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P18899 (DDR48_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. 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:
Stress protein DDR48
Alternative name(s):
DNA damage-responsive protein 48
Short name=DDRP 48
Flocculent-specific protein
YP 75
Gene names
Name:DDR48
Synonyms:FSP
Ordered Locus Names:YMR173W
ORF Names:YM8010.03
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Induction

Expression is induced by DNA damage, as well as by salt, oxidative, and heat-shock stress. Ref.5 Ref.7 Ref.10

Post-translational modification

Probably highly glycosylated. Ref.5

Disruption phenotype

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. Ref.1

Sequence similarities

Belongs to the DDR48 family.

Caution

(Ref.6) sequence is a contaminating peptide from a S.cerevisiae glycogen synthase purification.

Biophysicochemical properties

Kinetic parameters:

KM=0.29 mM for ATP Ref.5

KM=0.58 mM for GTP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5 Ref.6
Chain2 – 430429Stress protein DDR48
PRO_0000079849

Regions

Repeat74 – 8181
Repeat82 – 8982
Repeat90 – 9783
Repeat98 – 10584
Repeat106 – 11385
Repeat114 – 12186
Repeat124 – 13187; approximate
Repeat132 – 13988
Repeat141 – 14889
Repeat149 – 156810
Repeat157 – 164811
Repeat165 – 172812
Repeat175 – 182813; approximate
Repeat183 – 190814
Repeat191 – 198815
Repeat201 – 208816; approximate
Repeat209 – 216817
Repeat217 – 224818
Repeat225 – 232819
Repeat233 – 240820
Repeat243 – 250821; approximate
Repeat251 – 258822
Repeat260 – 267823
Repeat268 – 275824
Repeat278 – 285825; approximate
Repeat287 – 294826
Repeat296 – 303827
Repeat306 – 313828; approximate
Repeat314 – 321829
Repeat322 – 329830
Repeat332 – 339831; approximate
Repeat340 – 347832
Repeat348 – 355833
Repeat358 – 365834; approximate
Repeat366 – 373835
Repeat375 – 382836
Repeat393 – 400837; approximate
Repeat407 – 414838
Region74 – 41434138 X 8 AA approximate tandem repeats of S-[NS]-N-[ND]-D-S-Y-G

Amino acid modifications

Modified residue1831Phosphoserine Ref.9
Modified residue1911Phosphoserine Ref.9
Modified residue3141Phosphoserine Ref.9
Modified residue3221Phosphoserine Ref.9

Experimental info

Sequence conflict91Q → E AA sequence Ref.6
Sequence conflict381E → Q in AAA34563. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P18899 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 650212489A8828AC

FASTA43046,233
        10         20         30         40         50         60 
MGLFDKVKQF ANSNNNNNDS GNNNQGDYVT KAENMIGEDR VNQFKSKIGE DRFDKMESKV 

        70         80         90        100        110        120 
RQQFSNTSIN DNDSNNNDSY GSNNNDSYGS NNNDSYGSNN NDSYGSNNND SYGSNNDDSY 

       130        140        150        160        170        180 
GSSNKKKSSY GSNNDDSYGS SNNNDSYGSN NNDSYGSNNN DSYGSNNDDS YGSSNKNKSS 

       190        200        210        220        230        240 
YGSNNDDSYG SNNDDSYGSS NKKKSSYGSS NNDSYGSNND DSYGSNNNDS YGSNNDDSYG 

       250        260        270        280        290        300 
SSNKKKSSYG SNNDDSYGSS NNNDSYGSNN DDSYGSSNKN KSSYGSSSND DSYGSSNNDD 

       310        320        330        340        350        360 
SYGSSNKKKS SYGSNNDDSY GSNNDDSYGS SNKKKSSYGS SNNDSYGSNN DDSYGSSNKK 

       370        380        390        400        410        420 
KSSYGSNNDD SYGSSNNNDS YGSNNDDSYG SSNRNKNSYG SSNYGSSNND DSYGSSNRGG 

       430 
RNQYGGDDDY 

« Hide

References

« Hide 'large scale' references
[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]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M36110 Genomic DNA. Translation: AAA34563.1.
S73336 Genomic DNA. Translation: AAB31954.1.
Z49808 Genomic DNA. Translation: CAA89906.1.
BK006946 Genomic DNA. Translation: DAA10069.1.
PIRHHBYD8. S55120.
RefSeqNP_013897.1. NM_001182678.1.

3D structure databases

ProteinModelPortalP18899.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35351. 42 interactions.
DIPDIP-4424N.
IntActP18899. 3 interactions.
MINTMINT-546743.
STRING4932.YMR173W.

Proteomic databases

PaxDbP18899.
PeptideAtlasP18899.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYMR173W; YMR173W; YMR173W.
GeneID855210.
KEGGsce:YMR173W.

Organism-specific databases

SGDS000004784. DDR48.

Phylogenomic databases

eggNOGNOG301978.
GeneTreeENSGT00730000112695.
HOGENOMHOG000000764.
OMAKNSYGDD.
OrthoDBEOG70KH3D.

Enzyme and pathway databases

BioCycYEAST:G3O-32861-MONOMER.

Gene expression databases

GenevestigatorP18899.

Family and domain databases

ProtoNetSearch...

Other

NextBio978711.
PROP18899.

Entry information

Entry nameDDR48_YEAST
AccessionPrimary (citable) accession number: P18899
Secondary accession number(s): D6VZZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 112 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families