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P31374 (PSK1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein kinase PSK1

EC=2.7.11.1
Alternative name(s):
PAS kinase 1
Gene names
Name:PSK1
Ordered Locus Names:YAL017W
ORF Names:FUN31, YAL002
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1356 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine-protein kinase involved in the control of sugar metabolism and translation. Phosphorylates UGP1, which is required for normal glycogen and beta-(1,6)-glucan synthesis. This phosphorylation shifts glucose partitioning toward cell wall glucan synthesis at the expense of glycogen synthesis. Ref.3 Ref.7 Ref.12

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subcellular location

Cytoplasm Ref.8.

Miscellaneous

Present with 967 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 2 PAS (PER-ARNT-SIM) domains.

Contains 1 protein kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13561356Serine/threonine-protein kinase PSK1
PRO_0000086042

Regions

Domain450 – 51869PAS 1
Domain738 – 80770PAS 2
Domain1096 – 1354259Protein kinase
Nucleotide binding1102 – 11109ATP By similarity

Sites

Active site12301Proton acceptor By similarity
Binding site11251ATP By similarity

Amino acid modifications

Modified residue101Phosphoserine Ref.14
Modified residue1921Phosphoserine Ref.14
Modified residue2021Phosphoserine Ref.15
Modified residue2551Phosphoserine Ref.15
Modified residue2861Phosphoserine Ref.11
Modified residue3271Phosphoserine Ref.14
Modified residue9261Phosphoserine Ref.14
Modified residue10181Phosphoserine Ref.10
Modified residue10231Phosphoserine Ref.15
Modified residue10351Phosphoserine Ref.11 Ref.14
Modified residue10551Phosphoserine Ref.14 Ref.15
Modified residue10791Phosphothreonine Ref.13

Experimental info

Sequence conflict731E → Q no nucleotide entry Ref.1
Sequence conflict731E → Q no nucleotide entry Ref.2
Sequence conflict731E → Q no nucleotide entry Ref.3
Sequence conflict731E → Q in AAC04940. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P31374 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 9A2AF4A9C1785586

FASTA1,356152,332
        10         20         30         40         50         60 
MPYIGASNLS EHSFVNLKEK HAITHKGTSS SVASLQTPPS PDQENHIDNE LENYDTSLSD 

        70         80         90        100        110        120 
VSTPNKKEGD EFEQSLRDTF ASFRKTKPPP PLDFEQPRLP STASSSVDST VSSPLTDEDI 

       130        140        150        160        170        180 
KELEFLPNES THSYSYNPLS PNSLAVRLRI LKRSLEIIIQ NPSMLLEPTP DDLPPLKEFA 

       190        200        210        220        230        240 
GRRSSLPRTS ASANHLMNRN KSQIWNTTSA TLNAFVNNTS SSSAASSALS NKKPGTPVFP 

       250        260        270        280        290        300 
NLDPTHSQTF HRANSLAYLP SILPEQDPLL KHNNSLFRGD YGNNISPERP SFRQPFKDQT 

       310        320        330        340        350        360 
SNLRNSSLLN ERAYQEDETF LPHHGPSMDL LNEQRANLKS LLNLLNETLE KNTSERASDL 

       370        380        390        400        410        420 
HMISLFNLNK LMLGDPKKNN SERDKRTEKL KKILLDSLAE PFFEHYNFIG DNPIADTDEL 

       430        440        450        460        470        480 
KEEIDEFTGS GDTTAITDIR PQQDYGRILR TFTSTKNSAP QAIFTCSQED PWQFRAANDL 

       490        500        510        520        530        540 
ACLVFGISQN AIRALTLMDL IHTDSRNFVL HKLLSTEGQE MVFTGEIIGI VQPETLSSSK 

       550        560        570        580        590        600 
VVWASFWAKR KNGLLVCVFE KVPCDYVDVL LNLDDFGAEN IVDKCELLSD GPTLSSSSTL 

       610        620        630        640        650        660 
SLPKMASSPT GSKLEYSLER KILEKSYTKP TSTENRNGDE NQLDGDSHSE PSLSSSPVRS 

       670        680        690        700        710        720 
KKSVKFANDI KDVKSISQSL AKLMDDVRNG VVFDPDDDLL PMPIKVCNHI NETRYFTLNH 

       730        740        750        760        770        780 
LSYNIPCAVS STVLEDELKL KIHSLPYQAG LFIVDSHTLD IVSSNKSILK NMFGYHFAEL 

       790        800        810        820        830        840 
VGKSITEIIP SFPKFLQFIN DKYPALDITL HKNKGLVLTE HFFRKIQAEI MGDRKSFYTS 

       850        860        870        880        890        900 
VGIDGLHRDG CEIKIDFQLR VMNSKVILLW VTHSRDVVFE EYNTNPSQLK MLKESELSLM 

       910        920        930        940        950        960 
SSASSSASSS KKSSSRISTG TLKDMSNLST YEDLAHRTNK LKYEIGDDSR AHSQSTLSEQ 

       970        980        990       1000       1010       1020 
EQVPLENDKD SGEMMLADPE MKHKLELARI YSRDKSQFVK EGNFKVDENL IISKISLSPS 

      1030       1040       1050       1060       1070       1080 
TESLADSKSS GKGLSPLEEE KLIDENATEN GLAGSPKDED GIIMTNKRGN QPVSTFLRTP 

      1090       1100       1110       1120       1130       1140 
EKNIGAQKHV KKFSDFVSLQ KMGEGAYGKV NLCIHKKNRY IVVIKMIFKE RILVDTWVRD 

      1150       1160       1170       1180       1190       1200 
RKLGTIPSEI QIMATLNKKP HENILRLLDF FEDDDYYYIE TPVHGETGCI DLFDLIEFKT 

      1210       1220       1230       1240       1250       1260 
NMTEFEAKLI FKQVVAGIKH LHDQGIVHRD IKDENVIVDS KGFVKIIDFG SAAYVKSGPF 

      1270       1280       1290       1300       1310       1320 
DVFVGTIDYA APEVLGGNPY EGQPQDIWAI GILLYTVVFK ENPFYNIDEI LEGDLKFNNA 

      1330       1340       1350 
EEVSEDCIEL IKSILNRCVP KRPTIDDINN DKWLVI 

« Hide

References

« Hide 'large scale' references
[1]"Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of a 32 kb region between the LTE1 and SPO7 genes."
Ouellette B.F.F., Clark M.W., Keng T., Storms R.K., Zhong W.-W., Zeng B., Fortin N., Delaney S., Barton A.B., Kaback D.B., Bussey H.
Genome 36:32-42(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]"Identification of a Saccharomyces cerevisiae homolog of the SNF2 transcriptional regulator in the DNA sequence of an 8.6 kb region in the LTE1-CYS1 interval on the left arm of chromosome I."
Clark M.W., Zhong W.-W., Keng T., Storms R.K., Barton A.B., Kaback D.B., Bussey H.
Yeast 8:133-145(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]"The YAL017 gene on the left arm of chromosome I of Saccharomyces cerevisiae encodes a putative serine/threonine protein kinase."
Clark M.W., Zhong W.W., Keng T., Storms R.K., Ouellette B.F.F., Barton A., Kaback D.B., Bussey H.
Yeast 9:543-549(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: ATCC 204511 / S288c / AB972.
[4]"The nucleotide sequence of chromosome I from Saccharomyces cerevisiae."
Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., Storms R.K.
Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 73.
Strain: ATCC 204508 / S288c.
[6]"PAS kinase: an evolutionarily conserved PAS domain-regulated serine/threonine kinase."
Rutter J., Michnoff C.H., Harper S.M., Gardner K.H., McKnight S.L.
Proc. Natl. Acad. Sci. U.S.A. 98:8991-8996(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN.
[7]"Coordinate regulation of sugar flux and translation by PAS kinase."
Rutter J., Probst B.L., McKnight S.L.
Cell 111:17-28(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]"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-1018, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: YAL6B.
[11]"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-286 AND SER-1035, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[12]"Regulation of glucose partitioning by PAS kinase and Ugp1 phosphorylation."
Smith T.L., Rutter J.
Mol. Cell 26:491-499(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1079, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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-10; SER-192; SER-327; SER-926; SER-1035 AND SER-1055, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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-202; SER-255; SER-1023 AND SER-1055, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L05146 Genomic DNA. Translation: AAC04940.1.
BK006935 Genomic DNA. Translation: DAA06971.2.
PIRS33653.
RefSeqNP_009385.2. NM_001178162.2.

3D structure databases

ProteinModelPortalP31374.
SMRP31374. Positions 1055-1354.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31749. 77 interactions.
DIPDIP-6267N.
IntActP31374. 16 interactions.
MINTMINT-604653.
STRING4932.YAL017W.

Proteomic databases

MaxQBP31374.
PaxDbP31374.
PeptideAtlasP31374.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYAL017W; YAL017W; YAL017W.
GeneID851216.
KEGGsce:YAL017W.

Organism-specific databases

CYGDYAL017w.
SGDS000000015. PSK1.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00750000117599.
KOK08286.
OMASTHAYSY.
OrthoDBEOG7G4QPK.

Enzyme and pathway databases

BioCycYEAST:G3O-28829-MONOMER.

Gene expression databases

GenevestigatorP31374.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000014. PAS.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00091. PAS. 2 hits.
[Graphical view]
SUPFAMSSF55785. SSF55785. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio968103.

Entry information

Entry namePSK1_YEAST
AccessionPrimary (citable) accession number: P31374
Secondary accession number(s): D6VPK1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 27, 2011
Last modified: May 14, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome I

Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families