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Protein

DNA polymerase subunit gamma-2, mitochondrial

Gene

Polg2

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

Functioni

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

Catalytic activityi

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

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. DNA-directed DNA polymerase activity Source: MGI
  3. identical protein binding Source: IntAct

GO - Biological processi

  1. DNA biosynthetic process Source: GOC
  2. DNA repair Source: MGI
  3. DNA replication Source: MGI
  4. mitochondrial DNA replication Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Polg2
Synonyms:Mtpolb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1354947. Polg2.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: MGI
  2. mitochondrial chromosome Source: GO_Central
  3. mitochondrial nucleoid Source: MGI
  4. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 459DNA polymerase subunit gamma-2, mitochondrialPRO_0000007315
Transit peptidei1 – ?MitochondrionSequence Analysis

Proteomic databases

MaxQBiQ9QZM2.
PaxDbiQ9QZM2.
PRIDEiQ9QZM2.

PTM databases

PhosphoSiteiQ9QZM2.

Expressioni

Gene expression databases

BgeeiQ9QZM2.
ExpressionAtlasiQ9QZM2. baseline and differential.
GenevestigatoriQ9QZM2.

Interactioni

Subunit structurei

Heterotrimer composed of a catalytic subunit and a homodimer of accessory subunits.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-853043,EBI-853043

Protein-protein interaction databases

IntActiQ9QZM2. 1 interaction.
MINTiMINT-4093495.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi42 – 498Combined sources
Helixi57 – 604Combined sources
Helixi62 – 676Combined sources
Helixi75 – 9218Combined sources
Turni93 – 953Combined sources
Beta strandi99 – 1013Combined sources
Beta strandi106 – 1083Combined sources
Beta strandi120 – 1223Combined sources
Helixi124 – 1318Combined sources
Helixi138 – 15114Combined sources
Beta strandi152 – 1554Combined sources
Helixi160 – 1656Combined sources
Helixi167 – 1737Combined sources
Turni174 – 1763Combined sources
Beta strandi180 – 19213Combined sources
Beta strandi204 – 21714Combined sources
Helixi219 – 23820Combined sources
Helixi244 – 2463Combined sources
Beta strandi247 – 2537Combined sources
Beta strandi259 – 2679Combined sources
Beta strandi270 – 28213Combined sources
Helixi283 – 2886Combined sources
Helixi293 – 2953Combined sources
Beta strandi298 – 3003Combined sources
Beta strandi303 – 3053Combined sources
Beta strandi308 – 3158Combined sources
Helixi316 – 32712Combined sources
Turni350 – 3523Combined sources
Beta strandi357 – 3615Combined sources
Helixi366 – 38217Combined sources
Beta strandi387 – 3893Combined sources
Helixi390 – 3923Combined sources
Helixi399 – 40810Combined sources
Beta strandi412 – 4176Combined sources
Helixi419 – 4246Combined sources
Beta strandi426 – 4316Combined sources
Turni432 – 4343Combined sources
Beta strandi437 – 4415Combined sources
Turni442 – 4443Combined sources
Helixi445 – 45915Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G5HX-ray1.95A/B/C/D17-459[»]
1G5IX-ray2.30A/B/C/D17-459[»]
ProteinModelPortaliQ9QZM2.
SMRiQ9QZM2. Positions 40-459.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9QZM2.

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0423.
GeneTreeiENSGT00390000000244.
HOGENOMiHOG000049133.
HOVERGENiHBG051401.
InParanoidiQ9QZM2.
KOiK02333.
OMAiDHELLHM.
OrthoDBiEOG7S7SFV.
TreeFamiTF103005.

Family and domain databases

Gene3Di3.40.50.800. 1 hit.
InterProiIPR004154. Anticodon-bd.
IPR027031. Gly-tRNA_synthase/POLG2.
IPR027030. POLG2.
[Graphical view]
PANTHERiPTHR10745. PTHR10745. 1 hit.
PTHR10745:SF3. PTHR10745:SF3. 1 hit.
PfamiPF03129. HGTP_anticodon. 1 hit.
[Graphical view]
SUPFAMiSSF52954. SSF52954. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9QZM2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRCGGGARAC RRACRCWLSG YAGPADGTQQ PDAPEHAVAR EALVDLCRRR
60 70 80 90 100
HFFSGTPQQL STAALLSGCH ARFGPLGVEL RKNLASQWWS SMVVFREQVF
110 120 130 140 150
AVDSLHQEPG SSQPRDSAFR LVSPESIREI LQDREPSKEQ LVAFLENLLK
160 170 180 190 200
TSGKLRATLL HGALEHYVNC LDLVNRKLPF GLAQIGVCFH PVSNSNQTPS
210 220 230 240 250
SVTRVGEKTE ASLVWFTPTR TSSQWLDFWL RHRLLWWRKF AMSPSNFSSA
260 270 280 290 300
DCQDELGRKG SKLYYSFPWG KEPIETLWNL GDQELLHTYP GNVSTIQGRD
310 320 330 340 350
GRKNVVPCVL SVSGDVDLGT LAYLYDSFQL AENSFARKKS LQRKVLKLHP
360 370 380 390 400
CLAPIKVALD VGKGPTVELR QVCQGLLNEL LENGISVWPG YSETVHSSLE
410 420 430 440 450
QLHSKYDEMS VLFSVLVTET TLENGLIQLR SRDTTMKEMM HISKLRDFLV

KYLASASNV
Length:459
Mass (Da):51,467
Last modified:July 27, 2011 - v2
Checksum:i052C790C2AF9A249
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531F → L in AAD56641 (PubMed:10666468).Curated
Sequence conflicti226 – 2261L → S in AAB62894 (Ref. 3) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF177202 mRNA. Translation: AAD56641.1.
AL603664 Genomic DNA. Translation: CAM18563.1.
AF006072 mRNA. Translation: AAB62894.1.
CCDSiCCDS25561.1.
RefSeqiNP_056625.2. NM_015810.2.
UniGeneiMm.859.

Genome annotation databases

EnsembliENSMUST00000021060; ENSMUSP00000021060; ENSMUSG00000020718.
GeneIDi50776.
KEGGimmu:50776.
UCSCiuc007lzm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF177202 mRNA. Translation: AAD56641.1.
AL603664 Genomic DNA. Translation: CAM18563.1.
AF006072 mRNA. Translation: AAB62894.1.
CCDSiCCDS25561.1.
RefSeqiNP_056625.2. NM_015810.2.
UniGeneiMm.859.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G5HX-ray1.95A/B/C/D17-459[»]
1G5IX-ray2.30A/B/C/D17-459[»]
ProteinModelPortaliQ9QZM2.
SMRiQ9QZM2. Positions 40-459.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9QZM2. 1 interaction.
MINTiMINT-4093495.

PTM databases

PhosphoSiteiQ9QZM2.

Proteomic databases

MaxQBiQ9QZM2.
PaxDbiQ9QZM2.
PRIDEiQ9QZM2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021060; ENSMUSP00000021060; ENSMUSG00000020718.
GeneIDi50776.
KEGGimmu:50776.
UCSCiuc007lzm.2. mouse.

Organism-specific databases

CTDi11232.
MGIiMGI:1354947. Polg2.

Phylogenomic databases

eggNOGiCOG0423.
GeneTreeiENSGT00390000000244.
HOGENOMiHOG000049133.
HOVERGENiHBG051401.
InParanoidiQ9QZM2.
KOiK02333.
OMAiDHELLHM.
OrthoDBiEOG7S7SFV.
TreeFamiTF103005.

Miscellaneous databases

ChiTaRSiPolg2. mouse.
EvolutionaryTraceiQ9QZM2.
NextBioi307713.
PROiQ9QZM2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QZM2.
ExpressionAtlasiQ9QZM2. baseline and differential.
GenevestigatoriQ9QZM2.

Family and domain databases

Gene3Di3.40.50.800. 1 hit.
InterProiIPR004154. Anticodon-bd.
IPR027031. Gly-tRNA_synthase/POLG2.
IPR027030. POLG2.
[Graphical view]
PANTHERiPTHR10745. PTHR10745. 1 hit.
PTHR10745:SF3. PTHR10745:SF3. 1 hit.
PfamiPF03129. HGTP_anticodon. 1 hit.
[Graphical view]
SUPFAMiSSF52954. SSF52954. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiDPOG2_MOUSE
AccessioniPrimary (citable) accession number: Q9QZM2
Secondary accession number(s): B1ARB5, O35614
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: July 27, 2011
Last modified: February 4, 2015
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

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 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.