RFC1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RFC1_SCHPO
• UniProt AC: O60182
• Protein Name: Replication factor C subunit 1
• Gene Name: rfc1
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 934
• Subcellular Localization: Nucleus, nucleolus .
• Protein Description: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. Subunit 1 is essential for cell cycle progression. It may associate with components of the DNA replication machinery and serve to enhance the efficiency of DNA replication..
• Protein Sequence: MSNSDIRSFFGGGNAQKKPKVSPTPTSPKPKRSLKKKRIVLSDDEDGTIENSKVPASKSKVQKRNESEDISHSLPSIVHEDDKLVGSDGVSTTPDEYFEQQSTRSRSKPRIISNKETTTSKDVVHPVKTENFANDLDTTSDSKPVVHQTRATRKPAQPKAEKSTTSKSKSHTTTATTHTSRSSKSKGLPRFSDEVSQALKNVPLIDVDSMGVMAPGTFYERAATTQTPGSKPVPEGNSDCLSGISFVITGILETLTRQEATDLIKQYGGKVTGAPSVRTDFILLGENAGPRKVETIKQHKIPAINEDGLFYLITHLPASGGTGAAAQAAQQKKEQEEKKILETVARMDDSNKKESQPSQIWTSKYAPTSLKDICGNKGVVQKLQKWLQDYHKNRKSNFNKPGPDGLGLYKAVLLSGPPGIGKTTAAHLVAKLEGYDVLELNASDTRSKRLLDEQLFGVTDSQSLAGYFGTKANPVDMAKSRLVLIMDEIDGMSSGDRGGVGQLNMIIKKSMIPIICICNDRAHPKLRPLDRTTFDLRFRRPDANSMRSRIMSIAYREGLKLSPQAVDQLVQGTQSDMRQIINLLSTYKLSCSEMTPQNSQAVIKNSEKHIVMKPWDICSRYLHGGMFHPSSKSTINDKLELYFNDHEFSYLMVQENYLNTTPDRIRQEPPKMSHLKHLELISSAANSFSDSDLVDSMIHGPQQHWSLMPTHALMSCVRPASFVAGSGSRQIRFTNWLGNNSKTNKLYRMLREIQVHMRLKVSANKLDLRQHYIPILYESLPVKLSTGHSDVVPEIIELMDEYYLNREDFDSITELVLPADAGEKLMKTIPTAAKSAFTRKYNSSSHPIAFFGSSDVLPMKGSAQREVPDVEDAIEAEDEMLEEASDSEAANEEDIDLSKDKFISVPKKPKKRTKAKAEASSSSSTSRRSRKKTA

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
22	Phosphorylation	AQKKPKVSPTPTSPK CCCCCCCCCCCCCCC	29.23	25720772
24	Phosphorylation	KKPKVSPTPTSPKPK CCCCCCCCCCCCCCC	31.52	29996109
26	Phosphorylation	PKVSPTPTSPKPKRS CCCCCCCCCCCCCCC	61.20	24763107
27	Phosphorylation	KVSPTPTSPKPKRSL CCCCCCCCCCCCCCC	31.93	28889911
42	Phosphorylation	KKKRIVLSDDEDGTI CCCEEEEECCCCCCE	31.93	28889911
48	Phosphorylation	LSDDEDGTIENSKVP EECCCCCCEECCCCC	37.12	29996109
52	Phosphorylation	EDGTIENSKVPASKS CCCCEECCCCCCCHH	23.41	29996109
87	Phosphorylation	EDDKLVGSDGVSTTP CCCCCCCCCCCCCCH	24.58	29996109
91	Phosphorylation	LVGSDGVSTTPDEYF CCCCCCCCCCHHHHH	31.90	29996109
92	Phosphorylation	VGSDGVSTTPDEYFE CCCCCCCCCHHHHHH	39.68	29996109
93	Phosphorylation	GSDGVSTTPDEYFEQ CCCCCCCCHHHHHHH	22.64	29996109
885	Phosphorylation	DEMLEEASDSEAANE HHHHHHHCCCHHCCH	44.97	25720772
887	Phosphorylation	MLEEASDSEAANEED HHHHHCCCHHCCHHH	27.00	21712547
898	Phosphorylation	NEEDIDLSKDKFISV CHHHCCCCCCCCCCC	34.75	25720772

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

Oops, there are no upstream regulatory protein records of RFC1_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RFC1_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 RFC1_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RFC5_SCHPO	rfc5	genetic	16040599
CTF18_SCHPO	ctf18	genetic	16040599
DCC1_SCHPO	dcc1	genetic	16040599
ELG1_SCHPO	elg1	genetic	16040599

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-27, AND MASSSPECTROMETRY.
PubMed: 18257517