DPOD1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DPOD1_MOUSE
• UniProt AC: P52431
• Protein Name: DNA polymerase delta catalytic subunit
• Gene Name: Pold1
• Organism: Mus musculus (Mouse).
• Sequence Length: 1105
• Subcellular Localization: Nucleus . Colocalizes with PCNA and POLD3 at S phase replication sites. After UV irradiation, recruited to DNA damage sites within 2 hours, independently on the cell cycle phase, nor on PCNA ubiquitination. This recruitement requires POLD3, PCNA and
• Protein Description: As the catalytic component of the trimeric (Pol-delta3 complex) and tetrameric DNA polymerase delta complexes (Pol-delta4 complex), plays a crucial role in high fidelity genome replication, including in lagging strand synthesis, and repair. Exhibits both DNA polymerase and 3'- to 5'-exonuclease activities. Requires the presence of accessory proteins POLD2, POLD3 and POLD4 for full activity. Depending upon the absence (Pol-delta3) or the presence of POLD4 (Pol-delta4), displays differences in catalytic activity. Most notably, expresses higher proofreading activity in the context of Pol-delta3 compared with that of Pol-delta4. Although both Pol-delta3 and Pol-delta4 process Okazaki fragments in vitro, Pol-delta3 may 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, in the presence of POLD3 and POLD4, may catalyze 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..
• Protein Sequence: MDCKRRQGPGPGVPPKRARGHLWDEDEPSPSQFEANLALLEEIEAENRLQEAEEELQLPPEGTVGGQFSTADIDPRWRRPTLRALDPSTEPLIFQQLEIDHYVGSAPPLPEGPLPSRNSVPILRAFGVTDEGFSVCCHIQGFAPYFYTPAPPGFGAEHLSELQQELNAAISRDQRGGKELSGPAVLAIELCSRESMFGYHGHGPSPFLRITLALPRLMAPARRLLEQGVRVPGLGTPSFAPYEANVDFEIRFMVDADIVGCNWLELPAGKYVRRAEKKATLCQLEVDVLWSDVISHPPEGQWQRIAPLRVLSFDIECAGRKGIFPEPERDPVIQICSLGLRWGEPEPFLRLALTLRPCAPILGAKVQSYEREEDLLQAWADFILAMDPDVITGYNIQNFDLPYLISRAQALKVDRFPFLGRVTGLRSNIRDSSFQSRQVGRRDSKVISMVGRVQMDMLQVLLREHKLRSYTLNAVSFHFLGEQKEDVQHSIITDLQNGNEQTRRRLAVYCLKDAFLPLRLLERLMVLVNNVEMARVTGVPLGYLLTRGQQVKVVSQLLRQAMRQGLLMPVVKTEGSEDYTGATVIEPLKGYYDVPIATLDFSSLYPSIMMAHNLCYTTLLRPGAAQKLGLKPDEFIKTPTGDEFVKSSVRKGLLPQILENLLSARKRAKAELAQETDPLRRQVLDGRQLALKVSANSVYGFTGAQVGKLPCLEISQSVTGFGRQMIEKTKQLVESKYTVENGYDANAKVVYGDTDSVMCRFGVSSVAEAMSLGREAANWVSSHFPSPIRLEFEKVYFPYLLISKKRYAGLLFSSRSDAHDKMDCKGLEAVRRDNCPLVANLVTSSLRRILVDRDPDGAVAHAKDVISDLLCNRIDISQLVITKELTRAAADYAGKQAHVELAERMRKRDPGSAPSLGDRVPYVIIGAAKGVAAYMKSEDPLFVLEHSLPIDTQYYLEQQLAKPLLRIFEPILGEGRAESVLLRGDHTRCKTVLTSKVGGLLAFTKRRNCCIGCRSVIDHQGAVCKFCQPRESELYQKEVSHLNALEERFSRLWTQCQRCQGSLHEDVICTSRDCPIFYMRKKVRKDLEDQERLLQRFGPPGPEAW

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
19	Methylation	GVPPKRARGHLWDED CCCCCCCCCCCCCCC	36.78	-
29	Phosphorylation	LWDEDEPSPSQFEAN CCCCCCCCHHHHHHH	34.83	26160508
31	Phosphorylation	DEDEPSPSQFEANLA CCCCCCHHHHHHHHH	52.41	26160508
444	Phosphorylation	RQVGRRDSKVISMVG CCCCCCCCHHHHHHH	27.32	21454597
576	Phosphorylation	PVVKTEGSEDYTGAT EEEECCCCCCCCCCE	22.51	27841257
663	Phosphorylation	QILENLLSARKRAKA HHHHHHHHHHHHHHH	29.24	26745281
786	Phosphorylation	WVSSHFPSPIRLEFE HHHHHCCCCEEEEEE	31.83	27600695
845	Phosphorylation	VANLVTSSLRRILVD HHHHHHHHHHHHHCC	19.27	23140645
883	Ubiquitination	ISQLVITKELTRAAA HHHHHHHHHHHHHHH	39.33	-
1074	Glutathionylation	VICTSRDCPIFYMRK EEEECCCCCEEEEEH	2.43	24333276
1078	Phosphorylation	SRDCPIFYMRKKVRK CCCCCEEEEEHHHHC	9.20	28066266

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

Oops, there are no upstream regulatory protein records of DPOD1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DPOD1_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 DPOD1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TIM_MOUSE	Timeless	physical	17141802

Drug and Disease Associations

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