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Protein Page:
POLE (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
POLE Participates in DNA repair and in chromosomal DNA replication. Belongs to the DNA polymerase type-B family. Note: This description may include information from UniProtKB.
Protein type: DNA repair, damage; Nucleotide Metabolism - pyrimidine; EC 2.7.7.7; Transferase; Nucleotide Metabolism - purine; DNA replication
Cellular Component: epsilon DNA polymerase complex; nucleoplasm; cytoplasm; nucleolus; plasma membrane; nucleus
Molecular Function: DNA binding; zinc ion binding; 4 iron, 4 sulfur cluster binding; DNA-directed DNA polymerase activity; nucleotide binding; chromatin binding
Biological Process: DNA replication initiation; in utero embryonic development; DNA repair; base-excision repair, gap-filling; telomere maintenance via semi-conservative replication; DNA synthesis during DNA repair; nucleotide-excision repair; transcription-coupled nucleotide-excision repair; telomere maintenance via recombination; mitotic cell cycle; nucleotide-excision repair, DNA gap filling; DNA replication; telomere maintenance; G1/S transition of mitotic cell cycle
Reference #:  Q07864 (UniProtKB)
Alt. Names/Synonyms: DKFZp434F222; DNA polymerase epsilon catalytic subunit A; DNA polymerase II subunit A; DPOE1; FLJ21434; POLE; POLE1; polymerase (DNA directed), epsilon
Gene Symbols: POLE
Molecular weight: 261,518 Da
Basal Isoelectric point: 5.98  Predict pI for various phosphorylation states
Select Structure to View Below

POLE

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 Y84-p RLGSAVDyyFIQDDG
0 1 Y85-p LGSAVDyyFIQDDGS
0 1 Y100-p RFKVALPyKPYFYIA
0 1 S156-p KRNYIRLsFHTVEDL
0 1 G199 SSVLQRGGVItDEEE
0 8 T202-p LQRGGVItDEEETSk
0 1 S208 ItDEEETSkKIADQL
0 1 K209-ub tDEEETSkKIADQLD
0 3 S382-p RAAVHGLsMQQEIGF
0 1 K1050-ub LEDYGEQkSTSISTA
0 2 S1184-p VYKQKKIsELFTLEG
0 1 S1201-p QVTMAEAsEDsPRPS
0 1 S1204-p MAEAsEDsPRPSAPD
0 1 S1297-p RKRQRLEsAEGVLRP
0 2 S1317-p GPATGLGsFLRRTAR
0 1 Y1490-p SIRHIYLyHHAQAHK
0 1 S1797-p NTFRILKsMVVGWVK
0 27 S1940-p IHCGLQDsQKAGGAE
0 4 T2023-p RRSAPGStPVRRRGA
0 1 K2110-ub EFIKYVCkVLSLDTN
0 2 K2124-ub NITNQVNkLNRDLLR
0 1 K2210 LVEVLQKKLMAFtLQ
0 1 T2215-p QKKLMAFtLQDLVCL
0 1 - gap
0 1 - gap
  POLE iso2  
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
K3 _____VNKLNRDLLR
K89 LVEVLQKKLMAFTLQ
T94 QKKLMAFTLQDLkEA
K99-ac AFTLQDLkEADTPKC
K113-ac CEEKERRkRELRSSA
  mouse

 
Y84 RLVSAVDYYFIQDDG
Y85 LVSAVDYYFIQDDGS
Y100 RFKVALPYMPYFYIA
S156 KRSYIKLSFHTVEDL
S199 SSILQGGSVITDEDE
T202 LQGGSVITDEDETSK
S208 ITDEDETSKKIADQL
K209 TDEDETSKKIADQLD
S382 RAAIHGLSMYQEIGF
K1050 LEDYGEQKSTSISTA
S1184 IYKQKKISELFVLEG
S1201 QIVMAQASENSLSLC
S1204 MAQASENSLSLCTPD
S1296 RKKQRLESAEDMPRL
S1316 GPSTGLGSFLRRTAR
Y1489 SIRHIYLYHHTQGHK
S1796 STFRILKSMVVGWVK
E1939 IHCGQVKEQDSQARE
T2020 RHSAPGSTPVKRKGA
K2107 EFIKYVCKVLSLDTN
K2121 NITNQVNKLNRDLLR
K2207-ac LVEALQRkLMAFTLQ
T2212 QRkLMAFTLQDLVCL
- gap
- gap
  rat

 
Y84 RLVSAVDYYFIQDDG
Y85 LVSAVDYYFIQDDGS
Y100 RFKVALPYKPYFYIA
S156 KRSYIKLSFHTVEDL
S199-p SSILQGGsLItDEEE
T202-p LQGGsLItDEEETsK
S208-p ItDEEETsKKIADQL
K209 tDEEETsKKIADQLD
S382 RAAIHGLSMYQEIGF
K1053 LEDYGEQKSTSISTA
S1187 IYKQKKISELFVLEG
S1204 QIVMAQASENSLSLC
S1207 MAQASENSLSLCTPD
S1299 RKKQRLESAEDMPRL
S1319 GPATGLGSFLRRTAR
Y1492 SIRHIYLYHHTQGHK
S1799 STFRILKSMVVGWVK
E1942 IHCGQVREQDSQTRE
T2023 RHSAPGSTPVKRKGA
K2110 EFIKYVCKVLSLDTN
K2124 NITNQVNKLNRDLLR
K2210 LVEALQRKLMAFTLQ
T2215 QRKLMAFTLQDLVCL
- gap
- gap
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