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Protein

DNA polymerase eta

Gene

POLH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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: GO_Central
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, DNA-directed DNA polymerase, Mutator protein, Nucleotidyltransferase, Transferase
Biological processDNA damage, DNA repair, DNA replication, DNA synthesis
LigandMagnesium, Metal-binding, Schiff base

Enzyme and pathway databases

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-RKiQ9Y253
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

EuPathDBiHostDB:ENSG00000170734.11
HGNCiHGNC:9181 POLH
MIMi603968 gene
neXtProtiNX_Q9Y253

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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 dbSNP:rs756931657Ensembl.1
Natural variantiVAR_021227111R → H in XPV. Corresponds to variant dbSNP:rs758423288Ensembl.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 dbSNP:rs56307355EnsemblClinVar.1
Natural variantiVAR_021236589K → T in XPV. 1 PublicationCorresponds to variant dbSNP:rs121908565EnsemblClinVar.1
Natural variantiVAR_070839692T → A in XPV. 1 PublicationCorresponds to variant dbSNP:rs199562456Ensembl.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
GeneReviewsiPOLH
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

EPDiQ9Y253
PaxDbiQ9Y253
PeptideAtlasiQ9Y253
PRIDEiQ9Y253
ProteomicsDBi85655
85656 [Q9Y253-2]

PTM databases

iPTMnetiQ9Y253
PhosphoSitePlusiQ9Y253

Expressioni

Gene expression databases

BgeeiENSG00000170734 Expressed in 239 organ(s), highest expression level in buccal mucosa cell
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

Protein-protein interaction databases

BioGridi111425, 42 interactors
CORUMiQ9Y253
IntActiQ9Y253, 17 interactors
MINTiQ9Y253
STRINGi9606.ENSP00000361310

Chemistry databases

BindingDBiQ9Y253

Structurei

Secondary structure

1713
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

Phylogenomic databases

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

Family and domain databases

Gene3Di3.30.1490.100, 1 hit
InterProiView protein in InterPro
IPR036775 DNA_pol_Y-fam_lit_finger_sf
IPR017961 DNA_pol_Y-fam_little_finger
IPR001126 UmuC
PfamiView protein in Pfam
PF00817 IMS, 1 hit
PF11799 IMS_C, 1 hit
SUPFAMiSSF100879 SSF100879, 1 hit
PROSITEiView protein in PROSITE
PS50173 UMUC, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5JTF2Q5JTF2_HUMAN
DNA polymerase eta
POLH
71Annotation score:

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 dbSNP:rs756931657Ensembl.1
Natural variantiVAR_021227111R → H in XPV. Corresponds to variant dbSNP:rs758423288Ensembl.1
Natural variantiVAR_021228122T → P in XPV. 1 Publication1
Natural variantiVAR_036220153G → D in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs367709714Ensembl.1
Natural variantiVAR_021229209G → V1 PublicationCorresponds to variant dbSNP:rs2307456EnsemblClinVar.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 → W1 PublicationCorresponds to variant dbSNP:rs9333548Ensembl.1
Natural variantiVAR_021232361R → S in XPV. 1 Publication1
Natural variantiVAR_021233478T → M1 PublicationCorresponds to variant dbSNP:rs9296419Ensembl.1
Natural variantiVAR_021234535K → E in XPV. 1 PublicationCorresponds to variant dbSNP:rs56307355EnsemblClinVar.1
Natural variantiVAR_021235584L → P1 PublicationCorresponds to variant dbSNP:rs9333554Ensembl.1
Natural variantiVAR_021236589K → T in XPV. 1 PublicationCorresponds to variant dbSNP:rs121908565EnsemblClinVar.1
Natural variantiVAR_021237595M → V1 PublicationCorresponds to variant dbSNP:rs9333555EnsemblClinVar.1
Natural variantiVAR_021238647M → L1 PublicationCorresponds to variant dbSNP:rs6941583EnsemblClinVar.1
Natural variantiVAR_070839692T → A in XPV. 1 PublicationCorresponds to variant dbSNP:rs199562456Ensembl.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 Genomic DNA No translation available.
AL355802 Genomic DNA No translation available.
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

Similar proteinsi

Cross-referencesi

Web resourcesi

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 Genomic DNA No translation available.
AL355802 Genomic DNA No translation available.
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[»]
5F9LX-ray2.59A1-432[»]
5F9NX-ray2.23A1-432[»]
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[»]
6D0MX-ray1.83A1-432[»]
6D0ZX-ray1.75A1-432[»]
6M7OX-ray3.00A1-432[»]
6M7PX-ray1.75A1-432[»]
6M7TX-ray2.80A1-432[»]
6M7UX-ray3.40A1-432[»]
6M7VX-ray3.06A1-432[»]
ProteinModelPortaliQ9Y253
SMRiQ9Y253
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111425, 42 interactors
CORUMiQ9Y253
IntActiQ9Y253, 17 interactors
MINTiQ9Y253
STRINGi9606.ENSP00000361310

Chemistry databases

BindingDBiQ9Y253
ChEMBLiCHEMBL5542

PTM databases

iPTMnetiQ9Y253
PhosphoSitePlusiQ9Y253

Polymorphism and mutation databases

BioMutaiPOLH
DMDMi59798441

Proteomic databases

EPDiQ9Y253
PaxDbiQ9Y253
PeptideAtlasiQ9Y253
PRIDEiQ9Y253
ProteomicsDBi85655
85656 [Q9Y253-2]

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
EuPathDBiHostDB:ENSG00000170734.11
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
OMAiPVWEMPE
OrthoDBiEOG091G04Z9
PhylomeDBiQ9Y253
TreeFamiTF103010

Enzyme and pathway databases

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-RKiQ9Y253
SIGNORiQ9Y253

Miscellaneous databases

ChiTaRSiPOLH human
EvolutionaryTraceiQ9Y253
GeneWikiiDNA_polymerase_eta
GenomeRNAii5429
PROiPR:Q9Y253
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000170734 Expressed in 239 organ(s), highest expression level in buccal mucosa cell
CleanExiHS_POLH
ExpressionAtlasiQ9Y253 baseline and differential
GenevisibleiQ9Y253 HS

Family and domain databases

Gene3Di3.30.1490.100, 1 hit
InterProiView protein in InterPro
IPR036775 DNA_pol_Y-fam_lit_finger_sf
IPR017961 DNA_pol_Y-fam_little_finger
IPR001126 UmuC
PfamiView protein in Pfam
PF00817 IMS, 1 hit
PF11799 IMS_C, 1 hit
SUPFAMiSSF100879 SSF100879, 1 hit
PROSITEiView protein in PROSITE
PS50173 UMUC, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiPOLH_HUMAN
AccessioniPrimary (citable) accession number: Q9Y253
Secondary accession number(s): Q7L8E3, Q96BC4, Q9BX13
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: November 1, 1999
Last modified: November 7, 2018
This is version 162 of the entry and version 1 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
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