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

UniProtKB / Swiss-Prot ID :  DPOLB_HUMAN

Gene Name (Synonyms) : 
POLB  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. Cytoplasm. Note=Cytoplasmic in normal conditions. Translocates to the nucleus following DNA damage. 

Protein Function :  Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. Conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. 

Protein Sequence MSKRKAPQETLNGGITDMLTELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAKKLPGVGTKIA...
Predicted Secondary Structure CCCCCCCCCCCCHHHHHHHHHHHHHHHHHHCCHHHHHHHHHHHHHHHHCCCCCCCHHHHCCCCCCCHHHH...
Protein Variant
LocationDescription
242P -> R (in dbSNP:rs3136797). VAR_018881
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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
41Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NAYRKAASV
HHHHHHHHH
35.31Phosphositeplus
Link
41Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin).NAYRKAASV
HHHHHHHHH
35.31UniProtKB
Link
44PhosphoserineRKAASVIAK
HHHHHHHHH
20.93HPRD
Link
55PhosphoserineHKIKSGAEA
CCCCCHHHH
46.86HPRD
Link
61Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AEAKKLPGV
HHHCCCCCC
67.95Phosphositeplus
Link
61Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin).AEAKKLPGV
HHHCCCCCC
67.95UniProtKB
Link
72N6-acetyllysineKIAEKIDEF
HHHHHHHHH
46.57Phosphositeplus
Link
81Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LATGKLRKL
HHCCCCHHH
40.54Phosphositeplus
Link
81Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin).LATGKLRKL
HHCCCCHHH
40.54UniProtKB
Link
835-methylarginineTGKLRKLEK
CCCCHHHHH
45.02Phosphositeplus
Link
83Omega-N-methylarginine; by PRMT6.TGKLRKLEK
CCCCHHHHH
45.02UniProtKB
Link
1525-methylarginineKRIPREEML
CCCCHHHHH
50.57Phosphositeplus
Link
152Omega-N-methylarginine; by PRMT6.KRIPREEML
CCCCHHHHH
50.57UniProtKB
Link
250PhosphotyrosineDEKEYPHRR
CCCCCCEEE
18.53Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
APEX1_HUMANphysical interactionMINT-14903MINT9207062
JOSD3_HUMANphysical interaction
physical interaction
physical interaction
colocalization
EBI-1540813
EBI-1540795
EBI-1
intact15520167
15520167
15520167
15520167
TLE1_HUMANphysical interactionEBI-732893
intact16169070
MYST2_HUMANphysical interactionEBI-730540
intact16169070
APEX1_HUMANin vitroHPRD:07517HPRD9207062
KPCA_HUMANin vitroHPRD:07517HPRD2040602
PCNA_HUMANin vivo
yeast 2-hybrid
HPRD:07517HPRD12063248
XRCC1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:07517HPRD8978692
11467963
TLE1_HUMANyeast 2-hybridHPRD:07517HPRD16169070
APEX1_HUMANENSP00000265421STRING
DPOD2_HUMANENSP00000265421STRING
DPOD1_HUMANENSP00000265421STRING
XRCC1_HUMANENSP00000265421STRING
DNL1_HUMANENSP00000265421STRING
DPOD3_HUMANENSP00000265421STRING
DPOD4_HUMANENSP00000265421STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
DrugBank
DB00987Cytarabine
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Related Literatures of Post-Translational Modification
Methylation
ReferencePubMed
"Arginine methylation regulates DNA polymerase beta.";
El-Andaloussi N., Valovka T., Toueille M., Steinacher R., Focke F.,Gehrig P., Covic M., Hassa P.O., Schaer P., Huebscher U.,Hottiger M.O.;
Mol. Cell 22:51-62(2006).
Cited for: METHYLATION AT ARG-83 AND ARG-152 BY PRMT6, AND MUTAGENESIS OF ARG-83AND ARG-152.
Ubiquitylation
ReferencePubMed
"Ubiquitin ligase ARF-BP1/Mule modulates base excision repair.";
Parsons J.L., Tait P.S., Finch D., Dianova I.I., Edelmann M.J.,Khoronenkova S.V., Kessler B.M., Sharma R.A., McKenna W.G.,Dianov G.L.;
EMBO J. 28:3207-3215(2009).
Cited for: SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-41; LYS-61 AND LYS-81, ANDMUTAGENESIS OF LYS-41; LYS-61 AND LYS-81.
"USP47 is a deubiquitylating enzyme that regulates base excisionrepair by controlling steady-state levels of DNA Polymerase beta.";
Parsons J.L., Dianova I.I., Khoronenkova S.V., Edelmann M.J.,Kessler B.M., Dianov G.L.;
Mol. Cell 41:609-615(2011).
Cited for: FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-41; LYS-61 ANDLYS-81, DEUBIQUITINATION BY USP47, AND INTERACTION WITH USP47.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures