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Protein

Serine/threonine-protein kinase RAD53

Gene

RAD53

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

Functioni

Controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints. Phosphorylates proteins on serine, threonine, and tyrosine. Prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. Seems to be involved in the phosphorylation of RPH1.5 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei227 – 2271ATPPROSITE-ProRule annotation
Active sitei319 – 3191Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi204 – 2129ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • deoxyribonucleoside triphosphate biosynthetic process Source: SGD
  • DNA damage checkpoint Source: SGD
  • DNA repair Source: SGD
  • DNA replication initiation Source: SGD
  • negative regulation of phosphorylation Source: SGD
  • nucleobase-containing compound metabolic process Source: SGD
  • protein localization Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Cell cycle, DNA damage

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-34050-MONOMER.
BRENDAi2.7.12.1. 984.
ReactomeiR-SCE-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-SCE-69473. G2/M DNA damage checkpoint.
R-SCE-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase RAD53 (EC:2.7.12.1)
Alternative name(s):
CHEK2 homolog
Serine-protein kinase 1
Gene namesi
Name:RAD53
Synonyms:MEC2, SAD1, SPK1
Ordered Locus Names:YPL153C
ORF Names:P2588
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL153C.
SGDiS000006074. RAD53.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • cytosol Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 821821Serine/threonine-protein kinase RAD53PRO_0000086595Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241PhosphoserineCombined sources
Modified residuei175 – 1751PhosphoserineCombined sources
Modified residuei547 – 5471PhosphoserineCombined sources
Modified residuei560 – 5601PhosphoserineCombined sources
Modified residuei774 – 7741PhosphoserineCombined sources
Modified residuei793 – 7931PhosphoserineCombined sources

Post-translational modificationi

Autophosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP22216.
PeptideAtlasiP22216.

PTM databases

iPTMnetiP22216.

Interactioni

Subunit structurei

Interacts with PIN4.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ASF1P324478EBI-17843,EBI-3003
PIN4P342173EBI-17843,EBI-21256
RAD9P147378EBI-17843,EBI-14788
SGS1P351873EBI-17843,EBI-17059

Protein-protein interaction databases

BioGridi36030. 358 interactions.
DIPiDIP-2322N.
IntActiP22216. 14 interactions.
MINTiMINT-364105.

Structurei

Secondary structure

1
821
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 249Combined sources
Beta strandi31 – 4313Combined sources
Beta strandi46 – 505Combined sources
Helixi52 – 576Combined sources
Beta strandi59 – 613Combined sources
Beta strandi64 – 718Combined sources
Beta strandi74 – 774Combined sources
Turni82 – 854Combined sources
Beta strandi89 – 935Combined sources
Beta strandi95 – 973Combined sources
Beta strandi99 – 1035Combined sources
Beta strandi109 – 1113Combined sources
Beta strandi114 – 1163Combined sources
Beta strandi120 – 1234Combined sources
Beta strandi129 – 1324Combined sources
Helixi137 – 1393Combined sources
Beta strandi141 – 1477Combined sources
Helixi149 – 1546Combined sources
Beta strandi160 – 1623Combined sources
Helixi193 – 1964Combined sources
Beta strandi197 – 2015Combined sources
Beta strandi211 – 2177Combined sources
Turni218 – 2203Combined sources
Beta strandi223 – 2297Combined sources
Helixi241 – 2488Combined sources
Beta strandi259 – 2646Combined sources
Beta strandi269 – 2735Combined sources
Helixi281 – 2888Combined sources
Helixi293 – 31220Combined sources
Helixi322 – 3243Combined sources
Beta strandi325 – 3295Combined sources
Turni330 – 3334Combined sources
Beta strandi334 – 3374Combined sources
Helixi359 – 3613Combined sources
Helixi364 – 3674Combined sources
Turni384 – 3863Combined sources
Helixi387 – 40317Combined sources
Helixi413 – 4219Combined sources
Helixi428 – 4325Combined sources
Helixi437 – 44610Combined sources
Helixi451 – 4533Combined sources
Helixi457 – 4615Combined sources
Turni464 – 4674Combined sources
Helixi484 – 49310Combined sources
Beta strandi551 – 5577Combined sources
Helixi563 – 5653Combined sources
Beta strandi572 – 5754Combined sources
Beta strandi578 – 5825Combined sources
Beta strandi586 – 5883Combined sources
Beta strandi592 – 5976Combined sources
Beta strandi601 – 6066Combined sources
Beta strandi609 – 6124Combined sources
Beta strandi620 – 62910Combined sources
Beta strandi636 – 6383Combined sources
Beta strandi645 – 6517Combined sources
Beta strandi653 – 6553Combined sources
Beta strandi657 – 6593Combined sources
Beta strandi662 – 6643Combined sources
Beta strandi666 – 6716Combined sources
Beta strandi678 – 6803Combined sources
Turni684 – 6874Combined sources
Beta strandi688 – 6914Combined sources
Beta strandi692 – 6954Combined sources
Beta strandi703 – 7075Combined sources
Beta strandi710 – 7123Combined sources
Beta strandi716 – 7183Combined sources
Helixi721 – 7288Combined sources
Beta strandi804 – 8063Combined sources
Helixi811 – 8133Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DMZNMR-A573-730[»]
1FHQNMR-A573-730[»]
1FHRNMR-A573-730[»]
1G3GNMR-A1-164[»]
1G6GX-ray1.60A/B29-155[»]
1J4KNMR-A573-730[»]
1J4LNMR-A573-730[»]
1J4ONMR-A14-164[»]
1J4PNMR-A14-164[»]
1J4QNMR-A14-164[»]
1K2MNMR-A573-730[»]
1K2NNMR-A573-730[»]
1K3JNMR-A14-164[»]
1K3NNMR-A14-164[»]
1K3QNMR-A14-164[»]
1QU5NMR-A549-730[»]
2A0TNMR-A14-164[»]
2JQINMR-A14-164[»]
B3-12[»]
2JQLNMR-B3-12[»]
2YGVX-ray2.94E/F/G/H800-821[»]
4PDPX-ray2.59A/B170-512[»]
4PDSX-ray2.90A/B170-512[»]
ProteinModelPortaliP22216.
SMRiP22216. Positions 2-490, 549-730.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22216.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini66 – 11651FHA 1PROSITE-ProRule annotationAdd
BLAST
Domaini198 – 466269Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini601 – 66464FHA 2PROSITE-ProRule annotationAdd
BLAST

Domaini

FHA domains are phosphothreonine recognition modules, FHA 1 strongly selects for Asp at position +3 relative to phosphothreonine, whereas FHA 2 selects for Ile in this position.

Sequence similaritiesi

Contains 2 FHA domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00800000124190.
HOGENOMiHOG000074515.
InParanoidiP22216.
KOiK02831.
OMAiHLPFNGK.
OrthoDBiEOG7XWPXG.

Family and domain databases

Gene3Di2.60.200.20. 2 hits.
InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR000253. FHA_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR016256. Ser/Thr_kinase_Rad53.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 1 hit.
PfamiPF00498. FHA. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000661. Ser/Thr_PK_RAD53. 1 hit.
SMARTiSM00240. FHA. 2 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22216-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENITQPTQQ STQATQRFLI EKFSQEQIGE NIVCRVICTT GQIPIRDLSA
60 70 80 90 100
DISQVLKEKR SIKKVWTFGR NPACDYHLGN ISRLSNKHFQ ILLGEDGNLL
110 120 130 140 150
LNDISTNGTW LNGQKVEKNS NQLLSQGDEI TVGVGVESDI LSLVIFINDK
160 170 180 190 200
FKQCLEQNKV DRIRSNLKNT SKIASPGLTS STASSMVANK TGIFKDFSII
210 220 230 240 250
DEVVGQGAFA TVKKAIERTT GKTFAVKIIS KRKVIGNMDG VTRELEVLQK
260 270 280 290 300
LNHPRIVRLK GFYEDTESYY MVMEFVSGGD LMDFVAAHGA VGEDAGREIS
310 320 330 340 350
RQILTAIKYI HSMGISHRDL KPDNILIEQD DPVLVKITDF GLAKVQGNGS
360 370 380 390 400
FMKTFCGTLA YVAPEVIRGK DTSVSPDEYE ERNEYSSLVD MWSMGCLVYV
410 420 430 440 450
ILTGHLPFSG STQDQLYKQI GRGSYHEGPL KDFRISEEAR DFIDSLLQVD
460 470 480 490 500
PNNRSTAAKA LNHPWIKMSP LGSQSYGDFS QISLSQSLSQ QKLLENMDDA
510 520 530 540 550
QYEFVKAQRK LQMEQQLQEQ DQEDQDGKIQ GFKIPAHAPI RYTQPKSIEA
560 570 580 590 600
ETREQKLLHS NNTENVKSSK KKGNGRFLTL KPLPDSIIQE SLEIQQGVNP
610 620 630 640 650
FFIGRSEDCN CKIEDNRLSR VHCFIFKKRH AVGKSMYESP AQGLDDIWYC
660 670 680 690 700
HTGTNVSYLN NNRMIQGTKF LLQDGDEIKI IWDKNNKFVI GFKVEINDTT
710 720 730 740 750
GLFNEGLGML QEQRVVLKQT AEEKDLVKKL TQMMAAQRAN QPSASSSSMS
760 770 780 790 800
AKKPPVSDTN NNGNNSVLND LVESPINANT GNILKRIHSV SLSQSQIDPS
810 820
KKVKRAKLDQ TSKGPENLQF S
Length:821
Mass (Da):91,962
Last modified:August 1, 1991 - v1
Checksum:i84A9612229CA72D1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti204 – 2041V → A in AAT93028 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55623 Genomic DNA. Translation: AAA35070.1.
X96770 Genomic DNA. Translation: CAA65568.1.
Z73509 Genomic DNA. Translation: CAA97858.1.
AY693009 Genomic DNA. Translation: AAT93028.1.
BK006949 Genomic DNA. Translation: DAA11281.1.
PIRiA39616.
RefSeqiNP_015172.1. NM_001183967.1.

Genome annotation databases

EnsemblFungiiYPL153C; YPL153C; YPL153C.
GeneIDi855950.
KEGGisce:YPL153C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55623 Genomic DNA. Translation: AAA35070.1.
X96770 Genomic DNA. Translation: CAA65568.1.
Z73509 Genomic DNA. Translation: CAA97858.1.
AY693009 Genomic DNA. Translation: AAT93028.1.
BK006949 Genomic DNA. Translation: DAA11281.1.
PIRiA39616.
RefSeqiNP_015172.1. NM_001183967.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DMZNMR-A573-730[»]
1FHQNMR-A573-730[»]
1FHRNMR-A573-730[»]
1G3GNMR-A1-164[»]
1G6GX-ray1.60A/B29-155[»]
1J4KNMR-A573-730[»]
1J4LNMR-A573-730[»]
1J4ONMR-A14-164[»]
1J4PNMR-A14-164[»]
1J4QNMR-A14-164[»]
1K2MNMR-A573-730[»]
1K2NNMR-A573-730[»]
1K3JNMR-A14-164[»]
1K3NNMR-A14-164[»]
1K3QNMR-A14-164[»]
1QU5NMR-A549-730[»]
2A0TNMR-A14-164[»]
2JQINMR-A14-164[»]
B3-12[»]
2JQLNMR-B3-12[»]
2YGVX-ray2.94E/F/G/H800-821[»]
4PDPX-ray2.59A/B170-512[»]
4PDSX-ray2.90A/B170-512[»]
ProteinModelPortaliP22216.
SMRiP22216. Positions 2-490, 549-730.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36030. 358 interactions.
DIPiDIP-2322N.
IntActiP22216. 14 interactions.
MINTiMINT-364105.

PTM databases

iPTMnetiP22216.

Proteomic databases

MaxQBiP22216.
PeptideAtlasiP22216.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL153C; YPL153C; YPL153C.
GeneIDi855950.
KEGGisce:YPL153C.

Organism-specific databases

EuPathDBiFungiDB:YPL153C.
SGDiS000006074. RAD53.

Phylogenomic databases

GeneTreeiENSGT00800000124190.
HOGENOMiHOG000074515.
InParanoidiP22216.
KOiK02831.
OMAiHLPFNGK.
OrthoDBiEOG7XWPXG.

Enzyme and pathway databases

BioCyciYEAST:G3O-34050-MONOMER.
BRENDAi2.7.12.1. 984.
ReactomeiR-SCE-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-SCE-69473. G2/M DNA damage checkpoint.
R-SCE-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.

Miscellaneous databases

EvolutionaryTraceiP22216.
PROiP22216.

Family and domain databases

Gene3Di2.60.200.20. 2 hits.
InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR000253. FHA_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR016256. Ser/Thr_kinase_Rad53.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 1 hit.
PfamiPF00498. FHA. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000661. Ser/Thr_PK_RAD53. 1 hit.
SMARTiSM00240. FHA. 2 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Spk1, a new kinase from Saccharomyces cerevisiae, phosphorylates proteins on serine, threonine, and tyrosine."
    Stern D.F., Zheng P., Beidler D.R., Zerillo C.
    Mol. Cell. Biol. 11:987-1001(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a small nuclear RNA, a new putative protein kinase and two new putative regulators."
    Purnelle B., Coster F., Goffeau A.
    Yeast 12:1483-1492(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204511 / S288c / AB972.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "SPK1 is an essential S-phase-specific gene of Saccharomyces cerevisiae that encodes a nuclear serine/threonine/tyrosine kinase."
    Zheng P., Fay D.S., Burton J., Xiao H., Pinkham J.L., Stern D.F.
    Mol. Cell. Biol. 13:5829-5842(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "The SAD1/RAD53 protein kinase controls multiple checkpoints and DNA damage-induced transcription in yeast."
    Allen J.B., Zhou Z., Siede W., Friedberg E.C., Elledge S.J.
    Genes Dev. 8:2401-2415(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Activation of Rad53 kinase in response to DNA damage and its effect in modulating phosphorylation of the lagging strand DNA polymerase."
    Pellicioli A., Lucca C., Liberi G., Marini F., Lopes M., Plevani P., Romano A., Di Fiore P.P., Foiani M.
    EMBO J. 18:6561-6572(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  9. "Control of the DNA damage checkpoint by chk1 and rad53 protein kinases through distinct mechanisms."
    Sanchez Y., Bachant J., Wang H., Hu F., Liu D., Tetzlaff M., Elledge S.J.
    Science 286:1166-1171(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Phosphorylation of Rph1, a damage-responsive repressor of PHR1 in Saccharomyces cerevisiae, is dependent upon Rad53 kinase."
    Kim E.M., Jang Y.K., Park S.D.
    Nucleic Acids Res. 30:643-648(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF RPH1.
  11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  12. "Mdt1, a novel Rad53 FHA1 domain-interacting protein, modulates DNA damage tolerance and G(2)/M cell cycle progression in Saccharomyces cerevisiae."
    Pike B.L., Yongkiettrakul S., Tsai M.-D., Heierhorst J.
    Mol. Cell. Biol. 24:2779-2788(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PIN4.
  13. "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].
  14. "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-24; SER-175; SER-547; SER-560; SER-774 AND SER-793, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-774, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Structure and function of a new phosphopeptide-binding domain containing the FHA2 of Rad53."
    Liao H., Byeon I.-J.L., Tsai M.-D.
    J. Mol. Biol. 294:1041-1049(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 573-730.
  18. "Structure of the FHA1 domain of yeast Rad53 and identification of binding sites for both FHA1 and its target protein Rad9."
    Liao H., Yuan C., Su M.I., Yongkiettrakul S., Qin D., Li H., Byeon I.J., Pei D., Tsai M.D.
    J. Mol. Biol. 304:941-951(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 2-164.
  19. "The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms."
    Durocher D., Taylor I.A., Sarbassova D., Haire L.F., Westcott S.L., Jackson S.P., Smerdon S.J., Yaffe M.B.
    Mol. Cell 6:1169-1182(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 29-155.

Entry informationi

Entry nameiRAD53_YEAST
AccessioniPrimary (citable) accession number: P22216
Secondary accession number(s): D6W3L5, Q6B1S1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: June 8, 2016
This is version 184 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 6900 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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.