Q9NP87 (DPOLM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	494 AA.
Sequence status	Complete.
Protein existence	Evidence 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.10
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.

Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	Magnesium Metal-binding
Molecular function	DNA-directed DNA polymerase Nucleotidyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell differentiation Inferred from electronic annotation. Source: Compara DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW DNA repair Inferred from electronic annotation. Source: UniProtKB-KW somatic hypermutation of immunoglobulin genes Inferred from electronic annotation. Source: Compara
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed DNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 494

494

DNA-directed DNA/RNA polymerase mu

PRO_0000218787

Regions

Domain

22 – 122

101

BRCT

Region

323 – 332

10

Involved in ssDNA binding By similarity

Sites

Metal binding

330

1

Magnesium By similarity

Metal binding

332

1

Magnesium By similarity

Metal binding

418

1

Magnesium By similarity

Site

433

1

Responsible for the low discrimination between dNTP and rNTP

Amino acid modifications

Modified residue

12

1

Phosphoserine Ref.8 Ref.9

Natural variations

Natural variant

107

1

E → D. Ref.3
Corresponds to variant rs28382635 [ dbSNP | Ensembl ].

VAR_022287

Natural variant

220

1

G → A. Ref.3
Corresponds to variant rs28382644 [ dbSNP | Ensembl ].

VAR_022288

Natural variant

246

1

V → F. Ref.3
Corresponds to variant rs28382653 [ dbSNP | Ensembl ].

VAR_022289

Natural variant

484

1

L → F. Ref.3
Corresponds to variant rs28382661 [ dbSNP | Ensembl ].

VAR_022290

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

494

Helix Strand Turn

Details...

Beta strand

26 – 34

9

Helix

36 – 39

4

Helix

42 – 54

13

Beta strand

55 – 58

4

Beta strand

68 – 73

6

Helix

76 – 89

14

Beta strand

98 – 101

4

Helix

102 – 111

10

Turn

119 – 121

3

Sequences

	Sequence		Length	Mass (Da)
	Q9NP87 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: B944059725F8B61F	FASTA	494	54,816
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"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.
[11]	"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

NIEHS-SNPs

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.

IPI

IPI00002325.

RefSeq

NP_037416.1. NM_013284.2.

UniGene

Hs.596982.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DUN	NMR	-	A	24-143	[»]
2HTF	NMR	-	A	21-124	[»]

ProteinModelPortal

Q9NP87.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000242248.

PTM databases

PhosphoSite

Q9NP87.

Polymorphism databases

DMDM

17366980.

Proteomic databases

PaxDb

Q9NP87.

PRIDE

Q9NP87.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000242248; ENSP00000242248; ENSG00000122678.

GeneID

27434.

KEGG

hsa:27434.

UCSC

uc003tjt.3. human.

Organism-specific databases

CTD

27434.

GeneCards

GC07M044111.

H-InvDB

HIX0167826.

HGNC

HGNC:9185. POLM.

MIM

606344. gene.

neXtProt

NX_Q9NP87.

PharmGKB

PA33505.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1796.

HOGENOM

HOG000263600.

HOVERGEN

HBG003670.

KO

K03513.

OMA

PEQKTFF.

OrthoDB

EOG4JDH6X.

Gene expression databases

ArrayExpress

Q9NP87.

Bgee

Q9NP87.

CleanEx

HS_POLM.

Genevestigator

Q9NP87.

GermOnline

ENSG00000122678. Homo sapiens.

Family and domain databases

InterPro

IPR001357. BRCT_dom.
IPR002054. DNA-dir_DNA_pol_X.
IPR027249. DNA/RNApol_mu.
IPR019843. DNA_pol-X_BS.
IPR010996. DNA_pol_b-like_N.
IPR018944. DNA_pol_lambd_fingers_domain.
IPR022312. DNA_pol_X.
IPR001726. TdT/Mu.
[Graphical view]

PANTHER

PTHR11276:SF6. PTHR11276:SF6. 1 hit.

Pfam

PF10391. DNA_pol_lambd_f. 1 hit.
[Graphical view]

PIRSF

PIRSF000817. DNA_NT. 1 hit.
PIRSF501176. DNApol_mu. 1 hit.

PRINTS

PR00869. DNAPOLX.
PR00871. DNAPOLXTDT.

SMART

SM00292. BRCT. 1 hit.
SM00483. POLXc. 1 hit.
[Graphical view]

SUPFAM

SSF52113. BRCT. 1 hit.
SSF81585. DNA_pol_lambd_fingers_domain. 1 hit.
SSF47802. DNApol_B_N_like. 1 hit.

PROSITE

PS50172. BRCT. 1 hit.
PS00522. DNA_POLYMERASE_X. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q9NP87.

ChEMBL

CHEMBL1914260.

EvolutionaryTrace

Q9NP87.

GenomeRNAi

27434.

NextBio

50481.

SOURCE

Search...

Entry information

Entry name

DPOLM_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.