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Q9QZM2 (DPOG2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA polymerase subunit gamma-2, mitochondrial

EC=2.7.7.7
Alternative name(s):
DNA polymerase gamma accessory 55 kDa subunit
Short name=p55
Mitochondrial DNA polymerase accessory subunit
MtPolB
PolG-beta
Gene names
Name:Polg2
Synonyms:Mtpolb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length459 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mitochondrial polymerase processivity subunit. Stimulates the polymerase and exonuclease activities, and increases the processivity of the enzyme. Binds to ss-DNA.

Catalytic activity

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

Subunit structure

Heterotrimer composed of a catalytic subunit and a homodimer of accessory subunits. Ref.4

Subcellular location

Mitochondrion.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-853043,EBI-853043

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 459DNA polymerase subunit gamma-2, mitochondrialPRO_0000007315

Experimental info

Sequence conflict531F → L in AAD56641. Ref.1
Sequence conflict2261L → S in AAB62894. Ref.3

Secondary structure

...................................................................... 459
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9QZM2 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 052C790C2AF9A249

FASTA45951,467
        10         20         30         40         50         60 
MRCGGGARAC RRACRCWLSG YAGPADGTQQ PDAPEHAVAR EALVDLCRRR HFFSGTPQQL 

        70         80         90        100        110        120 
STAALLSGCH ARFGPLGVEL RKNLASQWWS SMVVFREQVF AVDSLHQEPG SSQPRDSAFR 

       130        140        150        160        170        180 
LVSPESIREI LQDREPSKEQ LVAFLENLLK TSGKLRATLL HGALEHYVNC LDLVNRKLPF 

       190        200        210        220        230        240 
GLAQIGVCFH PVSNSNQTPS SVTRVGEKTE ASLVWFTPTR TSSQWLDFWL RHRLLWWRKF 

       250        260        270        280        290        300 
AMSPSNFSSA DCQDELGRKG SKLYYSFPWG KEPIETLWNL GDQELLHTYP GNVSTIQGRD 

       310        320        330        340        350        360 
GRKNVVPCVL SVSGDVDLGT LAYLYDSFQL AENSFARKKS LQRKVLKLHP CLAPIKVALD 

       370        380        390        400        410        420 
VGKGPTVELR QVCQGLLNEL LENGISVWPG YSETVHSSLE QLHSKYDEMS VLFSVLVTET 

       430        440        450 
TLENGLIQLR SRDTTMKEMM HISKLRDFLV KYLASASNV 

« Hide

References

« Hide 'large scale' references
[1]"Protein sequences conserved in prokaryotic aminoacyl-tRNA synthetases are important for the activity of the processivity factor of human mitochondrial DNA polymerase."
Carrodeguas J.A., Bogenhagen D.F.
Nucleic Acids Res. 28:1237-1244(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Swiss Webster / NIH.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]Kaguni L.S.
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 164-459.
[4]"Crystal structure and deletion analysis show that the accessory subunit of mammalian DNA polymerase gamma, Pol gamma B, functions as a homodimer."
Carrodeguas J.A., Theis K., Bogenhagen D.F., Kisker C.
Mol. Cell 7:43-54(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-459, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF177202 mRNA. Translation: AAD56641.1.
AL603664 Genomic DNA. Translation: CAM18563.1.
AF006072 mRNA. Translation: AAB62894.1.
CCDSCCDS25561.1.
RefSeqNP_056625.2. NM_015810.2.
UniGeneMm.859.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G5HX-ray1.95A/B/C/D17-459[»]
1G5IX-ray2.30A/B/C/D17-459[»]
ProteinModelPortalQ9QZM2.
SMRQ9QZM2. Positions 40-459.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9QZM2. 1 interaction.
MINTMINT-4093495.

PTM databases

PhosphoSiteQ9QZM2.

Proteomic databases

PaxDbQ9QZM2.
PRIDEQ9QZM2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021060; ENSMUSP00000021060; ENSMUSG00000020718.
GeneID50776.
KEGGmmu:50776.
UCSCuc007lzm.2. mouse.

Organism-specific databases

CTD11232.
MGIMGI:1354947. Polg2.

Phylogenomic databases

eggNOGCOG0423.
GeneTreeENSGT00390000000244.
HOGENOMHOG000049133.
HOVERGENHBG051401.
InParanoidB1ARB5.
KOK02333.
OMADHELLHM.
OrthoDBEOG7S7SFV.
TreeFamTF103005.

Gene expression databases

ArrayExpressQ9QZM2.
BgeeQ9QZM2.
GenevestigatorQ9QZM2.

Family and domain databases

Gene3D3.40.50.800. 1 hit.
InterProIPR004154. Anticodon-bd.
IPR027031. Gly-tRNA_synthase/POLG2.
IPR027030. POLG2.
[Graphical view]
PANTHERPTHR10745. PTHR10745. 1 hit.
PTHR10745:SF3. PTHR10745:SF3. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
[Graphical view]
SUPFAMSSF52954. SSF52954. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9QZM2.
NextBio307713.
PROQ9QZM2.
SOURCESearch...

Entry information

Entry nameDPOG2_MOUSE
AccessionPrimary (citable) accession number: Q9QZM2
Secondary accession number(s): B1ARB5, O35614
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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