Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P31374

- PSK1_YEAST

UniProt

P31374 - PSK1_YEAST

Protein

Serine/threonine-protein kinase PSK1

Gene

PSK1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.3 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1125 – 11251ATPPROSITE-ProRule annotation
    Active sitei1230 – 12301Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1102 – 11109ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein serine/threonine kinase activity Source: SGD
    3. signal transducer activity Source: InterPro

    GO - Biological processi

    1. negative regulation of glycogen biosynthetic process Source: SGD
    2. protein phosphorylation Source: SGD
    3. regulation of (1->6)-beta-D-glucan biosynthetic process Source: SGD
    4. regulation of translation Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Translation regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-28829-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase PSK1 (EC:2.7.11.1)
    Alternative name(s):
    PAS kinase 1
    Gene namesi
    Name:PSK1
    Ordered Locus Names:YAL017W
    ORF Names:FUN31, YAL002
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome I

    Organism-specific databases

    CYGDiYAL017w.
    SGDiS000000015. PSK1.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13561356Serine/threonine-protein kinase PSK1PRO_0000086042Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei10 – 101Phosphoserine1 Publication
    Modified residuei192 – 1921Phosphoserine1 Publication
    Modified residuei202 – 2021Phosphoserine1 Publication
    Modified residuei255 – 2551Phosphoserine1 Publication
    Modified residuei286 – 2861Phosphoserine1 Publication
    Modified residuei327 – 3271Phosphoserine1 Publication
    Modified residuei926 – 9261Phosphoserine1 Publication
    Modified residuei1018 – 10181Phosphoserine1 Publication
    Modified residuei1023 – 10231Phosphoserine1 Publication
    Modified residuei1035 – 10351Phosphoserine2 Publications
    Modified residuei1055 – 10551Phosphoserine2 Publications
    Modified residuei1079 – 10791Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP31374.
    PaxDbiP31374.
    PeptideAtlasiP31374.

    Expressioni

    Gene expression databases

    GenevestigatoriP31374.

    Interactioni

    Protein-protein interaction databases

    BioGridi31749. 77 interactions.
    DIPiDIP-6267N.
    IntActiP31374. 16 interactions.
    MINTiMINT-604653.
    STRINGi4932.YAL017W.

    Structurei

    3D structure databases

    ProteinModelPortaliP31374.
    SMRiP31374. Positions 1055-1354.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini450 – 51869PAS 1Add
    BLAST
    Domaini738 – 80770PAS 2Add
    BLAST
    Domaini1096 – 1354259Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
    Contains 2 PAS (PER-ARNT-SIM) domains.Curated
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00750000117599.
    KOiK08286.
    OMAiSTHAYSY.
    OrthoDBiEOG7G4QPK.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000014. PAS.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00091. PAS. 2 hits.
    [Graphical view]
    SUPFAMiSSF55785. SSF55785. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P31374-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPYIGASNLS EHSFVNLKEK HAITHKGTSS SVASLQTPPS PDQENHIDNE     50
    LENYDTSLSD VSTPNKKEGD EFEQSLRDTF ASFRKTKPPP PLDFEQPRLP 100
    STASSSVDST VSSPLTDEDI KELEFLPNES THSYSYNPLS PNSLAVRLRI 150
    LKRSLEIIIQ NPSMLLEPTP DDLPPLKEFA GRRSSLPRTS ASANHLMNRN 200
    KSQIWNTTSA TLNAFVNNTS SSSAASSALS NKKPGTPVFP NLDPTHSQTF 250
    HRANSLAYLP SILPEQDPLL KHNNSLFRGD YGNNISPERP SFRQPFKDQT 300
    SNLRNSSLLN ERAYQEDETF LPHHGPSMDL LNEQRANLKS LLNLLNETLE 350
    KNTSERASDL HMISLFNLNK LMLGDPKKNN SERDKRTEKL KKILLDSLAE 400
    PFFEHYNFIG DNPIADTDEL KEEIDEFTGS GDTTAITDIR PQQDYGRILR 450
    TFTSTKNSAP QAIFTCSQED PWQFRAANDL ACLVFGISQN AIRALTLMDL 500
    IHTDSRNFVL HKLLSTEGQE MVFTGEIIGI VQPETLSSSK VVWASFWAKR 550
    KNGLLVCVFE KVPCDYVDVL LNLDDFGAEN IVDKCELLSD GPTLSSSSTL 600
    SLPKMASSPT GSKLEYSLER KILEKSYTKP TSTENRNGDE NQLDGDSHSE 650
    PSLSSSPVRS KKSVKFANDI KDVKSISQSL AKLMDDVRNG VVFDPDDDLL 700
    PMPIKVCNHI NETRYFTLNH LSYNIPCAVS STVLEDELKL KIHSLPYQAG 750
    LFIVDSHTLD IVSSNKSILK NMFGYHFAEL VGKSITEIIP SFPKFLQFIN 800
    DKYPALDITL HKNKGLVLTE HFFRKIQAEI MGDRKSFYTS VGIDGLHRDG 850
    CEIKIDFQLR VMNSKVILLW VTHSRDVVFE EYNTNPSQLK MLKESELSLM 900
    SSASSSASSS KKSSSRISTG TLKDMSNLST YEDLAHRTNK LKYEIGDDSR 950
    AHSQSTLSEQ EQVPLENDKD SGEMMLADPE MKHKLELARI YSRDKSQFVK 1000
    EGNFKVDENL IISKISLSPS TESLADSKSS GKGLSPLEEE KLIDENATEN 1050
    GLAGSPKDED GIIMTNKRGN QPVSTFLRTP EKNIGAQKHV KKFSDFVSLQ 1100
    KMGEGAYGKV NLCIHKKNRY IVVIKMIFKE RILVDTWVRD RKLGTIPSEI 1150
    QIMATLNKKP HENILRLLDF FEDDDYYYIE TPVHGETGCI DLFDLIEFKT 1200
    NMTEFEAKLI FKQVVAGIKH LHDQGIVHRD IKDENVIVDS KGFVKIIDFG 1250
    SAAYVKSGPF DVFVGTIDYA APEVLGGNPY EGQPQDIWAI GILLYTVVFK 1300
    ENPFYNIDEI LEGDLKFNNA EEVSEDCIEL IKSILNRCVP KRPTIDDINN 1350
    DKWLVI 1356
    Length:1,356
    Mass (Da):152,332
    Last modified:July 27, 2011 - v2
    Checksum:i9A2AF4A9C1785586
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti73 – 731E → Q no nucleotide entry (PubMed:8458570)Curated
    Sequence conflicti73 – 731E → Q no nucleotide entry (PubMed:1561836)Curated
    Sequence conflicti73 – 731E → Q no nucleotide entry (PubMed:8322517)Curated
    Sequence conflicti73 – 731E → Q in AAC04940. (PubMed:7731988)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L05146 Genomic DNA. Translation: AAC04940.1.
    BK006935 Genomic DNA. Translation: DAA06971.2.
    PIRiS33653.
    RefSeqiNP_009385.2. NM_001178162.2.

    Genome annotation databases

    EnsemblFungiiYAL017W; YAL017W; YAL017W.
    GeneIDi851216.
    KEGGisce:YAL017W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L05146 Genomic DNA. Translation: AAC04940.1 .
    BK006935 Genomic DNA. Translation: DAA06971.2 .
    PIRi S33653.
    RefSeqi NP_009385.2. NM_001178162.2.

    3D structure databases

    ProteinModelPortali P31374.
    SMRi P31374. Positions 1055-1354.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31749. 77 interactions.
    DIPi DIP-6267N.
    IntActi P31374. 16 interactions.
    MINTi MINT-604653.
    STRINGi 4932.YAL017W.

    Proteomic databases

    MaxQBi P31374.
    PaxDbi P31374.
    PeptideAtlasi P31374.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YAL017W ; YAL017W ; YAL017W .
    GeneIDi 851216.
    KEGGi sce:YAL017W.

    Organism-specific databases

    CYGDi YAL017w.
    SGDi S000000015. PSK1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117599.
    KOi K08286.
    OMAi STHAYSY.
    OrthoDBi EOG7G4QPK.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-28829-MONOMER.

    Miscellaneous databases

    NextBioi 968103.

    Gene expression databases

    Genevestigatori P31374.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000014. PAS.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00091. PAS. 2 hits.
    [Graphical view ]
    SUPFAMi SSF55785. SSF55785. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    9. 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].

    Entry informationi

    Entry nameiPSK1_YEAST
    AccessioniPrimary (citable) accession number: P31374
    Secondary accession number(s): D6VPK1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 140 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 967 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 I
      Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

    External Data

    Dasty 3