RIR3_YEAST - dbPTM
RIR3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RIR3_YEAST
UniProt AC P21672
Protein Name Ribonucleoside-diphosphate reductase large chain 2
Gene Name RNR3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 869
Subcellular Localization Cytoplasm .
Protein Description Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides..
Protein Sequence MYVIKRDGRKEPVQFDKITSRITRLSYGLDPNRIDAVKVTQRIISGVYSGVTTVELDNLAAETCAYMTTVHPDYATLAARIAISNLHKQTTKQFSKVIEDLHDWINPATGKHAPMISDEIYNIVMENKDTLNSAIVYDRDFQYTYFGFKTLERSYLLRLNGEVAERPQHLVMRVALGIHGSDIESVLKTYNLMSLRYFTHASPTLFNAGTPHPQMSSCFLIAMKDDSIEGIYDTLKECAMISKTAGGVGLHINNIRSTGSYIAGTNGTSNGLIPMIRVFNNTARYVDQGGNKRPGAFALFLEPWHADIFDFVDIRKTHGKEEIRARDLFPALWIPDLFMKRVQEDGPWTLFSPSAAPGLDDVWGDEFEELYTRYEREGRGKTIKAQKLWYAILQAQTETGTPFMVYKDACNRKTNQQNLGTIKSSNLCCEIVEYSSPDETAVCNLASIALPAFVEVSEDGKTASYNFERLHEIAKVITHNLNRVIDRNYYPVPEARNSNMKHRPIALGVQGLADTYMMLRLPFESEEAQTLNKQIFETIYHATLEASCELAQKEGKYSTFEGSPASKGILQFDMWNAKPFGMWDWETLRKDIVKHGLRNSLTMAPMPTASTSQILGYNECFEPVTSNMYSRRVLSGEFQVVNPYLLRDLVDLGIWDDSMKQYLITQNGSIQGLPNVPQELKELYKTVWEISQKTIINMAADRAIYIDQSHSLNLFLQAPSMGKITSMHFYGWKKGLKTGMYYLRTQAASAAIQFTIDQEVADQAATHIASVSELDRPVYVPKGTKFSEQKAASALTESSDNEKDASPVPSEQSSVSSAMSNVKLEDSVAPAVPTETIKEDSDEKKCDIYNEKVIACTAPTPEACESCSG
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
10UbiquitinationVIKRDGRKEPVQFDK
EECCCCCCCCCCHHH
72.4123749301
17UbiquitinationKEPVQFDKITSRITR
CCCCCHHHHHHHHHH
49.5317644757
154PhosphorylationGFKTLERSYLLRLNG
EEEECCHHHHHHHCC
15.6826447709
155PhosphorylationFKTLERSYLLRLNGE
EEECCHHHHHHHCCC
18.9026447709
227PhosphorylationLIAMKDDSIEGIYDT
EEEECCCCHHHHHHH
32.45-
269PhosphorylationIAGTNGTSNGLIPMI
EECCCCCCCCEEEEE
30.2328132839
489PhosphorylationNRVIDRNYYPVPEAR
HHHCCCCCCCCCCCC
15.2727017623
563PhosphorylationKYSTFEGSPASKGIL
CCCCCCCCCCCCCEE
15.3024930733
566PhosphorylationTFEGSPASKGILQFD
CCCCCCCCCCEEEEE
34.5024930733
635PhosphorylationMYSRRVLSGEFQVVN
CCCCCCCCCCCEEEC
33.1622369663
658PhosphorylationDLGIWDDSMKQYLIT
HHCCCCHHHHHEEEC
25.9630377154
793PhosphorylationFSEQKAASALTESSD
CCHHHHHHHHHCCCC
28.7719779198
796PhosphorylationQKAASALTESSDNEK
HHHHHHHHCCCCCCC
33.2719779198
798PhosphorylationAASALTESSDNEKDA
HHHHHHCCCCCCCCC
37.4422369663
799PhosphorylationASALTESSDNEKDAS
HHHHHCCCCCCCCCC
37.9222369663
806PhosphorylationSDNEKDASPVPSEQS
CCCCCCCCCCCCHHH
36.2425521595
810PhosphorylationKDASPVPSEQSSVSS
CCCCCCCCHHHHHHH
48.8028889911
817PhosphorylationSEQSSVSSAMSNVKL
CHHHHHHHHHHCCCC
26.3227017623
820PhosphorylationSSVSSAMSNVKLEDS
HHHHHHHHCCCCCCC
37.8827017623
827PhosphorylationSNVKLEDSVAPAVPT
HCCCCCCCCCCCCCC
15.7122369663
834PhosphorylationSVAPAVPTETIKEDS
CCCCCCCCCCCCCCC
38.8822369663
836PhosphorylationAPAVPTETIKEDSDE
CCCCCCCCCCCCCCC
39.5722369663
841PhosphorylationTETIKEDSDEKKCDI
CCCCCCCCCCCCCCC
49.0822369663
849PhosphorylationDEKKCDIYNEKVIAC
CCCCCCCCCCEEEEE
12.2019779198
860PhosphorylationVIACTAPTPEACESC
EEEEECCCHHHHHHC
31.1527017623
866PhosphorylationPTPEACESCSG----
CCHHHHHHCCC----
17.2928889911
868PhosphorylationPEACESCSG------
HHHHHHCCC------
57.7428889911

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of RIR3_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RIR3_YEAST !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of RIR3_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CBS_YEASTCYS4physical
11805837
RNQ1_YEASTRNQ1physical
11805837
RIR1_YEASTRNR1physical
11805837
ARP2_YEASTARP2physical
11805837
H2B1_YEASTHTB1physical
11805837
RPN12_YEASTRPN12physical
11805837
YNN4_YEASTYNL134Cphysical
11805837
RPN9_YEASTRPN9physical
11805837
MKT1_YEASTMKT1physical
11805837
MPPB_YEASTMAS1physical
11805837
MPPA_YEASTMAS2physical
11805837
SML1_YEASTSML1physical
11074005
RIR3_YEASTRNR3physical
11893751
MSH1_YEASTMSH1genetic
17314980
MED3_YEASTPGD1genetic
17314980
CG21_YEASTCLB1genetic
17314980
RIR1_YEASTRNR1genetic
18408719
SWD1_YEASTSWD1genetic
27708008
YAJ9_YEASTYAR029Wgenetic
27708008
PLPHP_YEASTYBL036Cgenetic
27708008
MUM2_YEASTMUM2genetic
27708008
CHK1_YEASTCHK1genetic
27708008
FRM2_YEASTFRM2genetic
27708008
STE50_YEASTSTE50genetic
27708008
NHP10_YEASTNHP10genetic
27708008
THI3_YEASTTHI3genetic
27708008
SNF1_YEASTSNF1genetic
27708008
ITC1_YEASTITC1genetic
27708008
VAM7_YEASTVAM7genetic
27708008
AP3B_YEASTAPL6genetic
27708008
MOG1_YEASTMOG1genetic
27708008
ILM1_YEASTILM1genetic
27708008
SMF3_YEASTSMF3genetic
27708008
METK1_YEASTSAM1genetic
27708008
RAD14_YEASTRAD14genetic
27708008
COQ2_YEASTCOQ2genetic
27708008
INO4_YEASTINO4genetic
27708008
REV1_YEASTREV1genetic
27708008
RL21B_YEASTRPL21Bgenetic
27708008
ARP8_YEASTARP8genetic
27453043
SERB_YEASTSER2genetic
27453043
DOM34_YEASTDOM34genetic
27453043
PALA_YEASTRIM20genetic
27453043
PRR2_YEASTPRR2genetic
27453043
OAC1_YEASTOAC1genetic
27453043
KPR4_YEASTPRS4genetic
27453043
ARA1_YEASTARA1genetic
27453043
SNF2_YEASTSNF2genetic
27453043
YIM1_YEASTYIM1genetic
27453043
ALDH3_YEASTALD3genetic
27453043
MBP1_YEASTMBP1genetic
27453043
MUP3_YEASTMUP3genetic
27453043
RS10A_YEASTRPS10Agenetic
27453043
DCAM_YEASTSPE2genetic
27453043
DCOR_YEASTSPE1genetic
27453043
SYFM_YEASTMSF1genetic
27453043
VPS71_YEASTVPS71genetic
27453043

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RIR3_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-799; SER-806; SER-810;SER-866 AND SER-868, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-806, AND MASSSPECTROMETRY.

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