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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MAERPEDLN ------CCCCHHHCC | 22.85 | 19413330 | |
20 | Ubiquitination | AVITRIIKEALPDGV HHHHHHHHHHCCCCC | 34.27 | - | |
31 | Acetylation | PDGVNISKEARSAIS CCCCCCCHHHHHHHH | 52.15 | 25953088 | |
31 | Ubiquitination | PDGVNISKEARSAIS CCCCCCCHHHHHHHH | 52.15 | 21890473 | |
35 | Phosphorylation | NISKEARSAISRAAS CCCHHHHHHHHHHHH | 36.68 | 20860994 | |
38 | Phosphorylation | KEARSAISRAASVFV HHHHHHHHHHHHHHH | 18.64 | 20860994 | |
62 | Ubiquitination | FAMKGKRKTLNASDV CHHCCCCCCCCHHHH | 61.93 | - | |
63 | Phosphorylation | AMKGKRKTLNASDVL HHCCCCCCCCHHHHH | 29.31 | 22617229 | |
67 | Phosphorylation | KRKTLNASDVLSAME CCCCCCHHHHHHHHH | 27.46 | 30576142 | |
71 | Phosphorylation | LNASDVLSAMEEMEF CCHHHHHHHHHHHHH | 25.97 | 20068231 | |
83 | Phosphorylation | MEFQRFVTPLKEALE HHHHHHHHHHHHHHH | 21.86 | 18669648 | |
86 | Ubiquitination | QRFVTPLKEALEAYR HHHHHHHHHHHHHHH | 41.99 | 21890473 | |
92 | Phosphorylation | LKEALEAYRREQKGK HHHHHHHHHHHHHCC | 10.79 | 23312004 | |
114 | Phosphorylation | KKDKDKKTDSEEQDK HHHHCCCCCHHHHHH | 50.96 | 28985074 | |
116 | Phosphorylation | DKDKKTDSEEQDKSR HHCCCCCHHHHHHHC | 48.54 | 30576142 | |
122 | Phosphorylation | DSEEQDKSRDEDNDE CHHHHHHHCCCCCHH | 53.94 | 26503892 | |
123 | Methylation | SEEQDKSRDEDNDED HHHHHHHCCCCCHHH | 58.01 | 115488093 | |
133 | Methylation | DNDEDEERLEEEEQN CCHHHHHHHHHHHHH | 45.40 | 115488085 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DPOE3_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
SMCA5_HUMAN | SMARCA5 | physical | 10880450 | |
BAZ1A_HUMAN | BAZ1A | physical | 10880450 | |
CHRC1_HUMAN | CHRAC1 | physical | 10880450 | |
BAZ1A_HUMAN | BAZ1A | physical | 14759371 | |
SMCA5_HUMAN | SMARCA5 | physical | 14759371 | |
DPOE4_HUMAN | POLE4 | physical | 10801849 | |
DPOE2_HUMAN | POLE2 | physical | 10801849 | |
DPOE1_HUMAN | POLE | physical | 21705323 | |
A4_HUMAN | APP | physical | 21832049 | |
DPOE4_HUMAN | POLE4 | physical | 22939629 | |
ANXA6_HUMAN | ANXA6 | physical | 22863883 | |
SIAS_HUMAN | NANS | physical | 22863883 | |
CHRC1_HUMAN | CHRAC1 | physical | 25416956 | |
ATAD2_HUMAN | ATAD2 | physical | 26344197 | |
DPOE1_HUMAN | POLE | physical | 26344197 | |
CHRC1_HUMAN | CHRAC1 | physical | 21516116 |
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 | |
DB00242 | Cladribine |
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Acetylation | |
Reference | PubMed |
"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 | |
Reference | PubMed |
"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. |