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Protein

Carbon catabolite-derepressing protein kinase

Gene

SNF1

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

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 serine/threonine kinase activity Source: SGD

GO - Biological processi

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

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_274868. Import of palmitoyl-CoA into the mitochondrial matrix.
REACT_300008. Regulation of AMPK activity via LKB1.
REACT_301208. 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 Componenti: Chromosome IV

Organism-specific databases

CYGDiYDR477w.
EuPathDBiFungiDB:YDR477W.
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
Complete GO annotation...

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 autocatalysis2 Publications
Modified residuei413 – 4131Phosphoserine3 Publications
Modified residuei487 – 4871Phosphoserine1 Publication
Modified residuei632 – 6321Phosphoserine1 Publication

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. 439 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 – 627Combined sources
Helixi64 – 663Combined sources
Beta strandi69 – 735Combined sources
Turni75 – 773Combined sources
Beta strandi80 – 878Combined sources
Helixi88 – 914Combined sources
Helixi97 – 10913Combined sources
Beta strandi118 – 1236Combined sources
Beta strandi125 – 1339Combined sources
Helixi139 – 1457Combined sources
Helixi151 – 17020Combined sources
Turni180 – 1823Combined sources
Beta strandi183 – 1853Combined sources
Beta strandi191 – 1933Combined sources
Turni207 – 2093Combined sources
Helixi215 – 2173Combined sources
Helixi220 – 2234Combined sources
Beta strandi224 – 2274Combined sources
Helixi232 – 24716Combined sources
Helixi257 – 26610Combined sources
Helixi277 – 28610Combined sources
Helixi291 – 2933Combined sources
Helixi297 – 3026Combined sources
Helixi304 – 3074Combined sources
Helixi312 – 3143Combined sources
Turni317 – 3193Combined sources
Helixi471 – 4733Combined sources
Helixi475 – 48511Combined sources
Helixi489 – 4924Combined sources
Beta strandi506 – 5116Combined sources
Helixi515 – 52915Combined sources
Beta strandi532 – 5343Combined sources
Helixi538 – 5403Combined sources
Beta strandi543 – 5486Combined sources
Beta strandi565 – 57612Combined sources
Beta strandi579 – 59012Combined sources
Helixi607 – 6104Combined sources
Helixi613 – 62816Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 18-390, 465-630.
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.
GeneTreeiENSGT00760000118892.
HOGENOMiHOG000233016.
InParanoidiP06782.
KOiK12761.
OMAiMSSFSAY.
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.
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

        10         20         30         40         50
MSSNNNTNTA PANANSSHHH HHHHHHHHHH GHGGSNSTLN NPKSSLADGA
60 70 80 90 100
HIGNYQIVKT LGEGSFGKVK LAYHTTTGQK VALKIINKKV LAKSDMQGRI
110 120 130 140 150
EREISYLRLL RHPHIIKLYD VIKSKDEIIM VIEYAGNELF DYIVQRDKMS
160 170 180 190 200
EQEARRFFQQ IISAVEYCHR HKIVHRDLKP ENLLLDEHLN VKIADFGLSN
210 220 230 240 250
IMTDGNFLKT SCGSPNYAAP EVISGKLYAG PEVDVWSCGV ILYVMLCRRL
260 270 280 290 300
PFDDESIPVL FKNISNGVYT LPKFLSPGAA GLIKRMLIVN PLNRISIHEI
310 320 330 340 350
MQDDWFKVDL PEYLLPPDLK PHPEEENENN DSKKDGSSPD NDEIDDNLVN
360 370 380 390 400
ILSSTMGYEK DEIYESLESS EDTPAFNEIR DAYMLIKENK SLIKDMKANK
410 420 430 440 450
SVSDELDTFL SQSPPTFQQQ SKSHQKSQVD HETAKQHARR MASAITQQRT
460 470 480 490 500
YHQSPFMDQY KEEDSTVSIL PTSLPQIHRA NMLAQGSPAA SKISPLVTKK
510 520 530 540 550
SKTRWHFGIR SRSYPLDVMG EIYIALKNLG AEWAKPSEED LWTIKLRWKY
560 570 580 590 600
DIGNKTNTNE KIPDLMKMVI QLFQIETNNY LVDFKFDGWE SSYGDDTTVS
610 620 630
NISEDEMSTF SAYPFLHLTT KLIMELAVNS QSN
Length:633
Mass (Da):72,045
Last modified:January 1, 1988 - v1
Checksum:iF5C63565C986C4E3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 18-390, 465-630.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32529. 439 interactions.
DIPiDIP-18N.
IntActiP06782. 25 interactions.
MINTiMINT-364314.
STRINGi4932.YDR477W.

Proteomic databases

MaxQBiP06782.
PaxDbiP06782.
PeptideAtlasiP06782.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYDR477w.
EuPathDBiFungiDB:YDR477W.
SGDiS000002885. SNF1.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118892.
HOGENOMiHOG000233016.
InParanoidiP06782.
KOiK12761.
OMAiMSSFSAY.
OrthoDBiEOG793BK1.

Enzyme and pathway databases

BioCyciYEAST:G3O-30003-MONOMER.
BRENDAi2.7.11.1. 984.
ReactomeiREACT_274868. Import of palmitoyl-CoA into the mitochondrial matrix.
REACT_300008. Regulation of AMPK activity via LKB1.
REACT_301208. AMPK inhibits chREBP transcriptional activation activity.

Miscellaneous databases

EvolutionaryTraceiP06782.
NextBioi970409.
PROiP06782.

Gene expression databases

GenevestigatoriP06782.

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.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 172 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

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 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.