DPOE2_HUMAN - dbPTM
DPOE2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPOE2_HUMAN
UniProt AC P56282
Protein Name DNA polymerase epsilon subunit 2
Gene Name POLE2
Organism Homo sapiens (Human).
Sequence Length 527
Subcellular Localization Nucleus.
Protein Description Participates in DNA repair and in chromosomal DNA replication..
Protein Sequence MAPERLRSRALSAFKLRGLLLRGEAIKYLTEALQSISELELEDKLEKIINAVEKQPLSSNMIERSVVEAAVQECSQSVDETIEHVFNIIGAFDIPRFVYNSERKKFLPLLMTNHPAPNLFGTPRDKAEMFRERYTILHQRTHRHELFTPPVIGSHPDESGSKFQLKTIETLLGSTTKIGDAIVLGMITQLKEGKFFLEDPTGTVQLDLSKAQFHSGLYTEACFVLAEGWFEDQVFHVNAFGFPPTEPSSTTRAYYGNINFFGGPSNTSVKTSAKLKQLEEENKDAMFVFLSDVWLDQVEVLEKLRIMFAGYSPAPPTCFILCGNFSSAPYGKNQVQALKDSLKTLADIICEYPDIHQSSRFVFVPGPEDPGFGSILPRPPLAESITNEFRQRVPFSVFTTNPCRIQYCTQEITVFREDLVNKMCRNCVRFPSSNLAIPNHFVKTILSQGHLTPLPLYVCPVYWAYDYALRVYPVPDLLVIADKYDPFTTTNTECLCINPGSFPRSGFSFKVFYPSNKTVEDSKLQGF
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
15UbiquitinationSRALSAFKLRGLLLR
HHHHHHHHHHHHHHH		36.6723000965
44UbiquitinationSELELEDKLEKIINA
HHCCHHHHHHHHHHH		49.5229967540
47UbiquitinationELEDKLEKIINAVEK
CHHHHHHHHHHHHHH		60.3629967540
54UbiquitinationKIINAVEKQPLSSNM
HHHHHHHHCCCCCCH		51.0921906983
59PhosphorylationVEKQPLSSNMIERSV
HHHCCCCCCHHHHHH		37.7924114839
85UbiquitinationVDETIEHVFNIIGAF
HHHHHHHHHHHHHHH		2.2622817900
89UbiquitinationIEHVFNIIGAFDIPR
HHHHHHHHHHHCCCC		3.2321963094
99PhosphorylationFDIPRFVYNSERKKF
HCCCCEEEECCCHHH		15.4022817900
105UbiquitinationVYNSERKKFLPLLMT
EEECCCHHHHHHHHC		59.35-
112PhosphorylationKFLPLLMTNHPAPNL
HHHHHHHCCCCCCCC		30.28-
114UbiquitinationLPLLMTNHPAPNLFG
HHHHHCCCCCCCCCC		15.6721963094
117UbiquitinationLMTNHPAPNLFGTPR
HHCCCCCCCCCCCHH		42.3722817900
122PhosphorylationPAPNLFGTPRDKAEM
CCCCCCCCHHHHHHH		14.0724719451
126UbiquitinationLFGTPRDKAEMFRER
CCCCHHHHHHHHHHH		47.75-
136UbiquitinationMFRERYTILHQRTHR
HHHHHHHHHHHHCCC		2.1022817900
140UbiquitinationRYTILHQRTHRHELF
HHHHHHHHCCCCCCC		23.0421963094
162UbiquitinationHPDESGSKFQLKTIE
CCCCCCCCCCHHHHH		40.4322817900
165UbiquitinationESGSKFQLKTIETLL
CCCCCCCHHHHHHHH		6.2621963094
166UbiquitinationSGSKFQLKTIETLLG
CCCCCCHHHHHHHHC		36.3521906983
168UbiquitinationSKFQLKTIETLLGST
CCCCHHHHHHHHCCC		3.4922817900
174PhosphorylationTIETLLGSTTKIGDA
HHHHHHCCCCCCCHH		32.6424905233
175PhosphorylationIETLLGSTTKIGDAI
HHHHHCCCCCCCHHH		30.2524905233
176PhosphorylationETLLGSTTKIGDAIV
HHHHCCCCCCCHHHH		23.5124905233
188PhosphorylationAIVLGMITQLKEGKF
HHHHHHHEEECCCCE		20.96-
191AcetylationLGMITQLKEGKFFLE
HHHHEEECCCCEEEE		55.3825953088
191UbiquitinationLGMITQLKEGKFFLE
HHHHEEECCCCEEEE		55.3821906983
193UbiquitinationMITQLKEGKFFLEDP
HHEEECCCCEEEECC		30.4022817900
194UbiquitinationITQLKEGKFFLEDPT
HEEECCCCEEEECCC		33.7521906983
197UbiquitinationLKEGKFFLEDPTGTV
ECCCCEEEECCCCEE		9.0922817900
199UbiquitinationEGKFFLEDPTGTVQL
CCCEEEECCCCEEEE		48.4822817900
244UbiquitinationVNAFGFPPTEPSSTT
EEECCCCCCCCCCCC		47.3222817900
248UbiquitinationGFPPTEPSSTTRAYY
CCCCCCCCCCCEEEE		33.8022817900
250UbiquitinationPPTEPSSTTRAYYGN
CCCCCCCCCEEEECC		25.3322817900
262UbiquitinationYGNINFFGGPSNTSV
ECCEEECCCCCCCCH		42.8622817900
266UbiquitinationNFFGGPSNTSVKTSA
EECCCCCCCCHHHHH		39.2322817900
270UbiquitinationGPSNTSVKTSAKLKQ
CCCCCCHHHHHHHHH		36.2122817900
274UbiquitinationTSVKTSAKLKQLEEE
CCHHHHHHHHHHHHH		56.8622817900
276UbiquitinationVKTSAKLKQLEEENK
HHHHHHHHHHHHHCC		52.7222817900
313UbiquitinationIMFAGYSPAPPTCFI
HHHCCCCCCCCEEEE		40.0622817900
317UbiquitinationGYSPAPPTCFILCGN
CCCCCCCEEEEEECC		20.9922817900
339UbiquitinationKNQVQALKDSLKTLA
HHHHHHHHHHHHHHH		48.5722817900
343UbiquitinationQALKDSLKTLADIIC
HHHHHHHHHHHHHHH		45.5022817900
422UbiquitinationFREDLVNKMCRNCVR
CCHHHHHHHHHHCCC		31.71-
440UbiquitinationSNLAIPNHFVKTILS
CCCCCCCHHHHHHHH		24.4222817900
446UbiquitinationNHFVKTILSQGHLTP
CHHHHHHHHCCCCCC		3.6522505724
462PhosphorylationPLYVCPVYWAYDYAL
CEEECCHHHHHHHHH		3.0227642862
465PhosphorylationVCPVYWAYDYALRVY
ECCHHHHHHHHHEEE		8.7122817900
467PhosphorylationPVYWAYDYALRVYPV
CHHHHHHHHHEEECC		8.5422817900
491UbiquitinationYDPFTTTNTECLCIN
CCCCCCCCCCEEEEC		31.6122817900
497UbiquitinationTNTECLCINPGSFPR
CCCCEEEECCCCCCC		4.4922505724
505PhosphorylationNPGSFPRSGFSFKVF
CCCCCCCCCEEEEEE		44.4124961811
508PhosphorylationSFPRSGFSFKVFYPS
CCCCCCEEEEEEECC		27.9029083192
513PhosphorylationGFSFKVFYPSNKTVE
CEEEEEEECCCCCCC		14.5629759185
515PhosphorylationSFKVFYPSNKTVEDS
EEEEEECCCCCCCCC		39.3129759185
517UbiquitinationKVFYPSNKTVEDSKL
EEEECCCCCCCCCCC		59.2821906983
518PhosphorylationVFYPSNKTVEDSKLQ
EEECCCCCCCCCCCC		33.1229759185
522PhosphorylationSNKTVEDSKLQGF--
CCCCCCCCCCCCC--		23.0429759185
523UbiquitinationNKTVEDSKLQGF---
CCCCCCCCCCCC---		58.0921906983
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 DPOE2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DPOE2_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 DPOE2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SAP18_HUMANSAP18physical
11872158
ERG28_HUMANC14orf1physical
16169070
EF1A1_HUMANEEF1A1physical
16169070
KAT5_HUMANKAT5physical
16169070
TLE1_HUMANTLE1physical
16169070
DPOE4_HUMANPOLE4physical
10801849
DPOE3_HUMANPOLE3physical
10801849
DPOE1_HUMANPOLEphysical
21705323
DPOE3_HUMANPOLE3physical
21705323
DPOD4_HUMANPOLD4physical
21705323
REL_HUMANRELphysical
25416956
TRI27_HUMANTRIM27physical
25416956
TBX15_HUMANTBX15physical
25416956
MARE1_HUMANMAPRE1physical
25416956
PEX19_HUMANPEX19physical
26344197
DPOE4_HUMANPOLE4physical
28514442
DPOE3_HUMANPOLE3physical
28514442
ZBT21_HUMANZBTB21physical
28514442
CP4FC_HUMANCYP4F12physical
28514442
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
DB00242Cladribine
Regulatory Network of DPOE2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-508, AND MASSSPECTROMETRY.

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