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Protein

SNF1-activating kinase 1

Gene

SAK1

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 that phosphorylates SNF1, the catalytic subunit of the SNF1 kinase complex. Acts as an activator of the SNF1 kinase complex and controls its nuclear localization upon glucose and nitrogen depletion. Also required for SNF1 kinase activation under other stress conditions like alkaline pH or presence of cadmium.13 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei162 – 1621ATPPROSITE-ProRule annotation
Active sitei277 – 2771Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi139 – 1479ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein serine/threonine kinase activity Source: SGD

GO - Biological processi

  • DNA-dependent DNA replication Source: SGD
  • glucose metabolic process Source: SGD
  • protein phosphorylation Source: SGD
  • pseudohyphal growth Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30292-MONOMER.
BRENDAi2.7.11.1. 984.
ReactomeiR-SCE-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-SCE-442717. CREB phosphorylation through the activation of CaMKK.

Names & Taxonomyi

Protein namesi
Recommended name:
SNF1-activating kinase 1 (EC:2.7.11.1)
Gene namesi
Name:SAK1
Synonyms:PAK1
Ordered Locus Names:YER129W
ORF Names:SYGP-ORF45
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YER129W.
SGDiS000000931. SAK1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11421142SNF1-activating kinase 1PRO_0000086464Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431PhosphothreonineCombined sources
Modified residuei964 – 9641PhosphoserineCombined sources
Modified residuei1126 – 11261PhosphoserineCombined sources

Post-translational modificationi

Autophosphorylated.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38990.
PeptideAtlasiP38990.

PTM databases

iPTMnetiP38990.

Interactioni

Subunit structurei

Associates with the SNF1 kinase complex. Interacts with SNF1 and REG1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC14Q006842EBI-12863,EBI-4192

Protein-protein interaction databases

BioGridi36873. 70 interactions.
DIPiDIP-5407N.
IntActiP38990. 14 interactions.
MINTiMINT-520035.

Structurei

3D structure databases

ProteinModelPortaliP38990.
SMRiP38990. Positions 56-518.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini133 – 448316Protein kinasePROSITE-ProRule annotationAdd
BLAST

Domaini

The kinase domain is not sufficient by themself for proper function and that the non-conserved N-terminal and C-terminal domains are critical for the biological activity. The C-terminus promotes interaction of ELM1 and TOS3 kinases with SNF1.2 Publications

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00530000063214.
HOGENOMiHOG000115426.
InParanoidiP38990.
KOiK07359.
OMAiTNRISLT.
OrthoDBiEOG76DV1W.

Family and domain databases

InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 3 hits.
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38990-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRSDKKVNV EEVNVPSNLQ IELEKSGTSS SVSLRSPTKS SATNLAGMAE
60 70 80 90 100
GARDNASIAS SSVDSLNMLL ERQRVRQLNH PQHQQHISSS LAKTPTTTSS
110 120 130 140 150
FCSSGSSKNK VKETNRISLT YDPVSKRKVL NTYEIIKELG HGQHGKVKLA
160 170 180 190 200
RDILSKQLVA IKIVDRHEKK QRKFFTFIKS SKISENDKIK REIAIMKKCH
210 220 230 240 250
HKHVVQLIEV LDDLKSRKIY LVLEYCSRGE VKWCPPDCME SDAKGPSLLS
260 270 280 290 300
FQETREILRG VVLGLEYLHY QGIIHRDIKP ANLLISGDGT VKISDFGVSL
310 320 330 340 350
AASSTNSSDS SESLDELELA KTVGTPAFFA PEMCLGEDAF TRYNLTKENL
360 370 380 390 400
FRGSCISFMI DIWAVGVTLY CLLFGMLPFF SDFELKLFEK IVNDPLKFPT
410 420 430 440 450
FKEIQSNKVS KVSCEEEYEM AKDLLLKLLE KNPQKRMTIP AIKKHPFVSW
460 470 480 490 500
DFDHVPENDE KLLSSVLEQK LRFQCNQTDQ FEPISISKHE LKNAVSGVGK
510 520 530 540 550
KIKESVLKSI PLKDPSDLSN KNYLHPTETT RGRGDANVIV SEGSVLSNIK
560 570 580 590 600
ELSANDGCLN TDSDTNININ DDDHYSGDDN DGHLTKRELE RELNKFDDKH
610 620 630 640 650
EAGNMVNLPI NSSFASLDSF YIDNFAMARM GMSSPEAGDS VSSVPNLPSA
660 670 680 690 700
PSSTRLGRSP VFSGVTNQPS PIRPVLPQQK SSFCATGRYD KSHNSLLRNS
710 720 730 740 750
SSHLTSYNSG RPSSRTGRMN SRNQNLPKIP NSLSKISTTK LTELRVPKDS
760 770 780 790 800
EIPSPAKNPN ADRLRRFPVK KNTKTPAIKD PPRININSSD KSGSKNSPIK
810 820 830 840 850
SLYQRMKQSK DNSKTFEVRR GNFFSHFNGD DDDSSSQSSV TSSGSESDSE
860 870 880 890 900
LSSTSSSCTS GTQSRNSSNN NAYSETESLP FEFGVDSEDG SGVLLRDLPN
910 920 930 940 950
EDQIRPFLDI QPCRRMKVKS SLNLEPPSVS SSSSSSSDED ELILNVGTAG
960 970 980 990 1000
HRRRHNSSKL SELSNSPQKG SNNFMYSNGS VHDSETTITP QNMDDLTLHQ
1010 1020 1030 1040 1050
ALSRSQPISK PGPLVLPKRL DQKKATTETS NLTDIVEFNG NNDHRKDKNF
1060 1070 1080 1090 1100
DKVLYSRDLL KDALSSTNAG RRRSIPSNKI RGRKDASITM STNVGNDEHA
1110 1120 1130 1140
RNTSCHGDKG QENGAIKQRT HERSRSLTVA ELNEEKRRSA LP
Length:1,142
Mass (Da):126,872
Last modified:February 1, 1995 - v1
Checksum:i425D71B8340B3F8F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti171 – 1711Q → H in AAC49840 (PubMed:9341678).Curated
Sequence conflicti266 – 2683EYL → DS in AAC49840 (PubMed:9341678).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18916 Genomic DNA. Translation: AAC03227.1.
U13398 Genomic DNA. Translation: AAC49840.1. Different termination.
BK006939 Genomic DNA. Translation: DAA07789.1.
PIRiS50632.
RefSeqiNP_011055.3. NM_001179019.3.

Genome annotation databases

EnsemblFungiiYER129W; YER129W; YER129W.
GeneIDi856866.
KEGGisce:YER129W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18916 Genomic DNA. Translation: AAC03227.1.
U13398 Genomic DNA. Translation: AAC49840.1. Different termination.
BK006939 Genomic DNA. Translation: DAA07789.1.
PIRiS50632.
RefSeqiNP_011055.3. NM_001179019.3.

3D structure databases

ProteinModelPortaliP38990.
SMRiP38990. Positions 56-518.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36873. 70 interactions.
DIPiDIP-5407N.
IntActiP38990. 14 interactions.
MINTiMINT-520035.

PTM databases

iPTMnetiP38990.

Proteomic databases

MaxQBiP38990.
PeptideAtlasiP38990.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYER129W; YER129W; YER129W.
GeneIDi856866.
KEGGisce:YER129W.

Organism-specific databases

EuPathDBiFungiDB:YER129W.
SGDiS000000931. SAK1.

Phylogenomic databases

GeneTreeiENSGT00530000063214.
HOGENOMiHOG000115426.
InParanoidiP38990.
KOiK07359.
OMAiTNRISLT.
OrthoDBiEOG76DV1W.

Enzyme and pathway databases

BioCyciYEAST:G3O-30292-MONOMER.
BRENDAi2.7.11.1. 984.
ReactomeiR-SCE-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-SCE-442717. CREB phosphorylation through the activation of CaMKK.

Miscellaneous databases

NextBioi983228.
PROiP38990.

Family and domain databases

InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 3 hits.
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Overexpression of the protein kinase Pak1 suppresses yeast DNA polymerase mutations."
    Hovland P.G., Tecklenberg M., Sclafani R.A.
    Mol. Gen. Genet. 256:45-53(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-657, FUNCTION.
    Strain: ATCC 204626 / S288c / A364A.
  4. "The protein kinases of budding yeast: six score and more."
    Hunter T., Plowman G.D.
    Trends Biochem. Sci. 22:18-22(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PREDICTION OF FUNCTION.
  5. "Elm1p is one of three upstream kinases for the Saccharomyces cerevisiae SNF1 complex."
    Sutherland C.M., Hawley S.A., McCartney R.R., Leech A., Stark M.J.R., Schmidt M.C., Hardie D.G.
    Curr. Biol. 13:1299-1305(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "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: FUNCTION, INTERACTION WITH SNF1.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Activation of yeast Snf1 and mammalian AMP-activated protein kinase by upstream kinases."
    Hong S.-P., Leiper F.C., Woods A., Carling D., Carlson M.
    Proc. Natl. Acad. Sci. U.S.A. 100:8839-8843(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Pak1 protein kinase regulates activation and nuclear localization of Snf1-Gal83 protein kinase."
    Hedbacker K., Hong S.-P., Carlson M.
    Mol. Cell. Biol. 24:8255-8263(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Snf1 kinase complexes with different beta subunits display stress-dependent preferences for the three Snf1-activating kinases."
    McCartney R.R., Rubenstein E.M., Schmidt M.C.
    Curr. Genet. 47:335-344(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1126, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  13. "Purification and characterization of the three Snf1-activating kinases of Saccharomyces cerevisiae."
    Elbing K., McCartney R.R., Schmidt M.C.
    Biochem. J. 393:797-805(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ASSOCIATION WITH THE SNF1 KINASE COMPLEX, INTERACTION WITH SNF1.
  14. "Regulatory domains of Snf1-activating kinases determine pathway specificity."
    Rubenstein E.M., McCartney R.R., Schmidt M.C.
    Eukaryot. Cell 5:620-627(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN.
  15. "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: FUNCTION, INTERACTION WITH SNF1.
  16. "Regulation of snf1 protein kinase in response to environmental stress."
    Hong S.-P., Carlson M.
    J. Biol. Chem. 282:16838-16845(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "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-1126, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  18. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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-964, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Genetic basis of arsenite and cadmium tolerance in Saccharomyces cerevisiae."
    Thorsen M., Perrone G.G., Kristiansson E., Traini M., Ye T., Dawes I.W., Nerman O., Tamas M.J.
    BMC Genomics 10:105-105(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "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 THR-43 AND SER-1126, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Roles of the Snf1-activating kinases during nitrogen limitation and pseudohyphal differentiation in Saccharomyces cerevisiae."
    Orlova M., Ozcetin H., Barrett L., Kuchin S.
    Eukaryot. Cell 9:208-214(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "Interaction of SNF1 protein kinase with its activating kinase Sak1."
    Liu Y., Xu X., Carlson M.
    Eukaryot. Cell 10:313-319(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN, INTERACTION WITH REG1 AND SNF1.

Entry informationi

Entry nameiSAK1_YEAST
AccessioniPrimary (citable) accession number: P38990
Secondary accession number(s): D3DM35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 11, 2016
This is version 157 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 752 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: 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.