DPOD1_HUMAN - dbPTM
DPOD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPOD1_HUMAN
UniProt AC P28340
Protein Name DNA polymerase delta catalytic subunit
Gene Name POLD1
Organism Homo sapiens (Human).
Sequence Length 1107
Subcellular Localization Nucleus . Colocalizes with PCNA and POLD3 at S phase replication sites (PubMed:11595739). After UV irradiation, recruited to DNA damage sites within 2 hours, independently on the cell cycle phase, nor on PCNA ubiquitination. This recruitement require
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. [PubMed: 16510448]
Protein Sequence MDGKRRPGPGPGVPPKRARGGLWDDDDAPRPSQFEEDLALMEEMEAEHRLQEQEEEELQSVLEGVADGQVPPSAIDPRWLRPTPPALDPQTEPLIFQQLEIDHYVGPAQPVPGGPPPSRGSVPVLRAFGVTDEGFSVCCHIHGFAPYFYTPAPPGFGPEHMGDLQRELNLAISRDSRGGRELTGPAVLAVELCSRESMFGYHGHGPSPFLRITVALPRLVAPARRLLEQGIRVAGLGTPSFAPYEANVDFEIRFMVDTDIVGCNWLELPAGKYALRLKEKATQCQLEADVLWSDVVSHPPEGPWQRIAPLRVLSFDIECAGRKGIFPEPERDPVIQICSLGLRWGEPEPFLRLALTLRPCAPILGAKVQSYEKEEDLLQAWSTFIRIMDPDVITGYNIQNFDLPYLISRAQTLKVQTFPFLGRVAGLCSNIRDSSFQSKQTGRRDTKVVSMVGRVQMDMLQVLLREYKLRSYTLNAVSFHFLGEQKEDVQHSIITDLQNGNDQTRRRLAVYCLKDAYLPLRLLERLMVLVNAVEMARVTGVPLSYLLSRGQQVKVVSQLLRQAMHEGLLMPVVKSEGGEDYTGATVIEPLKGYYDVPIATLDFSSLYPSIMMAHNLCYTTLLRPGTAQKLGLTEDQFIRTPTGDEFVKTSVRKGLLPQILENLLSARKRAKAELAKETDPLRRQVLDGRQLALKVSANSVYGFTGAQVGKLPCLEISQSVTGFGRQMIEKTKQLVESKYTVENGYSTSAKVVYGDTDSVMCRFGVSSVAEAMALGREAADWVSGHFPSPIRLEFEKVYFPYLLISKKRYAGLLFSSRPDAHDRMDCKGLEAVRRDNCPLVANLVTASLRRLLIDRDPEGAVAHAQDVISDLLCNRIDISQLVITKELTRAASDYAGKQAHVELAERMRKRDPGSAPSLGDRVPYVIISAAKGVAAYMKSEDPLFVLEHSLPIDTQYYLEQQLAKPLLRIFEPILGEGRAEAVLLRGDHTRCKTVLTGKVGGLLAFAKRRNCCIGCRTVLSHQGAVCEFCQPRESELYQKEVSHLNALEERFSRLWTQCQRCQGSLHEDVICTSRDCPIFYMRKKVRKDLEDQEQLLRRFGPPGPEAW
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
19MethylationGVPPKRARGGLWDDD
CCCCCCCCCCCCCCC		43.6924129315
32PhosphorylationDDDAPRPSQFEEDLA
CCCCCCCHHHHHHHH		49.1029523821
60PhosphorylationQEEEELQSVLEGVAD
HHHHHHHHHHHHHCC		41.0920873877
73PhosphorylationADGQVPPSAIDPRWL
CCCCCCHHHCCCCCC		31.6120873877
121PhosphorylationGPPPSRGSVPVLRAF
CCCCCCCCCCEEECC		23.3424719451
173PhosphorylationRELNLAISRDSRGGR
HHHHHCCCCCCCCCC		25.1624719451
176PhosphorylationNLAISRDSRGGRELT
HHCCCCCCCCCCCCC		31.5426546556
213PhosphorylationPSPFLRITVALPRLV
CCHHHHHHHHHHHHH		8.0329396449
272UbiquitinationWLELPAGKYALRLKE
EEECCCCEEHHHHHH		29.47-
280UbiquitinationYALRLKEKATQCQLE
EHHHHHHHHHHCCCC		55.96-
284GlutathionylationLKEKATQCQLEADVL
HHHHHHHCCCCCCEE		4.3022555962
314PhosphorylationIAPLRVLSFDIECAG
CCEEEEEEEEEECCC		20.3024905233
319GlutathionylationVLSFDIECAGRKGIF
EEEEEEECCCCCCCC		5.0622555962
323UbiquitinationDIECAGRKGIFPEPE
EEECCCCCCCCCCCC		56.28-
367UbiquitinationCAPILGAKVQSYEKE
CHHHHCCCCCCCCCH		38.72-
373UbiquitinationAKVQSYEKEEDLLQA
CCCCCCCCHHHHHHH		59.16-
414UbiquitinationISRAQTLKVQTFPFL
HHHHHCCCEECCCCH		35.3721906983
434PhosphorylationLCSNIRDSSFQSKQT
HHCCCCCCCCCCCCC		24.1728555341
439UbiquitinationRDSSFQSKQTGRRDT
CCCCCCCCCCCCCCC		40.8921906983
447UbiquitinationQTGRRDTKVVSMVGR
CCCCCCCCHHHHHHH		44.9521906983
447SumoylationQTGRRDTKVVSMVGR
CCCCCCCCHHHHHHH		44.95-
447SumoylationQTGRRDTKVVSMVGR
CCCCCCCCHHHHHHH		44.95-
486UbiquitinationFHFLGEQKEDVQHSI
EEECCCCCHHHCHHH		52.13-
511PhosphorylationTRRRLAVYCLKDAYL
HHHHHHHHHHHHCCH		6.10-
514UbiquitinationRLAVYCLKDAYLPLR
HHHHHHHHHCCHHHH		36.43-
554UbiquitinationLSRGQQVKVVSQLLR
HHCCHHHHHHHHHHH		32.3621906983
557PhosphorylationGQQVKVVSQLLRQAM
CHHHHHHHHHHHHHH		20.3523403867
574SumoylationGLLMPVVKSEGGEDY
CCEEEEEECCCCCCC		42.9228112733
574UbiquitinationGLLMPVVKSEGGEDY
CCEEEEEECCCCCCC		42.92-
574SumoylationGLLMPVVKSEGGEDY
CCEEEEEECCCCCCC		42.92-
581PhosphorylationKSEGGEDYTGATVIE
ECCCCCCCCCCEEEE		11.6329438985
593PhosphorylationVIEPLKGYYDVPIAT
EEECCCCCCCCEEEE		8.5623663014
594PhosphorylationIEPLKGYYDVPIATL
EECCCCCCCCEEEEC		21.0923663014
600PhosphorylationYYDVPIATLDFSSLY
CCCCEEEECCHHHHH		27.8123663014
604PhosphorylationPIATLDFSSLYPSIM
EEEECCHHHHHHHHH		21.0723663014
605PhosphorylationIATLDFSSLYPSIMM
EEECCHHHHHHHHHH		31.7323663014
607PhosphorylationTLDFSSLYPSIMMAH
ECCHHHHHHHHHHHH		9.2523663014
609PhosphorylationDFSSLYPSIMMAHNL
CHHHHHHHHHHHHHC		15.0123663014
618PhosphorylationMMAHNLCYTTLLRPG
HHHHHCHHHHCCCCC		13.1123663014
619PhosphorylationMAHNLCYTTLLRPGT
HHHHCHHHHCCCCCC		15.2423663014
620PhosphorylationAHNLCYTTLLRPGTA
HHHCHHHHCCCCCCH		9.4123663014
648UbiquitinationPTGDEFVKTSVRKGL
CCCCHHHHHHHHCCC		40.1621906983
653UbiquitinationFVKTSVRKGLLPQIL
HHHHHHHCCCHHHHH		52.3221906983
665PhosphorylationQILENLLSARKRAKA
HHHHHHHHHHHHHHH		29.2420873877
676AcetylationRAKAELAKETDPLRR
HHHHHHHHCCCHHHH		74.0019826707
676UbiquitinationRAKAELAKETDPLRR
HHHHHHHHCCCHHHH		74.00-
696PhosphorylationRQLALKVSANSVYGF
CCEEEEEECCCCCCC		21.8327080861
699PhosphorylationALKVSANSVYGFTGA
EEEEECCCCCCCCCC		19.2127080861
710UbiquitinationFTGAQVGKLPCLEIS
CCCCCCCCCCCEEEH		50.85-
732UbiquitinationRQMIEKTKQLVESKY
HHHHHHHHHHHHHCC		53.34-
738UbiquitinationTKQLVESKYTVENGY
HHHHHHHCCEEECCC		31.2821906983
739PhosphorylationKQLVESKYTVENGYS
HHHHHHCCEEECCCC		25.8729496907
746PhosphorylationYTVENGYSTSAKVVY
CEEECCCCCCEEEEE		19.7929496907
750UbiquitinationNGYSTSAKVVYGDTD
CCCCCCEEEEECCCC		31.81-
753PhosphorylationSTSAKVVYGDTDSVM
CCCEEEEECCCCCCC		16.5729496907
783PhosphorylationREAADWVSGHFPSPI
HHHHHHHCCCCCCCE		23.4621406692
788PhosphorylationWVSGHFPSPIRLEFE
HHCCCCCCCEEEEEE		31.8325159151
796UbiquitinationPIRLEFEKVYFPYLL
CEEEEEEEECCCEEE		47.7821906983
806UbiquitinationFPYLLISKKRYAGLL
CCEEEEECCCCCCCC		33.9921890473
806AcetylationFPYLLISKKRYAGLL
CCEEEEECCCCCCCC		33.9925953088
807UbiquitinationPYLLISKKRYAGLLF
CEEEEECCCCCCCCC		43.80-
809PhosphorylationLLISKKRYAGLLFSS
EEEECCCCCCCCCCC		17.56-
815PhosphorylationRYAGLLFSSRPDAHD
CCCCCCCCCCCCCCC		25.9630576142
827UbiquitinationAHDRMDCKGLEAVRR
CCCCCCCCCHHHHHH		63.37-
837GlutathionylationEAVRRDNCPLVANLV
HHHHHCCCCHHHHHH		3.0222555962
845PhosphorylationPLVANLVTASLRRLL
CHHHHHHHHHHHHHH		17.4420068231
847PhosphorylationVANLVTASLRRLLID
HHHHHHHHHHHHHCC		17.0320068231
879PhosphorylationLCNRIDISQLVITKE
HCCCCCHHHHHHHHH		17.4524732914
884PhosphorylationDISQLVITKELTRAA
CHHHHHHHHHHHHHH		15.8123403867
885UbiquitinationISQLVITKELTRAAS
HHHHHHHHHHHHHHH		39.3321906983
892PhosphorylationKELTRAASDYAGKQA
HHHHHHHHHHCHHHH		30.1226546556
8972-HydroxyisobutyrylationAASDYAGKQAHVELA
HHHHHCHHHHHHHHH		35.82-
897UbiquitinationAASDYAGKQAHVELA
HHHHHCHHHHHHHHH		35.8221906983
909UbiquitinationELAERMRKRDPGSAP
HHHHHHHHCCCCCCC		52.3821906983
914PhosphorylationMRKRDPGSAPSLGDR
HHHCCCCCCCCCCCC		42.2518669648
917PhosphorylationRDPGSAPSLGDRVPY
CCCCCCCCCCCCCCE		44.7118669648
921MethylationSAPSLGDRVPYVIIS
CCCCCCCCCCEEEEE		29.52115488057
931UbiquitinationYVIISAAKGVAAYMK
EEEEECCCCHHHHHC		54.34-
938UbiquitinationKGVAAYMKSEDPLFV
CCHHHHHCCCCCEEE		37.71-
938SumoylationKGVAAYMKSEDPLFV
CCHHHHHCCCCCEEE		37.71-
964UbiquitinationYLEQQLAKPLLRIFE
HHHHHCHHHHHHHHH		44.80-
985MethylationRAEAVLLRGDHTRCK
CEEEEEECCCCCCCE		44.31115488051
992UbiquitinationRGDHTRCKTVLTGKV
CCCCCCCEEEECCCH		38.08-
993PhosphorylationGDHTRCKTVLTGKVG
CCCCCCEEEECCCHH		25.11-
998AcetylationCKTVLTGKVGGLLAF
CEEEECCCHHHHHHH		32.2625953088
998UbiquitinationCKTVLTGKVGGLLAF
CEEEECCCHHHHHHH		32.2621906983
1007UbiquitinationGGLLAFAKRRNCCIG
HHHHHHHHHCCCEEC		45.4921906983
1007AcetylationGGLLAFAKRRNCCIG
HHHHHHHHHCCCEEC		45.4919608861
1017PhosphorylationNCCIGCRTVLSHQGA
CCEECCCCHHHCCCC		29.8527080861
1020PhosphorylationIGCRTVLSHQGAVCE
ECCCCHHHCCCCEEC		14.9327080861
1039UbiquitinationRESELYQKEVSHLNA
CCCHHHHHHHHHHHH		46.6721906983
1064PhosphorylationQCQRCQGSLHEDVIC
HHHHCCCCCCCCEEE		10.7322210691
1072PhosphorylationLHEDVICTSRDCPIF
CCCCEEEECCCCCEE		18.7022210691
1073PhosphorylationHEDVICTSRDCPIFY
CCCEEEECCCCCEEE		23.0122210691
1080PhosphorylationSRDCPIFYMRKKVRK
CCCCCEEEEEHHHHC		9.2022210691
1087UbiquitinationYMRKKVRKDLEDQEQ
EEEHHHHCCHHHHHH		70.4321906983
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 DPOD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DPOD1_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 DPOD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SCG1_HUMANCHGBphysical
16169070
CE126_HUMANKIAA1377physical
16169070
RENT2_HUMANUPF2physical
16488880
RENT1_HUMANUPF1physical
16488880
PCNA_HUMANPCNAphysical
12403614
SLD5_HUMANGINS4physical
21705323
RFA3_HUMANRPA3physical
22939629
RFA2_HUMANRPA2physical
22939629
RFA1_HUMANRPA1physical
22939629
MCM3_HUMANMCM3physical
22939629
PURB_HUMANPURBphysical
22939629
CDK2_HUMANCDK2physical
9545286
PCNA_HUMANPCNAphysical
16510448
DPOD2_HUMANPOLD2physical
16510448
DPOD4_HUMANPOLD4physical
16510448
TBD2A_HUMANTBC1D2physical
22863883
TBCD4_HUMANTBC1D4physical
22863883
WDR44_HUMANWDR44physical
22863883
DPOD2_HUMANPOLD2physical
26344197
2A5G_HUMANPPP2R5Cphysical
26344197
DPOD2_HUMANPOLD2physical
26496610
DPOD3_HUMANPOLD3physical
26496610
GAR1_HUMANGAR1physical
26496610
OTU1_HUMANYOD1physical
26496610
DPOD4_HUMANPOLD4physical
26496610
CRTC3_HUMANCRTC3physical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612591Colorectal cancer 10 (CRCS10)
615381Mandibular hypoplasia, deafness, progeroid features, and lipodystrophy syndrome (MDPL)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DPOD1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1007, 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 SER-914 AND SER-917, ANDMASS SPECTROMETRY.

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