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Q9UGP5

- DPOLL_HUMAN

UniProt

Q9UGP5 - DPOLL_HUMAN

Protein

DNA polymerase lambda

Gene

POLL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Repair polymerase. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Has both DNA polymerase and terminal transferase activities. Has a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.2 Publications

    Catalytic activityi

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

    Cofactori

    Manganese.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei312 – 3121Schiff-base intermediate with DNA
    Metal bindingi427 – 4271ManganeseBy similarity
    Metal bindingi429 – 4291ManganeseBy similarity
    Metal bindingi490 – 4901ManganeseBy similarity

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. DNA-directed DNA polymerase activity Source: UniProtKB
    3. lyase activity Source: UniProtKB-KW
    4. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. DNA-dependent DNA replication Source: GOC
    2. DNA replication Source: UniProtKB
    3. nucleotide-excision repair Source: UniProtKB
    4. somatic hypermutation of immunoglobulin genes Source: UniProtKB

    Keywords - Molecular functioni

    DNA-directed DNA polymerase, Lyase, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    DNA damage, DNA repair, DNA replication, DNA synthesis

    Keywords - Ligandi

    DNA-binding, Manganese, Metal-binding

    Enzyme and pathway databases

    SABIO-RKQ9UGP5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA polymerase lambda (EC:2.7.7.7, EC:4.2.99.-)
    Short name:
    Pol Lambda
    Alternative name(s):
    DNA polymerase beta-2
    Short name:
    Pol beta2
    DNA polymerase kappa
    Gene namesi
    Name:POLL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:9184. POLL.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi312 – 3121K → A: Reduces dRP lyase activity by over 90%. 1 Publication
    Mutagenesisi505 – 5051Y → A: No effect on polymerase activity. Reduces terminal transferase activitites. 1 Publication
    Mutagenesisi506 – 5061F → G or R: Strongly reduces polymerase and terminal transferase activitites. 1 Publication

    Organism-specific databases

    PharmGKBiPA33504.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 575575DNA polymerase lambdaPRO_0000218783Add
    BLAST

    Proteomic databases

    MaxQBiQ9UGP5.
    PaxDbiQ9UGP5.
    PRIDEiQ9UGP5.

    PTM databases

    PhosphoSiteiQ9UGP5.

    Expressioni

    Tissue specificityi

    Expressed in a number of tissues. Abundant in testis.

    Gene expression databases

    ArrayExpressiQ9UGP5.
    BgeeiQ9UGP5.
    CleanExiHS_POLL.
    GenevestigatoriQ9UGP5.

    Interactioni

    Subunit structurei

    Binds PCNA.1 Publication

    Protein-protein interaction databases

    BioGridi118155. 9 interactions.
    DIPiDIP-48999N.
    IntActiQ9UGP5. 2 interactions.
    MINTiMINT-3079892.
    STRINGi9606.ENSP00000299206.

    Structurei

    Secondary structure

    1
    575
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi37 – 393
    Helixi41 – 433
    Turni50 – 523
    Beta strandi55 – 573
    Helixi60 – 678
    Beta strandi82 – 854
    Beta strandi87 – 893
    Helixi91 – 977
    Beta strandi108 – 1114
    Helixi112 – 1209
    Helixi127 – 1293
    Beta strandi247 – 2504
    Helixi254 – 26916
    Helixi273 – 28715
    Beta strandi289 – 2913
    Helixi296 – 3005
    Helixi307 – 31812
    Beta strandi319 – 3213
    Helixi323 – 3275
    Helixi332 – 3398
    Helixi346 – 3549
    Helixi360 – 3667
    Helixi371 – 3788
    Turni379 – 3813
    Helixi382 – 3843
    Helixi389 – 40416
    Beta strandi411 – 4144
    Helixi416 – 4194
    Beta strandi423 – 43311
    Beta strandi435 – 4384
    Turni439 – 4424
    Helixi444 – 45310
    Beta strandi457 – 4626
    Beta strandi466 – 4683
    Beta strandi472 – 4776
    Beta strandi480 – 4834
    Beta strandi487 – 4937
    Helixi496 – 4983
    Helixi499 – 5079
    Helixi510 – 52213
    Beta strandi525 – 5273
    Beta strandi532 – 5354
    Beta strandi544 – 5463
    Beta strandi549 – 5513
    Helixi556 – 5627
    Helixi570 – 5734

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NZPNMR-A242-327[»]
    1RZTX-ray2.10A/E/I/M245-575[»]
    1XSLX-ray2.30A/E/I/M242-575[»]
    1XSNX-ray1.95A242-575[»]
    1XSPX-ray2.20A242-575[»]
    2BCQX-ray1.65A242-575[»]
    2BCRX-ray1.75A242-575[»]
    2BCSX-ray2.20A242-575[»]
    2BCUX-ray2.20A242-575[»]
    2BCVX-ray2.00A242-575[»]
    2GWSX-ray2.40A/E/I/M242-575[»]
    2JW5NMR-A34-135[»]
    2PFNX-ray1.90A242-575[»]
    2PFOX-ray2.00A242-575[»]
    2PFPX-ray2.10A242-575[»]
    2PFQX-ray2.10A242-575[»]
    3C5FX-ray2.25A/B242-575[»]
    3C5GX-ray2.20A/B242-575[»]
    3HW8X-ray1.95A242-575[»]
    3HWTX-ray1.95A242-575[»]
    3HX0X-ray3.00A/F/K/P242-575[»]
    3MDAX-ray2.03A252-575[»]
    3MDCX-ray2.00A252-575[»]
    3MGHX-ray2.40A/C242-462[»]
    A/C472-575[»]
    3MGIX-ray2.60A242-462[»]
    A472-575[»]
    3PMLX-ray2.60A/B242-575[»]
    3PMNX-ray2.20A242-575[»]
    3PNCX-ray2.00A242-575[»]
    3UPQX-ray1.95A242-575[»]
    3UQ0X-ray2.14A242-575[»]
    3UQ2X-ray2.25A242-575[»]
    4FO6X-ray2.01A242-575[»]
    ProteinModelPortaliQ9UGP5.
    SMRiQ9UGP5. Positions 34-135, 252-575.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UGP5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini36 – 13297BRCTPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni265 – 27915DNA bindingAdd
    BLAST
    Regioni345 – 3484DNA binding
    Regioni420 – 42910Involved in primer bindingBy similarity
    Regioni466 – 50540DNA bindingAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1796.
    HOGENOMiHOG000007787.
    HOVERGENiHBG002788.
    InParanoidiQ9UGP5.
    KOiK03512.
    OMAiWTEELIP.
    OrthoDBiEOG73Z2SX.
    PhylomeDBiQ9UGP5.
    TreeFamiTF103011.

    Family and domain databases

    Gene3Di1.10.150.110. 1 hit.
    3.30.210.10. 1 hit.
    3.40.50.10190. 1 hit.
    InterProiIPR001357. BRCT_dom.
    IPR002054. DNA-dir_DNA_pol_X.
    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.
    IPR002008. DNA_pol_X_beta-like.
    IPR027421. DNA_pol_X_lyase_dom.
    IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
    IPR029398. PolB_thumb.
    [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]
    PRINTSiPR00869. DNAPOLX.
    PR00870. DNAPOLXBETA.
    SMARTiSM00278. HhH1. 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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UGP5-1) [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

    MDPRGILKAF PKRQKIHADA SSKVLAKIPR REEGEEAEEW LSSLRAHVVR    50
    TGIGRARAEL FEKQIVQHGG QLCPAQGPGV THIVVDEGMD YERALRLLRL 100
    PQLPPGAQLV KSAWLSLCLQ ERRLVDVAGF SIFIPSRYLD HPQPSKAEQD 150
    ASIPPGTHEA LLQTALSPPP PPTRPVSPPQ KAKEAPNTQA QPISDDEASD 200
    GEETQVSAAD LEALISGHYP TSLEGDCEPS PAPAVLDKWV CAQPSSQKAT 250
    NHNLHITEKL EVLAKAYSVQ GDKWRALGYA KAINALKSFH KPVTSYQEAC 300
    SIPGIGKRMA EKIIEILESG HLRKLDHISE SVPVLELFSN IWGAGTKTAQ 350
    MWYQQGFRSL EDIRSQASLT TQQAIGLKHY SDFLERMPRE EATEIEQTVQ 400
    KAAQAFNSGL LCVACGSYRR GKATCGDVDV LITHPDGRSH RGIFSRLLDS 450
    LRQEGFLTDD LVSQEENGQQ QKYLGVCRLP GPGRRHRRLD IIVVPYSEFA 500
    CALLYFTGSA HFNRSMRALA KTKGMSLSEH ALSTAVVRNT HGCKVGPGRV 550
    LPTPTEKDVF RLLGLPYREP AERDW 575
    Length:575
    Mass (Da):63,482
    Last modified:May 1, 2000 - v1
    Checksum:iFD9196A1C94923C4
    GO
    Isoform 2 (identifier: Q9UGP5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-22: MDPRGILKAFPKRQKIHADASS → MLMHHQKYLQRFLGGKREKKQK
         23-297: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:300
    Mass (Da):33,839
    Checksum:iB67B993D5EC4A47C
    GO

    Sequence cautioni

    The sequence BAB14050.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti138 – 1381Y → C in AAG22519. (PubMed:10887191)Curated
    Sequence conflicti298 – 2981E → G in AAH68529. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti221 – 2211T → P.
    Corresponds to variant rs3730463 [ dbSNP | Ensembl ].
    VAR_020268
    Natural varianti438 – 4381R → W.1 Publication
    Corresponds to variant rs3730477 [ dbSNP | Ensembl ].
    VAR_020269

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2222MDPRG…ADASS → MLMHHQKYLQRFLGGKREKK QK in isoform 2. 1 PublicationVSP_056540Add
    BLAST
    Alternative sequencei23 – 297275Missing in isoform 2. 1 PublicationVSP_056541Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ131890 mRNA. Translation: CAB65074.1.
    AF161019 mRNA. Translation: AAF27541.1.
    AF283478 mRNA. Translation: AAG22519.1.
    AF525924 Genomic DNA. Translation: AAM77696.1.
    AL627424 Genomic DNA. Translation: CAI41032.1.
    CH471066 Genomic DNA. Translation: EAW49759.1.
    CH471066 Genomic DNA. Translation: EAW49760.1.
    CH471066 Genomic DNA. Translation: EAW49766.1.
    CH471066 Genomic DNA. Translation: EAW49768.1.
    BC003548 mRNA. Translation: AAH03548.2.
    BC068529 mRNA. Translation: AAH68529.1.
    AK022476 mRNA. Translation: BAB14050.1. Different initiation.
    CCDSiCCDS7513.1.
    RefSeqiNP_001167555.1. NM_001174084.1.
    NP_001167556.1. NM_001174085.1.
    NP_037406.1. NM_013274.3.
    XP_006717833.1. XM_006717770.1.
    XP_006717834.1. XM_006717771.1.
    XP_006717840.1. XM_006717777.1.
    UniGeneiHs.523230.

    Genome annotation databases

    EnsembliENST00000299206; ENSP00000299206; ENSG00000166169.
    ENST00000370158; ENSP00000359177; ENSG00000166169.
    ENST00000370162; ENSP00000359181; ENSG00000166169.
    ENST00000370169; ENSP00000359188; ENSG00000166169.
    GeneIDi27343.
    KEGGihsa:27343.
    UCSCiuc001ktg.1. human.

    Polymorphism databases

    DMDMi17367126.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ131890 mRNA. Translation: CAB65074.1 .
    AF161019 mRNA. Translation: AAF27541.1 .
    AF283478 mRNA. Translation: AAG22519.1 .
    AF525924 Genomic DNA. Translation: AAM77696.1 .
    AL627424 Genomic DNA. Translation: CAI41032.1 .
    CH471066 Genomic DNA. Translation: EAW49759.1 .
    CH471066 Genomic DNA. Translation: EAW49760.1 .
    CH471066 Genomic DNA. Translation: EAW49766.1 .
    CH471066 Genomic DNA. Translation: EAW49768.1 .
    BC003548 mRNA. Translation: AAH03548.2 .
    BC068529 mRNA. Translation: AAH68529.1 .
    AK022476 mRNA. Translation: BAB14050.1 . Different initiation.
    CCDSi CCDS7513.1.
    RefSeqi NP_001167555.1. NM_001174084.1.
    NP_001167556.1. NM_001174085.1.
    NP_037406.1. NM_013274.3.
    XP_006717833.1. XM_006717770.1.
    XP_006717834.1. XM_006717771.1.
    XP_006717840.1. XM_006717777.1.
    UniGenei Hs.523230.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NZP NMR - A 242-327 [» ]
    1RZT X-ray 2.10 A/E/I/M 245-575 [» ]
    1XSL X-ray 2.30 A/E/I/M 242-575 [» ]
    1XSN X-ray 1.95 A 242-575 [» ]
    1XSP X-ray 2.20 A 242-575 [» ]
    2BCQ X-ray 1.65 A 242-575 [» ]
    2BCR X-ray 1.75 A 242-575 [» ]
    2BCS X-ray 2.20 A 242-575 [» ]
    2BCU X-ray 2.20 A 242-575 [» ]
    2BCV X-ray 2.00 A 242-575 [» ]
    2GWS X-ray 2.40 A/E/I/M 242-575 [» ]
    2JW5 NMR - A 34-135 [» ]
    2PFN X-ray 1.90 A 242-575 [» ]
    2PFO X-ray 2.00 A 242-575 [» ]
    2PFP X-ray 2.10 A 242-575 [» ]
    2PFQ X-ray 2.10 A 242-575 [» ]
    3C5F X-ray 2.25 A/B 242-575 [» ]
    3C5G X-ray 2.20 A/B 242-575 [» ]
    3HW8 X-ray 1.95 A 242-575 [» ]
    3HWT X-ray 1.95 A 242-575 [» ]
    3HX0 X-ray 3.00 A/F/K/P 242-575 [» ]
    3MDA X-ray 2.03 A 252-575 [» ]
    3MDC X-ray 2.00 A 252-575 [» ]
    3MGH X-ray 2.40 A/C 242-462 [» ]
    A/C 472-575 [» ]
    3MGI X-ray 2.60 A 242-462 [» ]
    A 472-575 [» ]
    3PML X-ray 2.60 A/B 242-575 [» ]
    3PMN X-ray 2.20 A 242-575 [» ]
    3PNC X-ray 2.00 A 242-575 [» ]
    3UPQ X-ray 1.95 A 242-575 [» ]
    3UQ0 X-ray 2.14 A 242-575 [» ]
    3UQ2 X-ray 2.25 A 242-575 [» ]
    4FO6 X-ray 2.01 A 242-575 [» ]
    ProteinModelPortali Q9UGP5.
    SMRi Q9UGP5. Positions 34-135, 252-575.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118155. 9 interactions.
    DIPi DIP-48999N.
    IntActi Q9UGP5. 2 interactions.
    MINTi MINT-3079892.
    STRINGi 9606.ENSP00000299206.

    Chemistry

    BindingDBi Q9UGP5.
    ChEMBLi CHEMBL5367.

    PTM databases

    PhosphoSitei Q9UGP5.

    Polymorphism databases

    DMDMi 17367126.

    Proteomic databases

    MaxQBi Q9UGP5.
    PaxDbi Q9UGP5.
    PRIDEi Q9UGP5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000299206 ; ENSP00000299206 ; ENSG00000166169 .
    ENST00000370158 ; ENSP00000359177 ; ENSG00000166169 .
    ENST00000370162 ; ENSP00000359181 ; ENSG00000166169 .
    ENST00000370169 ; ENSP00000359188 ; ENSG00000166169 .
    GeneIDi 27343.
    KEGGi hsa:27343.
    UCSCi uc001ktg.1. human.

    Organism-specific databases

    CTDi 27343.
    GeneCardsi GC10M103328.
    HGNCi HGNC:9184. POLL.
    MIMi 606343. gene.
    neXtProti NX_Q9UGP5.
    PharmGKBi PA33504.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1796.
    HOGENOMi HOG000007787.
    HOVERGENi HBG002788.
    InParanoidi Q9UGP5.
    KOi K03512.
    OMAi WTEELIP.
    OrthoDBi EOG73Z2SX.
    PhylomeDBi Q9UGP5.
    TreeFami TF103011.

    Enzyme and pathway databases

    SABIO-RK Q9UGP5.

    Miscellaneous databases

    EvolutionaryTracei Q9UGP5.
    GeneWikii DNA_polymerase_lambda.
    GenomeRNAii 27343.
    NextBioi 50422.
    PROi Q9UGP5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UGP5.
    Bgeei Q9UGP5.
    CleanExi HS_POLL.
    Genevestigatori Q9UGP5.

    Family and domain databases

    Gene3Di 1.10.150.110. 1 hit.
    3.30.210.10. 1 hit.
    3.40.50.10190. 1 hit.
    InterProi IPR001357. BRCT_dom.
    IPR002054. DNA-dir_DNA_pol_X.
    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.
    IPR002008. DNA_pol_X_beta-like.
    IPR027421. DNA_pol_X_lyase_dom.
    IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
    IPR029398. PolB_thumb.
    [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 ]
    PRINTSi PR00869. DNAPOLX.
    PR00870. DNAPOLXBETA.
    SMARTi SM00278. HhH1. 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 kappa, a new mammalian meiotic polymerase."
      Garcia M., Dominguez O., Saniger M.L., Garcia M.J., Martinez C., Bernad A., Blanco L.
      Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Lymph node.
    3. "Identification and characterization of human DNA polymerase beta 2, a DNA polymerase beta-related enzyme."
      Nagasawa K.I., Kitamura K., Yasui A., Nimura Y., Ikeda K., Hirai M., Matsukage A., Nakanishi M.
      J. Biol. Chem. 275:31233-31238(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. NIEHS SNPs program
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TRP-438.
    5. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 1 AND 2).
      Tissue: Lung and Testis.
    8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-575 (ISOFORM 1).
      Tissue: Mammary gland.
    9. "Identification of an intrinsic 5'-deoxyribose-5-phosphate lyase activity in human DNA polymerase lambda: a possible role in base excision repair."
      Garcia-Diaz M., Bebenek K., Kunkel T.A., Blanco L.
      J. Biol. Chem. 276:34659-34663(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-312.
    10. "Human DNA polymerase lambda diverged in evolution from DNA polymerase beta toward specific Mn(++) dependence: a kinetic and thermodynamic study."
      Blanca G., Shevelev I., Ramadan K., Villani G., Spadari S., Huebscher U., Maga G.
      Biochemistry 42:7467-7476(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    11. "Mutagenesis of human DNA polymerase lambda: essential roles of Tyr505 and Phe506 for both DNA polymerase and terminal transferase activities."
      Shevelev I., Blanca G., Villani G., Ramadan K., Spadari S., Huebscher U., Maga G.
      Nucleic Acids Res. 31:6916-6925(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-505 AND PHE-506.
    12. "The human DNA polymerase lambda interacts with PCNA through a domain important for DNA primer binding and the interaction is inhibited by p21/WAF1/CIP1."
      Maga G., Blanca G., Shevelev I., Frouin I., Ramadan K., Spadari S., Villani G., Huebscher U.
      FASEB J. 18:1743-1745(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PCNA.
    13. "DNA elongation by the human DNA polymerase lambda polymerase and terminal transferase activities are differentially coordinated by proliferating cell nuclear antigen and replication protein A."
      Maga G., Ramadan K., Locatelli G.A., Shevelev I., Spadari S., Hubscher U.
      J. Biol. Chem. 280:1971-1981(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. Cited for: STRUCTURE BY NMR OF 241-327.
    15. "A structural solution for the DNA polymerase lambda-dependent repair of DNA gaps with minimal homology."
      Garcia-Diaz M., Bebenek K., Krahn J.M., Blanco L., Kunkel T.A., Pedersen L.C.
      Mol. Cell 13:561-572(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 245-575 IN COMPLEX WITH GAPPED DNA.

    Entry informationi

    Entry nameiDPOLL_HUMAN
    AccessioniPrimary (citable) accession number: Q9UGP5
    Secondary accession number(s): D3DR76
    , Q5JQP5, Q6NUM2, Q9BTN8, Q9HA10, Q9HB35
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 16, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 142 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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