dbPTM

RPA1_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RPA1_DROME
UniProt AC	P91875
Protein Name	DNA-directed RNA polymerase I subunit RPA1
Gene Name	RpI1
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	1642
Subcellular Localization	Nucleus, nucleolus.
Protein Description	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase I which synthesizes ribosomal RNA precursors. Forms the polymerase active center together with the second largest subunit. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol I by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition (By similarity)..
Protein Sequence	MGSKRAMDVHMFPSDLEFAVFTDQEIRKLSVVKVITGITFDALGHAIPGGLYDIRMGSYGRCMDPCGTCLKLQDCPGHMGHIELGTPVYNPFFIKFVQRLLCIFCLHCYKLQMKDHECEIIMLQLRLIDAGYIIEAQELELFKSEIVCQNTENLVAIKNGDMVHPHIAAMYKLLEKNEKNSSNSTKTSCSLRTAITHSALQRLGKKCRHCNKSMRFVRYMHRRLVFYVTLADIKERVGTGAETGGQNKVIFADECRRYLRQIYANYPELLKLLVPVLGLSNTDLTQGDRSPVDLFFMDTLPVTPPRARPLNMVGDMLKGNPQTDIYINIIENNHVLNVVLKYMKGGQEKLTEEAKAAYQTLKGETAHEKLYTAWLALQMSVDVLLDVNMSREMKSGEGLKQIIEKKSGLIRSHMMGKRVNYAARTVITPDPNINVDEIGIPDIFAKKLSYPVPVTEWNVTELRKMVMNGPDVHPGANYIQDKNGFTTYIPADNASKRESLAKLLLSNPKDGIKIVHRHVLNGDVLLLNRQPSLHKPSIMGHKARILHGEKTFRLHYSNCKAYNADFDGDEMNAHYPQSEVARAEAYNLVNVASNYLVPKDGTPLGGLIQDHVISGVKLSIRGRFFNREDYQQLVFQGLSQLKKDIKLLPPTILKPAVLWSGKQILSTIIINIIPEGYERINLDSFAKIAGKNWNVSRPRPPICGTNPEGNDLSESQVQIRNGELLVGVLDKQQYGATTYGLIHCMYELYGGDVSTLLLTAFTKVFTFFLQLEGFTLGVKDILVTDVADRKRRKIIRECRNVGNSAVAAALELEDEPPHDELVEKMEAAYVKDSKFRVLLDRKYKSLLDGYTNDINSTCLPRGLITKFPSNNLQLMVLSGAKGSMVNTMQISCLLGQIELEGKRPPLMISGKSLPSFTSFETSPKSGGFIDGRFMTGIQPQDFFFHCMAGREGLIDTAVKTSRSGYLQRCLIKHLEGLSVHYDLTVRDSDNSVVQFLYGEDGLDILKSKFFNDKFCADFLTQNATAILRPAQLQLMKDEEQLAKVQRHEKHIRSWEKKKPAKLRAAFTHFSEELREEVEVKRPNEINSKTGRRRFDEGLLKLWKKADAEDKALYRKKYARCPDPTVAVYKQDLYYGSVSERTRKLITDYAKRKPALKETIADIMRVKTIKSLAAPGEPVGLIAAQSIGEPSTQMTLNTFHFAGRGEMNVTLGIPRLREILMLASSNIKTPSMDIPIKPGQQHQAEKLRINLNSVTLANLLEYVHVSTGLTLDPERSYEYDMRFQFLPREVYKEDYGVRPKHIIKYMHQTFFKQLIRAILKVSNASRTTKIVVIDDKKDADKDDDNDLDNGDEVGRSKAKANDDDSSDDNDDDDATGVKLKQRKTDEKDYDDPDDVEELHDANDDDDEAEDEDDEEKGQDGNDNDGDDKAVERLLSNDMVKAYTYDKENHLWCQVKLNLSVRYQKPDLTSIIRELAGKSVVHQVQHIKRAIIYKGNDDDQLLKTDGINIGEMFQHNKILDLNRLYSNDIHAIARTYGIEAASQVIVKEVSNVFKVYGITVDRRHLSLIADYMTFDGTFQPLSRKGMEHSSSPLQQMSFESSLQFLKSAAGFGRADELSSPSSRLMVGLPVRNGTGAFELLTKIC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference	Orthologous Protein Cluster
1364	Phosphorylation	AKANDDDSSDDNDDD CCCCCCCCCCCCCCC	42.53	19429919
1365	Phosphorylation	KANDDDSSDDNDDDD CCCCCCCCCCCCCCC	56.85	19429919

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 RPA1_DROME !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RPA1_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 RPA1_DROME !!

Protein-Protein Interaction

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

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RPA1_DROME

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-1364 AND SER-1365, ANDMASS SPECTROMETRY.	18327897 [Abstract]