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P06782 (SNF1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carbon catabolite-derepressing protein kinase

EC=2.7.11.1
Gene names
Name:SNF1
Synonyms:CAT1, CCR1, GLC2, PAS14
Ordered Locus Names:YDR477W
ORF Names:D8035.20
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length633 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subunit structure

Interacts with CTK1, GAL83, SAK1, SIP1, SIP2 and SNF4. Ref.5 Ref.8 Ref.9

Subcellular location

Nucleus membrane; Peripheral membrane protein.

Miscellaneous

Present with 589 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentMembrane
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbiofilm formation

Inferred from mutant phenotype PubMed 12024013. Source: SGD

carbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

cell adhesion

Inferred from mutant phenotype PubMed 12556493. Source: SGD

cellular response to nitrogen starvation

Inferred from direct assay PubMed 12024013. Source: SGD

fungal-type cell wall assembly

Inferred from mutant phenotype PubMed 24486034. Source: SGD

invasive growth in response to glucose limitation

Inferred from mutant phenotype PubMed 11095711PubMed 12556493. Source: SGD

negative regulation of translation

Inferred from mutant phenotype PubMed 18955495. Source: SGD

positive regulation of filamentous growth of a population of unicellular organisms in response to starvation

Inferred from mutant phenotype PubMed 22904036. Source: SGD

positive regulation of gluconeogenesis

Inferred from mutant phenotype PubMed 8628258PubMed 8710504PubMed 9111319. Source: SGD

protein phosphorylation

Inferred from direct assay PubMed 11486005. Source: SGD

pseudohyphal growth

Inferred from mutant phenotype PubMed 12024013. Source: SGD

regulation of carbohydrate metabolic process

Inferred from genetic interaction PubMed 12167649. Source: SGD

replicative cell aging

Inferred from mutant phenotype PubMed 10921902. Source: SGD

   Cellular_componentAMP-activated protein kinase complex

Inferred from direct assay PubMed 12393914PubMed 2481228. Source: SGD

cytoplasm

Inferred from direct assay PubMed 17237508. Source: SGD

fungal-type vacuole

Inferred from physical interaction PubMed 11331606. Source: SGD

nuclear envelope lumen

Inferred from direct assay PubMed 17237508. Source: SGD

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 17237508. Source: SGD

   Molecular_functionAMP-activated protein kinase activity

Inferred from mutant phenotype PubMed 11486005PubMed 2557546PubMed 7913470. Source: SGD

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 10074103PubMed 10220464PubMed 10688190PubMed 10978279PubMed 11029705PubMed 11283351PubMed 11410349PubMed 11701881PubMed 11805826PubMed 11909951PubMed 12435362PubMed 16260785PubMed 16429126PubMed 18467557PubMed 18719252PubMed 20489023PubMed 21906795PubMed 8230216. Source: IntAct

protein serine/threonine kinase activity

Inferred from direct assay PubMed 11486005PubMed 2557546PubMed 7913470. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 633633Carbon catabolite-derepressing protein kinase
PRO_0000086670

Regions

Domain55 – 306252Protein kinase
Nucleotide binding61 – 699ATP By similarity
Compositional bias18 – 3215Poly-His

Sites

Active site1771Proton acceptor By similarity
Binding site841ATP By similarity

Amino acid modifications

Modified residue2101Phosphothreonine; by autocatalysis Ref.4 Ref.5
Modified residue4131Phosphoserine Ref.10 Ref.11 Ref.12
Modified residue4871Phosphoserine Ref.11
Modified residue6321Phosphoserine Ref.12

Secondary structure

.......................................................................... 633
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06782 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: F5C63565C986C4E3

FASTA63372,045
        10         20         30         40         50         60 
MSSNNNTNTA PANANSSHHH HHHHHHHHHH GHGGSNSTLN NPKSSLADGA HIGNYQIVKT 

        70         80         90        100        110        120 
LGEGSFGKVK LAYHTTTGQK VALKIINKKV LAKSDMQGRI EREISYLRLL RHPHIIKLYD 

       130        140        150        160        170        180 
VIKSKDEIIM VIEYAGNELF DYIVQRDKMS EQEARRFFQQ IISAVEYCHR HKIVHRDLKP 

       190        200        210        220        230        240 
ENLLLDEHLN VKIADFGLSN IMTDGNFLKT SCGSPNYAAP EVISGKLYAG PEVDVWSCGV 

       250        260        270        280        290        300 
ILYVMLCRRL PFDDESIPVL FKNISNGVYT LPKFLSPGAA GLIKRMLIVN PLNRISIHEI 

       310        320        330        340        350        360 
MQDDWFKVDL PEYLLPPDLK PHPEEENENN DSKKDGSSPD NDEIDDNLVN ILSSTMGYEK 

       370        380        390        400        410        420 
DEIYESLESS EDTPAFNEIR DAYMLIKENK SLIKDMKANK SVSDELDTFL SQSPPTFQQQ 

       430        440        450        460        470        480 
SKSHQKSQVD HETAKQHARR MASAITQQRT YHQSPFMDQY KEEDSTVSIL PTSLPQIHRA 

       490        500        510        520        530        540 
NMLAQGSPAA SKISPLVTKK SKTRWHFGIR SRSYPLDVMG EIYIALKNLG AEWAKPSEED 

       550        560        570        580        590        600 
LWTIKLRWKY DIGNKTNTNE KIPDLMKMVI QLFQIETNNY LVDFKFDGWE SSYGDDTTVS 

       610        620        630 
NISEDEMSTF SAYPFLHLTT KLIMELAVNS QSN 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13971 Genomic DNA. Translation: AAA35058.1.
U33050 Genomic DNA. Translation: AAB64904.1.
BK006938 Genomic DNA. Translation: DAA12310.1.
PIRA26030.
RefSeqNP_010765.3. NM_001180785.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP06782.
SMRP06782. Positions 18-630.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32529. 434 interactions.
DIPDIP-18N.
IntActP06782. 25 interactions.
MINTMINT-364314.
STRING4932.YDR477W.

Proteomic databases

MaxQBP06782.
PaxDbP06782.
PeptideAtlasP06782.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR477W; YDR477W; YDR477W.
GeneID852088.
KEGGsce:YDR477W.

Organism-specific databases

CYGDYDR477w.
SGDS000002885. SNF1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00740000115114.
HOGENOMHOG000233016.
KOK12761.
OMAKRMLIVN.
OrthoDBEOG793BK1.

Enzyme and pathway databases

BioCycYEAST:G3O-30003-MONOMER.
BRENDA2.7.11.1. 984.

Gene expression databases

GenevestigatorP06782.

Family and domain databases

InterProIPR028375. 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]
PfamPF00069. Pkinase. 1 hit.
PF08587. UBA_2. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF103243. SSF103243. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06782.
NextBio970409.

Entry information

Entry nameSNF1_YEAST
AccessionPrimary (citable) accession number: P06782
Secondary accession number(s): D6VTA0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: June 11, 2014
This is version 165 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references