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P14737 (RAD9_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 116. 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA repair protein RAD9
Gene names
Name:RAD9
Ordered Locus Names:YDR217C
ORF Names:YD9934.02C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length1309 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential for cell cycle arrest at the G2 stage following DNA damage by X-irradiation or inactivation of DNA ligase.

Subunit structure

Physically associates with RAD53.

Subcellular location

Nucleus.

Miscellaneous

Present with 400 molecules/cell in log phase SD medium. Ref.6

Sequence similarities

Contains 1 BRCT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13091309DNA repair protein RAD9
PRO_0000097158

Regions

Domain994 – 1122129BRCT

Amino acid modifications

Modified residue101Phosphoserine Ref.8
Modified residue111Phosphoserine Ref.7 Ref.8
Modified residue261Phosphoserine Ref.9
Modified residue501Phosphothreonine Ref.9
Modified residue561Phosphoserine Ref.9
Modified residue701Phosphoserine Ref.9
Modified residue761Phosphoserine Ref.9
Modified residue831Phosphoserine Ref.9
Modified residue1371Phosphoserine Ref.9
Modified residue1381Phosphoserine Ref.9
Modified residue1551Phosphothreonine Ref.9
Modified residue1881Phosphoserine Ref.9
Modified residue2051Phosphoserine Ref.9
Modified residue2181Phosphothreonine Ref.9
Modified residue2481Phosphoserine Ref.9
Modified residue2981Phosphoserine Ref.8 Ref.9
Modified residue2991Phosphoserine Ref.8
Modified residue3121Phosphoserine Ref.9
Modified residue3151Phosphoserine Ref.9
Modified residue3281Phosphoserine Ref.9
Modified residue3481Phosphothreonine Ref.9
Modified residue3981Phosphothreonine Ref.9
Modified residue4141Phosphoserine Ref.9
Modified residue4161Phosphoserine Ref.9
Modified residue4351Phosphoserine Ref.9
Modified residue4571Phosphothreonine Ref.9
Modified residue4621Phosphoserine Ref.9
Modified residue4711Phosphothreonine Ref.9
Modified residue4791Phosphoserine Ref.9
Modified residue5071Phosphoserine Ref.9
Modified residue5371Phosphoserine Ref.9
Modified residue5411Phosphothreonine Ref.9
Modified residue5501Phosphoserine Ref.9
Modified residue5681Phosphoserine Ref.9
Modified residue5981Phosphoserine Ref.9
Modified residue6031Phosphothreonine Ref.9
Modified residue6181Phosphoserine Ref.9
Modified residue7291Phosphoserine Ref.8 Ref.9
Modified residue7411Phosphoserine Ref.9
Modified residue8071Phosphothreonine Ref.9
Modified residue9311Phosphoserine Ref.9
Modified residue9371Phosphoserine Ref.9
Modified residue9891Phosphoserine Ref.8 Ref.9
Modified residue9901Phosphoserine Ref.9
Modified residue11361Phosphoserine Ref.8 Ref.9

Experimental info

Sequence conflict4331S → C in AAA34954. Ref.1
Sequence conflict4331S → C no nucleotide entry Ref.2

Sequences

Sequence LengthMass (Da)Tools
P14737 [UniParc].

Last modified October 5, 2010. Version 2.
Checksum: FCDAC16694484D8D

FASTA1,309148,398
        10         20         30         40         50         60 
MSGQLVQWKS SPDRVTQSAI KEALHSPLAD GDMNEMNVPV DPLENKVNST NIIEGSPKAN 

        70         80         90        100        110        120 
PNPVKFMNTS EIFQKSLGLL DESPRHDDEL NIEVGDNDRP NANILHNERT PDLDRIANFF 

       130        140        150        160        170        180 
KSNRTPGKEN LLTKYQSSDL EDTPLMLRKK MTFQTPTDPL EQKTFKKLKS DTGFCYYGEQ 

       190        200        210        220        230        240 
NDGEENASLE VTEADATFVQ MAERSADNYD CALEGIVTPK RYKDELSKSG GMQDERVQKT 

       250        260        270        280        290        300 
QIMISAESPN SISSYDKNKI TGNGRTTRNV NKVFNNNEDN IGAIEEKNPV KKKSENYSSD 

       310        320        330        340        350        360 
DLRERNNQII QSNESEEINE LEKNLNVSGR ENDVNNLDID INSAVSGTPS RNNAEEEMYS 

       370        380        390        400        410        420 
SESVNNREPS KKWIFRYSKD KTENNSNRST QIVNNPRTQE MPLDSISIDT QPLSKSFNTE 

       430        440        450        460        470        480 
TNNELETQII VSSLSQGISA QKGPVFHSTG QTEEIKTQII NSPEQNALNA TFETPVTLSR 

       490        500        510        520        530        540 
INFEPILEVP ETSSPSKNTM SKPSNSSPIP KEKDTFNIHE REVETNNVFS NDIQNSSNAA 

       550        560        570        580        590        600 
TRDDIIIAGS SDFNEQKEIT DRIYLQLSGK QISDSGSDET ERMSPNELDT KKESTIMSEV 

       610        620        630        640        650        660 
ELTQELPEVE EQQDLQTSPK KLVVEEETLM EIKKSKGNSL QLHDDNKECN SDKQDGTESL 

       670        680        690        700        710        720 
DVALIEHESK GQSSELQKNL MQLFPSESQE IIQNRRTIKR RQKDTIEIGE EEENRSTKTS 

       730        740        750        760        770        780 
PTKHLKRNSD LDAASIKREP SCSITIQTGE TGSGKDSKEQ SYVFPEGIRT ADNSFLSKDD 

       790        800        810        820        830        840 
IIFGNAVWCQ YTWNYKFYPG ILLEVDTNQD GCWIYFETGR SLTKDEDIYY LDIRIGDAVT 

       850        860        870        880        890        900 
FDGNEYVVVG LECRSHDLNI IRCIRGYDTV HLKKKNASGL LGKRTLIKAL SSISLDLSEW 

       910        920        930        940        950        960 
AKRAKIILED NEKNKGDAYR YLRHPIRGRK SMTNVLSPKK HTDDEKDINT HTEVYNNEIE 

       970        980        990       1000       1010       1020 
SSSEKKEIVK KDSRDALAEH AGAPSLLFSS GEIRTGNVFD KCIFVLTSLF ENREELRQTI 

      1030       1040       1050       1060       1070       1080 
ESQGGTVIES GFSTLFNFTH PLAKSLVNKG NTDNIRELAL KLAWKPHSLF ADCRFACLIT 

      1090       1100       1110       1120       1130       1140 
KRHLRSLKYL ETLALGWPTL HWKFISACIE KKRIVPHLIY QYLLPSGESF RLSLDSPSKG 

      1150       1160       1170       1180       1190       1200 
GIIKSNNIFS FYTQFLRGSN LRDQICGVKK MLNDYIVIVW GRSELDSFVK FAFACLSAGR 

      1210       1220       1230       1240       1250       1260 
MLTIDLPNID VDDTEPLLNA LDSLVPRIGS ELSNRKLKFL IYANENNGKS QMKLLERLRS 

      1270       1280       1290       1300 
QISLKFKKFN YIFHTESKEW LIQTIINEDT GFHDDITDND IYNTISEVR

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequence analysis of the Saccharomyces cerevisiae RAD9 gene and further evidence that its product is required for cell cycle arrest induced by DNA damage."
Schiestl R.H., Reynolds P., Prakash S., Prakash L.
Mol. Cell. Biol. 9:1882-1896(1989) [PubMed: 2664461] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Characterization of RAD9 of Saccharomyces cerevisiae and evidence that its function acts posttranslationally in cell cycle arrest after DNA damage."
Weinert T.A., Hartwell L.H.
Mol. Cell. Biol. 10:6554-6564(1990) [PubMed: 2247073] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[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. expand/collapse author list , 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: 9169867] [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]"The budding yeast Rad9 checkpoint protein is subjected to Mec1/Tel1-dependent hyperphosphorylation and interacts with Rad53 after DNA damage."
Vialard J.E., Gilbert C.S., Green C.M., Lowndes N.F.
EMBO J. 17:5679-5688(1998) [PubMed: 9755168] [Abstract]
Cited for: PHOSPHORYLATION, INTERACTION WITH RAD53.
[6]"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: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[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: 17287358] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, MASS SPECTROMETRY.
[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: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-11; SER-298; SER-299; SER-729; SER-989 AND SER-1136, 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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; THR-50; SER-56; SER-70; SER-76; SER-83; SER-137; SER-138; THR-155; SER-188; SER-205; THR-218; SER-248; SER-298; SER-312; SER-315; SER-328; THR-348; THR-398; SER-414; SER-416; SER-435; THR-457; SER-462; THR-471; SER-479; SER-507; SER-537; THR-541; SER-550; SER-568; SER-598; THR-603; SER-618; SER-729; SER-741; THR-807; SER-931; SER-937; SER-989; SER-990 AND SER-1136, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M26049 Genomic DNA. Translation: AAA34954.1.
Z48612 Genomic DNA. Translation: CAA88497.1.
BK006938 Genomic DNA. Translation: DAA12060.1.
PIRBVBYD9. S59424.
RefSeqNP_010503.1. NM_001180525.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FHRNMR-P826-832[»]
1J4KNMR-P826-832[»]
1J4LNMR-P599-607[»]
1J4PNMR-B149-161[»]
1J4QNMR-B188-200[»]
1K2MNMR-P826-832[»]
1K2NNMR-P599-607[»]
1K3NNMR-B149-161[»]
1K3QNMR-B188-200[»]
2FF4X-ray1.90E/F188-195[»]
ProteinModelPortalP14737.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2516N.
IntActP14737. 6 interactions.
MINTMINT-375284.
STRINGP14737.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR217C; YDR217C; YDR217C.
GeneID851803.
KEGGsce:YDR217C.

Organism-specific databases

SGDS000002625. RAD9.

Phylogenomic databases

eggNOGfuNOG09839.
GeneTreeEFGT00050000002547.
OMAESKEWLI.
OrthoDBEOG4K3Q56.

Gene expression databases

ArrayExpressP14737.
GenevestigatorP14737.
GermOnlineYDR217C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR001357. BRCT.
IPR013914. Rad9_Rad53-bd_fun.
[Graphical view]
KOK06661.
PfamPF00533. BRCT. 1 hit.
PF08605. Rad9_Rad53_bind. 1 hit.
[Graphical view]
SMARTSM00292. BRCT. 1 hit.
[Graphical view]
SUPFAMSSF52113. BRCT. 1 hit.
PROSITEPS50172. BRCT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRAD9_YEAST
AccessionPrimary (citable) accession number: P14737
Secondary accession number(s): D6VSK0, Q04920
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 5, 2010
Last modified: November 16, 2011
This is version 116 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents