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P06782

- SNF1_YEAST

UniProt

P06782 - SNF1_YEAST

Protein

Carbon catabolite-derepressing protein kinase

Gene

SNF1

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 167 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
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    Functioni

    Essential for release from glucose repression. It interacts and has functional relationship to the regulatory protein SNF4. Could phosphorylate CAT8. Phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac formation, and which is required for transcriptional activation through TBP recruitment to the promoters.1 Publication

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei84 – 841ATPPROSITE-ProRule annotation
    Active sitei177 – 1771Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi61 – 699ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. biofilm formation Source: SGD
    2. carbohydrate metabolic process Source: UniProtKB-KW
    3. cell adhesion Source: SGD
    4. cellular response to nitrogen starvation Source: SGD
    5. fungal-type cell wall assembly Source: SGD
    6. invasive growth in response to glucose limitation Source: SGD
    7. negative regulation of translation Source: SGD
    8. positive regulation of filamentous growth of a population of unicellular organisms in response to starvation Source: SGD
    9. positive regulation of gluconeogenesis Source: SGD
    10. protein phosphorylation Source: SGD
    11. pseudohyphal growth Source: SGD
    12. regulation of carbohydrate metabolic process Source: SGD
    13. replicative cell aging Source: SGD

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30003-MONOMER.
    BRENDAi2.7.11.1. 984.
    ReactomeiREACT_209479. Regulation of AMPK activity via LKB1.
    REACT_212098. AMPK inhibits chREBP transcriptional activation activity.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbon catabolite-derepressing protein kinase (EC:2.7.11.1)
    Gene namesi
    Name:SNF1
    Synonyms:CAT1, CCR1, GLC2, PAS14
    Ordered Locus Names:YDR477W
    ORF Names:D8035.20
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR477w.
    SGDiS000002885. SNF1.

    Subcellular locationi

    GO - Cellular componenti

    1. AMP-activated protein kinase complex Source: SGD
    2. cytoplasm Source: SGD
    3. fungal-type vacuole Source: SGD
    4. nuclear envelope lumen Source: SGD
    5. nuclear membrane Source: UniProtKB-SubCell
    6. nucleus Source: SGD

    Keywords - Cellular componenti

    Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 633633Carbon catabolite-derepressing protein kinasePRO_0000086670Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei210 – 2101Phosphothreonine; by autocatalysis3 Publications
    Modified residuei413 – 4131Phosphoserine4 Publications
    Modified residuei487 – 4871Phosphoserine2 Publications
    Modified residuei632 – 6321Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP06782.
    PaxDbiP06782.
    PeptideAtlasiP06782.

    Expressioni

    Gene expression databases

    GenevestigatoriP06782.

    Interactioni

    Subunit structurei

    Interacts with CTK1, GAL83, SAK1, SIP1, SIP2 and SNF4.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC14Q006842EBI-17516,EBI-4192
    GAL83Q047395EBI-17516,EBI-7244
    NPR1P222112EBI-17516,EBI-12207
    REG1Q008163EBI-17516,EBI-8270
    SIP2P341649EBI-17516,EBI-17187
    SNF4P1290416EBI-17516,EBI-17537

    Protein-protein interaction databases

    BioGridi32529. 435 interactions.
    DIPiDIP-18N.
    IntActiP06782. 25 interactions.
    MINTiMINT-364314.
    STRINGi4932.YDR477W.

    Structurei

    Secondary structure

    1
    633
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi56 – 627
    Helixi64 – 663
    Beta strandi69 – 735
    Turni75 – 773
    Beta strandi80 – 878
    Helixi88 – 914
    Helixi97 – 10913
    Beta strandi118 – 1236
    Beta strandi125 – 1339
    Helixi139 – 1457
    Helixi151 – 17020
    Turni180 – 1823
    Beta strandi183 – 1853
    Beta strandi191 – 1933
    Turni207 – 2093
    Helixi215 – 2173
    Helixi220 – 2234
    Beta strandi224 – 2274
    Helixi232 – 24716
    Helixi257 – 26610
    Helixi277 – 28610
    Helixi291 – 2933
    Helixi297 – 3026
    Helixi304 – 3074
    Helixi312 – 3143
    Turni317 – 3193
    Helixi471 – 4733
    Helixi475 – 48511
    Helixi489 – 4924
    Beta strandi506 – 5116
    Helixi515 – 52915
    Beta strandi532 – 5343
    Helixi538 – 5403
    Beta strandi543 – 5486
    Beta strandi565 – 57612
    Beta strandi579 – 59012
    Helixi607 – 6104
    Helixi613 – 62816

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FH9X-ray2.80A46-319[»]
    2QLVX-ray2.60A/D460-630[»]
    3DAEX-ray2.90A/B41-315[»]
    3HYHX-ray2.20A/B41-315[»]
    3MN3X-ray2.38A50-320[»]
    3T4NX-ray2.30A457-633[»]
    3TDHX-ray2.30A457-633[»]
    3TE5X-ray2.50A457-633[»]
    ProteinModelPortaliP06782.
    SMRiP06782. Positions 18-630.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06782.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini55 – 306252Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi18 – 3215Poly-HisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00740000115114.
    HOGENOMiHOG000233016.
    KOiK12761.
    OMAiKRMLIVN.
    OrthoDBiEOG793BK1.

    Family and domain databases

    InterProiIPR028375. KA1/Ssp2_C.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR013896. Ubiquitin-assoc_dom.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    PF08587. UBA_2. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF103243. SSF103243. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P06782-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSNNNTNTA PANANSSHHH HHHHHHHHHH GHGGSNSTLN NPKSSLADGA    50
    HIGNYQIVKT LGEGSFGKVK LAYHTTTGQK VALKIINKKV LAKSDMQGRI 100
    EREISYLRLL RHPHIIKLYD VIKSKDEIIM VIEYAGNELF DYIVQRDKMS 150
    EQEARRFFQQ IISAVEYCHR HKIVHRDLKP ENLLLDEHLN VKIADFGLSN 200
    IMTDGNFLKT SCGSPNYAAP EVISGKLYAG PEVDVWSCGV ILYVMLCRRL 250
    PFDDESIPVL FKNISNGVYT LPKFLSPGAA GLIKRMLIVN PLNRISIHEI 300
    MQDDWFKVDL PEYLLPPDLK PHPEEENENN DSKKDGSSPD NDEIDDNLVN 350
    ILSSTMGYEK DEIYESLESS EDTPAFNEIR DAYMLIKENK SLIKDMKANK 400
    SVSDELDTFL SQSPPTFQQQ SKSHQKSQVD HETAKQHARR MASAITQQRT 450
    YHQSPFMDQY KEEDSTVSIL PTSLPQIHRA NMLAQGSPAA SKISPLVTKK 500
    SKTRWHFGIR SRSYPLDVMG EIYIALKNLG AEWAKPSEED LWTIKLRWKY 550
    DIGNKTNTNE KIPDLMKMVI QLFQIETNNY LVDFKFDGWE SSYGDDTTVS 600
    NISEDEMSTF SAYPFLHLTT KLIMELAVNS QSN 633
    Length:633
    Mass (Da):72,045
    Last modified:January 1, 1988 - v1
    Checksum:iF5C63565C986C4E3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13971 Genomic DNA. Translation: AAA35058.1.
    U33050 Genomic DNA. Translation: AAB64904.1.
    BK006938 Genomic DNA. Translation: DAA12310.1.
    PIRiA26030.
    RefSeqiNP_010765.3. NM_001180785.3.

    Genome annotation databases

    EnsemblFungiiYDR477W; YDR477W; YDR477W.
    GeneIDi852088.
    KEGGisce:YDR477W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13971 Genomic DNA. Translation: AAA35058.1 .
    U33050 Genomic DNA. Translation: AAB64904.1 .
    BK006938 Genomic DNA. Translation: DAA12310.1 .
    PIRi A26030.
    RefSeqi NP_010765.3. NM_001180785.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FH9 X-ray 2.80 A 46-319 [» ]
    2QLV X-ray 2.60 A/D 460-630 [» ]
    3DAE X-ray 2.90 A/B 41-315 [» ]
    3HYH X-ray 2.20 A/B 41-315 [» ]
    3MN3 X-ray 2.38 A 50-320 [» ]
    3T4N X-ray 2.30 A 457-633 [» ]
    3TDH X-ray 2.30 A 457-633 [» ]
    3TE5 X-ray 2.50 A 457-633 [» ]
    ProteinModelPortali P06782.
    SMRi P06782. Positions 18-630.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32529. 435 interactions.
    DIPi DIP-18N.
    IntActi P06782. 25 interactions.
    MINTi MINT-364314.
    STRINGi 4932.YDR477W.

    Proteomic databases

    MaxQBi P06782.
    PaxDbi P06782.
    PeptideAtlasi P06782.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR477W ; YDR477W ; YDR477W .
    GeneIDi 852088.
    KEGGi sce:YDR477W.

    Organism-specific databases

    CYGDi YDR477w.
    SGDi S000002885. SNF1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000115114.
    HOGENOMi HOG000233016.
    KOi K12761.
    OMAi KRMLIVN.
    OrthoDBi EOG793BK1.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30003-MONOMER.
    BRENDAi 2.7.11.1. 984.
    Reactomei REACT_209479. Regulation of AMPK activity via LKB1.
    REACT_212098. AMPK inhibits chREBP transcriptional activation activity.

    Miscellaneous databases

    EvolutionaryTracei P06782.
    NextBioi 970409.

    Gene expression databases

    Genevestigatori P06782.

    Family and domain databases

    InterProi IPR028375. KA1/Ssp2_C.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR013896. Ubiquitin-assoc_dom.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    PF08587. UBA_2. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF103243. SSF103243. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A yeast gene that is essential for release from glucose repression encodes a protein kinase."
      Celenza J.L., Carlson M.
      Science 233:1175-1180(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "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 274-284; 528-539 AND 622-630, PHOSPHORYLATION AT THR-210.
    5. "Yeast Pak1 kinase associates with and activates Snf1."
      Nath N., McCartney R.R., Schmidt M.C.
      Mol. Cell. Biol. 23:3909-3917(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-210, INTERACTION WITH SAK1.
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. "Histone H3 phosphorylation can promote TBP recruitment through distinct promoter-specific mechanisms."
      Lo W.-S., Gamache E.R., Henry K.W., Yang D., Pillus L., Berger S.L.
      EMBO J. 24:997-1008(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
    8. "Glucose deprivation mediates interaction between CTDK-I and Snf1 in Saccharomyces cerevisiae."
      Van Driessche B., Coddens S., Van Mullem V., Vandenhaute J.
      FEBS Lett. 579:5318-5324(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CTK1.
    9. "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: PHOSPHORYLATION, INTERACTION WITH SAK1.
    10. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    11. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413 AND SER-487, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413 AND SER-632, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSNF1_YEAST
    AccessioniPrimary (citable) accession number: P06782
    Secondary accession number(s): D6VTA0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 167 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 589 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 IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3