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Q9NP87

- DPOLM_HUMAN

UniProt

Q9NP87 - DPOLM_HUMAN

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
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    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 – 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. 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

    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

    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

    ArrayExpressiQ9NP87.
    BgeeiQ9NP87.
    CleanExiHS_POLM.
    GenevestigatoriQ9NP87.

    Interactioni

    Protein-protein interaction databases

    BioGridi118168. 6 interactions.
    STRINGi9606.ENSP00000242248.

    Structurei

    Secondary structure

    1
    494
    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.
    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.
    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. 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:
    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]
    CCDS64635.1. [Q9NP87-2]
    CCDS64636.1. [Q9NP87-3]
    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. [Q9NP87-1]
    ENST00000335195; ENSP00000335141; ENSG00000122678. [Q9NP87-2]
    ENST00000395831; ENSP00000379174; ENSG00000122678. [Q9NP87-3]
    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 ]
    CCDS64635.1. [Q9NP87-2 ]
    CCDS64636.1. [Q9NP87-3 ]
    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...
    MobiDBi 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 . [Q9NP87-1 ]
    ENST00000335195 ; ENSP00000335141 ; ENSG00000122678 . [Q9NP87-2 ]
    ENST00000395831 ; ENSP00000379174 ; ENSG00000122678 . [Q9NP87-3 ]
    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

    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: October 1, 2014
    This is version 119 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