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P15454

- KGUA_YEAST

UniProt

P15454 - KGUA_YEAST

Protein

Guanylate kinase

Gene

GUK1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Essential for recycling GMP and indirectly, cGMP.

    Catalytic activityi

    ATP + GMP = ADP + GDP.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi9 – 168ATP
    Nucleotide bindingi35 – 8248GMPAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. guanylate kinase activity Source: UniProtKB

    GO - Biological processi

    1. GMP metabolic process Source: SGD
    2. nucleotide phosphorylation Source: GOC
    3. purine nucleotide metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER3O-102.
    YEAST:MONOMER3O-102.
    ReactomeiREACT_188930. Abacavir metabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Guanylate kinase (EC:2.7.4.8)
    Alternative name(s):
    GMP kinase
    Gene namesi
    Name:GUK1
    Ordered Locus Names:YDR454C
    ORF Names:D9461.39
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    SGDiS000002862. GUK1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 187186Guanylate kinasePRO_0000170655Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei149 – 1491Phosphoserine4 Publications
    Modified residuei157 – 1571Phosphotyrosine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP15454.
    PaxDbiP15454.
    PeptideAtlasiP15454.

    Expressioni

    Gene expression databases

    GenevestigatoriP15454.

    Interactioni

    Subunit structurei

    Monomer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself1EBI-9672,EBI-9672
    ACF2Q121681EBI-9672,EBI-32973
    UBX2Q042281EBI-9672,EBI-27730

    Protein-protein interaction databases

    BioGridi32509. 29 interactions.
    DIPiDIP-6721N.
    MINTiMINT-522729.
    STRINGi4932.YDR454C.

    Structurei

    Secondary structure

    1
    187
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 84
    Helixi15 – 2511
    Turni27 – 293
    Beta strandi30 – 323
    Beta strandi35 – 373
    Turni47 – 493
    Beta strandi50 – 534
    Helixi56 – 649
    Beta strandi68 – 747
    Beta strandi77 – 826
    Helixi83 – 9210
    Beta strandi94 – 996
    Helixi102 – 1098
    Helixi112 – 1143
    Beta strandi117 – 1226
    Helixi126 – 13611
    Helixi141 – 15818
    Turni159 – 1613
    Beta strandi163 – 1686
    Helixi172 – 18312

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EX6X-ray2.30A/B2-187[»]
    1EX7X-ray1.90A2-187[»]
    1GKYX-ray2.00A2-187[»]
    4F4JX-ray2.45A/B1-187[»]
    ProteinModelPortaliP15454.
    SMRiP15454. Positions 2-187.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15454.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 184183Guanylate kinase-likeAdd
    BLAST

    Sequence similaritiesi

    Belongs to the guanylate kinase family.Curated
    Contains 1 guanylate kinase-like domain.Curated

    Phylogenomic databases

    eggNOGiCOG0194.
    GeneTreeiENSGT00730000110700.
    HOGENOMiHOG000037640.
    KOiK00942.
    OMAiDAVFSIS.
    OrthoDBiEOG7TF7NW.

    Family and domain databases

    Gene3Di3.40.50.300. 3 hits.
    HAMAPiMF_00328. Guanylate_kinase.
    InterProiIPR008145. GK/Ca_channel_bsu.
    IPR008144. Guanylate_kin-like.
    IPR017665. Guanylate_kinase.
    IPR020590. Guanylate_kinase_CS.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00625. Guanylate_kin. 1 hit.
    [Graphical view]
    SMARTiSM00072. GuKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR03263. guanyl_kin. 1 hit.
    PROSITEiPS00856. GUANYLATE_KINASE_1. 1 hit.
    PS50052. GUANYLATE_KINASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P15454-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRPIVISGP SGTGKSTLLK KLFAEYPDSF GFSVSSTTRT PRAGEVNGKD    50
    YNFVSVDEFK SMIKNNEFIE WAQFSGNYYG STVASVKQVS KSGKTCILDI 100
    DMQGVKSVKA IPELNARFLF IAPPSVEDLK KRLEGRGTET EESINKRLSA 150
    AQAELAYAET GAHDKVIVND DLDKAYKELK DFIFAEK 187
    Length:187
    Mass (Da):20,637
    Last modified:January 23, 2007 - v2
    Checksum:i5DC4D2A22594BFB8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04683 Genomic DNA. Translation: AAA34657.1.
    U33007 Genomic DNA. Translation: AAB64881.1.
    BK006938 Genomic DNA. Translation: DAA12289.1.
    PIRiA45097. KIBYGU.
    RefSeqiNP_010742.1. NM_001180762.1.

    Genome annotation databases

    EnsemblFungiiYDR454C; YDR454C; YDR454C.
    GeneIDi852065.
    KEGGisce:YDR454C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L04683 Genomic DNA. Translation: AAA34657.1 .
    U33007 Genomic DNA. Translation: AAB64881.1 .
    BK006938 Genomic DNA. Translation: DAA12289.1 .
    PIRi A45097. KIBYGU.
    RefSeqi NP_010742.1. NM_001180762.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EX6 X-ray 2.30 A/B 2-187 [» ]
    1EX7 X-ray 1.90 A 2-187 [» ]
    1GKY X-ray 2.00 A 2-187 [» ]
    4F4J X-ray 2.45 A/B 1-187 [» ]
    ProteinModelPortali P15454.
    SMRi P15454. Positions 2-187.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32509. 29 interactions.
    DIPi DIP-6721N.
    MINTi MINT-522729.
    STRINGi 4932.YDR454C.

    Proteomic databases

    MaxQBi P15454.
    PaxDbi P15454.
    PeptideAtlasi P15454.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR454C ; YDR454C ; YDR454C .
    GeneIDi 852065.
    KEGGi sce:YDR454C.

    Organism-specific databases

    SGDi S000002862. GUK1.

    Phylogenomic databases

    eggNOGi COG0194.
    GeneTreei ENSGT00730000110700.
    HOGENOMi HOG000037640.
    KOi K00942.
    OMAi DAVFSIS.
    OrthoDBi EOG7TF7NW.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER3O-102.
    YEAST:MONOMER3O-102.
    Reactomei REACT_188930. Abacavir metabolism.

    Miscellaneous databases

    EvolutionaryTracei P15454.
    NextBioi 970349.
    PROi P15454.

    Gene expression databases

    Genevestigatori P15454.

    Family and domain databases

    Gene3Di 3.40.50.300. 3 hits.
    HAMAPi MF_00328. Guanylate_kinase.
    InterProi IPR008145. GK/Ca_channel_bsu.
    IPR008144. Guanylate_kin-like.
    IPR017665. Guanylate_kinase.
    IPR020590. Guanylate_kinase_CS.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00625. Guanylate_kin. 1 hit.
    [Graphical view ]
    SMARTi SM00072. GuKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR03263. guanyl_kin. 1 hit.
    PROSITEi PS00856. GUANYLATE_KINASE_1. 1 hit.
    PS50052. GUANYLATE_KINASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of the essential gene for guanylate kinase from yeast."
      Konrad M.
      J. Biol. Chem. 267:25652-25655(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Guanylate kinase from Saccharomyces cerevisiae. Isolation and characterization, crystallization and preliminary X-ray analysis, amino acid sequence and comparison with adenylate kinases."
      Berger A., Schiltz E., Schulz G.E.
      Eur. J. Biochem. 184:433-443(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-187, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2.
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "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-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    7. "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-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "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-149, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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-149 AND TYR-157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Three-dimensional structure of the complex of guanylate kinase from yeast with its substrate GMP."
      Stehle T., Schulz G.E.
      J. Mol. Biol. 211:249-254(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    11. "Refined structure of the complex between guanylate kinase and its substrate GMP at 2.0-A resolution."
      Stehle T., Schulz G.E.
      J. Mol. Biol. 224:1127-1141(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

    Entry informationi

    Entry nameiKGUA_YEAST
    AccessioniPrimary (citable) accession number: P15454
    Secondary accession number(s): D6VT79
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 155 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 20500 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3