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Q9NP87

- DPOLM_HUMAN

UniProt

Q9NP87 - DPOLM_HUMAN

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Protein

DNA-directed DNA/RNA polymerase mu

Gene

POLM

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

Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi330 – 3301MagnesiumBy similarity
Metal bindingi332 – 3321MagnesiumBy similarity
Metal bindingi418 – 4181MagnesiumBy 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: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. DNA recombination Source: UniProtKB-KW
  2. DNA repair Source: UniProtKB-KW
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-KW
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 muPRO_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

BgeeiQ9NP87.
CleanExiHS_POLM.
ExpressionAtlasiQ9NP87. baseline.
GenevestigatoriQ9NP87.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
P140793EBI-9675790,EBI-9675698From a different organism.

Protein-protein interaction databases

BioGridi118168. 6 interactions.
IntActiQ9NP87. 2 interactions.
STRINGi9606.ENSP00000242248.

Structurei

Secondary structure

1
494
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 346Combined sources
Helixi36 – 383Combined sources
Helixi41 – 5414Combined sources
Beta strandi57 – 593Combined sources
Beta strandi68 – 736Combined sources
Helixi76 – 8914Combined sources
Beta strandi98 – 1014Combined sources
Helixi103 – 1119Combined sources
Turni119 – 1213Combined sources
Helixi142 – 1443Combined sources
Helixi154 – 16916Combined sources
Helixi173 – 18816Combined sources
Beta strandi189 – 1913Combined sources
Helixi196 – 1994Combined sources
Helixi207 – 21913Combined sources
Helixi223 – 2308Combined sources
Helixi232 – 24110Combined sources
Helixi248 – 2569Combined sources
Helixi262 – 2665Combined sources
Helixi269 – 2713Combined sources
Helixi274 – 2818Combined sources
Helixi283 – 2864Combined sources
Helixi292 – 30918Combined sources
Beta strandi314 – 3174Combined sources
Helixi319 – 3224Combined sources
Beta strandi326 – 3294Combined sources
Beta strandi331 – 3366Combined sources
Turni340 – 3456Combined sources
Helixi346 – 35611Combined sources
Beta strandi360 – 3623Combined sources
Beta strandi387 – 39610Combined sources
Beta strandi411 – 42111Combined sources
Helixi424 – 4263Combined sources
Helixi427 – 4359Combined sources
Helixi438 – 45215Combined sources
Beta strandi461 – 4633Combined sources
Turni464 – 4674Combined sources
Helixi475 – 4817Combined sources
Helixi489 – 4913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NP87.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 122101BRCTPROSITE-ProRule annotationAdd
BLAST

Region

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

Sequence similaritiesi

Belongs to the DNA polymerase type-X family.Curated
Contains 1 BRCT domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1796.
GeneTreeiENSGT00530000063002.
HOGENOMiHOG000263600.
HOVERGENiHBG003670.
InParanoidiQ9NP87.
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

        10         20         30         40         50
MLPKRRRARV GSPSGDAASS TPPSTRFPGV AIYLVEPRMG RSRRAFLTGL
60 70 80 90 100
ARSKGFRVLD ACSSEATHVV MEETSAEEAV SWQERRMAAA PPGCTPPALL
110 120 130 140 150
DISWLTESLG AGQPVPVECR HRLEVAGPRK GPLSPAWMPA YACQRPTPLT
160 170 180 190 200
HHNTGLSEAL EILAEAAGFE GSEGRLLTFC RAASVLKALP SPVTTLSQLQ
210 220 230 240 250
GLPHFGEHSS RVVQELLEHG VCEEVERVRR SERYQTMKLF TQIFGVGVKT
260 270 280 290 300
ADRWYREGLR TLDDLREQPQ KLTQQQKAGL QHHQDLSTPV LRSDVDALQQ
310 320 330 340 350
VVEEAVGQAL PGATVTLTGG FRRGKLQGHD VDFLITHPKE GQEAGLLPRV
360 370 380 390 400
MCRLQDQGLI LYHQHQHSCC ESPTRLAQQS HMDAFERSFC IFRLPQPPGA
410 420 430 440 450
AVGGSTRPCP SWKAVRVDLV VAPVSQFPFA LLGWTGSKLF QRELRRFSRK
460 470 480 490
EKGLWLNSHG LFDPEQKTFF QAASEEDIFR HLGLEYLPPE QRNA
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. 1 PublicationVSP_055288Add
BLAST
Alternative sequencei277 – 35680Missing in isoform 3. 1 PublicationVSP_055289Add
BLAST
Alternative sequencei279 – 35678GLQHH…CRLQD → APPGPEHPSPAVRCRCPAAG GGGSCGAGPAWGHRHADRRL P in isoform 2. 1 PublicationVSP_055290Add
BLAST
Alternative sequencei467 – 49428KTFFQ…EQRNA → GSSSGKTPRSRKSCFCCRRH FSKRLQRKTSSDTWALSTFL QSRETPEPACVPHFHSGNWA APNLATECLQADMLPPDPHL HPSPPRPGSSGGQLCLQDQL SPCWCAAGCDEVGALSASLI TV in isoform 3. 1 PublicationVSP_055291Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS64635.1. [Q9NP87-2]
CCDS64636.1. [Q9NP87-3]
RefSeqiNP_001271259.1. NM_001284330.1. [Q9NP87-3]
NP_001271260.1. NM_001284331.1. [Q9NP87-2]
NP_037416.1. NM_013284.3. [Q9NP87-1]
UniGeneiHs.596982.
Hs.598038.

Genome annotation databases

EnsembliENST00000242248; ENSP00000242248; ENSG00000122678. [Q9NP87-1]
ENST00000335195; ENSP00000335141; ENSG00000122678. [Q9NP87-2]
ENST00000395831; ENSP00000379174; ENSG00000122678. [Q9NP87-3]
GeneIDi27434.
KEGGihsa:27434.
UCSCiuc003tjt.3. human. [Q9NP87-1]
uc003tju.3. human.
uc003tjx.2. human.

Polymorphism databases

DMDMi17366980.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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 ]
CCDS64635.1. [Q9NP87-2 ]
CCDS64636.1. [Q9NP87-3 ]
RefSeqi NP_001271259.1. NM_001284330.1. [Q9NP87-3 ]
NP_001271260.1. NM_001284331.1. [Q9NP87-2 ]
NP_037416.1. NM_013284.3. [Q9NP87-1 ]
UniGenei Hs.596982.
Hs.598038.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118168. 6 interactions.
IntActi Q9NP87. 2 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 . [Q9NP87-1 ]
ENST00000335195 ; ENSP00000335141 ; ENSG00000122678 . [Q9NP87-2 ]
ENST00000395831 ; ENSP00000379174 ; ENSG00000122678 . [Q9NP87-3 ]
GeneIDi 27434.
KEGGi hsa:27434.
UCSCi uc003tjt.3. human. [Q9NP87-1 ]
uc003tju.3. human.
uc003tjx.2. human.

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.
GeneTreei ENSGT00530000063002.
HOGENOMi HOG000263600.
HOVERGENi HBG003670.
InParanoidi Q9NP87.
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

Bgeei Q9NP87.
CleanExi HS_POLM.
ExpressionAtlasi Q9NP87. baseline.
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: November 26, 2014
This is version 121 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

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