RFC1_DROME - dbPTM
RFC1_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RFC1_DROME
UniProt AC P35600
Protein Name Replication factor C subunit 1
Gene Name Gnf1
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 986
Subcellular Localization Nucleus .
Protein Description The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins proliferating cell nuclear antigen (PCNA) and activator 1. This subunit binds to the primer-template junction (By similarity)..
Protein Sequence MQRGIDSFFKRLPAKAKSAEAENGETPSKAPKRRKAVIISSDEDEVVSPPETKKRKASKTASSEDDVVAATPEPIAKKARNGQKPALSKLKRHVDPTELFGGETKRVIVPKPKTKAVLEFENEDIDRSLMEVDLDESIKEAAPEKKVHSITRSSPSPKRAKNSSPEPPKPKSTKSKATTPRVKKEKPAADLESSVLTDEERHERKRASAVLYQKYKNRSSCLNPGSKEIPKGSPDCLSGLTFVVTGVLESMEREEAESVIKEYGGKVMTVVGKKLKYLVVGEEAGPKKLAVAEELNIPILSEDGLFDLIREKSGIAKQVKEEKKSPKKEHSSEEKGKKEVKTSRRSSDKKEKEATKLKYGEKHDIAKHKVKEEHTSPKETKDKLNDVPAVTLKVKKEPSSQKEHPPSPRTADLKTLDVVGMAWVDKHKPTSIKEIVGQAGAASNVTKLMNWLSKWYVNHDGNKKPQRPNPWAKNDDGSFYKAALLSGPPGIGKTTTATLVVKELGFDAVEFNASDTRSKRLLKDEVSTLLSNKSLSGYFTGQGQAVSRKHVLIMDEVDGMAGNEDRGGMQELIALIKDSSIPIICMCNDRNHPKIRSLVNYCYDLRFQRPRLEQIKGKIMSICFKEKVKISPAKVEEIIAATNNDIRQSINHIALLSAKEDASQKSGQQVATKDLKLGPWEVVRKVFTADEHKHMSFADKSDLFFHDYSLAPLFVQQNYLQVLPQGNKKDVLAKVAATADALSLGDLVEKRIRANSAWSLLPTQAFFSSVLPGEHMCGHFTGQINFPGWLGKNSKSGKRARLAQELHDHTRVCTSGSRLSVRLDYAPFLLDNIVRPLAKDGQEGVPAALDVMKDYHLLREDLDSLVELTSWPGKKSPLDAVDGRVKAALTRSYNKEVMAYSYSAQAGIKKKKSEAAGADDDYLDEGPGEEDGAGGHLSSEEDEDKDNLELDSLIKAKKRTTTSKASGGSKKATSSTASKSKAKAKK
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
7Phosphorylation-MQRGIDSFFKRLPA
-CCCCHHHHHHHCCH		30.5722817900
10AcetylationRGIDSFFKRLPAKAK
CCHHHHHHHCCHHHH		51.5221791702
17AcetylationKRLPAKAKSAEAENG
HHCCHHHHHHHHHCC		49.8721791702
18PhosphorylationRLPAKAKSAEAENGE
HCCHHHHHHHHHCCC		35.8822817900
26PhosphorylationAEAENGETPSKAPKR
HHHHCCCCCCCCCCC		33.9728490779
28PhosphorylationAENGETPSKAPKRRK
HHCCCCCCCCCCCCC		49.2028490779
40PhosphorylationRRKAVIISSDEDEVV
CCCEEEECCCCCCCC		22.1721082442
41PhosphorylationRKAVIISSDEDEVVS
CCEEEECCCCCCCCC		34.3121082442
48PhosphorylationSDEDEVVSPPETKKR
CCCCCCCCCCHHHCC		39.6528490779
52PhosphorylationEVVSPPETKKRKASK
CCCCCCHHHCCCCCC		47.8722817900
58PhosphorylationETKKRKASKTASSED
HHHCCCCCCCCCCCC		33.3122817900
60PhosphorylationKKRKASKTASSEDDV
HCCCCCCCCCCCCCC		29.3119429919
62PhosphorylationRKASKTASSEDDVVA
CCCCCCCCCCCCCEE		39.2221082442
63PhosphorylationKASKTASSEDDVVAA
CCCCCCCCCCCCEEC		42.4521082442
71PhosphorylationEDDVVAATPEPIAKK
CCCCEECCCHHHHHH		20.6019429919
128PhosphorylationENEDIDRSLMEVDLD
CCCCCCHHHHCCCCC		28.4622817900
137PhosphorylationMEVDLDESIKEAAPE
HCCCCCHHHHHHCCC		38.3322817900
149PhosphorylationAPEKKVHSITRSSPS
CCCCCCCCCCCCCCC		28.7422817900
151PhosphorylationEKKVHSITRSSPSPK
CCCCCCCCCCCCCCC		27.7519429919
153PhosphorylationKVHSITRSSPSPKRA
CCCCCCCCCCCCCCC		37.6419429919
154PhosphorylationVHSITRSSPSPKRAK
CCCCCCCCCCCCCCC		26.5519429919
156PhosphorylationSITRSSPSPKRAKNS
CCCCCCCCCCCCCCC		45.0319429919
163PhosphorylationSPKRAKNSSPEPPKP
CCCCCCCCCCCCCCC		46.7119429919
164PhosphorylationPKRAKNSSPEPPKPK
CCCCCCCCCCCCCCC		42.5519429919
179PhosphorylationSTKSKATTPRVKKEK
CCCCCCCCCCCCCCC		17.6027626673
194PhosphorylationPAADLESSVLTDEER
CCHHHHHHCCCHHHH		16.2722817900
197PhosphorylationDLESSVLTDEERHER
HHHHHCCCHHHHHHH		38.9319429919
208PhosphorylationRHERKRASAVLYQKY
HHHHHHHHHHHHHHH		23.9619429919
212PhosphorylationKRASAVLYQKYKNRS
HHHHHHHHHHHCCCH		9.0719429919
219PhosphorylationYQKYKNRSSCLNPGS
HHHHCCCHHCCCCCC		34.4927626673
375PhosphorylationHKVKEEHTSPKETKD
HHCCCCCCCCHHHHH		50.4319429919
376PhosphorylationKVKEEHTSPKETKDK
HCCCCCCCCHHHHHH		35.5619429919
407PhosphorylationSQKEHPPSPRTADLK
CCCCCCCCCCCCCCC		31.3125749252
631PhosphorylationFKEKVKISPAKVEEI
HHCCCCCCHHHHHHH		17.0622817900
649PhosphorylationTNNDIRQSINHIALL
CCCHHHHHHHHHHHH		18.6021082442
938PhosphorylationDGAGGHLSSEEDEDK
CCCCCCCCCCCCCCC		29.9919429919
939PhosphorylationGAGGHLSSEEDEDKD
CCCCCCCCCCCCCCC		51.9019429919
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 RFC1_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RFC1_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 RFC1_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KU70_DROMEIrbpphysical
22036573
PARP_DROMEParpphysical
22036573
RFC2_DROMERfC4physical
22036573
RFA1_DROMERpA-70physical
22036573
Y2199_DROMECG2199physical
22036573
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RFC1_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 SER-18; SER-28; SER-40;SER-41; SER-48; SER-58; THR-60; SER-62; SER-63; THR-71; SER-128;SER-137; SER-149; SER-154; SER-156; SER-164; SER-194; THR-197; SER-938AND SER-939, AND MASS SPECTROMETRY.

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