits chREBP transcriptional activation activity.

Miscellaneous databases

EvolutionaryTracei P12904.
NextBioi 972215.
PROi P12904.

Gene expression databases

Genevestigatori P12904.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
[Graphical view ]
Pfami PF00571. CBS. 3 hits.
[Graphical view ]
SMARTi SM00116. CBS. 4 hits.
[Graphical view ]
PROSITEi PS51371. CBS. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of yeast regulatory gene CAT3 necessary for glucose derepression and nuclear localization of its product."
    Schueller H.-J., Entian K.-D.
    Gene 67:247-257(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
  2. "Molecular analysis of the SNF4 gene of Saccharomyces cerevisiae: evidence for physical association of the SNF4 protein with the SNF1 protein kinase."
    Celenza J.L., Eng F.J., Carlson M.
    Mol. Cell. Biol. 9:5045-5054(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, INTERACTION WITH SNF1.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Correct end of the ORF for the CDC20 gene of Saccharomyces cerevisiae."
    Doi A., Doi K.
    Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
  6. "Mammalian AMP-activated protein kinase shares structural and functional homology with the catalytic domain of yeast Snf1 protein kinase."
    Mitchelhill K.I., Stapleton D., Gao G., House C., Michell B., Katsis F., Witters L.A., Kemp B.E.
    J. Biol. Chem. 269:2361-2364(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 30-34 AND 316-322.
  7. "New genes involved in carbon catabolite repression and derepression in the yeast Saccharomyces cerevisiae."
    Entian K.D., Zimmermann F.K.
    J. Bacteriol. 151:1123-1128(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Genes affecting the regulation of SUC2 gene expression by glucose repression in Saccharomyces cerevisiae."
    Neigeborn L., Carlson M.
    Genetics 108:845-858(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Upstream region of the SUC2 gene confers regulated expression to a heterologous gene in Saccharomyces cerevisiae."
    Sarokin L., Carlson M.
    Mol. Cell. Biol. 5:2521-2526(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "High-affinity glucose transport in Saccharomyces cerevisiae is under general glucose repression control."
    Bisson L.F.
    J. Bacteriol. 170:4838-4845(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Mutational analysis of the Saccharomyces cerevisiae SNF1 protein kinase and evidence for functional interaction with the SNF4 protein."
    Celenza J.L., Carlson M.
    Mol. Cell. Biol. 9:5034-5044(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Absence of glucose-induced cAMP signaling in the Saccharomyces cerevisiae mutants cat1 and cat3 which are deficient in derepression of glucose-repressible proteins."
    Arguelles J.C., Mbonyi K., Van Aelst L., Vanhalewyn M., Jans A.W., Thevelein J.M.
    Arch. Microbiol. 154:199-205(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "N-terminal mutations modulate yeast SNF1 protein kinase function."
    Estruch F., Treitel M.A., Yang X., Carlson M.
    Genetics 132:639-650(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SNF1.
  14. "Transcriptional regulation of the isocitrate lyase encoding gene in Saccharomyces cerevisiae."
    Fernandez E., Fernandez M., Moreno F., Rodicio R.
    FEBS Lett. 333:238-242(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE AMPK COMPLEX.
  15. "Mode of action of the qcr9 and cat3 mutations in restoring the ability of Saccharomyces cerevisiae tps1 mutants to grow on glucose."
    Blazquez M.A., Gancedo C.
    Mol. Gen. Genet. 249:655-664(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "Glucose regulates protein interactions within the yeast SNF1 protein kinase complex."
    Jiang R., Carlson M.
    Genes Dev. 10:3105-3115(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SNF1.
  17. "The Snf1 protein kinase and its activating subunit, Snf4, interact with distinct domains of the Sip1/Sip2/Gal83 component in the kinase complex."
    Jiang R., Carlson M.
    Mol. Cell. Biol. 17:2099-2106(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNF1; SIP1; SIP2 AND GAL83.
  18. "Catabolite repression mutants of Saccharomyces cerevisiae show altered fermentative metabolism as well as cell cycle behavior in glucose-limited chemostat cultures."
    Aon M.A., Cortassa S.
    Biotechnol. Bioeng. 59:203-213(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "Glucose-regulated interaction of a regulatory subunit of protein phosphatase 1 with the Snf1 protein kinase in Saccharomyces cerevisiae."
    Ludin K., Jiang R., Carlson M.
    Proc. Natl. Acad. Sci. U.S.A. 95:6245-6250(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SNF1.
  20. "Quantitation of the effects of disruption of catabolite (de)repression genes on the cell cycle behavior of Saccharomyces cerevisiae."
    Aon M.A., Cortassa S.
    Curr. Microbiol. 38:57-60(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  21. "Evidence for the involvement of the Glc7-Reg1 phosphatase and the Snf1-Snf4 kinase in the regulation of INO1 transcription in Saccharomyces cerevisiae."
    Shirra M.K., Arndt K.M.
    Genetics 152:73-87(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNIF1, FUNCTION OF THE AMPK COMPLEX.
  22. "Regulation of Snf1 kinase. Activation requires phosphorylation of threonine 210 by an upstream kinase as well as a distinct step mediated by the Snf4 subunit."
    McCartney R.R., Schmidt M.C.
    J. Biol. Chem. 276:36460-36466(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "Purification and characterization of Snf1 kinase complexes containing a defined beta subunit composition."
    Nath N., McCartney R.R., Schmidt M.C.
    J. Biol. Chem. 277:50403-50408(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE AMPK COMPLEX, FUNCTION OF THE AMPK COMPLEX.
  24. "The Snf1 protein kinase controls the induction of genes of the iron uptake pathway at the diauxic shift in Saccharomyces cerevisiae."
    Haurie V., Boucherie H., Sagliocco F.
    J. Biol. Chem. 278:45391-45396(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE AMPK COMPLEX.
  25. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  26. "Subunits of the Snf1 kinase heterotrimer show interdependence for association and activity."
    Elbing K., Rubenstein E.M., McCartney R.R., Schmidt M.C.
    J. Biol. Chem. 281:26170-26180(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE AMPK COMPLEX.
  27. "Glucose-responsive regulators of gene expression in Saccharomyces cerevisiae function at the nuclear periphery via a reverse recruitment mechanism."
    Sarma N.J., Haley T.M., Barbara K.E., Buford T.D., Willis K.A., Santangelo G.M.
    Genetics 175:1127-1135(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  28. "Roles of the glycogen-binding domain and Snf4 in glucose inhibition of SNF1 protein kinase."
    Momcilovic M., Iram S.H., Liu Y., Carlson M.
    J. Biol. Chem. 283:19521-19529(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF VAL-63; CYS-136; GLY-145; ARG-146; THR-166; ASN-177; ASN-251 AND HIS-293.
  29. "Structure of the Bateman2 domain of yeast Snf4: dimeric association and relevance for AMP binding."
    Rudolph M.J., Amodeo G.A., Iram S.H., Hong S.P., Pirino G., Carlson M., Tong L.
    Structure 15:65-74(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 179-322, MUTAGENESIS OF LEU-242; ARG-291 AND HIS-293.
  30. "Crystal structure of the heterotrimer core of Saccharomyces cerevisiae AMPK homologue SNF1."
    Amodeo G.A., Rudolph M.J., Tong L.
    Nature 449:492-495(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 7-321 IN COMPLEX WITH SNF1 AND SIP2.
  31. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-322, ADP-BINDING, FUNCTION.

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 3, 2014
This is version 130 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.

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

External Data

Dasty 3

Similar proteinsi