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P06782

- SNF1_YEAST

UniProt

P06782 - SNF1_YEAST

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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: 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. 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
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_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. membrane Source: UniProtKB-KW
  5. nuclear envelope lumen Source: SGD
  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. 436 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 18-390, 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.
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.
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:
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 18-390, 465-630.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32529. 436 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 ENSGT00760000118892.
HOGENOMi HOG000233016.
InParanoidi P06782.
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.
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

« 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: October 29, 2014
This is version 168 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