DPOD3_HUMAN - dbPTM
DPOD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPOD3_HUMAN
UniProt AC Q15054
Protein Name DNA polymerase delta subunit 3
Gene Name POLD3
Organism Homo sapiens (Human).
Sequence Length 466
Subcellular Localization Cytoplasm . Nucleus . Partially colocalizes with PCNA and POLD1 at S phase replication sites (PubMed:11595739). Recruited to DNA damage sites within 2 hours following UV irradiation (PubMed:20227374, PubMed:22801543).
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. Required for optimal Pol-delta activity. Stabilizes the Pol-delta complex and plays a major role in Pol-delta stimulation by PCNA. [PubMed: 10219083]
Protein Sequence MADQLYLENIDEFVTDQNKIVTYKWLSYTLGVHVNQAKQMLYDYVERKRKENSGAQLHVTYLVSGSLIQNGHSCHKVAVVREDKLEAVKSKLAVTASIHVYSIQKAMLKDSGPLFNTDYDILKSNLQNCSKFSAIQCAAAVPRAPAESSSSSKKFEQSHLHMSSETQANNELTTNGHGPPASKQVSQQPKGIMGMFASKAAAKTQETNKETKTEAKEVTNASAAGNKAPGKGNMMSNFFGKAAMNKFKVNLDSEQAVKEEKIVEQPTVSVTEPKLATPAGLKKSSKKAEPVKVLQKEKKRGKRVALSDDETKETENMRKKRRRIKLPESDSSEDEVFPDSPGAYEAESPSPPPPPSPPLEPVPKTEPEPPSVKSSSGENKRKRKRVLKSKTYLDGEGCIVTEKVYESESCTDSEEELNMKTSSVHRPPAMTVKKEPREERKGPKKGTAALGKANRQVSITGFFQRK
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------MADQLYLEN
------CCCCEEECC		17.1622223895
42PhosphorylationNQAKQMLYDYVERKR
HHHHHHHHHHHHHHH		10.4122817900
44PhosphorylationAKQMLYDYVERKRKE
HHHHHHHHHHHHHHH		7.2222817900
90PhosphorylationDKLEAVKSKLAVTAS
HHHHHHHHHHHHEEE		26.7120044836
95PhosphorylationVKSKLAVTASIHVYS
HHHHHHHEEEEEEEH		14.7420044836
101PhosphorylationVTASIHVYSIQKAML
HEEEEEEEHHHHHHH		5.9620044836
109UbiquitinationSIQKAMLKDSGPLFN
HHHHHHHHCCCCCCC		36.44-
117PhosphorylationDSGPLFNTDYDILKS
CCCCCCCCCHHHHHH		28.7128796482
119PhosphorylationGPLFNTDYDILKSNL
CCCCCCCHHHHHHHH		11.6628796482
123UbiquitinationNTDYDILKSNLQNCS
CCCHHHHHHHHCCCC		37.32-
124PhosphorylationTDYDILKSNLQNCSK
CCHHHHHHHHCCCCC		39.0528348404
130PhosphorylationKSNLQNCSKFSAIQC
HHHHCCCCCCCHHHH		44.2630576142
131SumoylationSNLQNCSKFSAIQCA
HHHCCCCCCCHHHHH		45.60-
131UbiquitinationSNLQNCSKFSAIQCA
HHHCCCCCCCHHHHH		45.60-
131SumoylationSNLQNCSKFSAIQCA
HHHCCCCCCCHHHHH		45.60-
131AcetylationSNLQNCSKFSAIQCA
HHHCCCCCCCHHHHH		45.6025953088
133PhosphorylationLQNCSKFSAIQCAAA
HCCCCCCCHHHHHHC		28.3525814448
137GlutathionylationSKFSAIQCAAAVPRA
CCCCHHHHHHCCCCC		1.9722555962
148PhosphorylationVPRAPAESSSSSKKF
CCCCCCCCCCCCHHH		37.3125852190
149PhosphorylationPRAPAESSSSSKKFE
CCCCCCCCCCCHHHH		26.2425852190
150PhosphorylationRAPAESSSSSKKFEQ
CCCCCCCCCCHHHHH		48.1625852190
151PhosphorylationAPAESSSSSKKFEQS
CCCCCCCCCHHHHHH		48.3930576142
152PhosphorylationPAESSSSSKKFEQSH
CCCCCCCCHHHHHHH		41.6425852190
173PhosphorylationTQANNELTTNGHGPP
HHHCCCCCCCCCCCC		16.4322210691
174PhosphorylationQANNELTTNGHGPPA
HHCCCCCCCCCCCCC		52.4022210691
199AcetylationIMGMFASKAAAKTQE
HHHHHHHHHHHHHHH		38.3225953088
203AcetylationFASKAAAKTQETNKE
HHHHHHHHHHHCCCH		46.127407547
207PhosphorylationAAAKTQETNKETKTE
HHHHHHHCCCHHHHH		41.60-
213PhosphorylationETNKETKTEAKEVTN
HCCCHHHHHHHHHHC		48.9028509920
216SumoylationKETKTEAKEVTNASA
CHHHHHHHHHHCHHH		46.62-
216SumoylationKETKTEAKEVTNASA
CHHHHHHHHHHCHHH		46.62-
216AcetylationKETKTEAKEVTNASA
CHHHHHHHHHHCHHH		46.6221339330
219PhosphorylationKTEAKEVTNASAAGN
HHHHHHHHCHHHCCC		26.5923532336
222PhosphorylationAKEVTNASAAGNKAP
HHHHHCHHHCCCCCC		22.2629255136
227AcetylationNASAAGNKAPGKGNM
CHHHCCCCCCCCCCH		55.8521339330
231SumoylationAGNKAPGKGNMMSNF
CCCCCCCCCCHHHHH		46.16-
231SumoylationAGNKAPGKGNMMSNF
CCCCCCCCCCHHHHH		46.16-
241AcetylationMMSNFFGKAAMNKFK
HHHHHHHHHHHHHHC		28.0221339330
246AcetylationFGKAAMNKFKVNLDS
HHHHHHHHHCCCCCH		33.2125953088
248MethylationKAAMNKFKVNLDSEQ
HHHHHHHCCCCCHHH		31.64115975241
253PhosphorylationKFKVNLDSEQAVKEE
HHCCCCCHHHHHHHH		34.4721406692
258AcetylationLDSEQAVKEEKIVEQ
CCHHHHHHHHHHCCC		64.2726051181
258SumoylationLDSEQAVKEEKIVEQ
CCHHHHHHHHHHCCC		64.2716934752
258SumoylationLDSEQAVKEEKIVEQ
CCHHHHHHHHHHCCC		64.27-
261SumoylationEQAVKEEKIVEQPTV
HHHHHHHHHCCCCCE		53.8228112733
267PhosphorylationEKIVEQPTVSVTEPK
HHHCCCCCEECCCCC		25.7123532336
269PhosphorylationIVEQPTVSVTEPKLA
HCCCCCEECCCCCCC		26.2925159151
274SumoylationTVSVTEPKLATPAGL
CEECCCCCCCCCCCC		44.51-
274SumoylationTVSVTEPKLATPAGL
CEECCCCCCCCCCCC		44.51-
277PhosphorylationVTEPKLATPAGLKKS
CCCCCCCCCCCCCCC		24.9025159151
282AcetylationLATPAGLKKSSKKAE
CCCCCCCCCCCCCCC		50.0925953088
2822-HydroxyisobutyrylationLATPAGLKKSSKKAE
CCCCCCCCCCCCCCC		50.09-
284PhosphorylationTPAGLKKSSKKAEPV
CCCCCCCCCCCCCCC		45.8921712546
286AcetylationAGLKKSSKKAEPVKV
CCCCCCCCCCCCCHH		64.1971167
287AcetylationGLKKSSKKAEPVKVL
CCCCCCCCCCCCHHH		60.9971159
292AcetylationSKKAEPVKVLQKEKK
CCCCCCCHHHHHHHH		48.2025953088
298AcetylationVKVLQKEKKRGKRVA
CHHHHHHHHCCCCCC		55.6071163
302AcetylationQKEKKRGKRVALSDD
HHHHHCCCCCCCCCC		47.9771155
307PhosphorylationRGKRVALSDDETKET
CCCCCCCCCCCCHHH		33.0229255136
311PhosphorylationVALSDDETKETENMR
CCCCCCCCHHHHHHH		40.9722167270
314PhosphorylationSDDETKETENMRKKR
CCCCCHHHHHHHHHH		33.9323927012
329PhosphorylationRRIKLPESDSSEDEV
HHCCCCCCCCCCCCC		40.6325137130
331PhosphorylationIKLPESDSSEDEVFP
CCCCCCCCCCCCCCC		44.9325137130
332PhosphorylationKLPESDSSEDEVFPD
CCCCCCCCCCCCCCC		54.8025137130
340PhosphorylationEDEVFPDSPGAYEAE
CCCCCCCCCCCCCCC		26.0225137130
344PhosphorylationFPDSPGAYEAESPSP
CCCCCCCCCCCCCCC		22.9125137130
348PhosphorylationPGAYEAESPSPPPPP
CCCCCCCCCCCCCCC		37.4125137130
350PhosphorylationAYEAESPSPPPPPSP
CCCCCCCCCCCCCCC		60.3625137130
356PhosphorylationPSPPPPPSPPLEPVP
CCCCCCCCCCCCCCC		44.9425137130
371PhosphorylationKTEPEPPSVKSSSGE
CCCCCCCCCCCCCCC		53.5525159151
374PhosphorylationPEPPSVKSSSGENKR
CCCCCCCCCCCCCHH		27.8120044836
375PhosphorylationEPPSVKSSSGENKRK
CCCCCCCCCCCCHHH		36.3220044836
405PhosphorylationCIVTEKVYESESCTD
EEEEEEEEECCCCCC		25.4625137130
407PhosphorylationVTEKVYESESCTDSE
EEEEEEECCCCCCCH		19.6825072903
409PhosphorylationEKVYESESCTDSEEE
EEEEECCCCCCCHHH		31.4325159151
411PhosphorylationVYESESCTDSEEELN
EEECCCCCCCHHHHH		52.4125159151
413PhosphorylationESESCTDSEEELNMK
ECCCCCCCHHHHHCC		28.8425159151
421PhosphorylationEEELNMKTSSVHRPP
HHHHHCCCCCCCCCC		18.5723186163
422PhosphorylationEELNMKTSSVHRPPA
HHHHCCCCCCCCCCC		25.5023186163
423PhosphorylationELNMKTSSVHRPPAM
HHHCCCCCCCCCCCC		27.4623401153
433SumoylationRPPAMTVKKEPREER
CCCCCCCCCCCHHHC		42.10-
433SumoylationRPPAMTVKKEPREER
CCCCCCCCCCCHHHC		42.1016934752
444SumoylationREERKGPKKGTAALG
HHHCCCCCCCHHHHH		72.93-
444AcetylationREERKGPKKGTAALG
HHHCCCCCCCHHHHH		72.9312429967
452AcetylationKGTAALGKANRQVSI
CCHHHHHHHCCEEEE		43.2525953088
458PhosphorylationGKANRQVSITGFFQR
HHHCCEEEEEEEEEC		13.1922617229
460PhosphorylationANRQVSITGFFQRK-
HCCEEEEEEEEECC-		22.0423403867
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
458SPhosphorylationKinasePRKACAP17612
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
458SPhosphorylation

18669648
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 DPOD3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PCNA_HUMANPCNAphysical
11595739
PCNA_SCHPOpcn1physical
16000169
DPOD2_HUMANPOLD2physical
16000169
PCNA_HUMANPCNAphysical
16000169
DPOD1_HUMANPOLD1physical
11328591
DPOD2_HUMANPOLD2physical
11328591
PCNA_HUMANPCNAphysical
16763556
SPRTN_HUMANSPRTNphysical
22902628
A4_HUMANAPPphysical
21832049
DPOLA_HUMANPOLA1physical
22939629
MCM3_HUMANMCM3physical
22939629
PCNA_HUMANPCNAphysical
16510448
REV1_HUMANREV1physical
23254330
MD2L2_HUMANMAD2L2physical
23254330
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
There are no disease associations of PTM sites.
Regulatory Network of DPOD3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND MASSSPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-277 AND SER-307, ANDMASS SPECTROMETRY.
"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 SER-307; SER-407; SER-409;THR-411; SER-413 AND SER-458, AND MASS SPECTROMETRY.
"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-307, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, 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-307; SER-407; SER-409;THR-411 AND SER-413, AND MASS SPECTROMETRY.

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