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)

Q12494

- KCS1_YEAST

UniProt

Q12494 - KCS1_YEAST

Protein

Inositol hexakisphosphate kinase 1

Gene

KCS1

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 110 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5). Involved in phosphate regulation and polyphosphate accumulation. Required for resistance to salt stress, cell wall integrity, vacuole morphogenesis, and telomere maintenance.7 Publications

    Catalytic activityi

    ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate.
    ATP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate.

    Kineticsi

    1. KM=3.3 µM for InsP61 Publication
    2. KM=1.2 µM for InsP51 Publication

    Vmax=2 µmol/min/mg enzyme1 Publication

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. inositol-1,3,4,5,6-pentakisphosphate kinase activity Source: SGD
    3. inositol-1,4,5-trisphosphate 3-kinase activity Source: InterPro
    4. inositol heptakisphosphate 5-kinase activity Source: SGD
    5. inositol heptakisphosphate kinase activity Source: SGD
    6. inositol hexakisphosphate 1-kinase activity Source: UniProtKB-EC
    7. inositol hexakisphosphate 3-kinase activity Source: UniProtKB-EC
    8. inositol hexakisphosphate 5-kinase activity Source: UniProtKB-EC
    9. inositol hexakisphosphate kinase activity Source: SGD

    GO - Biological processi

    1. inositol phosphate biosynthetic process Source: SGD
    2. regulation of inositol phosphate biosynthetic process Source: SGD

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29635-MONOMER.
    YEAST:MONOMER3O-205.
    ReactomeiREACT_188940. Synthesis of IPs in the nucleus.
    REACT_188944. Synthesis of pyrophosphates in the cytosol.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inositol hexakisphosphate kinase 1 (EC:2.7.4.21)
    Short name:
    InsP6 kinase 1
    Alternative name(s):
    InsP6 kinase KCS1
    PKC1 suppressor protein 1
    Gene namesi
    Name:KCS1
    Ordered Locus Names:YDR017C
    ORF Names:PZF1050
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR017c.
    SGDiS000002424. KCS1.

    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 – 10501050Inositol hexakisphosphate kinase 1PRO_0000255955Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei150 – 1501Phosphoserine2 Publications
    Modified residuei396 – 3961Phosphoserine2 Publications
    Modified residuei469 – 4691Phosphoserine1 Publication
    Modified residuei537 – 5371Phosphoserine3 Publications
    Modified residuei539 – 5391Phosphoserine1 Publication
    Modified residuei566 – 5661Phosphoserine1 Publication
    Modified residuei583 – 5831Phosphoserine1 Publication
    Modified residuei589 – 5891Phosphoserine1 Publication
    Modified residuei646 – 6461Phosphoserine1 Publication
    Modified residuei664 – 6641Phosphoserine1 Publication
    Modified residuei670 – 6701Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ12494.
    PaxDbiQ12494.
    PeptideAtlasiQ12494.

    Expressioni

    Gene expression databases

    GenevestigatoriQ12494.

    Interactioni

    Protein-protein interaction databases

    BioGridi32067. 277 interactions.
    DIPiDIP-1402N.
    IntActiQ12494. 5 interactions.
    MINTiMINT-397897.

    Structurei

    3D structure databases

    ProteinModelPortaliQ12494.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni772 – 7809Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG274869.
    GeneTreeiENSGT00390000014381.
    HOGENOMiHOG000001029.
    OMAiCATDTEE.
    OrthoDBiEOG7T1RKK.

    Family and domain databases

    InterProiIPR005522. IPK.
    [Graphical view]
    PANTHERiPTHR12400. PTHR12400. 1 hit.
    PfamiPF03770. IPK. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q12494-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDTSHEIHDK IPDTLREQQQ HLRQKESEGC ITTLKDLNVP ETKKLSSVLH     50
    GRKASTYLRI FRDDECLADN NNGVDSNNGG SVTCADKITR SEATPKSVPE 100
    GLQVSEKKNN PDTLSSSLSS FILSNHEEPA IKPNKHVAHR NNITETGQGS 150
    GEDIAKQQSH QPQVLHHQTS LKPIQNVDEG CISPKSTYQE SLHGISEDLT 200
    LKPVSSATYY PHKSKADSGY EEKDKMENDI DTIQPATINC ASGIATLPSS 250
    YNRHTFKVKT YSTLSQSLRQ ENVNNRSNEK KPQQFVPHSE SIKEKPNTFE 300
    QDKEGEQADE EEDEGDNEHR EYPLAVELKP FTNRVGGHTA IFRFSKRAVC 350
    KALVNRENRW YENIELCHKE LLQFMPRYIG VLNVRQHFQS KDDFLSDLDQ 400
    ENNGKNDTSN ENKDIEVNHN NNDDIALNTE PTGTPLTHIH SFPLEHSSRQ 450
    VLEKEHPEIE SVHPHVKRSL SSSNQPSLLP EVVLNDNRHI IPESLWYKYS 500
    DSPNSAPNDS YFSSSSSHNS CSFGERGNTN KLKRRDSGST MINTELKNLV 550
    IREVFAPKCF RRKRNSNTTT MGNHNARLGS SPSFLTQKSR ASSHDASNTS 600
    MKTLGDSSSQ ASLQMDDSKV NPNLQDPFLK KSLHEKISNA LDGSHSVMDL 650
    KQFHKNEQIK HKNSFCNSLS PILTATNSRD DGEFATSPNY ISNAQDGVFD 700
    MDEDTGNETI NMDNHGCHLD SGKNMIIKSL AYNVSNDYSH HDIESITFEE 750
    TSHTIVSKFI LLEDLTRNMN KPCALDLKMG TRQYGVDAKR AKQLSQRAKC 800
    LKTTSRRLGV RICGLKVWNK DYYITRDKYF GRRVKVGWQF ARVLARFLYD 850
    GKTIESLIRQ IPRLIKQLDT LYSEIFNLKG YRLYGASLLL MYDGDANKSN 900
    SKRKKAANVK VNLIDFARCV TKEDAMECMD KFRIPPKSPN IEDKGFLRGV 950
    KSLRFYLLLI WNYLTSDMPL IFDEVEMNDM ISEEADSNSF TSATGSKINF 1000
    NSKWDWLDEF DKEDEEMYND PNSKLRQKWR KYELIFDAEP RYNDDAQVSD 1050
    Length:1,050
    Mass (Da):119,550
    Last modified:November 1, 1996 - v1
    Checksum:i9C7507CA5F4B0FC7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S81651 Genomic DNA. Translation: AAB36234.1.
    X95966 Genomic DNA. Translation: CAA65208.1.
    Z49770 Genomic DNA. Translation: CAA89842.1.
    Z74313 Genomic DNA. Translation: CAA98837.1.
    Z74314 Genomic DNA. Translation: CAA98839.1.
    BK006938 Genomic DNA. Translation: DAA11863.1.
    PIRiS54640.
    RefSeqiNP_010300.3. NM_001180325.3.

    Genome annotation databases

    EnsemblFungiiYDR017C; YDR017C; YDR017C.
    GeneIDi851580.
    KEGGisce:YDR017C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S81651 Genomic DNA. Translation: AAB36234.1 .
    X95966 Genomic DNA. Translation: CAA65208.1 .
    Z49770 Genomic DNA. Translation: CAA89842.1 .
    Z74313 Genomic DNA. Translation: CAA98837.1 .
    Z74314 Genomic DNA. Translation: CAA98839.1 .
    BK006938 Genomic DNA. Translation: DAA11863.1 .
    PIRi S54640.
    RefSeqi NP_010300.3. NM_001180325.3.

    3D structure databases

    ProteinModelPortali Q12494.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32067. 277 interactions.
    DIPi DIP-1402N.
    IntActi Q12494. 5 interactions.
    MINTi MINT-397897.

    Proteomic databases

    MaxQBi Q12494.
    PaxDbi Q12494.
    PeptideAtlasi Q12494.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR017C ; YDR017C ; YDR017C .
    GeneIDi 851580.
    KEGGi sce:YDR017C.

    Organism-specific databases

    CYGDi YDR017c.
    SGDi S000002424. KCS1.

    Phylogenomic databases

    eggNOGi NOG274869.
    GeneTreei ENSGT00390000014381.
    HOGENOMi HOG000001029.
    OMAi CATDTEE.
    OrthoDBi EOG7T1RKK.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29635-MONOMER.
    YEAST:MONOMER3O-205.
    Reactomei REACT_188940. Synthesis of IPs in the nucleus.
    REACT_188944. Synthesis of pyrophosphates in the cytosol.

    Miscellaneous databases

    NextBioi 969043.

    Gene expression databases

    Genevestigatori Q12494.

    Family and domain databases

    InterProi IPR005522. IPK.
    [Graphical view ]
    PANTHERi PTHR12400. PTHR12400. 1 hit.
    Pfami PF03770. IPK. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Suppressors of a Saccharomyces cerevisiae pkc1 mutation identify alleles of the phosphatase gene PTC1 and of a novel gene encoding a putative basic leucine zipper protein."
      Huang K.N., Symington L.S.
      Genetics 141:1275-1285(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    2. "Sequencing and analysis of a 35.4 kb region on the right arm of chromosome IV from Saccharomyces cerevisiae reveal 23 open reading frames."
      Eide L.G., Sander C., Prydz H.
      Yeast 12:1085-1090(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Synthesis of diphosphoinositol pentakisphosphate by a newly identified family of higher inositol polyphosphate kinases."
      Saiardi A., Erdjument-Bromage H., Snowman A.M., Tempst P., Snyder S.H.
      Curr. Biol. 9:1323-1326(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "The inositol hexakisphosphate kinase family. Catalytic flexibility and function in yeast vacuole biogenesis."
      Saiardi A., Caffrey J.J., Snyder S.H., Shears S.B.
      J. Biol. Chem. 275:24686-24692(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    7. "In Saccharomyces cerevisiae, the inositol polyphosphate kinase activity of Kcs1p is required for resistance to salt stress, cell wall integrity, and vacuolar morphogenesis."
      Dubois E., Scherens B., Vierendeels F., Ho M.M.W., Messenguy F., Shears S.B.
      J. Biol. Chem. 277:23755-23763(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. "Inositol diphosphate signaling regulates telomere length."
      York S.J., Armbruster B.N., Greenwell P., Petes T.D., York J.D.
      J. Biol. Chem. 280:4264-4269(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Plc1p, Arg82p, and Kcs1p, enzymes involved in inositol pyrophosphate synthesis, are essential for phosphate regulation and polyphosphate accumulation in Saccharomyces cerevisiae."
      Auesukaree C., Tochio H., Shirakawa M., Kaneko Y., Harashima S.
      J. Biol. Chem. 280:25127-25133(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Molecular definition of a novel inositol polyphosphate metabolic pathway initiated by inositol 1,4,5-trisphosphate 3-kinase activity in Saccharomyces cerevisiae."
      Seeds A.M., Bastidas R.J., York J.D.
      J. Biol. Chem. 280:27654-27661(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: YAL6B.
    14. "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-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    15. "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 SER-537; SER-566 AND SER-589, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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-150; SER-396; SER-583 AND SER-670, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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-150; SER-396; SER-469; SER-537; SER-539; SER-646; SER-664 AND SER-670, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiKCS1_YEAST
    AccessioniPrimary (citable) accession number: Q12494
    Secondary accession number(s): D6VS03, P89899, Q7LGR2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2006
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 110 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 1940 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 IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3