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Q9NP87 (DPOLM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA-directed DNA/RNA polymerase mu

Short name=Pol Mu
EC=2.7.7.7
Alternative name(s):
Terminal transferase
Gene names
Name:POLM
Synonyms:polmu
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Gap-filling polymerase involved in repair of DNA double-strand breaks by non-homologous end joining (NHEJ). Participates in immunoglobulin (Ig) light chain gene rearrangement in V(D)J recombination. Ref.5 Ref.6 Ref.7 Ref.11

Catalytic activity

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

Cofactor

Magnesium By similarity.

Subcellular location

Nucleus By similarity.

Tissue specificity

Expressed in a number of tissues. Abundant in thymus.

Miscellaneous

DPOLM has a reduced ability to distinguish dNTP and rNTP as substrates, and elongates them on DNA primer strand with a similar efficiency. It is able to polymerize nucleotides on RNA primer strands.

Sequence similarities

Belongs to the DNA polymerase type-X family.

Contains 1 BRCT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 494494DNA-directed DNA/RNA polymerase mu
PRO_0000218787

Regions

Domain22 – 122101BRCT
Region323 – 33210Involved in ssDNA binding By similarity

Sites

Metal binding3301Magnesium By similarity
Metal binding3321Magnesium By similarity
Metal binding4181Magnesium By similarity
Site4331Responsible for the low discrimination between dNTP and rNTP

Amino acid modifications

Modified residue121Phosphoserine Ref.8 Ref.10

Natural variations

Natural variant1071E → D. Ref.3
Corresponds to variant rs28382635 [ dbSNP | Ensembl ].
VAR_022287
Natural variant2201G → A. Ref.3
Corresponds to variant rs28382644 [ dbSNP | Ensembl ].
VAR_022288
Natural variant2461V → F. Ref.3
Corresponds to variant rs28382653 [ dbSNP | Ensembl ].
VAR_022289
Natural variant4841L → F. Ref.3
Corresponds to variant rs28382661 [ dbSNP | Ensembl ].
VAR_022290

Secondary structure

................... 494
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NP87 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: B944059725F8B61F

FASTA49454,816
        10         20         30         40         50         60 
MLPKRRRARV GSPSGDAASS TPPSTRFPGV AIYLVEPRMG RSRRAFLTGL ARSKGFRVLD 

        70         80         90        100        110        120 
ACSSEATHVV MEETSAEEAV SWQERRMAAA PPGCTPPALL DISWLTESLG AGQPVPVECR 

       130        140        150        160        170        180 
HRLEVAGPRK GPLSPAWMPA YACQRPTPLT HHNTGLSEAL EILAEAAGFE GSEGRLLTFC 

       190        200        210        220        230        240 
RAASVLKALP SPVTTLSQLQ GLPHFGEHSS RVVQELLEHG VCEEVERVRR SERYQTMKLF 

       250        260        270        280        290        300 
TQIFGVGVKT ADRWYREGLR TLDDLREQPQ KLTQQQKAGL QHHQDLSTPV LRSDVDALQQ 

       310        320        330        340        350        360 
VVEEAVGQAL PGATVTLTGG FRRGKLQGHD VDFLITHPKE GQEAGLLPRV MCRLQDQGLI 

       370        380        390        400        410        420 
LYHQHQHSCC ESPTRLAQQS HMDAFERSFC IFRLPQPPGA AVGGSTRPCP SWKAVRVDLV 

       430        440        450        460        470        480 
VAPVSQFPFA LLGWTGSKLF QRELRRFSRK EKGLWLNSHG LFDPEQKTFF QAASEEDIFR 

       490 
HLGLEYLPPE QRNA 

« Hide

References

« Hide 'large scale' references
[1]"DNA polymerase mu (Pol mu), homologous to TdT, could act as a DNA mutator in eukaryotic cells."
Dominguez O., Ruiz J.F., Lain de Lera T., Garcia-Diaz M., Gonzalez M.A., Kirchhoff T., Martinez-A C., Bernad A., Blanco L.
EMBO J. 19:1731-1742(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[2]"Two novel human and mouse DNA polymerases of the polX family."
Aoufouchi S., Flatter E., Dahan A., Faili A., Bertocci B., Storck S., Delbos F., Cocea L., Gupta N., Weill J.-C., Reynaud C.-A.
Nucleic Acids Res. 28:3684-3693(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]NIEHS SNPs program
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASP-107; ALA-220; PHE-246 AND PHE-484.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Polymerase mu is a DNA-directed DNA/RNA polymerase."
Nick McElhinny S.A., Ramsden D.A.
Mol. Cell. Biol. 23:2309-2315(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Lack of sugar discrimination by human Pol mu requires a single glycine residue."
Ruiz J.F., Juarez R., Garcia-Diaz M., Terrados G., Picher A.J., Gonzalez-Barrera S., Fernandez de Henestrosa A.R., Blanco L.
Nucleic Acids Res. 31:4441-4449(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUGAR DISCRIMINATION SITE.
[7]"Involvement of DNA polymerase mu in the repair of a specific subset of DNA double-strand breaks in mammalian cells."
Capp J.P., Boudsocq F., Besnard A.G., Lopez B.S., Cazaux C., Hoffmann J.S., Canitrot Y.
Nucleic Acids Res. 35:3551-3560(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"Solution structure of polymerase mu's BRCT Domain reveals an element essential for its role in nonhomologous end joining."
DeRose E.F., Clarkson M.W., Gilmore S.A., Galban C.J., Tripathy A., Havener J.M., Mueller G.A., Ramsden D.A., London R.E., Lee A.L.
Biochemistry 46:12100-12110(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 21-124, FUNCTION.
[12]"Solution structure of BRCT domain of DNA polymerase mu."
RIKEN structural genomics initiative (RSGI)
Submitted (JAN-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 18-147.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ131891 mRNA. Translation: CAB65075.2.
AF176097 mRNA. Translation: AAF26284.1.
AY899911 Genomic DNA. Translation: AAW65376.1.
CH471128 Genomic DNA. Translation: EAW61122.1.
CH471128 Genomic DNA. Translation: EAW61123.1.
RefSeqNP_037416.1. NM_013284.3.
UniGeneHs.596982.
Hs.598038.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DUNNMR-A24-143[»]
2HTFNMR-A21-124[»]
ProteinModelPortalQ9NP87.
SMRQ9NP87. Positions 21-124, 138-494.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118168. 6 interactions.
STRING9606.ENSP00000242248.

Chemistry

BindingDBQ9NP87.
ChEMBLCHEMBL1914260.

PTM databases

PhosphoSiteQ9NP87.

Polymorphism databases

DMDM17366980.

Proteomic databases

PaxDbQ9NP87.
PRIDEQ9NP87.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000242248; ENSP00000242248; ENSG00000122678.
GeneID27434.
KEGGhsa:27434.
UCSCuc003tjt.3. human.

Organism-specific databases

CTD27434.
GeneCardsGC07M044111.
H-InvDBHIX0167826.
HGNCHGNC:9185. POLM.
MIM606344. gene.
neXtProtNX_Q9NP87.
PharmGKBPA33505.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1796.
HOGENOMHOG000263600.
HOVERGENHBG003670.
KOK03513.
OMAPEQKTFF.
TreeFamTF103012.

Gene expression databases

ArrayExpressQ9NP87.
BgeeQ9NP87.
CleanExHS_POLM.
GenevestigatorQ9NP87.

Family and domain databases

Gene3D1.10.150.110. 1 hit.
InterProIPR001357. BRCT_dom.
IPR002054. DNA-dir_DNA_pol_X.
IPR027249. DNA/RNApol_mu.
IPR019843. DNA_pol-X_BS.
IPR010996. DNA_pol_b-like_N.
IPR028207. DNA_pol_B_palm_palm.
IPR018944. DNA_pol_lambd_fingers_domain.
IPR022312. DNA_pol_X.
IPR027421. DNA_pol_X_lyase_dom.
IPR001726. TdT/Mu.
[Graphical view]
PANTHERPTHR11276:SF6. PTHR11276:SF6. 1 hit.
PfamPF14792. DNA_pol_B_palm. 1 hit.
PF10391. DNA_pol_lambd_f. 1 hit.
[Graphical view]
PIRSFPIRSF000817. DNA_NT. 1 hit.
PIRSF501176. DNApol_mu. 1 hit.
PRINTSPR00869. DNAPOLX.
PR00871. DNAPOLXTDT.
SMARTSM00292. BRCT. 1 hit.
SM00483. POLXc. 1 hit.
[Graphical view]
SUPFAMSSF47802. SSF47802. 1 hit.
SSF52113. SSF52113. 1 hit.
SSF81585. SSF81585. 1 hit.
PROSITEPS50172. BRCT. 1 hit.
PS00522. DNA_POLYMERASE_X. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9NP87.
GeneWikiDNA_polymerase_mu.
GenomeRNAi27434.
NextBio50481.
PROQ9NP87.
SOURCESearch...

Entry information

Entry nameDPOLM_HUMAN
AccessionPrimary (citable) accession number: Q9NP87
Secondary accession number(s): D3DVK4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: October 1, 2000
Last modified: March 19, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM