DPOD2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DPOD2_MOUSE
• UniProt AC: O35654
• Protein Name: DNA polymerase delta subunit 2
• Gene Name: Pold2
• Organism: Mus musculus (Mouse).
• Sequence Length: 469
• Subcellular Localization: Nucleus . Recruited to DNA damage sites within 2 hours following UV irradiation.
• Protein Description: As a component of the trimeric and tetrameric DNA polymerase delta complexes (Pol-delta3 and Pol-delta4, respectively), plays a role in high fidelity genome replication, including in lagging strand synthesis, and repair. Pol-delta3 and Pol-delta4 are characterized by the absence or the presence of POLD4. They exhibit differences in catalytic activity. Most notably, Pol-delta3 shows higher proofreading activity than Pol-delta4. Although both Pol-delta3 and Pol-delta4 process Okazaki fragments in vitro, Pol-delta3 may also be better suited to fulfill this task, exhibiting near-absence of strand displacement activity compared to Pol-delta4 and stalling on encounter with the 5'-blocking oligonucleotides. Pol-delta3 idling process may avoid the formation of a gap, while maintaining a nick that can be readily ligated. Along with DNA polymerase kappa, DNA polymerase delta carries out approximately half of nucleotide excision repair (NER) synthesis following UV irradiation. Under conditions of DNA replication stress, required for the repair of broken replication forks through break-induced replication (BIR). Involved in the translesion synthesis (TLS) of templates carrying O6-methylguanine or abasic sites performed by Pol-delta4, independently of DNA polymerase zeta (REV3L) or eta (POLH). Facilitates abasic site bypass by DNA polymerase delta by promoting extension from the nucleotide inserted opposite the lesion. Also involved in TLS as a component of the POLZ complex. Along with POLD3, dramatically increases the efficiency and processivity of DNA synthesis of the minimal DNA polymerase zeta complex, consisting of only REV3L and REV7..
• Protein Sequence: MFSEQAAQRAHTLLAPPSASNATFARVPVATYTNSSQPFRLGERSFNRQYAHIYATRLIQMRPFLVSRAQQHWGSRVEVKKLCELQPGEQCCVVGTLFKAMSLQPSILREISEEHNLVPQPPRSKYIHPDDELVLEDELQRIKLKGTIDVSKLVTGTVLAVLGSAKDDGRFQVEDHCFADLAPQKPVPPLDTDRFVLLVSGLGLGGGGGESLLGTQLLVDVVTGQLGDEGEQCSAAHVSRVILAGNLLSHNTQSRDSINKAKYLTKKTQAASVEAVKMLDEILLQLSASVPVDVMPGEFDPTNYTLPQQPLHPCMFPLATAYSTLQLVTNPYQATIDGVRFLGTSGQNVSDIFRYSSMEDHLEILEWTLRVRHISPTAPDTLGCYPFYKTDPFIFPECPHVYFCGNTPSFGSKIIRGPEDQVVLLVAVPDFSSTQTACLVNLRSLACQPISFAGFGAEQEDLEGLGLGP

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
1	Acetylation	-------MFSEQAAQ -------CCCHHHHH	8.22	-
20	O-linked_Glycosylation	LLAPPSASNATFARV HCCCCCCCCCCEEEE	31.19	30059200
257	Phosphorylation	HNTQSRDSINKAKYL CCCCCHHHHHHHHHH	27.27	-
268	Phosphorylation	AKYLTKKTQAASVEA HHHHCHHHHCCHHHH	25.62	25619855
272	Phosphorylation	TKKTQAASVEAVKML CHHHHCCHHHHHHHH	24.41	25619855

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

Oops, there are no upstream regulatory protein records of DPOD2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DPOD2_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of DPOD2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of DPOD2_MOUSE !!

Drug and Disease Associations

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