RIR2_YEAST - dbPTM
RIR2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RIR2_YEAST
UniProt AC P09938
Protein Name Ribonucleoside-diphosphate reductase small chain 1
Gene Name RNR2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 399
Subcellular Localization Nucleus . Found predominantly in the nucleus under normal growth conditions and is redistributed to the cytoplasm in damaged cells in a DNA replication and damage checkpoint-dependent manner. Nuclear localization is mediated by DIF1.
Protein Description Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. RNR2 provides the diiron-tyrosyl radical center..
Protein Sequence MPKETPSKAAADALSDLEIKDSKSNLNKELETLREENRVKSDMLKEKLSKDAENHKAYLKSHQVHRHKLKEMEKEEPLLNEDKERTVLFPIKYHEIWQAYKRAEASFWTAEEIDLSKDIHDWNNRMNENERFFISRVLAFFAASDGIVNENLVENFSTEVQIPEAKSFYGFQIMIENIHSETYSLLIDTYIKDPKESEFLFNAIHTIPEIGEKAEWALRWIQDADALFGERLVAFASIEGVFFSGSFASIFWLKKRGMMPGLTFSNELICRDEGLHTDFACLLFAHLKNKPDPAIVEKIVTEAVEIEQRYFLDALPVALLGMNADLMNQYVEFVADRLLVAFGNKKYYKVENPFDFMENISLAGKTNFFEKRVSDYQKAGVMSKSTKQEAGAFTFNEDF
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
5Phosphorylation---MPKETPSKAAAD
---CCCCCCCHHHHH		38.7024909858
7Phosphorylation-MPKETPSKAAADAL
-CCCCCCCHHHHHHH		42.2024909858
8AcetylationMPKETPSKAAADALS
CCCCCCCHHHHHHHH		43.1624489116
15PhosphorylationKAAADALSDLEIKDS
HHHHHHHHHCCCCCC		41.7022369663
20UbiquitinationALSDLEIKDSKSNLN
HHHHCCCCCCCCHHH		46.7223749301
20AcetylationALSDLEIKDSKSNLN
HHHHCCCCCCCCHHH		46.7224489116
20SuccinylationALSDLEIKDSKSNLN
HHHHCCCCCCCCHHH		46.7223954790
22PhosphorylationSDLEIKDSKSNLNKE
HHCCCCCCCCHHHHH		32.7422369663
232-HydroxyisobutyrylationDLEIKDSKSNLNKEL
HCCCCCCCCHHHHHH		54.20-
24PhosphorylationLEIKDSKSNLNKELE
CCCCCCCCHHHHHHH		50.9621082442
28UbiquitinationDSKSNLNKELETLRE
CCCCHHHHHHHHHHH		67.8324961812
28AcetylationDSKSNLNKELETLRE
CCCCHHHHHHHHHHH		67.8324489116
32PhosphorylationNLNKELETLREENRV
HHHHHHHHHHHHHHH		43.6821440633
402-HydroxyisobutyrylationLREENRVKSDMLKEK
HHHHHHHCHHHHHHH		37.18-
41PhosphorylationREENRVKSDMLKEKL
HHHHHHCHHHHHHHH		25.9517287358
50SuccinylationMLKEKLSKDAENHKA
HHHHHHHCHHHHHHH		71.9723954790
502-HydroxyisobutyrylationMLKEKLSKDAENHKA
HHHHHHHCHHHHHHH		71.97-
74SuccinylationHKLKEMEKEEPLLNE
HHHHHHHHHCCCCCC		67.1023954790
74AcetylationHKLKEMEKEEPLLNE
HHHHHHHHHCCCCCC		67.1024489116
83AcetylationEPLLNEDKERTVLFP
CCCCCCCCCCEEEEE		42.8124489116
92AcetylationRTVLFPIKYHEIWQA
CEEEEEEEHHHHHHH		40.5724489116
92UbiquitinationRTVLFPIKYHEIWQA
CEEEEEEEHHHHHHH		40.5723749301
101UbiquitinationHEIWQAYKRAEASFW
HHHHHHHHHHHHHCC		48.4223749301
290UbiquitinationLFAHLKNKPDPAIVE
HHHHHCCCCCHHHHH		49.5723749301
298AcetylationPDPAIVEKIVTEAVE
CCHHHHHHHHHHHHH		31.4224489116
345AcetylationLLVAFGNKKYYKVEN
HHHHCCCCCEEEECC		42.4024489116
349AcetylationFGNKKYYKVENPFDF
CCCCCEEEECCCHHH		39.7324489116
371UbiquitinationGKTNFFEKRVSDYQK
CCCCHHHHHHHHHHH		53.6023749301
3712-HydroxyisobutyrylationGKTNFFEKRVSDYQK
CCCCHHHHHHHHHHH		53.60-
374PhosphorylationNFFEKRVSDYQKAGV
CHHHHHHHHHHHHCC		34.3317563356
378AcetylationKRVSDYQKAGVMSKS
HHHHHHHHHCCCCCC		40.6625381059
378UbiquitinationKRVSDYQKAGVMSKS
HHHHHHHHHCCCCCC		40.6623749301
384UbiquitinationQKAGVMSKSTKQEAG
HHHCCCCCCCCCCCC		44.0123749301
385PhosphorylationKAGVMSKSTKQEAGA
HHCCCCCCCCCCCCC		33.2619779198
386PhosphorylationAGVMSKSTKQEAGAF
HCCCCCCCCCCCCCC		40.2527017623
387UbiquitinationGVMSKSTKQEAGAFT
CCCCCCCCCCCCCCC		53.9123749301
394PhosphorylationKQEAGAFTFNEDF--
CCCCCCCCCCCCC--		25.6428889911
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
-KUbiquitinationE3 ubiquitin ligaseRSP5P39940
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RIR2_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 RIR2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RIR2_YEASTRNR2physical
9774971
RIR4_YEASTRNR4physical
10716984
RIR2_YEASTRNR2physical
15196016
RFX1_YEASTRFX1genetic
9741624
IF4E_YEASTCDC33genetic
10585489
RIR4_YEASTRNR4physical
16429126
SMC1_YEASTSMC1physical
16429126
RIR4_YEASTRNR4physical
10535923
RIR4_YEASTRNR4physical
16489218
KA122_YEASTKAP122physical
16432237
RIR4_YEASTRNR4physical
16432237
WTM1_YEASTWTM1physical
16432237
WTM2_YEASTWTM2physical
16432237
DIF1_YEASTDIF1physical
18851834
RIR2_YEASTRNR2physical
11526232
RIR4_YEASTRNR4physical
11526232
RIR4_YEASTRNR4physical
20826334
ATP5E_YEASTATP15genetic
21623372
6PGD1_YEASTGND1genetic
21623372
TPS2_YEASTTPS2genetic
21623372
GGPPS_YEASTBTS1genetic
21623372
CEM1_YEASTCEM1genetic
21623372
ACON2_YEASTACO2genetic
21623372
ERG2_YEASTERG2genetic
21623372
DHOM_YEASTHOM6genetic
21623372
FABD_YEASTMCT1genetic
21623372
ACON_YEASTACO1genetic
21623372
METC_YEASTIRC7genetic
21623372
CTH1_YEASTCTH1physical
22152479
CTH2_YEASTTIS11physical
22152479
RIR4_YEASTRNR4physical
23532842
DRE2_YEASTDRE2physical
24733891
HUG1_YEASTHUG1genetic
25378334
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RIR2_YEAST

loading...

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-7; SER-15; SER-22;SER-24 AND SER-374, 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-15; SER-22 AND SER-374,AND MASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASSSPECTROMETRY.
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory