COM1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: COM1_SCHPO
• UniProt AC: O74986
• Protein Name: DNA endonuclease ctp1
• Gene Name: ctp1
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 294
• Subcellular Localization: Nucleus . Accumulates at DSBs.
• Protein Description: Endonuclease that cooperates with the MRN complex in processing meiotic and mitotic double-strand breaks by allowing the endonucleolytic removal of rec12 from the break sites and ensuring both resection and intrachromosomal association of the broken ends. Required for the formation of RPA-coated single strand DNA adjacent to the DSBs where it functions together with the MRN complex in 5'- 3' resection. Required for the repair of programmed meiotic DSBs. Involved also in an rhp51 recombinase-dependent recombinational repair pathway..
• Protein Sequence: MNEEEHNKSVHWSIVYRQLGNLLEQYEVEIARLKSQLVLEKKLRIQVEKELESVKTKQISSSASSKVSSNTIQELDSTTDEDEIPGSDTVDEEDPSLNAPFSEKNQSVKIPPHSPTLPVQNASAFVKPISVPLGNVKEEKFLDTNPIGAESFESSDGEMHLRARSPEDMILLRETQPLAPLDINTLGVSDNRQKKGTEKKRPFEPEFLNDDVIRGNKRKALPAYECPDCQKFYELHGPVKESSVAPTWNDENRLGGGSLPNCKHQPLVQKVGRHRKLNIPKPIPNGFWESDFVD

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
77	Phosphorylation	NTIQELDSTTDEDEI CCHHHHCCCCCCCCC	45.92	28889911
78	Phosphorylation	TIQELDSTTDEDEIP CHHHHCCCCCCCCCC	37.62	28889911
79	Phosphorylation	IQELDSTTDEDEIPG HHHHCCCCCCCCCCC	41.15	28889911
87	Phosphorylation	DEDEIPGSDTVDEED CCCCCCCCCCCCCCC	25.42	28889911
89	Phosphorylation	DEIPGSDTVDEEDPS CCCCCCCCCCCCCCC	31.39	28889911
114	Phosphorylation	SVKIPPHSPTLPVQN CCCCCCCCCCCCCCC	25.92	18378696
151	Phosphorylation	TNPIGAESFESSDGE CCCCCCCCCCCCCCC	33.51	25720772
154	Phosphorylation	IGAESFESSDGEMHL CCCCCCCCCCCCEEE	31.55	25720772
155	Phosphorylation	GAESFESSDGEMHLR CCCCCCCCCCCEEEE	42.30	25720772
165	Phosphorylation	EMHLRARSPEDMILL CEEEEECCHHHEEEE	31.49	18378696

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

Oops, there are no upstream regulatory protein records of COM1_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of COM1_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 COM1_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NBS1_SCHPO	nbs1	physical	20421724
RAD3_SCHPO	rad3	genetic	21098122
ATM_SCHPO	tel1	genetic	21098122
RHP9_SCHPO	crb2	genetic	21098122
HUS1_SCHPO	hus1	genetic	21098122
H2A2_SCHPO	hta2	genetic	21098122
NBS1_SCHPO	nbs1	genetic	21098122
KU80_SCHPO	pku80	genetic	21931565
KU70_SCHPO	pku70	genetic	21931565
COM1_SCHPO	ctp1	physical	25580577
KU80_SCHPO	pku80	genetic	25580577

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Nbs1 flexibly tethers Ctp1 and Mre11-Rad50 to coordinate DNA double-strand break processing and repair.";
Williams R.S., Dodson G.E., Limbo O., Yamada Y., Williams J.S.,Guenther G., Classen S., Glover J.N., Iwasaki H., Russell P.,Tainer J.A.;
Cell 139:87-99(2009).
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 72-84 IN COMPLEX WITH NBS1,INTERACTION WITH NBS1, SUBCELLULAR LOCATION, PHOSPHORYLATION ATSER-77; THR-78; THR-79; SER-87 AND THR-89, AND MUTAGENESIS OF77-SER--THR-79 AND 87-SER--THR-89.
PubMed: 19804755