Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9Y253

- POLH_HUMAN

UniProt

Q9Y253 - POLH_HUMAN

Protein

DNA polymerase eta

Gene

POLH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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. Plays an important role in the repair of UV-induced pyrimidine dimers. Depending on the context, it inserts the correct base, but causes frequent base transitions and transversions. May play a role in hypermutation at immunoglobulin genes. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity. Targets POLI to replication foci.5 Publications

    Catalytic activityi

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

    Cofactori

    Divalent metal cations. Prefers magnesium, but can also use manganese.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi13 – 131MagnesiumPROSITE-ProRule annotation
    Metal bindingi115 – 1151MagnesiumPROSITE-ProRule annotation

    GO - Molecular functioni

    1. damaged DNA binding Source: ProtInc
    2. DNA-directed DNA polymerase activity Source: Reactome
    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: Reactome
    3. DNA synthesis involved in DNA repair Source: UniProtKB
    4. postreplication repair Source: Ensembl
    5. pyrimidine dimer repair Source: Ensembl
    6. regulation of DNA repair Source: ProtInc
    7. response to UV-C Source: UniProtKB

    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

    Enzyme and pathway databases

    SABIO-RKQ9Y253.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA polymerase eta (EC:2.7.7.7)
    Alternative name(s):
    RAD30 homolog A
    Xeroderma pigmentosum variant type protein
    Gene namesi
    Name:POLH
    Synonyms:RAD30, RAD30A, XPV
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:9181. POLH.

    Subcellular locationi

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

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Xeroderma pigmentosum variant type (XPV) [MIM:278750]: An autosomal recessive pigmentary skin disorder characterized by solar hypersensitivity of the skin, high predisposition for developing cancers on areas exposed to sunlight and, in some cases, neurological abnormalities. XPV shows normal nucleotide excision repair, but an exaggerated delay in recovery of replicative DNA synthesis. Most patients with the variant type of xeroderma pigmentosum do not develop clinical symptoms and skin neoplasias until a later age. Clinical manifestations are limited to photo-induced deterioration of the skin and eyes.6 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti37 – 371Missing in XPV. 1 Publication
    VAR_070835
    Natural varianti75 – 751Missing in XPV; impairs translesion synthesis. 2 Publications
    VAR_021226
    Natural varianti93 – 931R → P in XPV. 1 Publication
    VAR_070836
    Natural varianti111 – 1111R → H in XPV.
    VAR_021227
    Natural varianti122 – 1221T → P in XPV. 1 Publication
    VAR_021228
    Natural varianti263 – 2631G → V in XPV; impairs translesion synthesis. 1 Publication
    VAR_021230
    Natural varianti266 – 2661V → D in XPV. 1 Publication
    VAR_070837
    Natural varianti295 – 2951G → R in XPV. 1 Publication
    VAR_070838
    Natural varianti361 – 3611R → S in XPV. 1 Publication
    VAR_021232
    Natural varianti535 – 5351K → E in XPV. 1 Publication
    Corresponds to variant rs56307355 [ dbSNP | Ensembl ].
    VAR_021234
    Natural varianti589 – 5891K → T in XPV. 1 Publication
    VAR_021236
    Natural varianti692 – 6921T → A in XPV. 1 Publication
    VAR_070839

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi52 – 521Y → A or F: Reduces DNA polymerase activity. 2 Publications
    Mutagenesisi52 – 521Y → E: Reduces DNA polymerase activity. Increases fidelity of replication and reduces translesion bypass. 2 Publications

    Keywords - Diseasei

    Disease mutation, Xeroderma pigmentosum

    Organism-specific databases

    MIMi278750. phenotype.
    Orphaneti90342. Xeroderma pigmentosum variant.
    PharmGKBiPA279.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 713713DNA polymerase etaPRO_0000173986Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki682 – 682Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
    Cross-linki686 – 686Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
    Cross-linki694 – 694Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
    Cross-linki709 – 709Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications

    Post-translational modificationi

    Monoubiquitinated by RCHY1/PIRH2; ubiquitination inhibits the ability of PolH to interact with PCNA and to bypass UV-induced lesions.2 Publications

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiQ9Y253.
    PaxDbiQ9Y253.
    PRIDEiQ9Y253.

    PTM databases

    PhosphoSiteiQ9Y253.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y253.
    BgeeiQ9Y253.
    CleanExiHS_POLH.
    GenevestigatoriQ9Y253.

    Organism-specific databases

    HPAiHPA006721.
    HPA026762.

    Interactioni

    Subunit structurei

    Interacts with REV1. Interacts with monoubiquitinated PCNA, but not unmodified PCNA. Interacts with POLI. Interacts with PALB2 and BRCA2; the interactions are direct and are involved in POLH localization at collapsed replication forks and DNA polymerization activity.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BRCA2P515876EBI-2827270,EBI-79792
    PALB2Q86YC27EBI-2827270,EBI-1222653
    PCNAQ6FI353EBI-2827270,EBI-8469539
    UBCP0CG484EBI-2827270,EBI-3390054

    Protein-protein interaction databases

    BioGridi111425. 20 interactions.
    IntActiQ9Y253. 8 interactions.
    MINTiMINT-2789553.
    STRINGi9606.ENSP00000361310.

    Structurei

    Secondary structure

    713
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1 – 33
    Beta strandi9 – 146
    Helixi17 – 259
    Helixi27 – 293
    Beta strandi34 – 385
    Turni41 – 444
    Beta strandi46 – 505
    Helixi52 – 554
    Turni56 – 583
    Beta strandi61 – 644
    Helixi65 – 717
    Beta strandi76 – 794
    Beta strandi81 – 833
    Beta strandi86 – 883
    Helixi90 – 10617
    Beta strandi109 – 1135
    Beta strandi116 – 1205
    Helixi122 – 13211
    Helixi139 – 1413
    Beta strandi145 – 1473
    Helixi159 – 1613
    Helixi163 – 17715
    Helixi186 – 20823
    Beta strandi212 – 2198
    Helixi220 – 22910
    Turni230 – 2334
    Beta strandi235 – 2373
    Helixi240 – 2423
    Helixi243 – 2486
    Helixi252 – 2543
    Helixi261 – 27010
    Helixi275 – 2806
    Helixi283 – 2908
    Helixi292 – 30110
    Turni302 – 3043
    Beta strandi313 – 3153
    Beta strandi319 – 3246
    Helixi327 – 3293
    Beta strandi331 – 3333
    Helixi334 – 35926
    Beta strandi360 – 37213
    Beta strandi376 – 3783
    Beta strandi380 – 3867
    Helixi392 – 40312
    Helixi404 – 4063
    Beta strandi414 – 43118
    Helixi532 – 5387
    Beta strandi632 – 6343
    Turni636 – 6383
    Beta strandi641 – 6433
    Helixi644 – 6463
    Helixi647 – 65913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2I5ONMR-A628-662[»]
    2LSKNMR-B524-539[»]
    3MR2X-ray1.83A1-432[»]
    3MR3X-ray1.75A1-432[»]
    3MR5X-ray1.80A1-432[»]
    3MR6X-ray1.90A1-432[»]
    3SI8X-ray2.15A1-432[»]
    3TQ1X-ray2.56A1-432[»]
    4DL2X-ray2.15A1-432[»]
    4DL3X-ray2.10A1-432[»]
    4DL4X-ray2.00A1-432[»]
    4DL5X-ray2.92A1-432[»]
    4DL6X-ray2.50A1-432[»]
    4DL7X-ray1.97A1-432[»]
    4ECQX-ray1.50A1-432[»]
    4ECRX-ray1.89A1-432[»]
    4ECSX-ray1.95A1-432[»]
    4ECTX-ray1.80A1-432[»]
    4ECUX-ray1.95A1-432[»]
    4ECVX-ray1.52A1-432[»]
    4ECWX-ray1.90A1-432[»]
    4ECXX-ray1.74A1-432[»]
    4ECYX-ray1.94A1-432[»]
    4ECZX-ray1.83A1-432[»]
    4ED0X-ray1.65A1-432[»]
    4ED1X-ray1.81A1-432[»]
    4ED2X-ray1.71A1-432[»]
    4ED3X-ray1.79A1-432[»]
    4ED6X-ray2.21A1-432[»]
    4ED7X-ray1.72A1-432[»]
    4ED8X-ray1.52A1-432[»]
    4EEYX-ray2.32A1-432[»]
    4J9KX-ray2.03A1-432[»]
    4J9LX-ray1.85A1-432[»]
    4J9MX-ray2.25A1-432[»]
    4J9NX-ray1.96A1-432[»]
    4J9OX-ray2.60A1-432[»]
    4J9PX-ray2.30A1-432[»]
    4J9QX-ray1.96A1-432[»]
    4J9RX-ray2.35A1-432[»]
    4J9SX-ray1.95A1-432[»]
    4O3NX-ray1.58A1-432[»]
    4O3OX-ray1.70A1-432[»]
    4O3PX-ray1.72A1-432[»]
    4O3QX-ray1.72A1-432[»]
    4O3RX-ray1.62A1-432[»]
    4O3SX-ray1.72A1-432[»]
    ProteinModelPortaliQ9Y253.
    SMRiQ9Y253. Positions 1-432, 629-662.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y253.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini9 – 259251UmuCPROSITE-ProRule annotationAdd
    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.
    HOGENOMiHOG000115605.
    HOVERGENiHBG053633.
    InParanoidiQ9Y253.
    KOiK03509.
    OMAiSPPLTML.
    PhylomeDBiQ9Y253.
    TreeFamiTF103010.

    Family and domain databases

    Gene3Di3.30.1490.100. 1 hit.
    InterProiIPR017061. DNA_pol_eta.
    IPR017961. 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]
    PIRSFiPIRSF036603. DPol_eta. 1 hit.
    SUPFAMiSSF100879. SSF100879. 1 hit.
    PROSITEiPS50173. UMUC. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y253-1) [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

    MATGQDRVVA LVDMDCFFVQ VEQRQNPHLR NKPCAVVQYK SWKGGGIIAV    50
    SYEARAFGVT RSMWADDAKK LCPDLLLAQV RESRGKANLT KYREASVEVM 100
    EIMSRFAVIE RASIDEAYVD LTSAVQERLQ KLQGQPISAD LLPSTYIEGL 150
    PQGPTTAEET VQKEGMRKQG LFQWLDSLQI DNLTSPDLQL TVGAVIVEEM 200
    RAAIERETGF QCSAGISHNK VLAKLACGLN KPNRQTLVSH GSVPQLFSQM 250
    PIRKIRSLGG KLGASVIEIL GIEYMGELTQ FTESQLQSHF GEKNGSWLYA 300
    MCRGIEHDPV KPRQLPKTIG CSKNFPGKTA LATREQVQWW LLQLAQELEE 350
    RLTKDRNDND RVATQLVVSI RVQGDKRLSS LRRCCALTRY DAHKMSHDAF 400
    TVIKNCNTSG IQTEWSPPLT MLFLCATKFS ASAPSSSTDI TSFLSSDPSS 450
    LPKVPVTSSE AKTQGSGPAV TATKKATTSL ESFFQKAAER QKVKEASLSS 500
    LTAPTQAPMS NSPSKPSLPF QTSQSTGTEP FFKQKSLLLK QKQLNNSSVS 550
    SPQQNPWSNC KALPNSLPTE YPGCVPVCEG VSKLEESSKA TPAEMDLAHN 600
    SQSMHASSAS KSVLEVTQKA TPNPSLLAAE DQVPCEKCGS LVPVWDMPEH 650
    MDYHFALELQ KSFLQPHSSN PQVVSAVSHQ GKRNPKSPLA CTNKRPRPEG 700
    MQTLESFFKP LTH 713
    Length:713
    Mass (Da):78,413
    Last modified:November 1, 1999 - v1
    Checksum:i6D1D35A0F56ECE89
    GO
    Isoform 2 (identifier: Q9Y253-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         415-713: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:414
    Mass (Da):46,283
    Checksum:i9ABB24D0511A45EB
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti37 – 371Missing in XPV. 1 Publication
    VAR_070835
    Natural varianti75 – 751Missing in XPV; impairs translesion synthesis. 2 Publications
    VAR_021226
    Natural varianti93 – 931R → P in XPV. 1 Publication
    VAR_070836
    Natural varianti111 – 1111R → H in XPV.
    VAR_021227
    Natural varianti122 – 1221T → P in XPV. 1 Publication
    VAR_021228
    Natural varianti153 – 1531G → D in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036220
    Natural varianti209 – 2091G → V.1 Publication
    Corresponds to variant rs2307456 [ dbSNP | Ensembl ].
    VAR_021229
    Natural varianti263 – 2631G → V in XPV; impairs translesion synthesis. 1 Publication
    VAR_021230
    Natural varianti266 – 2661V → D in XPV. 1 Publication
    VAR_070837
    Natural varianti295 – 2951G → R in XPV. 1 Publication
    VAR_070838
    Natural varianti334 – 3341R → W.1 Publication
    Corresponds to variant rs9333548 [ dbSNP | Ensembl ].
    VAR_021231
    Natural varianti361 – 3611R → S in XPV. 1 Publication
    VAR_021232
    Natural varianti478 – 4781T → M.1 Publication
    Corresponds to variant rs9296419 [ dbSNP | Ensembl ].
    VAR_021233
    Natural varianti535 – 5351K → E in XPV. 1 Publication
    Corresponds to variant rs56307355 [ dbSNP | Ensembl ].
    VAR_021234
    Natural varianti584 – 5841L → P.1 Publication
    Corresponds to variant rs9333554 [ dbSNP | Ensembl ].
    VAR_021235
    Natural varianti589 – 5891K → T in XPV. 1 Publication
    VAR_021236
    Natural varianti595 – 5951M → V.1 Publication
    Corresponds to variant rs9333555 [ dbSNP | Ensembl ].
    VAR_021237
    Natural varianti647 – 6471M → L.1 Publication
    Corresponds to variant rs6941583 [ dbSNP | Ensembl ].
    VAR_021238
    Natural varianti692 – 6921T → A in XPV. 1 Publication
    VAR_070839

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei415 – 713299Missing in isoform 2. 1 PublicationVSP_012799Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB024313 mRNA. Translation: BAA81666.1.
    AF158185 mRNA. Translation: AAD43810.1.
    AB038008 Genomic DNA. Translation: BAB18601.1.
    AY388614 Genomic DNA. Translation: AAQ81300.1.
    AL353602, AL355802 Genomic DNA. Translation: CAI12786.1.
    AL353602, AL355802 Genomic DNA. Translation: CAI12787.1.
    AL355802, AL353602 Genomic DNA. Translation: CAI42641.1.
    AL355802, AL353602 Genomic DNA. Translation: CAI42642.1.
    BC015742 mRNA. Translation: AAH15742.1.
    CCDSiCCDS4902.1. [Q9Y253-1]
    RefSeqiNP_006493.1. NM_006502.2. [Q9Y253-1]
    UniGeneiHs.655467.

    Genome annotation databases

    EnsembliENST00000372226; ENSP00000361300; ENSG00000170734. [Q9Y253-2]
    ENST00000372236; ENSP00000361310; ENSG00000170734. [Q9Y253-1]
    GeneIDi5429.
    KEGGihsa:5429.
    UCSCiuc003ovq.4. human. [Q9Y253-1]

    Polymorphism databases

    DMDMi59798441.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Allelic variations of the XP genes
    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB024313 mRNA. Translation: BAA81666.1 .
    AF158185 mRNA. Translation: AAD43810.1 .
    AB038008 Genomic DNA. Translation: BAB18601.1 .
    AY388614 Genomic DNA. Translation: AAQ81300.1 .
    AL353602 , AL355802 Genomic DNA. Translation: CAI12786.1 .
    AL353602 , AL355802 Genomic DNA. Translation: CAI12787.1 .
    AL355802 , AL353602 Genomic DNA. Translation: CAI42641.1 .
    AL355802 , AL353602 Genomic DNA. Translation: CAI42642.1 .
    BC015742 mRNA. Translation: AAH15742.1 .
    CCDSi CCDS4902.1. [Q9Y253-1 ]
    RefSeqi NP_006493.1. NM_006502.2. [Q9Y253-1 ]
    UniGenei Hs.655467.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2I5O NMR - A 628-662 [» ]
    2LSK NMR - B 524-539 [» ]
    3MR2 X-ray 1.83 A 1-432 [» ]
    3MR3 X-ray 1.75 A 1-432 [» ]
    3MR5 X-ray 1.80 A 1-432 [» ]
    3MR6 X-ray 1.90 A 1-432 [» ]
    3SI8 X-ray 2.15 A 1-432 [» ]
    3TQ1 X-ray 2.56 A 1-432 [» ]
    4DL2 X-ray 2.15 A 1-432 [» ]
    4DL3 X-ray 2.10 A 1-432 [» ]
    4DL4 X-ray 2.00 A 1-432 [» ]
    4DL5 X-ray 2.92 A 1-432 [» ]
    4DL6 X-ray 2.50 A 1-432 [» ]
    4DL7 X-ray 1.97 A 1-432 [» ]
    4ECQ X-ray 1.50 A 1-432 [» ]
    4ECR X-ray 1.89 A 1-432 [» ]
    4ECS X-ray 1.95 A 1-432 [» ]
    4ECT X-ray 1.80 A 1-432 [» ]
    4ECU X-ray 1.95 A 1-432 [» ]
    4ECV X-ray 1.52 A 1-432 [» ]
    4ECW X-ray 1.90 A 1-432 [» ]
    4ECX X-ray 1.74 A 1-432 [» ]
    4ECY X-ray 1.94 A 1-432 [» ]
    4ECZ X-ray 1.83 A 1-432 [» ]
    4ED0 X-ray 1.65 A 1-432 [» ]
    4ED1 X-ray 1.81 A 1-432 [» ]
    4ED2 X-ray 1.71 A 1-432 [» ]
    4ED3 X-ray 1.79 A 1-432 [» ]
    4ED6 X-ray 2.21 A 1-432 [» ]
    4ED7 X-ray 1.72 A 1-432 [» ]
    4ED8 X-ray 1.52 A 1-432 [» ]
    4EEY X-ray 2.32 A 1-432 [» ]
    4J9K X-ray 2.03 A 1-432 [» ]
    4J9L X-ray 1.85 A 1-432 [» ]
    4J9M X-ray 2.25 A 1-432 [» ]
    4J9N X-ray 1.96 A 1-432 [» ]
    4J9O X-ray 2.60 A 1-432 [» ]
    4J9P X-ray 2.30 A 1-432 [» ]
    4J9Q X-ray 1.96 A 1-432 [» ]
    4J9R X-ray 2.35 A 1-432 [» ]
    4J9S X-ray 1.95 A 1-432 [» ]
    4O3N X-ray 1.58 A 1-432 [» ]
    4O3O X-ray 1.70 A 1-432 [» ]
    4O3P X-ray 1.72 A 1-432 [» ]
    4O3Q X-ray 1.72 A 1-432 [» ]
    4O3R X-ray 1.62 A 1-432 [» ]
    4O3S X-ray 1.72 A 1-432 [» ]
    ProteinModelPortali Q9Y253.
    SMRi Q9Y253. Positions 1-432, 629-662.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111425. 20 interactions.
    IntActi Q9Y253. 8 interactions.
    MINTi MINT-2789553.
    STRINGi 9606.ENSP00000361310.

    Chemistry

    BindingDBi Q9Y253.
    ChEMBLi CHEMBL5542.

    PTM databases

    PhosphoSitei Q9Y253.

    Polymorphism databases

    DMDMi 59798441.

    Proteomic databases

    MaxQBi Q9Y253.
    PaxDbi Q9Y253.
    PRIDEi Q9Y253.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000372226 ; ENSP00000361300 ; ENSG00000170734 . [Q9Y253-2 ]
    ENST00000372236 ; ENSP00000361310 ; ENSG00000170734 . [Q9Y253-1 ]
    GeneIDi 5429.
    KEGGi hsa:5429.
    UCSCi uc003ovq.4. human. [Q9Y253-1 ]

    Organism-specific databases

    CTDi 5429.
    GeneCardsi GC06P043543.
    GeneReviewsi POLH.
    HGNCi HGNC:9181. POLH.
    HPAi HPA006721.
    HPA026762.
    MIMi 278750. phenotype.
    603968. gene.
    neXtProti NX_Q9Y253.
    Orphaneti 90342. Xeroderma pigmentosum variant.
    PharmGKBi PA279.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0389.
    HOGENOMi HOG000115605.
    HOVERGENi HBG053633.
    InParanoidi Q9Y253.
    KOi K03509.
    OMAi SPPLTML.
    PhylomeDBi Q9Y253.
    TreeFami TF103010.

    Enzyme and pathway databases

    SABIO-RK Q9Y253.

    Miscellaneous databases

    EvolutionaryTracei Q9Y253.
    GeneWikii DNA_polymerase_eta.
    GenomeRNAii 5429.
    NextBioi 21005.
    PROi Q9Y253.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y253.
    Bgeei Q9Y253.
    CleanExi HS_POLH.
    Genevestigatori Q9Y253.

    Family and domain databases

    Gene3Di 3.30.1490.100. 1 hit.
    InterProi IPR017061. DNA_pol_eta.
    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 ]
    PIRSFi PIRSF036603. DPol_eta. 1 hit.
    SUPFAMi SSF100879. SSF100879. 1 hit.
    PROSITEi PS50173. UMUC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The XPV (Xeroderma pigmentosum variant) gene encodes human DNA polymerase eta."
      Masutani C., Kusumoto R., Yamada A., Dohmae N., Yokoi M., Yuasa M., Araki M., Iwai S., Takio K., Hanaoka F.
      Nature 399:700-704(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 132-163; 395-404; 429-450 AND 495-511, FUNCTION, INVOLVEMENT IN XPV, ALTERNATIVE SPLICING.
      Tissue: Cervix carcinoma.
    2. "hRAD30 mutations in the variant form of xeroderma pigmentosum."
      Johnson R.E., Kondratick C.M., Prakash S., Prakash L.
      Science 285:263-265(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT XPV LEU-75 DEL.
    3. "Genomic structure, chromosomal localization and identification of mutations in the xeroderma pigmentosum variant (XPV) gene."
      Yuasa M., Masutani C., Eki T., Hanaoka F.
      Oncogene 19:4721-4728(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN XPV.
    4. NIEHS SNPs program
      Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-209; TRP-334; MET-478; PRO-584; VAL-595 AND LEU-647.
    5. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 2).
      Tissue: Skin.
    7. "Mutations in human DNA polymerase eta motif II alter bypass of DNA lesions."
      Glick E., Vigna K.L., Loeb L.A.
      EMBO J. 20:7303-7312(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS.
    8. "DNA polymerase eta is an A-T mutator in somatic hypermutation of immunoglobulin variable genes."
      Zeng X., Winter D.B., Kasmer C., Kraemer K.H., Lehmann A.R., Gearhart P.J.
      Nat. Immunol. 2:537-541(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "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 POLI.
    10. "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.
    11. "Amino acid substitutions at conserved tyrosine 52 alter fidelity and bypass efficiency of human DNA polymerase eta."
      Glick E., Chau J.S., Vigna K.L., McCulloch S.D., Adman E.T., Kunkel T.A., Loeb L.A.
      J. Biol. Chem. 278:19341-19346(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-52.
    12. "DNA polymerase eta is involved in hypermutation occurring during immunoglobulin class switch recombination."
      Faili A., Aoufouchi S., Weller S., Vuillier F., Stary A., Sarasin A., Reynaud C.-A., Weill J.-C.
      J. Exp. Med. 199:265-270(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Interaction of human DNA polymerase eta with monoubiquitinated PCNA: a possible mechanism for the polymerase switch in response to DNA damage."
      Kannouche P.L., Wing J., Lehmann A.R.
      Mol. Cell 14:491-500(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MONOUBIQUITINATED PCNA.
    14. "Regulation of translesion synthesis DNA polymerase eta by monoubiquitination."
      Bienko M., Green C.M., Sabbioneda S., Crosetto N., Matic I., Hibbert R.G., Begovic T., Niimi A., Mann M., Lehmann A.R., Dikic I.
      Mol. Cell 37:396-407(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-682; LYS-686; LYS-694 AND LYS-709.
    15. "Pirh2 E3 ubiquitin ligase monoubiquitinates DNA polymerase eta to suppress translesion DNA synthesis."
      Jung Y.S., Hakem A., Hakem R., Chen X.
      Mol. Cell. Biol. 31:3997-4006(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY RCHY1/PIRH2.
    16. "Breast cancer proteins PALB2 and BRCA2 stimulate polymerase eta in recombination-associated DNA synthesis at blocked replication forks."
      Buisson R., Niraj J., Pauty J., Maity R., Zhao W., Coulombe Y., Sung P., Masson J.Y.
      Cell Rep. 6:553-564(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PALB2 AND BRCA2.
    17. "Xeroderma pigmentosum variant heterozygotes show reduced levels of recovery of replicative DNA synthesis in the presence of caffeine after ultraviolet irradiation."
      Itoh T., Linn S., Kamide R., Tokushige H., Katori N., Hosaka Y., Yamaizumi M.
      J. Invest. Dermatol. 115:981-985(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS XPV GLU-535 AND THR-589.
    18. Cited for: VARIANTS XPV LEU-75 DEL; HIS-111 PRO-122; VAL-263 AND SER-361.
    19. "Correlation of phenotype/genotype in a cohort of 23 xeroderma pigmentosum-variant patients reveals 12 new disease-causing POLH mutations."
      Opletalova K., Bourillon A., Yang W., Pouvelle C., Armier J., Despras E., Ludovic M., Mateus C., Robert C., Kannouche P., Soufir N., Sarasin A.
      Hum. Mutat. 35:117-128(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS XPV VAL-37 DEL; PRO-93; ASP-266; ARG-295 AND ALA-692.
    20. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASP-153.

    Entry informationi

    Entry nameiPOLH_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y253
    Secondary accession number(s): Q7L8E3, Q96BC4, Q9BX13
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 15, 2005
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 124 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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