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P12904

- AAKG_YEAST

UniProt

P12904 - AAKG_YEAST

Protein

5'-AMP-activated protein kinase subunit gamma

Gene

SNF4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Oct 1989)
      Previous versions | rss
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    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

    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

    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

    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.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. 313 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.
    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

    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. 313 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

    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: October 1, 2014
    This is version 131 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

    External Data

    Dasty 3