POL2/YNL262W Protein Information

Standard Name	Pol2p 1
Systematic Name	Ynl262wp
Alias	Dun2p 2
ORF Classification	Verified
Description	Catalytic subunit of DNA polymerase (II) epsilon, a chromosomal DNA replication polymerase that exhibits processivity and proofreading exonuclease activity; also involved in DNA synthesis during DNA repair; interacts extensively with Mrc1p (3, 4, 5)
Name Description	POLymerase 1

Experimental Data
Molecules/cell	1970 6

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	2,222
Molecular Weight (Da)	255,669
Isoelectric Point (pI)	6.92

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Pol2p (InterPro)
Physical Interactions	There are 103 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI00001297C9 \| P21951 MIPS: YNL262W NCBI: 1045247 \| 118841 \| 1302317 \| 171409 \| 6324067 \| NP_014137.1 GenBank/EMBL/DDBJ: DAA10297.1 \| M60416 \| X92494 \| Z71538
External Classifications	EC: 2.7.7.7 [DNA-directed DNA polymerase]

Amino Acid Sequence (or in FASTA format)
1 MMFGKKKNNG GSSTARYSAG NKYNTLSNNY ALSAQQLLNA SKIDDIDSMM 51 GFERYVPPQY NGRFDAKDID QIPGRVGWLT NMHATLVSQE TLSSGSNGGG 101 NSNDGERVTT NQGISGVDFY FLDEEGGSFK STVVYDPYFF IACNDESRVN 151 DVEELVKKYL ESCLKSLQII RKEDLTMDNH LLGLQKTLIK LSFVNSNQLF 201 EARKLLRPIL QDNANNNVQR NIYNVAANGS EKVDAKHLIE DIREYDVPYH 251 VRVSIDKDIR VGKWYKVTQQ GFIEDTRKIA FADPVVMAFD IETTKPPLKF 301 PDSAVDQIMM ISYMIDGEGF LITNREIISE DIEDFEYTPK PEYPGFFTIF 351 NENDEVALLQ RFFEHIRDVR PTVISTFNGD FFDWPFIHNR SKIHGLDMFD 401 EIGFAPDAEG EYKSSYCSHM DCFRWVKRDS YLPQGSQGLK AVTQSKLGYN 451 PIELDPELMT PYAFEKPQHL SEYSVSDAVA TYYLYMKYVH PFIFSLCTII 501 PLNPDETLRK GTGTLCEMLL MVQAYQHNIL LPNKHTDPIE RFYDGHLLES 551 ETYVGGHVES LEAGVFRSDL KNEFKIDPSA IDELLQELPE ALKFSVEVEN 601 KSSVDKVTNF EEIKNQITQK LLELKENNIR NELPLIYHVD VASMYPNIMT 651 TNRLQPDSIK AERDCASCDF NRPGKTCARK LKWAWRGEFF PSKMDEYNMI 701 KRALQNETFP NKNKFSKKKV LTFDELSYAD QVIHIKKRLT EYSRKVYHRV 751 KVSEIVEREA IVCQRENPFY VDTVKSFRDR RYEFKGLAKT WKGNLSKIDP 801 SDKHARDEAK KMIVLYDSLQ LAHKVILNSF YGYVMRKGSR WYSMEMAGIT 851 CLTGATIIQM ARALVERVGR PLELDTDGIW CILPKSFPET YFFTLENGKK 901 LYLSYPCSML NYRVHQKFTN HQYQELKDPL NYIYETHSEN TIFFEVDGPY 951 KAMILPSSKE EGKGIKKRYA VFNEDGSLAE LKGFELKRRG ELQLIKNFQS 1001 DIFKVFLEGD TLEGCYSAVA SVCNRWLDVL DSHGLMLEDE DLVSLICENR 1051 SMSKTLKEYE GQKSTSITTA RRLGDFLGED MVKDKGLQCK YIISSKPFNA 1101 PVTERAIPVA IFSADIPIKR SFLRRWTLDP SLEDLDIRTI IDWGYYRERL 1151 GSAIQKIITI PAALQGVSNP VPRVEHPDWL KRKIATKEDK FKQTSLTKFF 1201 SKTKNVPTMG KIKDIEDLFE PTVEEDNAKI KIARTTKKKA VSKRKRNQLT 1251 NEEDPLVLPS EIPSMDEDYV GWLNYQKIKW KIQARDRKRR DQLFGNTNSS 1301 RERSALGSMI RKQAESYANS TWEVLQYKDS GEPGVLEVFV TINGKVQNIT 1351 FHIPKTIYMK FKSQTMPLQK IKNCLIEKSS ASLPNNPKTS NPAGGQLFKI 1401 TLPESVFLEE KENCTSIFND ENVLGVFEGT ITPHQRAIMD LGASVTFRSK 1451 AMGALGKGIQ QGFEMKDLSM AENERYLSGF SMDIGYLLHF PTSIGYEFFS 1501 LFKSWGDTIT ILVLKPSNQA QEINASSLGQ IYKQMFEKKK GKIETYSYLV 1551 DIKEDINFEF VYFTDISKLY RRLSQETTKL KEERGLQFLL LLQSPFITKL 1601 LGTIRLLNQM PIVKLSLNEV LLPQLNWQPT LLKKLVNHVL SSGSWISHLI 1651 KLSQYSNIPI CNLRLDSMDY IIDVLYARKL KKENIVLWWN EKAPLPDHGG 1701 IQNDFDLNTS WIMNDSEFPK INNSGVYDNV VLDVGVDNLT VNTILTSALI 1751 NDAEGSDLVN NNMGIDDKDA VINSPSEFVH DAFSNDALNV LRGMLKEWWD 1801 EALKENSTAD LLVNSLASWV QNPNAKLFDG LLRYHVHNLT KKALLQLVNE 1851 FSALGSTIVY ADRNQILIKT NKYSPENCYA YSQYMMKAVR TNPMFSYLDL 1901 NIKRYWDLLI WMDKFNFSGL ACIEIEEKEN QDYTAVSQWQ LKKFLSPIYQ 1951 PEFEDWMMII LDSMLKTKQS YLKLNSGTQR PTQIVNVKKQ DKEDSVENSL 2001 NGFSHLFSKP LMKRVKKLFK NQQEFILDPQ YEADYVIPVL PGSHLNVKNP 2051 LLELVKSLCH VMLLSKSTIL EIRTLRKELL KIFELREFAK VAEFKDPSLS 2101 LVVPDFLCEY CFFISDIDFC KAAPESIFSC VRCHKAFNQV LLQEHLIQKL 2151 RSDIESYLIQ DLRCSRCHKV KRDYMSAHCP CAGAWEGTLP RESIVQKLNV 2201 FKQVAKYYGF DILLSCIADL TI*

Amino Acid Sequence (or in FASTA format)

       1  MMFGKKKNNG GSSTARYSAG NKYNTLSNNY ALSAQQLLNA SKIDDIDSMM
      51  GFERYVPPQY NGRFDAKDID QIPGRVGWLT NMHATLVSQE TLSSGSNGGG
     101  NSNDGERVTT NQGISGVDFY FLDEEGGSFK STVVYDPYFF IACNDESRVN
     151  DVEELVKKYL ESCLKSLQII RKEDLTMDNH LLGLQKTLIK LSFVNSNQLF
     201  EARKLLRPIL QDNANNNVQR NIYNVAANGS EKVDAKHLIE DIREYDVPYH
     251  VRVSIDKDIR VGKWYKVTQQ GFIEDTRKIA FADPVVMAFD IETTKPPLKF
     301  PDSAVDQIMM ISYMIDGEGF LITNREIISE DIEDFEYTPK PEYPGFFTIF
     351  NENDEVALLQ RFFEHIRDVR PTVISTFNGD FFDWPFIHNR SKIHGLDMFD
     401  EIGFAPDAEG EYKSSYCSHM DCFRWVKRDS YLPQGSQGLK AVTQSKLGYN
     451  PIELDPELMT PYAFEKPQHL SEYSVSDAVA TYYLYMKYVH PFIFSLCTII
     501  PLNPDETLRK GTGTLCEMLL MVQAYQHNIL LPNKHTDPIE RFYDGHLLES
     551  ETYVGGHVES LEAGVFRSDL KNEFKIDPSA IDELLQELPE ALKFSVEVEN
     601  KSSVDKVTNF EEIKNQITQK LLELKENNIR NELPLIYHVD VASMYPNIMT
     651  TNRLQPDSIK AERDCASCDF NRPGKTCARK LKWAWRGEFF PSKMDEYNMI
     701  KRALQNETFP NKNKFSKKKV LTFDELSYAD QVIHIKKRLT EYSRKVYHRV
     751  KVSEIVEREA IVCQRENPFY VDTVKSFRDR RYEFKGLAKT WKGNLSKIDP
     801  SDKHARDEAK KMIVLYDSLQ LAHKVILNSF YGYVMRKGSR WYSMEMAGIT
     851  CLTGATIIQM ARALVERVGR PLELDTDGIW CILPKSFPET YFFTLENGKK
     901  LYLSYPCSML NYRVHQKFTN HQYQELKDPL NYIYETHSEN TIFFEVDGPY
     951  KAMILPSSKE EGKGIKKRYA VFNEDGSLAE LKGFELKRRG ELQLIKNFQS
    1001  DIFKVFLEGD TLEGCYSAVA SVCNRWLDVL DSHGLMLEDE DLVSLICENR
    1051  SMSKTLKEYE GQKSTSITTA RRLGDFLGED MVKDKGLQCK YIISSKPFNA
    1101  PVTERAIPVA IFSADIPIKR SFLRRWTLDP SLEDLDIRTI IDWGYYRERL
    1151  GSAIQKIITI PAALQGVSNP VPRVEHPDWL KRKIATKEDK FKQTSLTKFF
    1201  SKTKNVPTMG KIKDIEDLFE PTVEEDNAKI KIARTTKKKA VSKRKRNQLT
    1251  NEEDPLVLPS EIPSMDEDYV GWLNYQKIKW KIQARDRKRR DQLFGNTNSS
    1301  RERSALGSMI RKQAESYANS TWEVLQYKDS GEPGVLEVFV TINGKVQNIT
    1351  FHIPKTIYMK FKSQTMPLQK IKNCLIEKSS ASLPNNPKTS NPAGGQLFKI
    1401  TLPESVFLEE KENCTSIFND ENVLGVFEGT ITPHQRAIMD LGASVTFRSK
    1451  AMGALGKGIQ QGFEMKDLSM AENERYLSGF SMDIGYLLHF PTSIGYEFFS
    1501  LFKSWGDTIT ILVLKPSNQA QEINASSLGQ IYKQMFEKKK GKIETYSYLV
    1551  DIKEDINFEF VYFTDISKLY RRLSQETTKL KEERGLQFLL LLQSPFITKL
    1601  LGTIRLLNQM PIVKLSLNEV LLPQLNWQPT LLKKLVNHVL SSGSWISHLI
    1651  KLSQYSNIPI CNLRLDSMDY IIDVLYARKL KKENIVLWWN EKAPLPDHGG
    1701  IQNDFDLNTS WIMNDSEFPK INNSGVYDNV VLDVGVDNLT VNTILTSALI
    1751  NDAEGSDLVN NNMGIDDKDA VINSPSEFVH DAFSNDALNV LRGMLKEWWD
    1801  EALKENSTAD LLVNSLASWV QNPNAKLFDG LLRYHVHNLT KKALLQLVNE
    1851  FSALGSTIVY ADRNQILIKT NKYSPENCYA YSQYMMKAVR TNPMFSYLDL
    1901  NIKRYWDLLI WMDKFNFSGL ACIEIEEKEN QDYTAVSQWQ LKKFLSPIYQ
    1951  PEFEDWMMII LDSMLKTKQS YLKLNSGTQR PTQIVNVKKQ DKEDSVENSL
    2001  NGFSHLFSKP LMKRVKKLFK NQQEFILDPQ YEADYVIPVL PGSHLNVKNP
    2051  LLELVKSLCH VMLLSKSTIL EIRTLRKELL KIFELREFAK VAEFKDPSLS
    2101  LVVPDFLCEY CFFISDIDFC KAAPESIFSC VRCHKAFNQV LLQEHLIQKL
    2151  RSDIESYLIQ DLRCSRCHKV KRDYMSAHCP CAGAWEGTLP RESIVQKLNV
    2201  FKQVAKYYGF DILLSCIADL TI*

external links for Pol2p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	YPL+
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YeastGFP
Aspergillus (AspGD)	BioPIXIE	MIPS	YeastRC Public Image Repository
Candida (CGD)	CYC2008 (complexes)	Pfam domains
Candida (CandidaDB)	Complexome	YeastRC Structure Prediction (Seattle)
YGOB	DIP
YOGY	GeneMANIA

References cited on this page View Complete Literature Guide for Pol2p

1)	Morrison A, et al. (1990) A third essential DNA polymerase in S. cerevisiae. Cell 62(6):1143-51
2)	Navas TA, et al. (1995) DNA polymerase epsilon links the DNA replication machinery to the S phase checkpoint. Cell 80(1):29-39
3)	Burgers PM (1998) Eukaryotic DNA polymerases in DNA replication and DNA repair. Chromosoma 107(4):218-27
4)	Shimizu K, et al. (2002) Fidelity of DNA polymerase epsilon holoenzyme from budding yeast Saccharomyces cerevisiae. J Biol Chem 277(40):37422-9
5)	Lou H, et al. (2008) Mrc1 and DNA polymerase epsilon function together in linking DNA replication and the S phase checkpoint. Mol Cell 32(1):106-17
6)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41