RIR1_DROME - dbPTM
RIR1_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RIR1_DROME
UniProt AC P48591
Protein Name Ribonucleoside-diphosphate reductase large subunit
Gene Name RnrL
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 812
Subcellular Localization
Protein Description Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides..
Protein Sequence MLKNKSMKTSKLYVIKRDGRQEEVHFDKITSRIQKLCYNLNMDFVDPVTITLQVINGLYCGVTTQELDNLAAEIAAGLTCNHPDYAILAARIAVSNLHKETKKAFSDVFEDLYNHVNKETNQKVPLVSEFHYNVVKKNATRLNSSIIYDRDFGYNYFGFKTLERSYLLKRNGKIAERPQHMLMRVAIGIHGEDIDAAVETYNLLSERYFTHASPTLFAAATNRPQLSSCFLLTMTADSIEGIFKSVEQCAMISKSAGGIGLNVHCIRAKGTSICGTNGTSNGLVPMLRVFNNVARYVDQGGGKRPGAFAIYLEPWHSDVFEFLELKKNTGKEENRARDLFYALWIPDLFMKRVEANGDWSLMCPHKCPGLHDVWGDEFEKLYEKYEQEGRANRTVKAQSLWFAIIEAQVETGNPYMLFKDACNRKSNQQNVGTIKCSNLCTEIVEYSAPDEIAVCNLASIALNMFVTPEKTYDFKKLKEVTKIVTKNLNKIIDINYYPLPEARKSNLRHRPVGIGIQGFADALILMRFPYESEEAGLLNQQIFETIYYGALEASCELAQTEGPYETYEGSPVSKGILQYDMWDKVPTNLWDWQKLKESIRMHGVRNSLLVAPMPTASTAQIMGNNESFEPYTTNIYTRRVLSGEFQVVNHHLLRDLTELDLWDDDMKNQIISSRGSIQNIETIPPKVRDLYKTVWEISVKSTIKMAADRGAFIDQSQSFNIHVAEPNYGKLTSIHFYSWKAGLKTGMYYLRTKPAANAIQFTVNKKQGAVSMNGQNGTAEGSPQKYEEDRERKMADMVCSLENKDACMSCGS
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
11AcetylationNKSMKTSKLYVIKRD
CCCCCCCEEEEEEEC
49.4121791702
28AcetylationQEEVHFDKITSRIQK
CEEECHHHHHHHHHH
47.1121791702
642PhosphorylationIYTRRVLSGEFQVVN
EEECCCCCCCCEEEC
33.1619429919
762PhosphorylationAANAIQFTVNKKQGA
CCCEEEEEEECCCCC
13.5421082442
771PhosphorylationNKKQGAVSMNGQNGT
ECCCCCEEECCCCCC
13.1423607784
778PhosphorylationSMNGQNGTAEGSPQK
EECCCCCCCCCCHHH
29.1423607784
782PhosphorylationQNGTAEGSPQKYEED
CCCCCCCCHHHHHHH
18.7019429919
786PhosphorylationAEGSPQKYEEDRERK
CCCCHHHHHHHHHHH
21.2122817900
800PhosphorylationKMADMVCSLENKDAC
HHHHHHHHHCCHHHH
27.5822817900
812PhosphorylationDACMSCGS-------
HHHHCCCC-------
41.1818327897

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 RIR1_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RIR1_DROME !!

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 RIR1_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RIR1_DROME !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RIR1_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-778; SER-782 ANDTYR-786, AND MASS SPECTROMETRY.

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