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Q9NP87

- DPOLM_HUMAN

UniProt

Q9NP87 - DPOLM_HUMAN

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Protein
DNA-directed DNA/RNA polymerase mu
Gene
POLM, polmu
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications

Catalytic activityi

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

Cofactori

Magnesium By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi330 – 3301Magnesium By similarity
Metal bindingi332 – 3321Magnesium By similarity
Metal bindingi418 – 4181Magnesium By similarity
Sitei433 – 4331Responsible for the low discrimination between dNTP and rNTP

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. DNA-directed DNA polymerase activity Source: InterPro
  3. metal ion binding Source: UniProtKB-KW
  4. nucleotidyltransferase activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. B cell differentiation Source: Ensembl
  2. DNA recombination Source: UniProtKB-KW
  3. DNA repair Source: UniProtKB-KW
  4. somatic hypermutation of immunoglobulin genes Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed DNA/RNA polymerase mu (EC:2.7.7.7)
Short name:
Pol Mu
Alternative name(s):
Terminal transferase
Gene namesi
Name:POLM
Synonyms:polmu
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:9185. POLM.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33505.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 494494DNA-directed DNA/RNA polymerase mu
PRO_0000218787Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NP87.
PaxDbiQ9NP87.
PRIDEiQ9NP87.

PTM databases

PhosphoSiteiQ9NP87.

Expressioni

Tissue specificityi

Expressed in a number of tissues. Abundant in thymus.

Gene expression databases

ArrayExpressiQ9NP87.
BgeeiQ9NP87.
CleanExiHS_POLM.
GenevestigatoriQ9NP87.

Interactioni

Protein-protein interaction databases

BioGridi118168. 6 interactions.
STRINGi9606.ENSP00000242248.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 346
Helixi36 – 383
Helixi41 – 5414
Beta strandi57 – 593
Beta strandi68 – 736
Helixi76 – 8914
Beta strandi98 – 1014
Helixi103 – 1119
Turni119 – 1213
Helixi142 – 1443
Helixi154 – 16916
Helixi173 – 18816
Beta strandi189 – 1913
Helixi196 – 1994
Helixi207 – 21913
Helixi223 – 2308
Helixi232 – 24110
Helixi248 – 2569
Helixi262 – 2665
Helixi269 – 2713
Helixi274 – 2818
Helixi283 – 2864
Helixi292 – 30918
Beta strandi314 – 3174
Helixi319 – 3224
Beta strandi326 – 3294
Beta strandi331 – 3366
Turni340 – 3456
Helixi346 – 35611
Beta strandi360 – 3623
Beta strandi387 – 39610
Beta strandi411 – 42111
Helixi424 – 4263
Helixi427 – 4359
Helixi438 – 45215
Beta strandi461 – 4633
Turni464 – 4674
Helixi475 – 4817
Helixi489 – 4913

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DUNNMR-A24-143[»]
2HTFNMR-A21-124[»]
4LZDX-ray1.85A132-397[»]
A411-494[»]
4LZGX-ray1.60A132-397[»]
A411-494[»]
4M04X-ray1.90A132-397[»]
A411-494[»]
4M0AX-ray1.85A132-397[»]
A411-494[»]
ProteinModelPortaliQ9NP87.
SMRiQ9NP87. Positions 21-124, 137-494.

Miscellaneous databases

EvolutionaryTraceiQ9NP87.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 122101BRCT
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni323 – 33210Involved in ssDNA binding By similarity

Sequence similaritiesi

Contains 1 BRCT domain.

Phylogenomic databases

eggNOGiCOG1796.
HOGENOMiHOG000263600.
HOVERGENiHBG003670.
KOiK03513.
OMAiPEQKTFF.
PhylomeDBiQ9NP87.
TreeFamiTF103012.

Family and domain databases

Gene3Di1.10.150.110. 1 hit.
3.30.210.10. 1 hit.
InterProiIPR001357. 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.
IPR029398. PolB_thumb.
IPR001726. TdT/Mu.
[Graphical view]
PfamiPF14792. DNA_pol_B_palm. 1 hit.
PF14791. DNA_pol_B_thumb. 1 hit.
PF10391. DNA_pol_lambd_f. 1 hit.
[Graphical view]
PIRSFiPIRSF000817. DNA_NT. 1 hit.
PIRSF501176. DNApol_mu. 1 hit.
PRINTSiPR00869. DNAPOLX.
PR00871. DNAPOLXTDT.
SMARTiSM00292. BRCT. 1 hit.
SM00483. POLXc. 1 hit.
[Graphical view]
SUPFAMiSSF47802. SSF47802. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEiPS50172. BRCT. 1 hit.
PS00522. DNA_POLYMERASE_X. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NP87-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MLPKRRRARV GSPSGDAASS TPPSTRFPGV AIYLVEPRMG RSRRAFLTGL    50
ARSKGFRVLD ACSSEATHVV MEETSAEEAV SWQERRMAAA PPGCTPPALL 100
DISWLTESLG AGQPVPVECR HRLEVAGPRK GPLSPAWMPA YACQRPTPLT 150
HHNTGLSEAL EILAEAAGFE GSEGRLLTFC RAASVLKALP SPVTTLSQLQ 200
GLPHFGEHSS RVVQELLEHG VCEEVERVRR SERYQTMKLF TQIFGVGVKT 250
ADRWYREGLR TLDDLREQPQ KLTQQQKAGL QHHQDLSTPV LRSDVDALQQ 300
VVEEAVGQAL PGATVTLTGG FRRGKLQGHD VDFLITHPKE GQEAGLLPRV 350
MCRLQDQGLI LYHQHQHSCC ESPTRLAQQS HMDAFERSFC IFRLPQPPGA 400
AVGGSTRPCP SWKAVRVDLV VAPVSQFPFA LLGWTGSKLF QRELRRFSRK 450
EKGLWLNSHG LFDPEQKTFF QAASEEDIFR HLGLEYLPPE QRNA 494
Length:494
Mass (Da):54,816
Last modified:October 1, 2000 - v1
Checksum:iB944059725F8B61F
GO
Isoform 2 (identifier: Q9NP87-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     279-356: GLQHHQDLST...LPRVMCRLQD → APPGPEHPSP...GHRHADRRLP

Note: No experimental confirmation available.

Show »
Length:457
Mass (Da):50,430
Checksum:iDE56D41438283CF3
GO
Isoform 3 (identifier: Q9NP87-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     234-276: YQTMKLFTQI...EQPQKLTQQQ → APAPPGPEHP...GHRHADRRLP
     277-356: Missing.
     467-494: KTFFQAASEEDIFRHLGLEYLPPEQRNA → GSSSGKTPRS...GALSASLITV

Note: No experimental confirmation available.

Show »
Length:508
Mass (Da):55,070
Checksum:i25EF59F10FC7D7FB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti107 – 1071E → D.1 Publication
Corresponds to variant rs28382635 [ dbSNP | Ensembl ].
VAR_022287
Natural varianti220 – 2201G → A.1 Publication
Corresponds to variant rs28382644 [ dbSNP | Ensembl ].
VAR_022288
Natural varianti246 – 2461V → F.1 Publication
Corresponds to variant rs28382653 [ dbSNP | Ensembl ].
VAR_022289
Natural varianti484 – 4841L → F.1 Publication
Corresponds to variant rs28382661 [ dbSNP | Ensembl ].
VAR_022290

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei234 – 27643YQTMK…LTQQQ → APAPPGPEHPSPAVRCRCPA AGGGGSCGAGPAWGHRHADR RLP in isoform 3.
VSP_055288Add
BLAST
Alternative sequencei277 – 35680Missing in isoform 3.
VSP_055289Add
BLAST
Alternative sequencei279 – 35678GLQHH…CRLQD → APPGPEHPSPAVRCRCPAAG GGGSCGAGPAWGHRHADRRL P in isoform 2.
VSP_055290Add
BLAST
Alternative sequencei467 – 49428KTFFQ…EQRNA → GSSSGKTPRSRKSCFCCRRH FSKRLQRKTSSDTWALSTFL QSRETPEPACVPHFHSGNWA APNLATECLQADMLPPDPHL HPSPPRPGSSGGQLCLQDQL SPCWCAAGCDEVGALSASLI TV in isoform 3.
VSP_055291Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ131891 mRNA. Translation: CAB65075.2.
AF176097 mRNA. Translation: AAF26284.1.
AY899911 Genomic DNA. Translation: AAW65376.1.
AC017116 Genomic DNA. No translation available.
CH471128 Genomic DNA. Translation: EAW61122.1.
CH471128 Genomic DNA. Translation: EAW61123.1.
CH471128 Genomic DNA. Translation: EAW61124.1.
CH471128 Genomic DNA. Translation: EAW61126.1.
BC049202 mRNA. Translation: AAH49202.2.
BC062590 mRNA. Translation: AAH62590.1.
CCDSiCCDS34625.1. [Q9NP87-1]
RefSeqiNP_001271259.1. NM_001284330.1.
NP_001271260.1. NM_001284331.1.
NP_037416.1. NM_013284.3.
UniGeneiHs.596982.
Hs.598038.

Genome annotation databases

EnsembliENST00000242248; ENSP00000242248; ENSG00000122678.
ENST00000335195; ENSP00000335141; ENSG00000122678.
ENST00000395831; ENSP00000379174; ENSG00000122678.
GeneIDi27434.
KEGGihsa:27434.
UCSCiuc003tjt.3. human. [Q9NP87-1]

Polymorphism databases

DMDMi17366980.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ131891 mRNA. Translation: CAB65075.2 .
AF176097 mRNA. Translation: AAF26284.1 .
AY899911 Genomic DNA. Translation: AAW65376.1 .
AC017116 Genomic DNA. No translation available.
CH471128 Genomic DNA. Translation: EAW61122.1 .
CH471128 Genomic DNA. Translation: EAW61123.1 .
CH471128 Genomic DNA. Translation: EAW61124.1 .
CH471128 Genomic DNA. Translation: EAW61126.1 .
BC049202 mRNA. Translation: AAH49202.2 .
BC062590 mRNA. Translation: AAH62590.1 .
CCDSi CCDS34625.1. [Q9NP87-1 ]
RefSeqi NP_001271259.1. NM_001284330.1.
NP_001271260.1. NM_001284331.1.
NP_037416.1. NM_013284.3.
UniGenei Hs.596982.
Hs.598038.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DUN NMR - A 24-143 [» ]
2HTF NMR - A 21-124 [» ]
4LZD X-ray 1.85 A 132-397 [» ]
A 411-494 [» ]
4LZG X-ray 1.60 A 132-397 [» ]
A 411-494 [» ]
4M04 X-ray 1.90 A 132-397 [» ]
A 411-494 [» ]
4M0A X-ray 1.85 A 132-397 [» ]
A 411-494 [» ]
ProteinModelPortali Q9NP87.
SMRi Q9NP87. Positions 21-124, 137-494.
ModBasei Search...

Protein-protein interaction databases

BioGridi 118168. 6 interactions.
STRINGi 9606.ENSP00000242248.

Chemistry

BindingDBi Q9NP87.
ChEMBLi CHEMBL1914260.

PTM databases

PhosphoSitei Q9NP87.

Polymorphism databases

DMDMi 17366980.

Proteomic databases

MaxQBi Q9NP87.
PaxDbi Q9NP87.
PRIDEi Q9NP87.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000242248 ; ENSP00000242248 ; ENSG00000122678 .
ENST00000335195 ; ENSP00000335141 ; ENSG00000122678 .
ENST00000395831 ; ENSP00000379174 ; ENSG00000122678 .
GeneIDi 27434.
KEGGi hsa:27434.
UCSCi uc003tjt.3. human. [Q9NP87-1 ]

Organism-specific databases

CTDi 27434.
GeneCardsi GC07M044111.
H-InvDB HIX0167826.
HGNCi HGNC:9185. POLM.
MIMi 606344. gene.
neXtProti NX_Q9NP87.
PharmGKBi PA33505.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1796.
HOGENOMi HOG000263600.
HOVERGENi HBG003670.
KOi K03513.
OMAi PEQKTFF.
PhylomeDBi Q9NP87.
TreeFami TF103012.

Miscellaneous databases

EvolutionaryTracei Q9NP87.
GeneWikii DNA_polymerase_mu.
GenomeRNAii 27434.
NextBioi 50481.
PROi Q9NP87.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NP87.
Bgeei Q9NP87.
CleanExi HS_POLM.
Genevestigatori Q9NP87.

Family and domain databases

Gene3Di 1.10.150.110. 1 hit.
3.30.210.10. 1 hit.
InterProi IPR001357. 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.
IPR029398. PolB_thumb.
IPR001726. TdT/Mu.
[Graphical view ]
Pfami PF14792. DNA_pol_B_palm. 1 hit.
PF14791. DNA_pol_B_thumb. 1 hit.
PF10391. DNA_pol_lambd_f. 1 hit.
[Graphical view ]
PIRSFi PIRSF000817. DNA_NT. 1 hit.
PIRSF501176. DNApol_mu. 1 hit.
PRINTSi PR00869. DNAPOLX.
PR00871. DNAPOLXTDT.
SMARTi SM00292. BRCT. 1 hit.
SM00483. POLXc. 1 hit.
[Graphical view ]
SUPFAMi SSF47802. SSF47802. 1 hit.
SSF52113. SSF52113. 1 hit.
PROSITEi PS50172. BRCT. 1 hit.
PS00522. DNA_POLYMERASE_X. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1).
    Tissue: Placenta.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 2 AND 3).
    Tissue: Blood and Brain.
  7. "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.
  8. Cited for: FUNCTION, SUGAR DISCRIMINATION SITE.
  9. "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.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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].
  12. "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.
  13. "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.
  14. "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.

Entry informationi

Entry nameiDPOLM_HUMAN
AccessioniPrimary (citable) accession number: Q9NP87
Secondary accession number(s): D3DVK4, Q6P5X8, Q86WQ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: October 1, 2000
Last modified: September 3, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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