DUS3_YEAST - dbPTM
DUS3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DUS3_YEAST
UniProt AC Q06053
Protein Name tRNA-dihydrouridine(47) synthase [NAD(P)(+)]
Gene Name DUS3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 668
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Specifically modifies U47 in cytoplasmic tRNAs..
Protein Sequence MEQNAEKRSIVGDDNSTVKRQDTSPSKGIAHIKPEYIVPLKQNENQKVAIYDEEMSSDRMTNEFAGGTNKKNKNGRGKKRGQNKNRDNRQVKEQNVLCPRLIHGDISKCSFGDNCRFVHDINLYLSTKKPEVESNIFPSCPVFNSLGFCPMGFKCRFLSSHLNKEDNILISKKEIDPDAQTIWSVKGEVNHISPERKLDLIKRRFPFTKSNEILEIIDSFQQECRDSMKPEEEVESTPQLKKQDPDVEQPVAPQVEQRNKELSEHRMKQREVYLKYKDTRYFAQEKKPLDLYHKKIVSPLTTVGNLPYRRLMRKLGADVTYSEMALAVPLIQGTNSEWALPKAHTSEFPGFGVQVACSKAWQAAKAAEALANSVSEISEINLNSGCPIDLLYRQGSGSALLDNPARMIRCLNAMNYVSKDIPITVKIRTGTKEGHPIAEGLVKRLVNETDVAAITLHGRSRQQRYTKSADWDYVSQVADTLRSAEADFIETEQGKEGRDSKNRIQFVGNGDVNNFEDWYRYLNGNENIDSVMVARGALIKPWIFEEVESQQYLDKTSTERLDILRDYAQFSMEHWGTDEYGISQCRRFFCEFMSFFHRYVPMGICERYPVKLNERPPNWCGRDELETLMGSTDVNDWIKLSDLFFGKTDENFVFVPKHKSSSYANRDS
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
7Acetylation-MEQNAEKRSIVGDD
-CCCCHHHCCCCCCC		49.3825381059
9PhosphorylationEQNAEKRSIVGDDNS
CCCHHHCCCCCCCCC		32.4722369663
16PhosphorylationSIVGDDNSTVKRQDT
CCCCCCCCCCCCCCC		41.3922369663
17PhosphorylationIVGDDNSTVKRQDTS
CCCCCCCCCCCCCCC		35.9822369663
23PhosphorylationSTVKRQDTSPSKGIA
CCCCCCCCCCCCCCC		33.9128889911
24PhosphorylationTVKRQDTSPSKGIAH
CCCCCCCCCCCCCCC		35.1525752575
26PhosphorylationKRQDTSPSKGIAHIK
CCCCCCCCCCCCCCC		43.1928889911
33AcetylationSKGIAHIKPEYIVPL
CCCCCCCCCCCEEEC		23.1724489116
56PhosphorylationAIYDEEMSSDRMTNE
EEEECCCCCCHHCCC		32.1630377154
57PhosphorylationIYDEEMSSDRMTNEF
EEECCCCCCHHCCCC		28.1128889911
171PhosphorylationKEDNILISKKEIDPD
CCCCEEEECCCCCCC		33.9419795423
173AcetylationDNILISKKEIDPDAQ
CCEEEECCCCCCCCC		53.7824489116
193PhosphorylationKGEVNHISPERKLDL
ECCCCCCCHHHHHHH		17.1028889911
227PhosphorylationFQQECRDSMKPEEEV
HHHHHHHCCCHHHHH		14.8926447709
229AcetylationQECRDSMKPEEEVES
HHHHHCCCHHHHHCC		53.9124489116
236PhosphorylationKPEEEVESTPQLKKQ
CHHHHHCCCCCHHCC		51.0322369663
237PhosphorylationPEEEVESTPQLKKQD
HHHHHCCCCCHHCCC		11.1022369663
241AcetylationVESTPQLKKQDPDVE
HCCCCCHHCCCCCCC		43.0425381059
242UbiquitinationESTPQLKKQDPDVEQ
CCCCCHHCCCCCCCC		69.4023749301
396PhosphorylationDLLYRQGSGSALLDN
CEEEECCCCCHHCCC		22.6427017623
398PhosphorylationLYRQGSGSALLDNPA
EEECCCCCHHCCCHH		19.9027017623
468PhosphorylationRQQRYTKSADWDYVS
HHHHHCCCCCHHHHH		24.5427017623
657AcetylationENFVFVPKHKSSSYA
CCEEEEECCCCCCCC		59.3624489116
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 DUS3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DUS3_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 DUS3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HIS5_YEASTHIS7physical
16554755
MET22_YEASTMET22genetic
18443146
PAP2_YEASTPAP2genetic
18443146
RRP6_YEASTRRP6genetic
18443146
UGA4_YEASTUGA4genetic
19061648
POP8_YEASTPOP8genetic
19061648
PUS1_YEASTPUS1genetic
19061648
EFM7_YEASTNNT1genetic
19061648
HIR2_YEASTHIR2genetic
19061648
ITT1_YEASTITT1genetic
19061648
TREA_YEASTNTH1genetic
27708008
ARO1_YEASTARO1genetic
27708008
LIS1_YEASTPAC1genetic
27708008
SYH1_YEASTSYH1genetic
27708008
PUS1_YEASTPUS1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DUS3_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-193 AND THR-237, ANDMASS SPECTROMETRY.

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