RPA1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RPA1_SCHPO
• UniProt AC: P15398
• Protein Name: DNA-directed RNA polymerase I subunit rpa1
• Gene Name: rpa1
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 1689
• 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: MNIAQPVSSEIKSVKFGIYDVDDVEKISVKQIVNPVLLDNLNHPTNGGLYDLALGPYLKNSVCATCHLDERYCPGHFGHIVLPIPAYHPLFFSQMYNLLRSTCLYCHHFKLSKVKVHLFFCRLKLLDYGLLNESEMVENVSLTEAIIKNSNGTPLEDGSDSEDSGLGHDDIAKDAATLMRIRDEFVAKSIADSRQNAHIDAQLTTLLLHERKKVVRAFYHAISSRKQCDNCQSFSPNFRKEGFAKIFEIPLSGKNLQFMEQTGKIRSDVLRDTSKKHHEDEGYDGDSDSSNESEVEGIDLFEEDPNPLKNKSKSPIAHGAKYMTSTEVRNHLRRLFVKENVVLSRLYAHKRGKPASADMFFLQNIAVPPTRFRPASKMGDEVHENIQNELLTRILQSSIQIASLSKDSTVEVNPDEKEGLERRSRAFELLINAFVQLQHDVNSLIDSNRNPSSGGQSRTVPPGIKQILEKKEGLFRKHMMGKRVNYAARSVISPDPNIETNEIGVPPVFATKLTYPEPVTLYNFNEMRNAVINGPHKWPGASHIQNEDGTLISLMPLTIEQRTALANQLLTPQSNLISSPYSYSRLINTNKKVYRHVRNGDMLILNRQPTLHKPSMMAHKARILPGEKTIRMHYANCNSYNADFDGDEMNMHFPQSTNARSEAQFIANTDSQYLVPTSGDPLRGLIQDHVVMGVWLTCKDTFYTRDEYQQLLFQALKPDETGMYGRIKTLPPAIQRPGIYWTGKQIISSVLLNLKPSDRPGLNLKSKAKVPGKYWSPDSEEGSVLFDDGELLCGILDKSSFGASAFGLVHSVHELYGPDIAGRLLSVLSRLFTAYAQMRGFTCRMDDLRLDEQGDNWRRQLLENGKSFGLEAASEYVGLSTDSPIALLNANLEEVYRDDEKLQGLDAAMKGKMNGLTSSIINKCIPDGLLTKFPYNHMQTMTVSGAKGSNVNVSQISCLLGQQELEGRRVPLMVSGKSLPSFVPYETSAKSGGFIASRFLTGIAPQEYYFHCMAGREGLIDTAVKTSRSGYLQRCLMKHLEGLCVQYDHTVRDSDGSIVQFHYGEDSLDVTKQKHLTQFEFSAKNYKSLIQKYKVKSVLSAVDSETASSYAKKALKKPYKYDPVLDKYPPSRYLGSVSEKFQRAVDEYTQKNPDKLIASKKESKLDDSLLNESKFKALMQLRYQQSLVDPGESVGVLASQSIGEPSTQMTLNTFHFAGFGAKNVTLGIPRLREIIMTASANIQTPTMTLRLNDGVSDKRASAFCKEVNKLVLSEVVRQVRVTEKISGQGSDEQSKTYAIRLDLYSRDEYQDEYGVLQEEIESTFSNRFLKILNRIIKSYLAKSKQRKSGGKDDTVPEVGQALKPLEDIDEAPIEGRAQEALEDEDNDATNEKMVSRSKQHASYEGPDEADKVALRQLKGSNKVEDVNMDEEEDEGFKSDESVSDFKERKLLEKQNTVSISERRELQLKTAKEILSNCKHLDFDYVNGEWATVELVFPINTEKLLMVSLVEKACSETVIHEIPGITRCFSKPPDSALDTVPKVITEGVNLKAIWEFYNEISMNDIYTNDIAAILRIYGVEAARNAIVHEVSSVFGVYGIAVDPRHLSLIADYMTFEGGYKAFNRMGIEYNTSPFAKMSFETTCHFLTEAALRGDVDDLSNPSSRLVVGRVGNFGTGSFDIFTPVVDSPAN

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
150	Phosphorylation	TEAIIKNSNGTPLED CHHHHHCCCCCCCCC	31.47	21712547
153	Phosphorylation	IIKNSNGTPLEDGSD HHHCCCCCCCCCCCC	29.02	24763107
159	Phosphorylation	GTPLEDGSDSEDSGL CCCCCCCCCCCCCCC	50.73	28889911
161	Phosphorylation	PLEDGSDSEDSGLGH CCCCCCCCCCCCCCC	45.03	28889911
164	Phosphorylation	DGSDSEDSGLGHDDI CCCCCCCCCCCCHHH	31.69	28889911
283	Phosphorylation	KHHEDEGYDGDSDSS HCCCCCCCCCCCCCC	18.07	21712547
287	Phosphorylation	DEGYDGDSDSSNESE CCCCCCCCCCCCCHH	44.94	21712547
289	Phosphorylation	GYDGDSDSSNESEVE CCCCCCCCCCCHHHC	38.73	21712547
290	Phosphorylation	YDGDSDSSNESEVEG CCCCCCCCCCHHHCC	50.00	21712547
490	Phosphorylation	RVNYAARSVISPDPN HHHHHHHHCCCCCCC	21.05	29996109
1438	Phosphorylation	EEDEGFKSDESVSDF HHCCCCCCCCCHHHH	44.33	28889911
1441	Phosphorylation	EGFKSDESVSDFKER CCCCCCCCHHHHHHH	31.73	28889911
1443	Phosphorylation	FKSDESVSDFKERKL CCCCCCHHHHHHHHH	46.76	25720772

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RPA1_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RPA1_SCHPO !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RPA1_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RTI1_SCHPO	rti1	physical	11560889
RRN5_SCHPO	rrn5	genetic	17538026

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159; SER-161; SER-1438AND SER-1441, AND MASS SPECTROMETRY.
PubMed: 18257517