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P18899

- DDR48_YEAST

UniProt

P18899 - DDR48_YEAST

Protein

Stress protein DDR48

Gene

DDR48

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 114 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    DNA damage-responsive protein that may be required for maintaining the rate of spontaneous mutagenesis. Shows low ATP and GTP hydrolysis activity. Dispensable for acquisition of thermotolerance and does not play a significant role in recovery or protection of cells from acute heat shock.1 Publication

    Kineticsi

    1. KM=0.29 mM for ATP1 Publication
    2. KM=0.58 mM for GTP1 Publication

    GO - Molecular functioni

    1. ATPase activity Source: SGD
    2. GTPase activity Source: SGD

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. DNA repair Source: SGD
    3. GTP catabolic process Source: GOC

    Keywords - Biological processi

    Stress response

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32861-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Stress protein DDR48
    Alternative name(s):
    DNA damage-responsive protein 48
    Short name:
    DDRP 48
    Flocculent-specific protein
    YP 75
    Gene namesi
    Name:DDR48
    Synonyms:FSP
    Ordered Locus Names:YMR173W
    ORF Names:YM8010.03
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XIII

    Organism-specific databases

    SGDiS000004784. DDR48.

    Pathology & Biotechi

    Disruption phenotypei

    Shows a slightly altered sensitivity to killing by 4-nitroquinoline-1-oxide and to heat shock; and a 6- to 14-fold reduction of the spontaneous mutation rate of reversion of a HIS4 mutation.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 430429Stress protein DDR48PRO_0000079849Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei183 – 1831Phosphoserine1 Publication
    Modified residuei191 – 1911Phosphoserine1 Publication
    Modified residuei314 – 3141Phosphoserine1 Publication
    Modified residuei322 – 3221Phosphoserine1 Publication

    Post-translational modificationi

    Probably highly glycosylated.1 Publication

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP18899.
    PaxDbiP18899.
    PeptideAtlasiP18899.

    Expressioni

    Inductioni

    Expression is induced by DNA damage, as well as by salt, oxidative, and heat-shock stress.3 Publications

    Gene expression databases

    GenevestigatoriP18899.

    Interactioni

    Protein-protein interaction databases

    BioGridi35351. 42 interactions.
    DIPiDIP-4424N.
    IntActiP18899. 3 interactions.
    MINTiMINT-546743.
    STRINGi4932.YMR173W.

    Structurei

    3D structure databases

    ProteinModelPortaliP18899.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati74 – 8181
    Repeati82 – 8982
    Repeati90 – 9783
    Repeati98 – 10584
    Repeati106 – 11385
    Repeati114 – 12186
    Repeati124 – 13187; approximate
    Repeati132 – 13988
    Repeati141 – 14889
    Repeati149 – 156810
    Repeati157 – 164811
    Repeati165 – 172812
    Repeati175 – 182813; approximate
    Repeati183 – 190814
    Repeati191 – 198815
    Repeati201 – 208816; approximate
    Repeati209 – 216817
    Repeati217 – 224818
    Repeati225 – 232819
    Repeati233 – 240820
    Repeati243 – 250821; approximate
    Repeati251 – 258822
    Repeati260 – 267823
    Repeati268 – 275824
    Repeati278 – 285825; approximate
    Repeati287 – 294826
    Repeati296 – 303827
    Repeati306 – 313828; approximate
    Repeati314 – 321829
    Repeati322 – 329830
    Repeati332 – 339831; approximate
    Repeati340 – 347832
    Repeati348 – 355833
    Repeati358 – 365834; approximate
    Repeati366 – 373835
    Repeati375 – 382836
    Repeati393 – 400837; approximate
    Repeati407 – 414838

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni74 – 41434138 X 8 AA approximate tandem repeats of S-[NS]-N-[ND]-D-S-Y-GAdd
    BLAST

    Sequence similaritiesi

    Belongs to the DDR48 family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG301978.
    GeneTreeiENSGT00730000112695.
    HOGENOMiHOG000000764.
    OMAiKNSYGDD.
    OrthoDBiEOG70KH3D.

    Sequencei

    Sequence statusi: Complete.

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

    P18899-1 [UniParc]FASTAAdd to Basket

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    MGLFDKVKQF ANSNNNNNDS GNNNQGDYVT KAENMIGEDR VNQFKSKIGE    50
    DRFDKMESKV RQQFSNTSIN DNDSNNNDSY GSNNNDSYGS NNNDSYGSNN 100
    NDSYGSNNND SYGSNNDDSY GSSNKKKSSY GSNNDDSYGS SNNNDSYGSN 150
    NNDSYGSNNN DSYGSNNDDS YGSSNKNKSS YGSNNDDSYG SNNDDSYGSS 200
    NKKKSSYGSS NNDSYGSNND DSYGSNNNDS YGSNNDDSYG SSNKKKSSYG 250
    SNNDDSYGSS NNNDSYGSNN DDSYGSSNKN KSSYGSSSND DSYGSSNNDD 300
    SYGSSNKKKS SYGSNNDDSY GSNNDDSYGS SNKKKSSYGS SNNDSYGSNN 350
    DDSYGSSNKK KSSYGSNNDD SYGSSNNNDS YGSNNDDSYG SSNRNKNSYG 400
    SSNYGSSNND DSYGSSNRGG RNQYGGDDDY 430
    Length:430
    Mass (Da):46,233
    Last modified:January 23, 2007 - v4
    Checksum:i650212489A8828AC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 91Q → E AA sequence (PubMed:2114092)Curated
    Sequence conflicti38 – 381E → Q in AAA34563. (PubMed:2111448)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M36110 Genomic DNA. Translation: AAA34563.1.
    S73336 Genomic DNA. Translation: AAB31954.1.
    Z49808 Genomic DNA. Translation: CAA89906.1.
    BK006946 Genomic DNA. Translation: DAA10069.1.
    PIRiS55120. HHBYD8.
    RefSeqiNP_013897.1. NM_001182678.1.

    Genome annotation databases

    EnsemblFungiiYMR173W; YMR173W; YMR173W.
    GeneIDi855210.
    KEGGisce:YMR173W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M36110 Genomic DNA. Translation: AAA34563.1 .
    S73336 Genomic DNA. Translation: AAB31954.1 .
    Z49808 Genomic DNA. Translation: CAA89906.1 .
    BK006946 Genomic DNA. Translation: DAA10069.1 .
    PIRi S55120. HHBYD8.
    RefSeqi NP_013897.1. NM_001182678.1.

    3D structure databases

    ProteinModelPortali P18899.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 35351. 42 interactions.
    DIPi DIP-4424N.
    IntActi P18899. 3 interactions.
    MINTi MINT-546743.
    STRINGi 4932.YMR173W.

    Proteomic databases

    MaxQBi P18899.
    PaxDbi P18899.
    PeptideAtlasi P18899.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YMR173W ; YMR173W ; YMR173W .
    GeneIDi 855210.
    KEGGi sce:YMR173W.

    Organism-specific databases

    SGDi S000004784. DDR48.

    Phylogenomic databases

    eggNOGi NOG301978.
    GeneTreei ENSGT00730000112695.
    HOGENOMi HOG000000764.
    OMAi KNSYGDD.
    OrthoDBi EOG70KH3D.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32861-MONOMER.

    Miscellaneous databases

    NextBioi 978711.
    PROi P18899.

    Gene expression databases

    Genevestigatori P18899.

    Family and domain databases

    ProtoNeti Search...

    Publicationsi

    1. "Structure of the DNA damage-inducible gene DDR48 and evidence for its role in mutagenesis in Saccharomyces cerevisiae."
      Treger J.M., McEntee K.
      Mol. Cell. Biol. 10:3174-3184(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE.
    2. "Molecular cloning of the gene encoding a highly expressed protein in SFL1 gene-disrupted flocculating yeast."
      Tonouchi A., Fujita A., Kuhara S.
      J. Biochem. 115:683-688(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Purification and characterization of Saccharomyces cerevisiae DNA damage-responsive protein 48 (DDRP 48)."
      Sheng S., Schuster S.M.
      J. Biol. Chem. 268:4752-4758(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-31, CLEAVAGE OF INITIATOR METHIONINE, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION, INDUCTION.
    6. "Purification, characterization and partial amino acid sequence of glycogen synthase from Saccharomyces cerevisiae."
      Carabaza A., Arino J., Fox J.W., Villar-Palasi C., Guinovart J.J.
      Biochem. J. 268:401-407(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-12.
    7. "DNA damage and heat shock dually regulate genes in Saccharomyces cerevisiae."
      McClanahan T., McEntee K.
      Mol. Cell. Biol. 6:90-96(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    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: 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-183; SER-191; SER-314 AND SER-322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Yeast adapts to a changing stressful environment by evolving cross-protection and anticipatory gene regulation."
      Dhar R., Sagesser R., Weikert C., Wagner A.
      Mol. Biol. Evol. 30:573-588(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.

    Entry informationi

    Entry nameiDDR48_YEAST
    AccessioniPrimary (citable) accession number: P18899
    Secondary accession number(s): D6VZZ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 114 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Caution

    sequence is a contaminating peptide from a S.cerevisiae glycogen synthase purification.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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 XIII
      Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

    External Data

    Dasty 3