RIR4_YEAST - dbPTM
RIR4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RIR4_YEAST
UniProt AC P49723
Protein Name Ribonucleoside-diphosphate reductase small chain 2
Gene Name RNR4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 345
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. RNR4 is required for proper folding of RNR2 and assembly with the large subunits..
Protein Sequence MEAHNQFLKTFQKERHDMKEAEKDEILLMENSRRFVMFPIKYHEIWAAYKKVEASFWTAEEIELAKDTEDFQKLTDDQKTYIGNLLALSISSDNLVNKYLIENFSAQLQNPEGKSFYGFQIMMENIYSEVYSMMVDAFFKDPKNIPLFKEIANLPEVKHKAAFIERWISNDDSLYAERLVAFAAKEGIFQAGNYASMFWLTDKKIMPGLAMANRNICRDRGAYTDFSCLLFAHLRTKPNPKIIEKIITEAVEIEKEYYSNSLPVEKFGMDLKSIHTYIEFVADGLLQGFGNEKYYNAVNPFEFMEDVATAGKTTFFEKKVSDYQKASDMSKSATPSKEINFDDDF
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
1Acetylation-------MEAHNQFL
-------CHHHHHHH		10.4222814378
9AcetylationEAHNQFLKTFQKERH
HHHHHHHHHHHHHHH		48.8924489116
9SuccinylationEAHNQFLKTFQKERH
HHHHHHHHHHHHHHH		48.8923954790
19AcetylationQKERHDMKEAEKDEI
HHHHHCCHHHHHCCE		60.8824489116
23SuccinylationHDMKEAEKDEILLME
HCCHHHHHCCEEEEE		68.6523954790
23AcetylationHDMKEAEKDEILLME
HCCHHHHHCCEEEEE		68.6524489116
32PhosphorylationEILLMENSRRFVMFP
CEEEEECCCCEEEEE		16.1328889911
41AcetylationRFVMFPIKYHEIWAA
CEEEEEECHHHHHHH		40.5724489116
50AcetylationHEIWAAYKKVEASFW
HHHHHHHHHHHHHCC		45.6924489116
50UbiquitinationHEIWAAYKKVEASFW
HHHHHHHHHHHHHCC		45.6923749301
51UbiquitinationEIWAAYKKVEASFWT
HHHHHHHHHHHHCCC		32.4122817900
55PhosphorylationAYKKVEASFWTAEEI
HHHHHHHHCCCHHHH		14.0717287358
73AcetylationKDTEDFQKLTDDQKT
CCCHHHHHCCCCCHH		54.0424489116
73SuccinylationKDTEDFQKLTDDQKT
CCCHHHHHCCCCCHH		54.0423954790
80PhosphorylationKLTDDQKTYIGNLLA
HCCCCCHHHHHHHHH		18.1021126336
81PhosphorylationLTDDQKTYIGNLLAL
CCCCCHHHHHHHHHH		17.5421126336
91PhosphorylationNLLALSISSDNLVNK
HHHHHHCCCCCHHHH		28.4128889911
99PhosphorylationSDNLVNKYLIENFSA
CCCHHHHHHHHHHHH		14.0127017623
143AcetylationDAFFKDPKNIPLFKE
HHHCCCCCCCCHHHH		77.1022865919
143SuccinylationDAFFKDPKNIPLFKE
HHHCCCCCCCCHHHH		77.1023954790
149SuccinylationPKNIPLFKEIANLPE
CCCCCHHHHHHCCHH		56.7623954790
149AcetylationPKNIPLFKEIANLPE
CCCCCHHHHHHCCHH		56.7624489116
158UbiquitinationIANLPEVKHKAAFIE
HHCCHHHHHHHHHHH		37.4122817900
158AcetylationIANLPEVKHKAAFIE
HHCCHHHHHHHHHHH		37.4124489116
160UbiquitinationNLPEVKHKAAFIERW
CCHHHHHHHHHHHHH		35.3722817900
169PhosphorylationAFIERWISNDDSLYA
HHHHHHHCCCCCHHH		27.5217287358
258PhosphorylationVEIEKEYYSNSLPVE
HHHHHHHHHCCCCHH		11.5027017623
266AcetylationSNSLPVEKFGMDLKS
HCCCCHHHHCCCHHH		47.6724489116
318UbiquitinationGKTTFFEKKVSDYQK
CCEEEEEEHHCHHHH		54.0023749301
321PhosphorylationTFFEKKVSDYQKASD
EEEEEHHCHHHHHHH		39.2119823750
323PhosphorylationFEKKVSDYQKASDMS
EEEHHCHHHHHHHCC		12.3827017623
325AcetylationKKVSDYQKASDMSKS
EHHCHHHHHHHCCCC		43.5622865919
325UbiquitinationKKVSDYQKASDMSKS
EHHCHHHHHHHCCCC		43.5623749301
327PhosphorylationVSDYQKASDMSKSAT
HCHHHHHHHCCCCCC		40.6625005228
330PhosphorylationYQKASDMSKSATPSK
HHHHHHCCCCCCCCC		28.5721082442
331UbiquitinationQKASDMSKSATPSKE
HHHHHCCCCCCCCCC		37.1623749301
331AcetylationQKASDMSKSATPSKE
HHHHHCCCCCCCCCC		37.1624489116
332PhosphorylationKASDMSKSATPSKEI
HHHHCCCCCCCCCCC		30.0222369663
334PhosphorylationSDMSKSATPSKEINF
HHCCCCCCCCCCCCC		34.8822369663
336PhosphorylationMSKSATPSKEINFDD
CCCCCCCCCCCCCCC		38.2722369663
337UbiquitinationSKSATPSKEINFDDD
CCCCCCCCCCCCCCC		64.9123749301
337AcetylationSKSATPSKEINFDDD
CCCCCCCCCCCCCCC		64.9125381059
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 RIR4_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RIR4_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 RIR4_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RIR2_YEASTRNR2physical
9315670
RIR4_YEASTRNR4physical
15196016
RIR1_YEASTRNR1genetic
9315670
RIR3_YEASTRNR3genetic
9315670
RAD53_YEASTRAD53genetic
9315670
UBC2_YEASTRAD6physical
16554755
RIR2_YEASTRNR2physical
16554755
IMB1_YEASTKAP95physical
16554755
IMA1_YEASTSRP1physical
16554755
YP191_YEASTYPL191Cphysical
16554755
RIR2_YEASTRNR2physical
16429126
RIR2_YEASTRNR2physical
16489218
KA122_YEASTKAP122physical
16432237
WTM1_YEASTWTM1physical
16432237
RAD18_YEASTRAD18genetic
18400565
WTM2_YEASTWTM2physical
18719252
WTM1_YEASTWTM1physical
18719252
DIF1_YEASTDIF1physical
18851834
RIR2_YEASTRNR2physical
11526232
RIR4_YEASTRNR4physical
11526232
SRS2_YEASTSRS2genetic
21459050
DRE2_YEASTDRE2genetic
21931161
CTH1_YEASTCTH1physical
22152479
CTH2_YEASTTIS11physical
22152479
NDOR1_YEASTTAH18genetic
24733891
DBF4_YEASTDBF4genetic
27708008
PDC2_YEASTPDC2genetic
27708008
TCPZ_YEASTCCT6genetic
27708008
GPI17_YEASTGPI17genetic
27708008
HSP77_YEASTSSC1genetic
27708008
CBF3B_YEASTCEP3genetic
27708008
LST8_YEASTLST8genetic
27708008
SEC63_YEASTSEC63genetic
27708008
IPL1_YEASTIPL1genetic
27708008
VPS71_YEASTVPS71genetic
27708008
RFA1_YEASTRFA1genetic
27708008
SYIC_YEASTILS1genetic
27708008
PRP6_YEASTPRP6genetic
27708008
TSC3_YEASTTSC3genetic
27708008
MCM7_YEASTMCM7genetic
27708008
TRS20_YEASTTRS20genetic
27708008
APC11_YEASTAPC11genetic
27708008
TECR_YEASTTSC13genetic
27708008
DPOD_YEASTPOL3genetic
27708008
UAP1_YEASTQRI1genetic
27708008
NSE4_YEASTNSE4genetic
27708008
DAD1_YEASTDAD1genetic
27708008
SLU7_YEASTSLU7genetic
27708008
SECU_YEASTPDS1genetic
27708008
SMT3_YEASTSMT3genetic
27708008
PSB3_YEASTPUP3genetic
27708008
COG3_YEASTCOG3genetic
27708008
CDC4_YEASTCDC4genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ACT_YEASTACT1genetic
27708008
RPN11_YEASTRPN11genetic
27708008
PSB7_YEASTPRE4genetic
27708008
PRS8_YEASTRPT6genetic
27708008
CDC20_YEASTCDC20genetic
27708008
CDC23_YEASTCDC23genetic
27708008
STS1_YEASTSTS1genetic
27708008
RPC9_YEASTRPC17genetic
27708008
ESS1_YEASTESS1genetic
27708008
NUP85_YEASTNUP85genetic
27708008
KTHY_YEASTCDC8genetic
27708008
CDC11_YEASTCDC11genetic
27708008
CDC16_YEASTCDC16genetic
27708008
TOR2_YEASTTOR2genetic
27708008
BET3_YEASTBET3genetic
27708008
NSE1_YEASTNSE1genetic
27708008
MED14_YEASTRGR1genetic
27708008
SEC22_YEASTSEC22genetic
27708008
TAD3_YEASTTAD3genetic
27708008
TAF11_YEASTTAF11genetic
27708008
ERB1_YEASTERB1genetic
27708008
NOP2_YEASTNOP2genetic
27708008
RPC6_YEASTRPC34genetic
27708008
BRX1_YEASTBRX1genetic
27708008
MED7_YEASTMED7genetic
27708008
TYSY_YEASTCDC21genetic
27708008
PROF_YEASTPFY1genetic
27708008
CLP1_YEASTCLP1genetic
27708008
PRS10_YEASTRPT4genetic
27708008
RRS1_YEASTRRS1genetic
27708008
SEC16_YEASTSEC16genetic
27708008
IF6_YEASTTIF6genetic
27708008
SEC8_YEASTSEC8genetic
27708008
TF2B_YEASTSUA7genetic
27708008
SRP54_YEASTSRP54genetic
27708008
RDS3_YEASTRDS3genetic
27708008
PSB5_YEASTPRE2genetic
27708008
BUD31_YEASTBUD31genetic
27708008
CSM1_YEASTCSM1genetic
27708008
NHP10_YEASTNHP10genetic
27708008
PP2C1_YEASTPTC1genetic
27708008
GET2_YEASTGET2genetic
27708008
UBP6_YEASTUBP6genetic
27708008
KA122_YEASTKAP122genetic
27708008
GET1_YEASTGET1genetic
27708008
RAD54_YEASTRAD54genetic
27708008
ATC1_YEASTPMR1genetic
27708008
HUR1_YEASTHUR1genetic
27708008
RIR3_YEASTRNR3genetic
27708008
IMPX_YEASTIMP2genetic
27708008
YJC7_YEASTYJL027Cgenetic
27708008
RPA34_YEASTRPA34genetic
27708008
DPOD3_YEASTPOL32genetic
27708008
ELM1_YEASTELM1genetic
27708008
SFK1_YEASTSFK1genetic
27708008
FRMSR_YEASTYKL069Wgenetic
27708008
DBP7_YEASTDBP7genetic
27708008
NU133_YEASTNUP133genetic
27708008
RL8B_YEASTRPL8Bgenetic
27708008
RAD5_YEASTRAD5genetic
27708008
ALAM_YEASTALT1genetic
27708008
AHP1_YEASTAHP1genetic
27708008
SRN2_YEASTSRN2genetic
27708008
UPS2_YEASTUPS2genetic
27708008
TOP3_YEASTTOP3genetic
27708008
SST2_YEASTSST2genetic
27708008
TSA1_YEASTTSA1genetic
27708008
RAD52_YEASTRAD52genetic
27708008
MAC1_YEASTMAC1genetic
27708008
SGS1_YEASTSGS1genetic
27708008
PUB1_YEASTPUB1genetic
27708008
2A5D_YEASTRTS1genetic
27708008
DIA2_YEASTDIA2genetic
27708008
WTM2_YEASTWTM2genetic
27708008
RMI1_YEASTRMI1genetic
27708008
UBA3_YEASTUBA3genetic
27708008
MED1_YEASTMED1genetic
27708008
UBC9_HUMANUBE2Iphysical
27107014
RNF41_HUMANRNF41physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RIR4_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-91; SER-169; SER-330;SER-332; THR-334 AND SER-336, 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-55 AND SER-169, AND MASSSPECTROMETRY.
"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 THR-334, 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 THR-334, AND MASSSPECTROMETRY.

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