DPOE_SCHPO - dbPTM
DPOE_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPOE_SCHPO
UniProt AC P87154
Protein Name DNA polymerase epsilon catalytic subunit A
Gene Name pol2
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 2199
Subcellular Localization Nucleus.
Protein Description DNA polymerase II participates in chromosomal DNA replication..
Protein Sequence MPLKTARGASKYQFRKFNGNYNGKSKSNGRTFAKSTEEVGFNDPMKIVYKKNEIDRMMGFDSYEGGQPREAWLLNVHPTVIESTKGNSTLSAVDFYFIQDDGDTFRCTIPYSPYFYIAAREGKEALVDDYLKKKFVGLIKSTTRIFKEDLQLKNHIVGYQKLYIKLVFDNLNDLQAVRKSLMSAVKANSSQQDAVDAYTNLSSENLNGIIENAFEDPLNHVLDIREYDVPYHSRTLIDLNIRVGQWYTVSYHEGHVQISLLASRIERAEPTIMAFDIETTKLPLKFPDSSFDKIMMISYMIDGQGFLITNREIISQNIEDFHYTPREEFEGPFIIFNEPDEVGLLHRFFKHIRSAKPSVIVTYNGDFFDWPFVDARAAFHGLNLTEETGFFRDAEDEYKSSYCSHMDAFRWVKRDSYLPQGSQGLKAVTVSKLGYNPIELDPELMTPYASEKPQVLAQYSVSDAVATYFLYMKYVHPFIFSLCNIIPLNPDEVLRKGTGTLCETLLTVEACTKNIILPNKHVDASQKFFDGHLLASETYVGGHVESLESGVFRSDLPTNFNMDPKVYEELILQLDKALDFSLTVENNVNVDEIENYEEVRDSILKKLSDLRDRPKRSEKPRIYHLDVASMYPNIMITNRLQPDSVKDESFCATCDLNVPNKTCDRRMVWAWRGEYYPAKKGEYHMIYSALQSERFPGPTPFSPFRSFQELSPSEQAAMVQKRIADYSRKVYHRLYDNTVIERETIICQKENSFYIDTVKSFRDRRYDFKGLQKKWVKQLAAIKEKGGLAEIEEAKKMVVLYDSLQLAHKVILNSFYGYVMRKGSRWYSIEMAGITCLTGATIIQMARQIVERAGRPLELDTDGIWCILPESFPENFEFKKKSGGKVFISYPCVMLNHLVHEKFTNHQYSALKDPEKLVYETTSENSIFFEVDGPYRAMILPASTEEGKNLKKRYAVFNFDGSLAELKGFEVKRRGELKLIKDFQSQIFKVFLKGDSLEECYQEVAYVADTWLEILFTKGSNLTDDELIELISENRSMSKALSEYGSQKSTSITTARRLADFLGDQMTKDKGLACRFIISASPKGRPVAERAVPVAIFFAEESVKRHFLRLWLKDNGLYDVDIRDIIDWDYYLKRLGSVVQKLISIPAALQRISNPVTRFPLPDWLQKRVAVLNSKYQQKKIDSIFSLAPTNPSTINNTKVTDIEDLGSVTHKDKRIVARVTKRKLLQQSGNSEAPVSFEVKPVSFMDGYSNWLKYAKKKWKYQKQVKLRRRHLIGFQSRQFTNVLQSSAEVMFENLWHILQIRETDVPGILHAWVIIRNRLTSIRFIVNRKFFVCFKDETLPNVEIEGCLIEKSNAILPHGSTSDKLFLLEIPEKSYLTEKVSISMIFAHPSVSGIYETRIEPIERLILEMGSRKRFNNSVPGALGKGFEFGFESKMFTDPSDNDVSYLDGVEMNYLYAFHFSISNRFVFSLFMPHLKKVEAIIYDKLPGSDMSFPSISKIYEELRSKFDNLIKESSIEYPDTLSCNVIFSGNERKAYKLIDEKLLQYFSTKTKNSLLIIESSLPHILKANVKQIEELPYIMIPRLESNIQSLSWKQHIATKMIQHFLAIGSWLFHRIQLSRFSDIPLCNFESDDIQYSIDVVYSRKLKEHNIILWWNKGPTPDLGGIEKDSILQIASPKDPLEVNNPGAYSNACVDISLSNLALCSILNSALINDIEGIGDMAALNDNYMTAINDDLEEKLGIHDNIGLTHSLPVLKALVKTWWNEAASGNNLADLIIQHLARWISSSKSYLYSPLLSSHVEVIMRKTFLQLLSEIKRLGAHIIHASANKILIKTSKLIVQNAVTYSNYLLKSIKTLPLFHFLDLNVTEYWDYLLWMDSVNYGGKMVAANFSATNEEPQTVVSWHIKSHLPPIIQPEFQSWIVEFIEEVYKQKLEKSNTKVGFVRVKNNNADEDSEIVGSGILKSKLIHPLKRKVAQVRRCFQELQLDENTREDLKFPKLPGSFLNYTDGALELVKSICAVFELSHDLNLEVRFLKKSLLSLLQIQEFSTQAVFRYPSRRLSLDQIPCKQCGVHQDFDLCLHEHLWPTRDDMGTLVFSDGWSCSSCNLVYDRWVFEETLVDNLYHQLTLYQLQDLICSKCKTVKQWSLKERCSCSGEWVLQLSPTKFREMLNVYQSVADFYEFSILQNSVQSILSVLN
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
752PhosphorylationIICQKENSFYIDTVK
EEEECCCCEEEECHH		22.1025720772
757PhosphorylationENSFYIDTVKSFRDR
CCCEEEECHHHHHHC		21.9225720772
760PhosphorylationFYIDTVKSFRDRRYD
EEEECHHHHHHCCCC		22.6025720772
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 DPOE_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DPOE_SCHPO !!
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 DPOE_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHK1_SCHPOchk1genetic
11416129
RAD3_SCHPOrad3genetic
11416129
HUS1_SCHPOhus1genetic
11416129
DPOD_SCHPOcdc6genetic
11416129
RAD17_SCHPOrad17genetic
10683155
CHK1_SCHPOchk1genetic
10683155
SWI1_SCHPOswi1genetic
18667534
SWI3_SCHPOswi3genetic
18667534
CDS1_SCHPOcds1genetic
18667534
CHK1_SCHPOchk1genetic
18667534
RAD1_SCHPOrad1genetic
18667534
RAD9_SCHPOrad9genetic
18667534
RAD3_SCHPOrad3genetic
18667534
RAD26_SCHPOrad26genetic
18667534
RAD17_SCHPOrad17genetic
18667534
MRC1_SCHPOmrc1genetic
18667534
RHP9_SCHPOcrb2genetic
18667534
MUS81_SCHPOmus81genetic
18667534
HUS2_SCHPOrqh1genetic
18667534
RAD24_SCHPOrad24genetic
18667534
MES1_SCHPOmes1physical
18331722
RAF2_SCHPOraf2physical
21725325
MMS19_SCHPOmms19physical
21725325
MSH2_SCHPOmsh2genetic
22144917
DPB2_SCHPOdpb2genetic
22718908
RHP9_SCHPOcrb2genetic
9407031
RHP9_SCHPOcrb2genetic
14739927
CHK1_SCHPOchk1genetic
14739927
HUS2_SCHPOrqh1genetic
9891047
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DPOE_SCHPO

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Related Literatures of Post-Translational Modification

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