DPOE3_HUMAN - dbPTM
DPOE3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPOE3_HUMAN
UniProt AC Q9NRF9
Protein Name DNA polymerase epsilon subunit 3
Gene Name POLE3
Organism Homo sapiens (Human).
Sequence Length 147
Subcellular Localization Nucleus .
Protein Description Forms a complex with DNA polymerase epsilon subunit CHRAC1 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome-remodeling activity of ISWI/SNF2H and ACF1..
Protein Sequence MAERPEDLNLPNAVITRIIKEALPDGVNISKEARSAISRAASVFVLYATSCANNFAMKGKRKTLNASDVLSAMEEMEFQRFVTPLKEALEAYRREQKGKKEASEQKKKDKDKKTDSEEQDKSRDEDNDEDEERLEEEEQNEEEEVDN
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
2Acetylation------MAERPEDLN
------CCCCHHHCC
22.8519413330
20UbiquitinationAVITRIIKEALPDGV
HHHHHHHHHHCCCCC
34.27-
31AcetylationPDGVNISKEARSAIS
CCCCCCCHHHHHHHH
52.1525953088
31UbiquitinationPDGVNISKEARSAIS
CCCCCCCHHHHHHHH
52.1521890473
35PhosphorylationNISKEARSAISRAAS
CCCHHHHHHHHHHHH
36.6820860994
38PhosphorylationKEARSAISRAASVFV
HHHHHHHHHHHHHHH
18.6420860994
62UbiquitinationFAMKGKRKTLNASDV
CHHCCCCCCCCHHHH
61.93-
63PhosphorylationAMKGKRKTLNASDVL
HHCCCCCCCCHHHHH
29.3122617229
67PhosphorylationKRKTLNASDVLSAME
CCCCCCHHHHHHHHH
27.4630576142
71PhosphorylationLNASDVLSAMEEMEF
CCHHHHHHHHHHHHH
25.9720068231
83PhosphorylationMEFQRFVTPLKEALE
HHHHHHHHHHHHHHH
21.8618669648
86UbiquitinationQRFVTPLKEALEAYR
HHHHHHHHHHHHHHH
41.9921890473
92PhosphorylationLKEALEAYRREQKGK
HHHHHHHHHHHHHCC
10.7923312004
114PhosphorylationKKDKDKKTDSEEQDK
HHHHCCCCCHHHHHH
50.9628985074
116PhosphorylationDKDKKTDSEEQDKSR
HHCCCCCHHHHHHHC
48.5430576142
122PhosphorylationDSEEQDKSRDEDNDE
CHHHHHHHCCCCCHH
53.9426503892
123MethylationSEEQDKSRDEDNDED
HHHHHHHCCCCCHHH
58.01115488093
133MethylationDNDEDEERLEEEEQN
CCHHHHHHHHHHHHH
45.40115488085

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 DPOE3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DPOE3_HUMAN !!

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 DPOE3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMCA5_HUMANSMARCA5physical
10880450
BAZ1A_HUMANBAZ1Aphysical
10880450
CHRC1_HUMANCHRAC1physical
10880450
BAZ1A_HUMANBAZ1Aphysical
14759371
SMCA5_HUMANSMARCA5physical
14759371
DPOE4_HUMANPOLE4physical
10801849
DPOE2_HUMANPOLE2physical
10801849
DPOE1_HUMANPOLEphysical
21705323
A4_HUMANAPPphysical
21832049
DPOE4_HUMANPOLE4physical
22939629
ANXA6_HUMANANXA6physical
22863883
SIAS_HUMANNANSphysical
22863883
CHRC1_HUMANCHRAC1physical
25416956
ATAD2_HUMANATAD2physical
26344197
DPOE1_HUMANPOLEphysical
26344197
CHRC1_HUMANCHRAC1physical
21516116

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00242Cladribine
Regulatory Network of DPOE3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-83 AND SER-122, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND MASSSPECTROMETRY.

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