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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

Serine/threonine protein kinase essential for release from glucose repression (PubMed:3526554, PubMed:6366512, PubMed:3049551, PubMed:1944227, PubMed:8289797, PubMed:8628258, PubMed:25869125). Catalytic subunit of the AMP-activated protein kinase complex also known as the SNF1 kinase complex (Snf1c), a central regulator of cellular energy homeostasis, which, in response to a fall in intracellular ATP levels, activates energy-producing pathways and inhibits energy-consuming processes (PubMed:8289797, PubMed:26667037). The complex phosphorylates histone H3 to form H3S10ph, which promotes H3K14ac formation, leading to transcriptional activation through TBP recruitment to the promoters (PubMed:15719021). The complex also negatively regulates the HOG1 MAPK pathway in ER stress response including unfolded protein response (UPR) (PubMed:25730376, PubMed:26394309). Under nutrient/energy depletion, the complex phosphorylates and activates PAS kinase PSK1 which in turn activates PBS1, leading to the inhibition of the TORC1 signaling pathway (PubMed:25428989). SNF1 also interacts and phosphorylates adenylate cyclase CYR1 and negatively regulates the protein kinase A signaling pathway (PubMed:26309257). Also phosphorylates and regulates the transcriptional activator CAT8 (PubMed:15121831).14 Publications

Miscellaneous

Present with 589 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.3 Publications

Enzyme regulationi

The kinase activity is positively regulated by SNF4 via sequestration of the SNF1 auto-inhibitory domain (AID) (PubMed:2557546, PubMed:17851534).2 Publications

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
  • mitotic cell cycle Source: GO_Central
  • 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

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processCarbohydrate metabolism
LigandATP-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-165158. Activation of AKT2.
R-SCE-199418. Negative regulation of the PI3K/AKT network.
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 kinase1 Publication (EC:2.7.11.13 Publications)
Alternative name(s):
Sucrose nonfermentating protein 11 Publication
Gene namesi
Name:SNF11 Publication
Synonyms:CAT1, CCR11 Publication, 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

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi53G → R: Exhibits greater activity than wild-type SNFl in an immune complex assay where other associated molecules are present, but exhibits the same activity in a protein blot assay. 1 Publication1
Mutagenesisi84K → R: Inactivates the kinase activity without affecting protein levels. 2 Publications1
Mutagenesisi210T → A: Inactivates the kinase activity without affecting protein levels. 2 Publications1
Mutagenesisi357G → A: Alters kinase activation and biological activity, including enhanced allosteric subunit associations and increased oxidative stress resistance and life span; when associated with I-367. 1 Publication1
Mutagenesisi367L → I: Alters kinase activation and biological activity, including enhanced allosteric subunit associations and increased oxidative stress resistance and life span; when associated with A-357. 1 Publication1
Mutagenesisi549K → R: Decreases sumoylation of SNF1. 1 Publication1

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 autocatalysis5 Publications1
Modified residuei413PhosphoserineCombined sources1
Cross-linki461Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei487PhosphoserineCombined sources1
Cross-linki549Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei632PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylation at Thr-210 in response to glucose limitation leads to activation of kinase activity (PubMed:11486005, PubMed:12748292). ADP, but not AMP, protects the enzyme from dephosphorylation at Thr-210 by GLC7 (PubMed:22019086).2 Publications
Sumoylation by the SUMO (E3) ligase MMS21 leads to inhibition by interaction of SUMO attached to Lys-549 with a SUMO-interacting sequence motif located near the active site of SNF1, and by targeting SNF1 for glucose-induced destruction via the SLX5-SLX8 (SUMO-directed) ubiquitin ligase (PubMed:24108357).1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP06782.
PRIDEiP06782.

PTM databases

iPTMnetiP06782.

Expressioni

Inductioni

Expression of the SNF1 gene itself is not glucose repressible (PubMed:6366513).1 Publication

Interactioni

Subunit structurei

Component of the AMP-activated protein kinase complex also known as the SNF1 kinase complex (Snf1c), an heterotrimeric complex composed of an alpha subunit (SNF1), a regulatory subunit beta (GAL83 and substoichiometric alternate beta subunits SIP1 and SIP2), and a regulatory subunit gamma (SNF4) (PubMed:2557546, PubMed:2481228, PubMed:7813428, PubMed:9121458, PubMed:15719021, PubMed:17851534). Inrteracts with the transcriptional activator SIP4 (PubMed:8628258). Interacts with SAK1 (PubMed:12748292, PubMed:16847059). Interacts with CTK1 (PubMed:16182287): Interacts with adenylate cyclase CYR1 (PubMed:26309257).11 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi32529. 797 interactors.
DIPiDIP-18N.
IntActiP06782. 26 interactors.
MINTiMINT-364314.
STRINGi4932.YDR477W.

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 annotation2 PublicationsAdd BLAST252
Domaini348 – 389UBA1 PublicationAdd BLAST42

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni313 – 392Auto-inhibitory domain (AID)2 PublicationsAdd BLAST80

Compositional bias

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

Domaini

The regulatory domain (RS) also called auto-inhibitory domain (AID) inhibits kinase activity of the protein kinase domain (KD) (PubMed:19474788, PubMed:20823513). The AID is sequestered by SNF4 within the AMP-activated protein kinase complex which might correspond to the activated SNF1 form (PubMed:17851534).3 Publications
The ubiquitin-associated domain (UBA) localized within the AID dampens kinase activation, probably by restraining SNF1-SNF4 associations (PubMed:25869125). Moreover, the UBA domain influences life span in a FKH1- and FKH2-dependent mechanism (PubMed:25869125).1 Publication

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00790000122947.
HOGENOMiHOG000233016.
InParanoidiP06782.
KOiK12761.
OMAiRWHFGIR.
OrthoDBiEOG092C0QJU.

Family and domain databases

CDDicd14334. UBA_SNF1_fungi. 1 hit.
InterProiView protein in InterPro
IPR032270. 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.
PfamiView protein in Pfam
PF16579. AdenylateSensor. 1 hit.
PF00069. Pkinase. 1 hit.
PF08587. UBA_2. 1 hit.
SMARTiView protein in SMART
SM00220. S_TKc. 1 hit.
SUPFAMiSSF103243. SSF103243. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiView protein in PROSITE
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.

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.

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.

Entry informationi

Entry nameiSNF1_YEAST
AccessioniPrimary (citable) accession number: P06782
Secondary accession number(s): D6VTA0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: July 5, 2017
This is version 195 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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