REPAIRtoire - a database of DNA repair pathways

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POLE

Protein FULL name:

DNA polymerase epsilon catalytic subunit A [Homo sapiens].


POLE (Homo sapiens) is product of expression of POLE gene.


POLE is involved in:

NER in Homo sapiens BER in Homo sapiens MMR in Homo sapiens
     


Keywords:



FUNCTION: Participates in DNA repair and in chromosomal DNA replication.

CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

SUBUNIT: Consists of two subunits (258 kDa and 55 kDa). Interacts with RAD17 and TOPBP1.

INTERACTION: P49842:STK19; NbExp=1; IntAct=EBI-348526, EBI-347581;

SUBCELLULAR LOCATION: Nucleus.

DOMAIN: The DNA polymerase activity domain resides in the N- terminal half of the protein, while the C-terminus is necessary for complexing subunits B and C. The C-terminus may also regulate the catalytic activities of the enzyme.

PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.

SIMILARITY: Belongs to the DNA polymerase type-B family.

SEQUENCE CAUTION: Sequence=AAA15448.1; Type=Frameshift; Positions=443, 448; Sequence=AAA15448.1; Type=Miscellaneous discrepancy;

WEB RESOURCE: Name=NIEHS-SNPs; [LINK]


NCBI GenPept GI number(s): 62198237
116241339
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q07864 Q07864
PFAM: - Q07864 (Link - using uniprot id)
InterPro: - Q07864 (Link - using uniprot id)
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MSLRSGGRRRADPGADGEASRDDGATSSVSALKRLERSQWTDKMDLRFGF
ERLKEPGEKTGWLINMHPTEILDEDKRLGSAVDYYFIQDDGSRFKVALPY
KPYFYIATRKGCEREVSSFLSKKFQGKIAKVETVPKEDLDLPNHLVGLKR
NYIRLSFHTVEDLVKVRKEISPAVKKNREQDHASDAYTALLSSVLQRGGV
ITDEEETSKKIADQLDNIVDMREYDVPYHIRLSIDLKIHVAHWYNVRYRG
NAFPVEITRRDDLVERPDPVVLAFDIETTKLPLKFPDAETDQIMMISYMI
DGQGYLITNREIVSEDIEDFEFTPKPEYEGPFCVFNEPDEAHLIQRWFEH
VQETKPTIMVTYNGDFFDWPFVEARAAVHGLSMQQEIGFQKDSQGEYKAP
QCIHMDCLRWVKRDSYLPVGSHNLKAAAKAKLGYDPVELDPEDMCRMATE
QPQTLATYSVSDAVATYYLYMKYVHPFIFALCTIIPMEPDEVLRKGSGTL
CEALLMVQAFHANIIFPNKQEQEFNKLTDDGHVLDSETYVGGHVEALESG
VFRSDIPCRFRMNPAAFDFLLQRVEKTLRHALEEEEKVPVEQVTNFEEVC
DEIKSKLASLKDVPSRIECPLIYHLDVGAMYPNIILTNRLQPSAMVDEAT
CAACDFNKPGANCQRKMAWQWRGEFMPASRSEYHRIQHQLESEKFPPLFP
EGPARAFHELSREEQAKYEKRRLADYCRKAYKKIHITKVEERLTTICQRE
NSFYVDTVRAFRDRRYEFKGLHKVWKKKLSAAVEVGDAAEVKRCKNMEVL
YDSLQLAHKCILNSFYGYVMRKGARWYSMEMAGIVCFTGANIITQARELI
EQIGRPLELDTDGIWCVLPNSFPENFVFKTTNVKKPKVTISYPGAMLNIM
VKEGFTNDQYQELAEPSSLTYVTRSENSIFFEVDGPYLAMILPASKEEGK
KLKKRYAVFNEDGSLAELKGFEVKRRGELQLIKIFQSSVFEAFLKGSTLE
EVYGSVAKVADYWLDVLYSKAANMPDSELFELISENRSMSRKLEDYGEQK
STSISTAKRLAEFLGDQMVKDAGLSCRYIISRKPEGSPVTERAIPLAIFQ
AEPTVRKHFLRKWLKSSSLQDFDIRAILDWDYYIERLGSAIQKIITIPAA
LQQVKNPVPRVKHPDWLHKKLLEKNDVYKQKKISELFTLEGRRQVTMAEA
SEDSPRPSAPDMEDFGLVKLPHPAAPVTVKRKRVLWESQEESQDLTPTVP
WQEILGQPPALGTSQEEWLVWLRFHKKKWQLQARQRLARRKRQRLESAEG
VLRPGAIRDGPATGLGSFLRRTARSILDLPWQIVQISETSQAGLFRLWAL
VGSDLHCIRLSIPRVFYVNQRVAKAEEGASYRKVNRVLPRSNMVYNLYEY
SVPEDMYQEHINEINAELSAPDIEGVYETQVPLLFRALVHLGCVCVVNKQ
LVRHLSGWEAETFALEHLEMRSLAQFSYLEPGSIRHIYLYHHAQAHKALF
GIFIPSQRRASVFVLDTVRSNQMPSLGALYSAEHGLLLEKVGPELLPPPK
HTFEVRAETDLKTICRAIQRFLLAYKEERRGPTLIAVQSSWELKRLASEI
PVLEEFPLVPICVADKINYGVLDWQRHGARRMIRHYLNLDTCLSQAFEMS
RYFHIPIGNLPEDISTFGSDLFFARHLQRHNHLLWLSPTARPDLGGKEAD
DNCLVMEFDDQATVEINSSGCYSTVCVELDLQNLAVNTILQSHHVNDMEG
ADSMGISFDVIQQASLEDMITGGQAASAPASYDETALCSNTFRILKSMVV
GWVKEITQYHNIYADNQVMHFYRWLRSPSSLLHDPALHRTLHNMMKKLFL
QLIAEFKRLGSSVIYANFNRIILCTKKRRVEDAIAYVEYITSSIHSKETF
HSLTISFSRCWEFLLWMDPSNYGGIKGKVSSRIHCGLQDSQKAGGAEDEQ
ENEDDEEERDGEEEEEAEESNVEDLLENNWNILQFLPQAASCQNYFLMIV
SAYIVAVYHCMKDGLRRSAPGSTPVRRRGASQLSQEAEGAVGALPGMITF
SQDYVANELTQSFFTITQKIQKKVTGSRNSTELSEMFPVLPGSHLLLNNP
ALEFIKYVCKVLSLDTNITNQVNKLNRDLLRLVDVGEFSEEAQFRDPCRS
YVLPEVICRSCNFCRDLDLCKDSSFSEDGAVLPQWLCSNCQAPYDSSAIE
MTLVEVLQKKLMAFTLQDLVCLKCRGVKETSMPVYCSCAGDFALTIHTQV
FMEQIGIFRNIAQHYGMSYLLETLEWLLQKNPQLGH

POLE (Homo sapiens) is able to recognize following damages:
POLE (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal
Molecular cloning of the cDNA for the catalytic subunit of human DNA polymerase epsilon. Kesti T, Frantti H, Syvaoja JE J Biol Chem May 15, 1993
BRCT domain-containing protein TopBP1 functions in DNA replication and damage response. Makiniemi M, Hillukkala T, Tuusa J, Reini K, Vaara M, Huang D, Pospiech H, Majuri I, Westerling T, Makela TP, Syvaoja JE J Biol Chem Aug. 10, 2001
The human checkpoint Rad protein Rad17 is chromatin-associated throughout the cell cycle, localizes to DNA replication sites, and interacts with DNA polymerase epsilon. Post SM, Tomkinson AE, Lee EY Nucleic Acids Res Oct. 1, 2003
ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ Science May 25, 2007


Last modification of this entry: Oct. 19, 2010.

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