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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: -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
  • identical protein binding Source: IntAct
  • 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
  • positive regulation of pseudohyphal growth Source: SGD
  • protein phosphorylation 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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
PaxDbiP06782
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

GO - Molecular functioni

  • ARF guanyl-nucleotide exchange factor activity Source: SGD
  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi32529, 823 interactors
DIPiDIP-18N
IntActiP06782, 56 interactors
MINTiP06782
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

GeneTreeiENSGT00900000140868
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_sf
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

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: May 23, 2018
This is version 204 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health