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Q02805 (ROD1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 99. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein ROD1
Alternative name(s):
Resistance to o-dinitrobenzene protein 1
Gene names
Name:ROD1
Ordered Locus Names:YOR018W
ORF Names:OR26.08
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length837 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates resistance to o-dinitrobenzene, calcium and zinc. Ref.1 Ref.4

Subunit structure

Interacts with RSP5 via its 2 PY-motifs. Ref.4

Subcellular location

Membrane; Peripheral membrane protein. Note: Membrane-associated or associated to a complex that cofractionates with plasma membrane. Ref.1

Domain

The PY-motifs are required for the interaction with RSP5 ubiquitin-ligase and important for resistance to o-dinitrobenzene. Ref.4

Miscellaneous

Present with 386 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the arrestin family.

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RSP5P399403EBI-15679,EBI-16219

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 837837Protein ROD1
PRO_0000097396

Regions

Motif487 – 4904PY-motif
Motif656 – 6594PY-motif
Compositional bias3 – 64Poly-Ser
Compositional bias524 – 60178Asn-rich
Compositional bias684 – 815132Ser-rich

Amino acid modifications

Modified residue1231Phosphoserine Ref.9
Modified residue1241Phosphoserine Ref.9
Modified residue1251Phosphothreonine Ref.6
Modified residue1381Phosphoserine Ref.9
Modified residue1391Phosphothreonine Ref.9
Modified residue1411Phosphoserine Ref.7 Ref.9
Modified residue4361Phosphoserine Ref.7 Ref.9
Modified residue5361Phosphoserine Ref.9
Modified residue6021Phosphoserine Ref.8 Ref.9
Modified residue6041Phosphoserine Ref.9
Modified residue6061Phosphothreonine Ref.9
Modified residue6261Phosphoserine Ref.8 Ref.9
Modified residue6841Phosphoserine Ref.9
Modified residue6851Phosphothreonine Ref.9
Modified residue7201Phosphoserine Ref.7 Ref.9
Modified residue7231Phosphoserine Ref.9
Modified residue7251Phosphoserine Ref.9
Modified residue8131Phosphoserine Ref.9
Modified residue8151Phosphoserine Ref.9

Experimental info

Mutagenesis487 – 4882PP → QA: Reduced binding to RSP5. Ref.4
Mutagenesis656 – 6572PP → QA: Reduced binding to RSP5. Ref.4
Sequence conflict6181Y → D in AAB03678. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q02805 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: FD9A64174B1DC443

FASTA83792,349
        10         20         30         40         50         60 
MFSSSSRPSK EPLLFDIRLR NLDNDVLLIK GPPDEASSVL LSGTIVLSIT EPIQIKSLAL 

        70         80         90        100        110        120 
RLFGRLRLNI PTVLQTVHGP HKRYSKFERN IYSHFWDDFN IKSYFQNLYD NHNNGKITIS 

       130        140        150        160        170        180 
SKSSTNLAAL PKRKRALSTA SLISSNGQTS ASKNYHTLVK GNYEFPFSAI IPGSLVESVE 

       190        200        210        220        230        240 
GLPNAAVTYA LEATIERPKQ PDLICKKHLR VIRTLAIDAV ELSETVSVDN SWPEKVDYTI 

       250        260        270        280        290        300 
SIPTKAIAIG SSTMINILIV PILKGLKLGP VRISLVENSQ YCGSYGGVIN QERMVAKLKL 

       310        320        330        340        350        360 
KDPLKHVAQI KKKRSLNEAA DEGVDTDTGE FQDKWEVRAL LNIPASLTKC SQDCRILSNI 

       370        380        390        400        410        420 
KVRHKIKFTI SLLNPDGHIS ELRAALPVQL FISPFVPVNV KTSDVIERTL KTFGPSYQVT 

       430        440        450        460        470        480 
SQHDNSFSSK NFVDDSEEDV IFQRSASALQ LSSMPTIVSG STLNINSTDA EATAVADTTM 

       490        500        510        520        530        540 
VTSLMVPPNY GNHVYDRVYG EVTNEDETSA SASSSAVESQ AIHNIQNLYI SDSNNSNNPI 

       550        560        570        580        590        600 
LAPNPQIKIE DDSLNNCDSR GDSVNNSNLN LVNSNLTISE NWNNNSPSAN RYNNIINAGL 

       610        620        630        640        650        660 
NSPSLTPSFA HLSRRNSYSR QTSSTSLKND LELTDLSRVP SYDKAMKSDM IGEDLPPAYP 

       670        680        690        700        710        720 
EEELGVQENK KIELERPQIL HHKSTSSLLP LPGSSKSSNN LKRSSSRTHL SHSPLPRNNS 

       730        740        750        760        770        780 
GSSVSLQQLA RNNTDSSFNL NLSFTSAKSS TGSRHFPFNM TTSFTSNSSS KNNSHFDKTD 

       790        800        810        820        830 
STSDANKPRE EENYTSATHN RRSRSSSVRS NNSNSPLRQG TGSFANLMEM FTKRDRS 

« Hide

References

« Hide 'large scale' references
[1]"ROD1, a novel gene conferring multiple resistance phenotypes in Saccharomyces cerevisiae."
Wu A.L., Hallstrom T.C., Moye-Rowley W.S.
J. Biol. Chem. 271:2914-2920(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"PY motifs of Rod1 are required for binding to Rsp5 and for drug resistance."
Andoh T., Hirata Y., Kikuchi A.
FEBS Lett. 525:131-134(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DOMAIN, INTERACTION WITH RSP5, MUTAGENESIS OF 487-PRO-PRO-488 AND 656-PRO-PRO-657.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"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 THR-125, MASS SPECTROMETRY.
Strain: YAL6B.
[7]"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-141; SER-436 AND SER-720, MASS SPECTROMETRY.
Strain: ADR376.
[8]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-602 AND SER-626, MASS SPECTROMETRY.
[9]"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-123; SER-124; SER-138; THR-139; SER-141; SER-436; SER-536; SER-602; SER-604; THR-606; SER-626; SER-684; THR-685; SER-720; SER-723; SER-725; SER-813 AND SER-815, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U40561 Genomic DNA. Translation: AAB03678.1.
X87331 Genomic DNA. Translation: CAA60767.1.
Z74926 Genomic DNA. Translation: CAA99208.1.
BK006948 Genomic DNA. Translation: DAA10800.1.
PIRS54624.
RefSeqNP_014661.1. NM_001183437.1.

3D structure databases

ProteinModelPortalQ02805.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-4189N.
IntActQ02805. 5 interactions.
MINTMINT-523247.
STRING4932.YOR018W.

Proteomic databases

PaxDbQ02805.
PeptideAtlasQ02805.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOR018W; YOR018W; YOR018W.
GeneID854183.
KEGGsce:YOR018W.

Organism-specific databases

CYGDYOR018w.
SGDS000005544. ROD1.

Phylogenomic databases

eggNOGNOG275030.
GeneTreeENSGT00530000067129.
HOGENOMHOG000248143.
OMADNTWPKK.
OrthoDBEOG4KSST1.

Gene expression databases

GenevestigatorQ02805.
GermOnlineYOR018W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR011021. Arrestin-like_N.
IPR011022. Arrestin_C-like.
[Graphical view]
PfamPF02752. Arrestin_C. 1 hit.
PF00339. Arrestin_N. 1 hit.
[Graphical view]
SMARTSM01017. Arrestin_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio975990.

Entry information

Entry nameROD1_YEAST
AccessionPrimary (citable) accession number: Q02805
Secondary accession number(s): D6W284, Q12475
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 3, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XV

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

SIMILARITY comments

Index of protein domains and families