Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA polymerase epsilon subunit 4

Gene

Pole4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase epsilon subunit 4 (EC:2.7.7.7)
Alternative name(s):
DNA polymerase II subunit 4
DNA polymerase epsilon subunit p12
Gene namesi
Name:Pole4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1914229. Pole4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 118117DNA polymerase epsilon subunit 4PRO_0000191747Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei11 – 111PhosphothreonineBy similarity
Modified residuei25 – 251PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9CQ36.
MaxQBiQ9CQ36.
PaxDbiQ9CQ36.
PRIDEiQ9CQ36.

2D gel databases

REPRODUCTION-2DPAGEQ9CQ36.

PTM databases

PhosphoSiteiQ9CQ36.

Expressioni

Gene expression databases

BgeeiQ9CQ36.
ExpressionAtlasiQ9CQ36. baseline and differential.
GenevisibleiQ9CQ36. MM.

Interactioni

Subunit structurei

Component of the epsilon DNA polymerase complex consisting of four subunits: POLE, POLE2, POLE3 and POLE4. Interaction with POLE3 is a prerequisite for further binding with POLE and POLE2 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000093462.

Structurei

3D structure databases

ProteinModelPortaliQ9CQ36.
SMRiQ9CQ36. Positions 42-113.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiKOG1658. Eukaryota.
ENOG41122NU. LUCA.
GeneTreeiENSGT00530000063560.
HOGENOMiHOG000007271.
HOVERGENiHBG051399.
InParanoidiQ9CQ36.
KOiK03506.
PhylomeDBiQ9CQ36.
TreeFamiTF103009.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR003958. CBFA_NFYB_domain.
IPR009072. Histone-fold.
[Graphical view]
PfamiPF00808. CBFD_NFYB_HMF. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CQ36-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAAAAGSG TPREEEAPGG EAAASQAQAP TSAPGGVRLS RLPLARVKAL
60 70 80 90 100
VKADPDVTLA GQEAIFILAR AAELFVETIA KDAYCCAQQG KRKTLQRRDL
110
DNAIEAVDEF AFLEGTLD
Length:118
Mass (Da):12,240
Last modified:June 1, 2001 - v1
Checksum:iCE6B47CD7BC93A09
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010135 mRNA. Translation: BAB26722.1.
AK010300 mRNA. Translation: BAB26833.1.
AK011595 mRNA. Translation: BAB27723.1.
AK160582 mRNA. Translation: BAE35889.1.
AK167631 mRNA. Translation: BAE39682.1.
BC023189 mRNA. Translation: AAH23189.1.
CCDSiCCDS39524.1.
RefSeqiNP_080158.1. NM_025882.3.
UniGeneiMm.195753.

Genome annotation databases

EnsembliENSMUST00000095786; ENSMUSP00000093462; ENSMUSG00000030042.
GeneIDi66979.
KEGGimmu:66979.
UCSCiuc009clk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010135 mRNA. Translation: BAB26722.1.
AK010300 mRNA. Translation: BAB26833.1.
AK011595 mRNA. Translation: BAB27723.1.
AK160582 mRNA. Translation: BAE35889.1.
AK167631 mRNA. Translation: BAE39682.1.
BC023189 mRNA. Translation: AAH23189.1.
CCDSiCCDS39524.1.
RefSeqiNP_080158.1. NM_025882.3.
UniGeneiMm.195753.

3D structure databases

ProteinModelPortaliQ9CQ36.
SMRiQ9CQ36. Positions 42-113.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000093462.

PTM databases

PhosphoSiteiQ9CQ36.

2D gel databases

REPRODUCTION-2DPAGEQ9CQ36.

Proteomic databases

EPDiQ9CQ36.
MaxQBiQ9CQ36.
PaxDbiQ9CQ36.
PRIDEiQ9CQ36.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000095786; ENSMUSP00000093462; ENSMUSG00000030042.
GeneIDi66979.
KEGGimmu:66979.
UCSCiuc009clk.1. mouse.

Organism-specific databases

CTDi56655.
MGIiMGI:1914229. Pole4.

Phylogenomic databases

eggNOGiKOG1658. Eukaryota.
ENOG41122NU. LUCA.
GeneTreeiENSGT00530000063560.
HOGENOMiHOG000007271.
HOVERGENiHBG051399.
InParanoidiQ9CQ36.
KOiK03506.
PhylomeDBiQ9CQ36.
TreeFamiTF103009.

Miscellaneous databases

ChiTaRSiPole4. mouse.
NextBioi323206.
PROiQ9CQ36.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQ36.
ExpressionAtlasiQ9CQ36. baseline and differential.
GenevisibleiQ9CQ36. MM.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR003958. CBFA_NFYB_domain.
IPR009072. Histone-fold.
[Graphical view]
PfamiPF00808. CBFD_NFYB_HMF. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Placenta.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver, Spleen and Testis.

Entry informationi

Entry nameiDPOE4_MOUSE
AccessioniPrimary (citable) accession number: Q9CQ36
Secondary accession number(s): Q3TJ13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: June 1, 2001
Last modified: March 16, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.