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P14737

- RAD9_YEAST

UniProt

P14737 - RAD9_YEAST

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Protein

DNA repair protein RAD9

Gene

RAD9

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. double-stranded DNA binding Source: SGD
  2. enzyme activator activity Source: SGD
  3. histone binding Source: SGD

GO - Biological processi

  1. DNA damage checkpoint Source: SGD
  2. DNA repair Source: SGD
  3. G1 DNA damage checkpoint Source: SGD
  4. intra-S DNA damage checkpoint Source: SGD
  5. mitotic G1 DNA damage checkpoint Source: SGD
  6. negative regulation of DNA replication Source: UniProtKB-KW
  7. nucleotide-excision repair Source: SGD
  8. positive regulation of catalytic activity Source: GOC
  9. positive regulation of transcription from RNA polymerase II promoter Source: SGD
  10. regulation of cell cycle Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

DNA replication inhibitor

Keywords - Biological processi

Cell cycle, DNA damage

Enzyme and pathway databases

BioCyciYEAST:G3O-29798-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair protein RAD9
Gene namesi
Name:RAD9
Ordered Locus Names:YDR217C
ORF Names:YD9934.02C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

SGDiS000002625. RAD9.

Subcellular locationi

GO - Cellular componenti

  1. chromatin Source: SGD
  2. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13091309DNA repair protein RAD9PRO_0000097158Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei26 – 261Phosphoserine2 Publications
Modified residuei56 – 561Phosphoserine2 Publications
Modified residuei205 – 2051Phosphoserine1 Publication
Modified residuei218 – 2181Phosphothreonine1 Publication
Modified residuei248 – 2481Phosphoserine1 Publication
Modified residuei312 – 3121Phosphoserine1 Publication
Modified residuei315 – 3151Phosphoserine2 Publications
Modified residuei462 – 4621Phosphoserine2 Publications
Modified residuei471 – 4711Phosphothreonine1 Publication
Modified residuei474 – 4741Phosphothreonine1 Publication
Modified residuei568 – 5681Phosphoserine1 Publication
Modified residuei729 – 7291Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP14737.
PaxDbiP14737.

Expressioni

Gene expression databases

GenevestigatoriP14737.

Interactioni

Subunit structurei

Physically associates with RAD53.

Binary interactionsi

WithEntry#Exp.IntActNotes
DPB11P470279EBI-14788,EBI-25984
RAD53P222163EBI-14788,EBI-17843

Protein-protein interaction databases

BioGridi32270. 356 interactions.
DIPiDIP-2516N.
IntActiP14737. 8 interactions.
MINTiMINT-375284.
STRINGi4932.YDR217C.

Structurei

Secondary structure

1
1309
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi190 – 1923

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP14737.
SMRiP14737. Positions 784-854, 998-1132.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14737.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini994 – 1122129BRCTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 BRCT domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG323789.
InParanoidiP14737.
KOiK06661.
OrthoDBiEOG75J0WC.

Family and domain databases

Gene3Di3.40.50.10190. 1 hit.
InterProiIPR001357. BRCT_dom.
IPR013914. Rad9_Rad53-bd_dom_fun.
[Graphical view]
PfamiPF00533. BRCT. 1 hit.
PF08605. Rad9_Rad53_bind. 1 hit.
[Graphical view]
SMARTiSM00292. BRCT. 1 hit.
[Graphical view]
SUPFAMiSSF52113. SSF52113. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P14737-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGQLVQWKS SPDRVTQSAI KEALHSPLAD GDMNEMNVPV DPLENKVNST
60 70 80 90 100
NIIEGSPKAN PNPVKFMNTS EIFQKSLGLL DESPRHDDEL NIEVGDNDRP
110 120 130 140 150
NANILHNERT PDLDRIANFF KSNRTPGKEN LLTKYQSSDL EDTPLMLRKK
160 170 180 190 200
MTFQTPTDPL EQKTFKKLKS DTGFCYYGEQ NDGEENASLE VTEADATFVQ
210 220 230 240 250
MAERSADNYD CALEGIVTPK RYKDELSKSG GMQDERVQKT QIMISAESPN
260 270 280 290 300
SISSYDKNKI TGNGRTTRNV NKVFNNNEDN IGAIEEKNPV KKKSENYSSD
310 320 330 340 350
DLRERNNQII QSNESEEINE LEKNLNVSGR ENDVNNLDID INSAVSGTPS
360 370 380 390 400
RNNAEEEMYS SESVNNREPS KKWIFRYSKD KTENNSNRST QIVNNPRTQE
410 420 430 440 450
MPLDSISIDT QPLSKSFNTE TNNELETQII VSSLSQGISA QKGPVFHSTG
460 470 480 490 500
QTEEIKTQII NSPEQNALNA TFETPVTLSR INFEPILEVP ETSSPSKNTM
510 520 530 540 550
SKPSNSSPIP KEKDTFNIHE REVETNNVFS NDIQNSSNAA TRDDIIIAGS
560 570 580 590 600
SDFNEQKEIT DRIYLQLSGK QISDSGSDET ERMSPNELDT KKESTIMSEV
610 620 630 640 650
ELTQELPEVE EQQDLQTSPK KLVVEEETLM EIKKSKGNSL QLHDDNKECN
660 670 680 690 700
SDKQDGTESL DVALIEHESK GQSSELQKNL MQLFPSESQE IIQNRRTIKR
710 720 730 740 750
RQKDTIEIGE EEENRSTKTS PTKHLKRNSD LDAASIKREP SCSITIQTGE
760 770 780 790 800
TGSGKDSKEQ SYVFPEGIRT ADNSFLSKDD IIFGNAVWCQ YTWNYKFYPG
810 820 830 840 850
ILLEVDTNQD GCWIYFETGR SLTKDEDIYY LDIRIGDAVT FDGNEYVVVG
860 870 880 890 900
LECRSHDLNI IRCIRGYDTV HLKKKNASGL LGKRTLIKAL SSISLDLSEW
910 920 930 940 950
AKRAKIILED NEKNKGDAYR YLRHPIRGRK SMTNVLSPKK HTDDEKDINT
960 970 980 990 1000
HTEVYNNEIE SSSEKKEIVK KDSRDALAEH AGAPSLLFSS GEIRTGNVFD
1010 1020 1030 1040 1050
KCIFVLTSLF ENREELRQTI ESQGGTVIES GFSTLFNFTH PLAKSLVNKG
1060 1070 1080 1090 1100
NTDNIRELAL KLAWKPHSLF ADCRFACLIT KRHLRSLKYL ETLALGWPTL
1110 1120 1130 1140 1150
HWKFISACIE KKRIVPHLIY QYLLPSGESF RLSLDSPSKG GIIKSNNIFS
1160 1170 1180 1190 1200
FYTQFLRGSN LRDQICGVKK MLNDYIVIVW GRSELDSFVK FAFACLSAGR
1210 1220 1230 1240 1250
MLTIDLPNID VDDTEPLLNA LDSLVPRIGS ELSNRKLKFL IYANENNGKS
1260 1270 1280 1290 1300
QMKLLERLRS QISLKFKKFN YIFHTESKEW LIQTIINEDT GFHDDITDND

IYNTISEVR
Length:1,309
Mass (Da):148,398
Last modified:October 5, 2010 - v2
Checksum:iFCDAC16694484D8D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti433 – 4331S → C in AAA34954. (PubMed:2664461)Curated
Sequence conflicti433 – 4331S → C no nucleotide entry (PubMed:2247073)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M26049 Genomic DNA. Translation: AAA34954.1.
Z48612 Genomic DNA. Translation: CAA88497.1.
BK006938 Genomic DNA. Translation: DAA12060.1.
PIRiS59424. BVBYD9.
RefSeqiNP_010503.1. NM_001180525.1.

Genome annotation databases

EnsemblFungiiYDR217C; YDR217C; YDR217C.
GeneIDi851803.
KEGGisce:YDR217C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M26049 Genomic DNA. Translation: AAA34954.1 .
Z48612 Genomic DNA. Translation: CAA88497.1 .
BK006938 Genomic DNA. Translation: DAA12060.1 .
PIRi S59424. BVBYD9.
RefSeqi NP_010503.1. NM_001180525.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FHR NMR - P 826-832 [» ]
1J4K NMR - P 826-832 [» ]
1J4L NMR - P 599-607 [» ]
1J4P NMR - B 149-161 [» ]
1J4Q NMR - B 188-200 [» ]
1K2M NMR - P 826-832 [» ]
1K2N NMR - P 599-607 [» ]
1K3N NMR - B 149-161 [» ]
1K3Q NMR - B 188-200 [» ]
2FF4 X-ray 1.90 E/F 188-195 [» ]
ProteinModelPortali P14737.
SMRi P14737. Positions 784-854, 998-1132.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32270. 356 interactions.
DIPi DIP-2516N.
IntActi P14737. 8 interactions.
MINTi MINT-375284.
STRINGi 4932.YDR217C.

Proteomic databases

MaxQBi P14737.
PaxDbi P14737.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR217C ; YDR217C ; YDR217C .
GeneIDi 851803.
KEGGi sce:YDR217C.

Organism-specific databases

SGDi S000002625. RAD9.

Phylogenomic databases

eggNOGi NOG323789.
InParanoidi P14737.
KOi K06661.
OrthoDBi EOG75J0WC.

Enzyme and pathway databases

BioCyci YEAST:G3O-29798-MONOMER.

Miscellaneous databases

EvolutionaryTracei P14737.
NextBioi 969644.

Gene expression databases

Genevestigatori P14737.

Family and domain databases

Gene3Di 3.40.50.10190. 1 hit.
InterProi IPR001357. BRCT_dom.
IPR013914. Rad9_Rad53-bd_dom_fun.
[Graphical view ]
Pfami PF00533. BRCT. 1 hit.
PF08605. Rad9_Rad53_bind. 1 hit.
[Graphical view ]
SMARTi SM00292. BRCT. 1 hit.
[Graphical view ]
SUPFAMi SSF52113. SSF52113. 1 hit.
PROSITEi PS50172. BRCT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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.
    , 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.
  4. 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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, INTERACTION WITH RAD53.
  6. 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] [Europe PMC] [Abstract]
    Cited for: 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-26; SER-56; SER-205; THR-218; SER-248; SER-312; SER-315; SER-462; SER-568 AND SER-729, 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-26; SER-56; SER-315; SER-462; THR-471; THR-474 AND SER-729, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRAD9_YEAST
AccessioniPrimary (citable) accession number: P14737
Secondary accession number(s): D6VSK0, Q04920
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 5, 2010
Last modified: October 29, 2014
This is version 142 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 400 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, 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