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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)DescriptionActionsGraphical viewLength
Binding sitei84ATPPROSITE-ProRule annotation1
Active sitei177Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi61 – 69ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • AMP-activated protein kinase activity Source: SGD
  • ARF guanyl-nucleotide exchange factor activity Source: SGD
  • ATP binding Source: UniProtKB-KW
  • protein serine/threonine kinase activity Source: SGD

GO - Biological processi

  • carbohydrate metabolic process Source: UniProtKB-KW
  • cell adhesion Source: SGD
  • cellular response to nitrogen starvation Source: SGD
  • fungal-type cell wall assembly Source: SGD
  • intracellular signal transduction Source: GO_Central
  • invasive growth in response to glucose limitation Source: SGD
  • negative regulation of translation Source: SGD
  • positive regulation of filamentous growth of a population of unicellular organisms in response to starvation Source: SGD
  • positive regulation of gluconeogenesis Source: SGD
  • positive regulation of macroautophagy Source: SGD
  • protein phosphorylation Source: SGD
  • pseudohyphal growth Source: SGD
  • replicative cell aging Source: SGD
  • response to unfolded protein Source: SGD
  • 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.
ReactomeiR-SCE-163680. AMPK inhibits chREBP transcriptional activation activity.
R-SCE-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-SCE-380972. Energy dependent regulation of mTOR by LKB1-AMPK.

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
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR477W.
SGDiS000002885. SNF1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • fungal-type vacuole Source: SGD
  • nuclear envelope lumen Source: SGD
  • nuclear membrane Source: UniProtKB-SubCell
  • nucleotide-activated protein kinase complex Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000866701 – 633Carbon catabolite-derepressing protein kinaseAdd BLAST633

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei210Phosphothreonine; by autocatalysis2 Publications1
Modified residuei413PhosphoserineCombined sources1
Cross-linki461Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei487PhosphoserineCombined sources1
Modified residuei632PhosphoserineCombined sources1

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP06782.
PRIDEiP06782.

PTM databases

iPTMnetiP06782.

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. 488 interactors.
DIPiDIP-18N.
IntActiP06782. 26 interactors.
MINTiMINT-364314.

Structurei

Secondary structure

1633
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi56 – 62Combined sources7
Helixi64 – 66Combined sources3
Beta strandi69 – 73Combined sources5
Turni75 – 77Combined sources3
Beta strandi80 – 87Combined sources8
Helixi88 – 91Combined sources4
Helixi97 – 109Combined sources13
Beta strandi118 – 123Combined sources6
Beta strandi125 – 133Combined sources9
Helixi139 – 145Combined sources7
Helixi151 – 170Combined sources20
Turni180 – 182Combined sources3
Beta strandi183 – 185Combined sources3
Beta strandi191 – 193Combined sources3
Turni207 – 209Combined sources3
Helixi215 – 217Combined sources3
Helixi220 – 223Combined sources4
Beta strandi224 – 227Combined sources4
Helixi232 – 247Combined sources16
Helixi257 – 266Combined sources10
Helixi277 – 286Combined sources10
Helixi291 – 293Combined sources3
Helixi297 – 302Combined sources6
Helixi304 – 307Combined sources4
Helixi312 – 314Combined sources3
Turni317 – 319Combined sources3
Helixi471 – 473Combined sources3
Helixi475 – 485Combined sources11
Helixi489 – 492Combined sources4
Beta strandi506 – 511Combined sources6
Helixi515 – 529Combined sources15
Beta strandi532 – 534Combined sources3
Helixi538 – 540Combined sources3
Beta strandi543 – 548Combined sources6
Beta strandi565 – 576Combined sources12
Beta strandi579 – 590Combined sources12
Helixi607 – 610Combined sources4
Helixi613 – 628Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06782.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini55 – 306Protein kinasePROSITE-ProRule annotationAdd BLAST252

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi18 – 32Poly-HisAdd BLAST15

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00790000122947.
HOGENOMiHOG000233016.
InParanoidiP06782.
KOiK12761.
OMAiPLDIMHE.
OrthoDBiEOG092C0QJU.

Family and domain databases

CDDicd14334. UBA_SNF1_fungi. 1 hit.
InterProiIPR032270. AMPK_C.
IPR028375. KA1/Ssp2_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR013896. SNF1_UBA.
[Graphical view]
PfamiPF16579. AdenylateSensor. 1 hit.
PF00069. 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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32529. 488 interactors.
DIPiDIP-18N.
IntActiP06782. 26 interactors.
MINTiMINT-364314.

PTM databases

iPTMnetiP06782.

Proteomic databases

MaxQBiP06782.
PRIDEiP06782.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YDR477W.
SGDiS000002885. SNF1.

Phylogenomic databases

GeneTreeiENSGT00790000122947.
HOGENOMiHOG000233016.
InParanoidiP06782.
KOiK12761.
OMAiPLDIMHE.
OrthoDBiEOG092C0QJU.

Enzyme and pathway databases

BioCyciYEAST:G3O-30003-MONOMER.
BRENDAi2.7.11.1. 984.
ReactomeiR-SCE-163680. AMPK inhibits chREBP transcriptional activation activity.
R-SCE-200425. Import of palmitoyl-CoA into the mitochondrial matrix.
R-SCE-380972. Energy dependent regulation of mTOR by LKB1-AMPK.

Miscellaneous databases

EvolutionaryTraceiP06782.
PROiP06782.

Family and domain databases

CDDicd14334. UBA_SNF1_fungi. 1 hit.
InterProiIPR032270. AMPK_C.
IPR028375. KA1/Ssp2_C.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR013896. SNF1_UBA.
[Graphical view]
PfamiPF16579. AdenylateSensor. 1 hit.
PF00069. 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...

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: November 2, 2016
This is version 189 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

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 one 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.