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Q9UNA4

- POLI_HUMAN

UniProt

Q9UNA4 - POLI_HUMAN

Protein

DNA polymerase iota

Gene

POLI

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 3 (05 Apr 2011)
      Previous versions | rss
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    Functioni

    Error-prone DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Favors Hoogsteen base-pairing in the active site. Inserts the correct base with high-fidelity opposite an adenosine template. Exhibits low fidelity and efficiency opposite a thymidine template, where it will preferentially insert guanosine. May play a role in hypermutation of immunogobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but may not have lyase activity.7 Publications

    Catalytic activityi

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

    Cofactori

    Magnesium.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi59 – 591Magnesium
    Binding sitei64 – 641dNTP
    Binding sitei96 – 961dNTP
    Metal bindingi151 – 1511Magnesium
    Active sitei152 – 1521Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. damaged DNA binding Source: InterPro
    2. DNA-directed DNA polymerase activity Source: ProtInc
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct

    GO - Biological processi

    1. DNA-dependent DNA replication Source: GOC
    2. DNA repair Source: ProtInc

    Keywords - Molecular functioni

    DNA-directed DNA polymerase, Mutator protein, Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    DNA damage, DNA repair, DNA replication, DNA synthesis

    Keywords - Ligandi

    DNA-binding, Magnesium, Metal-binding, Schiff base

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA polymerase iota (EC:2.7.7.7)
    Alternative name(s):
    Eta2
    RAD30 homolog B
    Gene namesi
    Name:POLI
    Synonyms:RAD30B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:9182. POLI.

    Subcellular locationi

    Nucleus 1 Publication
    Note: Accumulates at replication forks after DNA damage.

    GO - Cellular componenti

    1. intracellular Source: LIFEdb
    2. intracellular membrane-bounded organelle Source: HPA
    3. nucleoplasm Source: ProtInc
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33502.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 740740DNA polymerase iotaPRO_0000173988Add
    BLAST

    Proteomic databases

    MaxQBiQ9UNA4.
    PaxDbiQ9UNA4.
    PRIDEiQ9UNA4.

    PTM databases

    PhosphoSiteiQ9UNA4.

    Expressioni

    Tissue specificityi

    Ubiquitous. Highly expressed in testis.2 Publications

    Gene expression databases

    ArrayExpressiQ9UNA4.
    BgeeiQ9UNA4.
    CleanExiHS_POLI.
    GenevestigatoriQ9UNA4.

    Organism-specific databases

    HPAiHPA012000.

    Interactioni

    Subunit structurei

    Interacts with REV1 By similarity. Interacts with POLH.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DAZAP2Q150383EBI-741774,EBI-724310
    PCNAQ6FI352EBI-741774,EBI-8469539
    UBCP0CG484EBI-741774,EBI-3390054
    XRCC1P188872EBI-741774,EBI-947466

    Protein-protein interaction databases

    BioGridi116370. 13 interactions.
    IntActiQ9UNA4. 9 interactions.
    MINTiMINT-1189678.
    STRINGi9606.ENSP00000217800.

    Structurei

    Secondary structure

    1
    740
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi55 – 606
    Helixi63 – 719
    Helixi73 – 753
    Beta strandi76 – 783
    Beta strandi80 – 845
    Beta strandi87 – 915
    Helixi93 – 964
    Turni97 – 993
    Beta strandi102 – 1054
    Helixi106 – 1127
    Beta strandi113 – 1153
    Beta strandi117 – 1204
    Helixi125 – 14117
    Beta strandi145 – 1484
    Turni149 – 1513
    Beta strandi152 – 1565
    Helixi158 – 16710
    Beta strandi170 – 1723
    Helixi173 – 1753
    Beta strandi180 – 1823
    Helixi183 – 1853
    Helixi193 – 21624
    Beta strandi220 – 2278
    Helixi228 – 2358
    Beta strandi236 – 2383
    Turni239 – 2413
    Beta strandi243 – 2453
    Helixi248 – 2503
    Helixi251 – 2577
    Helixi261 – 2633
    Helixi269 – 2779
    Helixi283 – 2886
    Helixi291 – 31020
    Beta strandi325 – 3328
    Turni334 – 3363
    Beta strandi339 – 3413
    Helixi342 – 36019
    Beta strandi362 – 37413
    Turni377 – 3793
    Beta strandi383 – 3886
    Turni391 – 3933
    Beta strandi397 – 3993
    Helixi401 – 4044
    Helixi405 – 41915
    Beta strandi422 – 4243
    Beta strandi427 – 43913
    Beta strandi704 – 7074
    Helixi710 – 7134
    Helixi718 – 73114

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1T3NX-ray2.30A/B52-439[»]
    1ZETX-ray2.30A52-439[»]
    2ALZX-ray2.50A50-439[»]
    2DPIX-ray2.30A26-445[»]
    2DPJX-ray2.30A26-445[»]
    2FLLX-ray2.60A26-445[»]
    2FLNX-ray2.50A26-445[»]
    2FLPX-ray2.40A26-445[»]
    2KHUNMR-A697-740[»]
    2KHWNMR-A697-740[»]
    2KTFNMR-B704-730[»]
    2L0FNMR-B699-740[»]
    2L0GNMR-A704-730[»]
    2MBBNMR-A516-520[»]
    3EPGX-ray2.50A26-445[»]
    3EPIX-ray2.90A26-445[»]
    3G6VX-ray2.20A26-445[»]
    3G6XX-ray2.08A26-445[»]
    3G6YX-ray2.10A26-445[»]
    3GV5X-ray2.00B/D26-445[»]
    3GV7X-ray2.20B26-445[»]
    3GV8X-ray2.00B26-445[»]
    3H40X-ray2.30A51-439[»]
    3H4BX-ray2.85A50-439[»]
    3H4DX-ray2.20A50-439[»]
    3NGDX-ray2.80A26-445[»]
    3OSNX-ray1.90A26-445[»]
    3Q8PX-ray1.95B26-445[»]
    3Q8QX-ray2.03B26-445[»]
    3Q8RX-ray2.45B26-445[»]
    3Q8SX-ray2.09B26-445[»]
    4EBCX-ray2.90A26-445[»]
    4EBDX-ray2.57A26-445[»]
    4EBEX-ray2.10A26-445[»]
    4EYHX-ray2.90B26-445[»]
    4EYIX-ray2.90B26-445[»]
    4FS1X-ray2.50A26-445[»]
    4FS2X-ray2.05A26-445[»]
    ProteinModelPortaliQ9UNA4.
    SMRiQ9UNA4. Positions 52-439, 518-553, 701-732.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UNA4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini55 – 268214UmuCPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni325 – 3328DNA binding
    Regioni368 – 38619DNA bindingAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi589 – 61729Ser-richAdd
    BLAST

    Domaini

    The catalytic core consists of fingers, palm and thumb subdomains, but the fingers and thumb subdomains are much smaller than in high-fidelity polymerases; residues from five sequence motifs of the Y-family cluster around an active site cleft that can accommodate DNA and nucleotide substrates with relaxed geometric constraints, with consequently higher rates of misincorporation and low processivity.

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0389.
    HOGENOMiHOG000234325.
    HOVERGENiHBG053634.
    InParanoidiQ9UNA4.
    KOiK03510.
    OMAiCFCNLKA.
    OrthoDBiEOG7C8GGJ.
    PhylomeDBiQ9UNA4.
    TreeFamiTF324222.

    Family and domain databases

    Gene3Di3.30.1490.100. 1 hit.
    InterProiIPR017961. DNA_pol_Y-fam_little_finger.
    IPR001126. DNA_repair_prot_UmuC-like.
    IPR017963. DNA_repair_prot_UmuC-like_N.
    [Graphical view]
    PfamiPF00817. IMS. 1 hit.
    PF11799. IMS_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF100879. SSF100879. 1 hit.
    PROSITEiPS50173. UMUC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9UNA4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEKLGVEPEE EGGGDDDEED AEAWAMELAD VGAAASSQGV HDQVLPTPNA    50
    SSRVIVHVDL DCFYAQVEMI SNPELKDKPL GVQQKYLVVT CNYEARKLGV 100
    KKLMNVRDAK EKCPQLVLVN GEDLTRYREM SYKVTELLEE FSPVVERLGF 150
    DENFVDLTEM VEKRLQQLQS DELSAVTVSG HVYNNQSINL LDVLHIRLLV 200
    GSQIAAEMRE AMYNQLGLTG CAGVASNKLL AKLVSGVFKP NQQTVLLPES 250
    CQHLIHSLNH IKEIPGIGYK TAKCLEALGI NSVRDLQTFS PKILEKELGI 300
    SVAQRIQKLS FGEDNSPVIL SGPPQSFSEE DSFKKCSSEV EAKNKIEELL 350
    ASLLNRVCQD GRKPHTVRLI IRRYSSEKHY GRESRQCPIP SHVIQKLGTG 400
    NYDVMTPMVD ILMKLFRNMV NVKMPFHLTL LSVCFCNLKA LNTAKKGLID 450
    YYLMPSLSTT SRSGKHSFKM KDTHMEDFPK DKETNRDFLP SGRIESTRTR 500
    ESPLDTTNFS KEKDINEFPL CSLPEGVDQE VFKQLPVDIQ EEILSGKSRE 550
    KFQGKGSVSC PLHASRGVLS FFSKKQMQDI PINPRDHLSS SKQVSSVSPC 600
    EPGTSGFNSS SSSYMSSQKD YSYYLDNRLK DERISQGPKE PQGFHFTNSN 650
    PAVSAFHSFP NLQSEQLFSR NHTTDSHKQT VATDSHEGLT ENREPDSVDE 700
    KITFPSDIDP QVFYELPEAV QKELLAEWKR AGSDFHIGHK 740
    Length:740
    Mass (Da):83,006
    Last modified:April 5, 2011 - v3
    Checksum:iC1A5BF0894E91FDF
    GO

    Sequence cautioni

    The sequence AAD50381.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAF63383.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH32662.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAB66605.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAM11872.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti15 – 151Missing in AAD50381. (PubMed:10458907)Curated
    Sequence conflicti15 – 151Missing in CAB66605. (PubMed:11230166)Curated
    Sequence conflicti15 – 151Missing in AAF63383. 1 PublicationCurated
    Sequence conflicti337 – 3371S → T in CAB66605. (PubMed:11230166)Curated
    Sequence conflicti433 – 4331V → A in AAF63383. 1 PublicationCurated
    Sequence conflicti514 – 5141D → G in AAF63383. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti96 – 961R → G.1 Publication
    Corresponds to variant rs3218778 [ dbSNP | Ensembl ].
    VAR_021239
    Natural varianti261 – 2611I → M.1 Publication
    Corresponds to variant rs3218784 [ dbSNP | Ensembl ].
    VAR_021240
    Natural varianti276 – 2761E → K.1 Publication
    Corresponds to variant rs3218783 [ dbSNP | Ensembl ].
    VAR_021241
    Natural varianti474 – 4741H → R.1 Publication
    Corresponds to variant rs3730823 [ dbSNP | Ensembl ].
    VAR_021242
    Natural varianti532 – 5321F → S.2 Publications
    Corresponds to variant rs3218786 [ dbSNP | Ensembl ].
    VAR_021243
    Natural varianti560 – 5601C → R.1 Publication
    Corresponds to variant rs3218787 [ dbSNP | Ensembl ].
    VAR_021244
    Natural varianti731 – 7311A → T.2 Publications
    Corresponds to variant rs8305 [ dbSNP | Ensembl ].
    VAR_021245

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY094607 Genomic DNA. Translation: AAM11872.1. Sequence problems.
    AC093462 Genomic DNA. No translation available.
    AF140501 mRNA. Translation: AAD50381.1. Different initiation.
    AL136670 mRNA. Translation: CAB66605.1. Different initiation.
    BC032662 mRNA. Translation: AAH32662.1. Different initiation.
    AF245438 mRNA. Translation: AAF63383.1. Different initiation.
    CCDSiCCDS11954.2.
    RefSeqiNP_009126.2. NM_007195.2.
    UniGeneiHs.438533.

    Genome annotation databases

    EnsembliENST00000579534; ENSP00000462664; ENSG00000101751.
    GeneIDi11201.
    KEGGihsa:11201.
    UCSCiuc002lfj.4. human.

    Polymorphism databases

    DMDMi327478565.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY094607 Genomic DNA. Translation: AAM11872.1 . Sequence problems.
    AC093462 Genomic DNA. No translation available.
    AF140501 mRNA. Translation: AAD50381.1 . Different initiation.
    AL136670 mRNA. Translation: CAB66605.1 . Different initiation.
    BC032662 mRNA. Translation: AAH32662.1 . Different initiation.
    AF245438 mRNA. Translation: AAF63383.1 . Different initiation.
    CCDSi CCDS11954.2.
    RefSeqi NP_009126.2. NM_007195.2.
    UniGenei Hs.438533.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1T3N X-ray 2.30 A/B 52-439 [» ]
    1ZET X-ray 2.30 A 52-439 [» ]
    2ALZ X-ray 2.50 A 50-439 [» ]
    2DPI X-ray 2.30 A 26-445 [» ]
    2DPJ X-ray 2.30 A 26-445 [» ]
    2FLL X-ray 2.60 A 26-445 [» ]
    2FLN X-ray 2.50 A 26-445 [» ]
    2FLP X-ray 2.40 A 26-445 [» ]
    2KHU NMR - A 697-740 [» ]
    2KHW NMR - A 697-740 [» ]
    2KTF NMR - B 704-730 [» ]
    2L0F NMR - B 699-740 [» ]
    2L0G NMR - A 704-730 [» ]
    2MBB NMR - A 516-520 [» ]
    3EPG X-ray 2.50 A 26-445 [» ]
    3EPI X-ray 2.90 A 26-445 [» ]
    3G6V X-ray 2.20 A 26-445 [» ]
    3G6X X-ray 2.08 A 26-445 [» ]
    3G6Y X-ray 2.10 A 26-445 [» ]
    3GV5 X-ray 2.00 B/D 26-445 [» ]
    3GV7 X-ray 2.20 B 26-445 [» ]
    3GV8 X-ray 2.00 B 26-445 [» ]
    3H40 X-ray 2.30 A 51-439 [» ]
    3H4B X-ray 2.85 A 50-439 [» ]
    3H4D X-ray 2.20 A 50-439 [» ]
    3NGD X-ray 2.80 A 26-445 [» ]
    3OSN X-ray 1.90 A 26-445 [» ]
    3Q8P X-ray 1.95 B 26-445 [» ]
    3Q8Q X-ray 2.03 B 26-445 [» ]
    3Q8R X-ray 2.45 B 26-445 [» ]
    3Q8S X-ray 2.09 B 26-445 [» ]
    4EBC X-ray 2.90 A 26-445 [» ]
    4EBD X-ray 2.57 A 26-445 [» ]
    4EBE X-ray 2.10 A 26-445 [» ]
    4EYH X-ray 2.90 B 26-445 [» ]
    4EYI X-ray 2.90 B 26-445 [» ]
    4FS1 X-ray 2.50 A 26-445 [» ]
    4FS2 X-ray 2.05 A 26-445 [» ]
    ProteinModelPortali Q9UNA4.
    SMRi Q9UNA4. Positions 52-439, 518-553, 701-732.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116370. 13 interactions.
    IntActi Q9UNA4. 9 interactions.
    MINTi MINT-1189678.
    STRINGi 9606.ENSP00000217800.

    Chemistry

    ChEMBLi CHEMBL5391.

    PTM databases

    PhosphoSitei Q9UNA4.

    Polymorphism databases

    DMDMi 327478565.

    Proteomic databases

    MaxQBi Q9UNA4.
    PaxDbi Q9UNA4.
    PRIDEi Q9UNA4.

    Protocols and materials databases

    DNASUi 11201.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000579534 ; ENSP00000462664 ; ENSG00000101751 .
    GeneIDi 11201.
    KEGGi hsa:11201.
    UCSCi uc002lfj.4. human.

    Organism-specific databases

    CTDi 11201.
    GeneCardsi GC18P051731.
    H-InvDB HIX0014457.
    HGNCi HGNC:9182. POLI.
    HPAi HPA012000.
    MIMi 605252. gene.
    neXtProti NX_Q9UNA4.
    PharmGKBi PA33502.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0389.
    HOGENOMi HOG000234325.
    HOVERGENi HBG053634.
    InParanoidi Q9UNA4.
    KOi K03510.
    OMAi CFCNLKA.
    OrthoDBi EOG7C8GGJ.
    PhylomeDBi Q9UNA4.
    TreeFami TF324222.

    Miscellaneous databases

    ChiTaRSi POLI. human.
    EvolutionaryTracei Q9UNA4.
    GeneWikii POLI.
    GenomeRNAii 11201.
    NextBioi 42637.
    PROi Q9UNA4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UNA4.
    Bgeei Q9UNA4.
    CleanExi HS_POLI.
    Genevestigatori Q9UNA4.

    Family and domain databases

    Gene3Di 3.30.1490.100. 1 hit.
    InterProi IPR017961. DNA_pol_Y-fam_little_finger.
    IPR001126. DNA_repair_prot_UmuC-like.
    IPR017963. DNA_repair_prot_UmuC-like_N.
    [Graphical view ]
    Pfami PF00817. IMS. 1 hit.
    PF11799. IMS_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF100879. SSF100879. 1 hit.
    PROSITEi PS50173. UMUC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. NIEHS SNPs program
      Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLY-96; MET-261; LYS-276; ARG-474; SER-532 AND ARG-560.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Novel human and mouse homologs of Saccharomyces cerevisiae DNA polymerase eta."
      McDonald J.P., Rapic-Otrin V., Epstein J.A., Broughton B.C., Wang X., Lehmann A.R., Wolgemuth D.J., Woodgate R.
      Genomics 60:20-30(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-740, VARIANT THR-731, TISSUE SPECIFICITY.
      Tissue: Umbilical vein endothelial cell.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-740, VARIANT SER-532.
      Tissue: Brain.
    5. "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] OF 12-740.
      Tissue: Uterus.
    6. "Human eta2 gene homologous to bacterial UmuC and Rev1 genes."
      Poltoratsky V.P., Scharff M.D.
      Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-740, VARIANT THR-731.
    7. "Misinsertion and bypass of thymine-thymine dimers by human DNA polymerase iota."
      Tissier A., Frank E.G., McDonald J.P., Iwai S., Hanaoka F., Woodgate R.
      EMBO J. 19:5259-5266(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "5'-deoxyribose phosphate lyase activity of human DNA polymerase iota in vitro."
      Bebenek K., Tissier A., Frank E.G., McDonald J.P., Prasad R., Wilson S.H., Woodgate R., Kunkel T.A.
      Science 291:2156-2159(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SCHIFF BASE FORMATION.
    9. "Altered nucleotide misinsertion fidelity associated with poliota-dependent replication at the end of a DNA template."
      Frank E.G., Tissier A., McDonald J.P., Rapic-Otrin V., Zeng X., Gearhart P.J., Woodgate R.
      EMBO J. 20:2914-2922(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    10. "Induction of somatic hypermutation in immunoglobulin genes is dependent on DNA polymerase iota."
      Faili A., Aoufouchi S., Flatter E., Gueranger Q., Reynaud C.-A., Weill J.-C.
      Nature 419:944-947(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Localization of DNA polymerases eta and iota to the replication machinery is tightly co-ordinated in human cells."
      Kannouche P.L., Fernandez de Henestrosa A.R., Coull B., Vidal A.E., Gray C., Zicha D., Woodgate R., Lehmann A.R.
      EMBO J. 22:1223-1233(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH POLH.
    12. "A mechanism for the exclusion of low-fidelity human Y-family DNA polymerases from base excision repair."
      Haracska L., Prakash L., Prakash S.
      Genes Dev. 17:2777-2785(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SCHIFF BASE FORMATION.
    13. "Efficient and error-free replication past a minor-groove DNA adduct by the sequential action of human DNA polymerases iota and kappa."
      Washington M.T., Minko I.G., Johnson R.E., Wolfle W.T., Harris T.M., Lloyd R.S., Prakash S., Prakash L.
      Mol. Cell. Biol. 24:5687-5693(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Replication by human DNA polymerase-iota occurs by Hoogsteen base-pairing."
      Nair D.T., Johnson R.E., Prakash S., Prakash L., Aggarwal A.K.
      Nature 430:377-380(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 52-439 IN COMPLEX WITH DNA AND NUCLEOTIDE, FUNCTION.

    Entry informationi

    Entry nameiPOLI_HUMAN
    AccessioniPrimary (citable) accession number: Q9UNA4
    Secondary accession number(s): Q8N590, Q9H0S1, Q9NYH6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 15, 2005
    Last sequence update: April 5, 2011
    Last modified: October 1, 2014
    This is version 121 of the entry and version 3 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 18
      Human chromosome 18: 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