Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA polymerase eta

Gene

POLH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

DNA polymerase specifically involved in the DNA repair by translesion synthesis (TLS) (PubMed:10385124, PubMed:11743006, PubMed:24449906). Due to low processivity on both damaged and normal DNA, cooperates with the heterotetrameric (REV3L, REV7, POLD2 and POLD3) POLZ complex for complete bypass of DNA lesions. Inserts one or 2 nucleotide(s) opposite the lesion, the primer is further extended by the tetrameric POLZ complex. In the case of 1,2-intrastrand d(GpG)-cisplatin cross-link, inserts dCTP opposite the 3' guanine (PubMed:24449906). Particularly important for the repair of UV-induced pyrimidine dimers (PubMed:10385124, PubMed:11743006). Although inserts the correct base, may cause base transitions and transversions depending upon the context. May play a role in hypermutation at immunoglobulin genes (PubMed:11376341, PubMed:14734526). Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have any lyase activity, preventing the release of the 5'-deoxyribose phosphate (5'-dRP) residue. This covalent trapping of the enzyme by the 5'-dRP residue inhibits its DNA synthetic activity during base excision repair, thereby avoiding high incidence of mutagenesis (PubMed:14630940). Targets POLI to replication foci (PubMed:12606586).7 Publications

Catalytic activityi

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

Cofactori

Mg2+, Mn2+Note: Divalent metal cations. Prefers Mg2+, but can also use Mn2+.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi13MagnesiumPROSITE-ProRule annotation1
Metal bindingi115MagnesiumPROSITE-ProRule annotation1

GO - Molecular functioni

  • damaged DNA binding Source: ProtInc
  • DNA-directed DNA polymerase activity Source: Reactome
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cellular response to UV-C Source: Ensembl
  • DNA repair Source: ProtInc
  • DNA replication Source: UniProtKB-KW
  • DNA synthesis involved in DNA repair Source: UniProtKB
  • error-free translesion synthesis Source: Reactome
  • pyrimidine dimer repair Source: Ensembl
  • regulation of DNA repair Source: ProtInc
  • response to UV-C Source: UniProtKB
  • translesion synthesis Source: Reactome
Complete GO annotation...

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

BioCyciZFISH:HS10171-MONOMER.
BRENDAi2.7.7.7. 2681.
ReactomeiR-HSA-110320. Translesion Synthesis by POLH.
R-HSA-5656169. Termination of translesion DNA synthesis.
R-HSA-5685942. HDR through Homologous Recombination (HRR).
SABIO-RKQ9Y253.
SIGNORiQ9Y253.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:9181. POLH.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Xeroderma pigmentosum variant type (XPV)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:278750
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07083537Missing in XPV. 1 Publication1
Natural variantiVAR_02122675Missing in XPV; impairs translesion synthesis. 2 Publications1
Natural variantiVAR_07083693R → P in XPV. 1 PublicationCorresponds to variant rs756931657dbSNPEnsembl.1
Natural variantiVAR_021227111R → H in XPV. Corresponds to variant rs758423288dbSNPEnsembl.1
Natural variantiVAR_021228122T → P in XPV. 1 Publication1
Natural variantiVAR_021230263G → V in XPV; impairs translesion synthesis. 1 Publication1
Natural variantiVAR_070837266V → D in XPV. 1 Publication1
Natural variantiVAR_070838295G → R in XPV. 1 Publication1
Natural variantiVAR_021232361R → S in XPV. 1 Publication1
Natural variantiVAR_021234535K → E in XPV. 1 PublicationCorresponds to variant rs56307355dbSNPEnsembl.1
Natural variantiVAR_021236589K → T in XPV. 1 PublicationCorresponds to variant rs121908565dbSNPEnsembl.1
Natural variantiVAR_070839692T → A in XPV. 1 PublicationCorresponds to variant rs199562456dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi52Y → A or F: Reduces DNA polymerase activity. 1 Publication1
Mutagenesisi52Y → E: Reduces DNA polymerase activity. Increases fidelity of replication and reduces translesion bypass. 1 Publication1
Mutagenesisi62S → G: Increased DNA polymerase activity and translesion bypass compared to wild-type. 1 Publication1
Mutagenesisi68A → S or V: Severe reduction in thymine dimer translesion bypass. 1 Publication1

Keywords - Diseasei

Disease mutation, Xeroderma pigmentosum

Organism-specific databases

DisGeNETi5429.
MalaCardsiPOLH.
MIMi278750. phenotype.
OpenTargetsiENSG00000170734.
Orphaneti90342. Xeroderma pigmentosum variant.
PharmGKBiPA279.

Chemistry databases

ChEMBLiCHEMBL5542.

Polymorphism and mutation databases

BioMutaiPOLH.
DMDMi59798441.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001739861 – 713DNA polymerase etaAdd BLAST713

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki682Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki686Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki694Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki709Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

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

PaxDbiQ9Y253.
PeptideAtlasiQ9Y253.
PRIDEiQ9Y253.

PTM databases

iPTMnetiQ9Y253.
PhosphoSitePlusiQ9Y253.

Expressioni

Gene expression databases

BgeeiENSG00000170734.
CleanExiHS_POLH.
ExpressionAtlasiQ9Y253. baseline and differential.
GenevisibleiQ9Y253. HS.

Organism-specific databases

HPAiHPA006721.
HPA026762.

Interactioni

Subunit structurei

Interacts with REV1 (By similarity). Interacts with monoubiquitinated PCNA, but not unmodified PCNA (PubMed:15149598). Interacts with POLI; this interaction targets POLI to the replication machinery (PubMed:12606586). Interacts with PALB2 and BRCA2; the interactions are direct and are required to sustain the recruitment of POLH at blocked replication forks and to stimulate POLH-dependent DNA synthesis on D loop substrates (PubMed:24485656).By similarity3 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. 40 interactors.
IntActiQ9Y253. 16 interactors.
MINTiMINT-2789553.
STRINGi9606.ENSP00000361310.

Chemistry databases

BindingDBiQ9Y253.

Structurei

Secondary structure

1713
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1 – 3Combined sources3
Beta strandi9 – 14Combined sources6
Helixi17 – 25Combined sources9
Helixi27 – 29Combined sources3
Beta strandi34 – 38Combined sources5
Turni41 – 44Combined sources4
Beta strandi46 – 50Combined sources5
Helixi52 – 55Combined sources4
Turni56 – 58Combined sources3
Beta strandi61 – 64Combined sources4
Helixi65 – 71Combined sources7
Beta strandi76 – 79Combined sources4
Beta strandi81 – 83Combined sources3
Beta strandi86 – 88Combined sources3
Helixi90 – 103Combined sources14
Turni104 – 106Combined sources3
Beta strandi109 – 113Combined sources5
Beta strandi116 – 120Combined sources5
Helixi122 – 132Combined sources11
Helixi139 – 141Combined sources3
Beta strandi145 – 147Combined sources3
Helixi159 – 161Combined sources3
Helixi163 – 177Combined sources15
Helixi186 – 208Combined sources23
Beta strandi212 – 219Combined sources8
Helixi220 – 229Combined sources10
Turni230 – 233Combined sources4
Beta strandi235 – 237Combined sources3
Helixi240 – 242Combined sources3
Helixi243 – 248Combined sources6
Helixi252 – 254Combined sources3
Turni256 – 259Combined sources4
Helixi261 – 270Combined sources10
Helixi275 – 280Combined sources6
Helixi283 – 290Combined sources8
Helixi292 – 301Combined sources10
Turni302 – 304Combined sources3
Beta strandi313 – 315Combined sources3
Beta strandi319 – 324Combined sources6
Helixi327 – 329Combined sources3
Beta strandi331 – 333Combined sources3
Helixi334 – 359Combined sources26
Beta strandi360 – 372Combined sources13
Turni373 – 375Combined sources3
Beta strandi376 – 378Combined sources3
Beta strandi380 – 386Combined sources7
Helixi392 – 403Combined sources12
Helixi404 – 406Combined sources3
Beta strandi414 – 431Combined sources18
Helixi532 – 538Combined sources7
Beta strandi632 – 634Combined sources3
Turni636 – 638Combined sources3
Beta strandi641 – 643Combined sources3
Helixi644 – 646Combined sources3
Helixi647 – 659Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2I5ONMR-A628-662[»]
2LSKNMR-B524-539[»]
3JAAelectron microscopy22.00A1-432[»]
3MR2X-ray1.83A1-432[»]
3MR3X-ray1.75A1-432[»]
3MR5X-ray1.80A1-432[»]
3MR6X-ray1.90A1-432[»]
3SI8X-ray2.15A1-432[»]
3TQ1X-ray2.56A1-432[»]
3WUPX-ray1.60A630-665[»]
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[»]
4Q8EX-ray1.55A1-432[»]
4Q8FX-ray2.80A1-432[»]
4RNMX-ray2.14A1-432[»]
4RNNX-ray1.81A1-432[»]
4RNOX-ray2.82A1-432[»]
4RU9X-ray2.65A1-432[»]
4YP3X-ray1.89A1-432[»]
4YQWX-ray2.06A1-432[»]
4YR0X-ray1.78A1-432[»]
4YR2X-ray1.95A1-432[»]
4YR3X-ray2.00A1-432[»]
5DG7X-ray2.26A1-432[»]
5DG8X-ray2.12A1-432[»]
5DG9X-ray2.15A1-432[»]
5DGAX-ray2.30A1-432[»]
5DGBX-ray1.79A1-432[»]
5DLFX-ray1.97A1-432[»]
5DLGX-ray2.35A1-432[»]
5DQGX-ray2.29A1-432[»]
5DQHX-ray1.99A1-432[»]
5DQIX-ray2.30A1-432[»]
5EWEX-ray1.66A1-432[»]
5EWFX-ray1.78A1-432[»]
5EWGX-ray1.75A1-432[»]
5JUMX-ray2.60A1-432[»]
5KFAX-ray1.51A1-432[»]
5KFBX-ray1.55A1-432[»]
5KFCX-ray1.50A1-432[»]
5KFDX-ray1.65A1-432[»]
5KFEX-ray1.55A1-432[»]
5KFFX-ray1.70A1-432[»]
5KFGX-ray1.55A1-432[»]
5KFHX-ray1.72A1-432[»]
5KFIX-ray1.65A1-432[»]
5KFJX-ray1.70A1-432[»]
5KFKX-ray1.70A1-432[»]
5KFLX-ray1.65A1-432[»]
5KFMX-ray1.60A1-432[»]
5KFNX-ray1.45A1-432[»]
5KFOX-ray1.52A1-432[»]
5KFPX-ray1.70A1-432[»]
5KFQX-ray1.55A1-432[»]
5KFRX-ray1.75A1-432[»]
5KFSX-ray1.46A1-432[»]
5KFTX-ray1.52A1-432[»]
5KFUX-ray1.55A1-432[»]
5KFVX-ray1.60A1-432[»]
5KFWX-ray1.62A1-432[»]
5KFXX-ray1.52A1-432[»]
5KFYX-ray1.70A1-432[»]
5KFZX-ray1.44A1-432[»]
5KG0X-ray1.60A1-432[»]
5KG1X-ray1.62A1-432[»]
5KG2X-ray1.60A1-432[»]
5KG3X-ray1.70A1-432[»]
5KG4X-ray1.60A1-432[»]
5KG5X-ray1.60A1-432[»]
5KG6X-ray1.55A1-432[»]
5KG7X-ray1.75A1-432[»]
5L1IX-ray2.78A1-432[»]
5L1JX-ray1.94A1-432[»]
5L1KX-ray1.82A1-432[»]
5L1LX-ray1.62A1-432[»]
5L9XX-ray1.90A1-432[»]
ProteinModelPortaliQ9Y253.
SMRiQ9Y253.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y253.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 259UmuCPROSITE-ProRule annotationAdd BLAST251

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

eggNOGiKOG2095. Eukaryota.
COG0389. LUCA.
GeneTreeiENSGT00530000062942.
HOGENOMiHOG000115605.
HOVERGENiHBG053633.
InParanoidiQ9Y253.
KOiK03509.
OMAiRNKPCAV.
OrthoDBiEOG091G04Z9.
PhylomeDBiQ9Y253.
TreeFamiTF103010.

Family and domain databases

Gene3Di3.30.1490.100. 1 hit.
InterProiIPR017061. DNA_pol_eta/kappa.
IPR017961. DNA_pol_Y-fam_little_finger.
IPR001126. UmuC.
[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. AlignAdd to basket

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

        10         20         30         40         50
MATGQDRVVA LVDMDCFFVQ VEQRQNPHLR NKPCAVVQYK SWKGGGIIAV
60 70 80 90 100
SYEARAFGVT RSMWADDAKK LCPDLLLAQV RESRGKANLT KYREASVEVM
110 120 130 140 150
EIMSRFAVIE RASIDEAYVD LTSAVQERLQ KLQGQPISAD LLPSTYIEGL
160 170 180 190 200
PQGPTTAEET VQKEGMRKQG LFQWLDSLQI DNLTSPDLQL TVGAVIVEEM
210 220 230 240 250
RAAIERETGF QCSAGISHNK VLAKLACGLN KPNRQTLVSH GSVPQLFSQM
260 270 280 290 300
PIRKIRSLGG KLGASVIEIL GIEYMGELTQ FTESQLQSHF GEKNGSWLYA
310 320 330 340 350
MCRGIEHDPV KPRQLPKTIG CSKNFPGKTA LATREQVQWW LLQLAQELEE
360 370 380 390 400
RLTKDRNDND RVATQLVVSI RVQGDKRLSS LRRCCALTRY DAHKMSHDAF
410 420 430 440 450
TVIKNCNTSG IQTEWSPPLT MLFLCATKFS ASAPSSSTDI TSFLSSDPSS
460 470 480 490 500
LPKVPVTSSE AKTQGSGPAV TATKKATTSL ESFFQKAAER QKVKEASLSS
510 520 530 540 550
LTAPTQAPMS NSPSKPSLPF QTSQSTGTEP FFKQKSLLLK QKQLNNSSVS
560 570 580 590 600
SPQQNPWSNC KALPNSLPTE YPGCVPVCEG VSKLEESSKA TPAEMDLAHN
610 620 630 640 650
SQSMHASSAS KSVLEVTQKA TPNPSLLAAE DQVPCEKCGS LVPVWDMPEH
660 670 680 690 700
MDYHFALELQ KSFLQPHSSN PQVVSAVSHQ GKRNPKSPLA CTNKRPRPEG
710
MQTLESFFKP LTH
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_07083537Missing in XPV. 1 Publication1
Natural variantiVAR_02122675Missing in XPV; impairs translesion synthesis. 2 Publications1
Natural variantiVAR_07083693R → P in XPV. 1 PublicationCorresponds to variant rs756931657dbSNPEnsembl.1
Natural variantiVAR_021227111R → H in XPV. Corresponds to variant rs758423288dbSNPEnsembl.1
Natural variantiVAR_021228122T → P in XPV. 1 Publication1
Natural variantiVAR_036220153G → D in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs367709714dbSNPEnsembl.1
Natural variantiVAR_021229209G → V.1 PublicationCorresponds to variant rs2307456dbSNPEnsembl.1
Natural variantiVAR_021230263G → V in XPV; impairs translesion synthesis. 1 Publication1
Natural variantiVAR_070837266V → D in XPV. 1 Publication1
Natural variantiVAR_070838295G → R in XPV. 1 Publication1
Natural variantiVAR_021231334R → W.1 PublicationCorresponds to variant rs9333548dbSNPEnsembl.1
Natural variantiVAR_021232361R → S in XPV. 1 Publication1
Natural variantiVAR_021233478T → M.1 PublicationCorresponds to variant rs9296419dbSNPEnsembl.1
Natural variantiVAR_021234535K → E in XPV. 1 PublicationCorresponds to variant rs56307355dbSNPEnsembl.1
Natural variantiVAR_021235584L → P.1 PublicationCorresponds to variant rs9333554dbSNPEnsembl.1
Natural variantiVAR_021236589K → T in XPV. 1 PublicationCorresponds to variant rs121908565dbSNPEnsembl.1
Natural variantiVAR_021237595M → V.1 PublicationCorresponds to variant rs9333555dbSNPEnsembl.1
Natural variantiVAR_021238647M → L.1 PublicationCorresponds to variant rs6941583dbSNPEnsembl.1
Natural variantiVAR_070839692T → A in XPV. 1 PublicationCorresponds to variant rs199562456dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_012799415 – 713Missing in isoform 2. 1 PublicationAdd BLAST299

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
CCDS78147.1. [Q9Y253-2]
RefSeqiNP_001278899.1. NM_001291970.1. [Q9Y253-2]
NP_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.5. human. [Q9Y253-1]

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:
EMBLi
GenBanki
DDBJi
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]
CCDS78147.1. [Q9Y253-2]
RefSeqiNP_001278899.1. NM_001291970.1. [Q9Y253-2]
NP_006493.1. NM_006502.2. [Q9Y253-1]
UniGeneiHs.655467.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2I5ONMR-A628-662[»]
2LSKNMR-B524-539[»]
3JAAelectron microscopy22.00A1-432[»]
3MR2X-ray1.83A1-432[»]
3MR3X-ray1.75A1-432[»]
3MR5X-ray1.80A1-432[»]
3MR6X-ray1.90A1-432[»]
3SI8X-ray2.15A1-432[»]
3TQ1X-ray2.56A1-432[»]
3WUPX-ray1.60A630-665[»]
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[»]
4Q8EX-ray1.55A1-432[»]
4Q8FX-ray2.80A1-432[»]
4RNMX-ray2.14A1-432[»]
4RNNX-ray1.81A1-432[»]
4RNOX-ray2.82A1-432[»]
4RU9X-ray2.65A1-432[»]
4YP3X-ray1.89A1-432[»]
4YQWX-ray2.06A1-432[»]
4YR0X-ray1.78A1-432[»]
4YR2X-ray1.95A1-432[»]
4YR3X-ray2.00A1-432[»]
5DG7X-ray2.26A1-432[»]
5DG8X-ray2.12A1-432[»]
5DG9X-ray2.15A1-432[»]
5DGAX-ray2.30A1-432[»]
5DGBX-ray1.79A1-432[»]
5DLFX-ray1.97A1-432[»]
5DLGX-ray2.35A1-432[»]
5DQGX-ray2.29A1-432[»]
5DQHX-ray1.99A1-432[»]
5DQIX-ray2.30A1-432[»]
5EWEX-ray1.66A1-432[»]
5EWFX-ray1.78A1-432[»]
5EWGX-ray1.75A1-432[»]
5JUMX-ray2.60A1-432[»]
5KFAX-ray1.51A1-432[»]
5KFBX-ray1.55A1-432[»]
5KFCX-ray1.50A1-432[»]
5KFDX-ray1.65A1-432[»]
5KFEX-ray1.55A1-432[»]
5KFFX-ray1.70A1-432[»]
5KFGX-ray1.55A1-432[»]
5KFHX-ray1.72A1-432[»]
5KFIX-ray1.65A1-432[»]
5KFJX-ray1.70A1-432[»]
5KFKX-ray1.70A1-432[»]
5KFLX-ray1.65A1-432[»]
5KFMX-ray1.60A1-432[»]
5KFNX-ray1.45A1-432[»]
5KFOX-ray1.52A1-432[»]
5KFPX-ray1.70A1-432[»]
5KFQX-ray1.55A1-432[»]
5KFRX-ray1.75A1-432[»]
5KFSX-ray1.46A1-432[»]
5KFTX-ray1.52A1-432[»]
5KFUX-ray1.55A1-432[»]
5KFVX-ray1.60A1-432[»]
5KFWX-ray1.62A1-432[»]
5KFXX-ray1.52A1-432[»]
5KFYX-ray1.70A1-432[»]
5KFZX-ray1.44A1-432[»]
5KG0X-ray1.60A1-432[»]
5KG1X-ray1.62A1-432[»]
5KG2X-ray1.60A1-432[»]
5KG3X-ray1.70A1-432[»]
5KG4X-ray1.60A1-432[»]
5KG5X-ray1.60A1-432[»]
5KG6X-ray1.55A1-432[»]
5KG7X-ray1.75A1-432[»]
5L1IX-ray2.78A1-432[»]
5L1JX-ray1.94A1-432[»]
5L1KX-ray1.82A1-432[»]
5L1LX-ray1.62A1-432[»]
5L9XX-ray1.90A1-432[»]
ProteinModelPortaliQ9Y253.
SMRiQ9Y253.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111425. 40 interactors.
IntActiQ9Y253. 16 interactors.
MINTiMINT-2789553.
STRINGi9606.ENSP00000361310.

Chemistry databases

BindingDBiQ9Y253.
ChEMBLiCHEMBL5542.

PTM databases

iPTMnetiQ9Y253.
PhosphoSitePlusiQ9Y253.

Polymorphism and mutation databases

BioMutaiPOLH.
DMDMi59798441.

Proteomic databases

PaxDbiQ9Y253.
PeptideAtlasiQ9Y253.
PRIDEiQ9Y253.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372226; ENSP00000361300; ENSG00000170734. [Q9Y253-2]
ENST00000372236; ENSP00000361310; ENSG00000170734. [Q9Y253-1]
GeneIDi5429.
KEGGihsa:5429.
UCSCiuc003ovq.5. human. [Q9Y253-1]

Organism-specific databases

CTDi5429.
DisGeNETi5429.
GeneCardsiPOLH.
GeneReviewsiPOLH.
HGNCiHGNC:9181. POLH.
HPAiHPA006721.
HPA026762.
MalaCardsiPOLH.
MIMi278750. phenotype.
603968. gene.
neXtProtiNX_Q9Y253.
OpenTargetsiENSG00000170734.
Orphaneti90342. Xeroderma pigmentosum variant.
PharmGKBiPA279.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2095. Eukaryota.
COG0389. LUCA.
GeneTreeiENSGT00530000062942.
HOGENOMiHOG000115605.
HOVERGENiHBG053633.
InParanoidiQ9Y253.
KOiK03509.
OMAiRNKPCAV.
OrthoDBiEOG091G04Z9.
PhylomeDBiQ9Y253.
TreeFamiTF103010.

Enzyme and pathway databases

BioCyciZFISH:HS10171-MONOMER.
BRENDAi2.7.7.7. 2681.
ReactomeiR-HSA-110320. Translesion Synthesis by POLH.
R-HSA-5656169. Termination of translesion DNA synthesis.
R-HSA-5685942. HDR through Homologous Recombination (HRR).
SABIO-RKQ9Y253.
SIGNORiQ9Y253.

Miscellaneous databases

ChiTaRSiPOLH. human.
EvolutionaryTraceiQ9Y253.
GeneWikiiDNA_polymerase_eta.
GenomeRNAii5429.
PROiQ9Y253.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000170734.
CleanExiHS_POLH.
ExpressionAtlasiQ9Y253. baseline and differential.
GenevisibleiQ9Y253. HS.

Family and domain databases

Gene3Di3.30.1490.100. 1 hit.
InterProiIPR017061. DNA_pol_eta/kappa.
IPR017961. DNA_pol_Y-fam_little_finger.
IPR001126. UmuC.
[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]
ProtoNetiSearch...

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: November 30, 2016
This is version 148 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.