Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  DNA polymerase epsilon subunit 4  

UniProtKB / Swiss-Prot ID :  DPOE4_HUMAN

Gene Name (Synonyms) : 
POLE4  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus (Potential). 

Protein Function :  May play a role in allowing polymerase epsilon to carry out its replication and/or repair function. 

Protein Sequence MAAAAAAGSGTPREEEGPAGEAAASQPQAPTSVPGARLSRLPLARVKALVKADPDVTLAGQEAIFILARA...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCHHHCCCCCCCCCCCCCCCCCCHHHHHHHHHCCCHHHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
17G -> V (in dbSNP:rs12366). VAR_028050
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAAAAA
---CCCCCC
13.05UniProtKB
Link-
11PhosphothreonineAGSGTPREE
CCCCCCCCC
22.37HPRD
Link-
11PhosphothreonineAGSGTPREE
CCCCCCCCC
22.37Phosphositeplus
Link-
11Phosphothreonine.AGSGTPREE
CCCCCCCCC
22.37UniProtKB
Link-
25PhosphoserineEAAASQPQA
CHHHCCCCC
37.35PhosphoELM
Link-
25PhosphoserineEAAASQPQA
CHHHCCCCC
37.35Phosphositeplus
Link-
25Phosphoserine.EAAASQPQA
CHHHCCCCC
37.35UniProtKB
Link-
84S-nitrosocysteineKDAYCCAQQ
HHHHHHHHH
1.34dbSNO
Link-
85S-nitrosocysteineDAYCCAQQG
HHHHHHHHC
2.20dbSNO
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
DPOE3_HUMANphysical interaction
physical interaction
physical interaction
EBI-867043
EBI-867075
EBI-867
intact10801849
10801849
10801849
DPOE3_HUMANin vitroHPRD:16238HPRD10801849
DPOE2_HUMANin vitroHPRD:16238HPRD10801849
DPOE1_HUMANin vitroHPRD:16238HPRD10801849
DPOE2_HUMANENSP00000233699STRING
DPOE1_HUMANENSP00000233699STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB00242Cladribine
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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-11, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-11, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures