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UniProtKB - Q9Y253 (POLH_HUMAN)

Entry version 181 (29 Sep 2021)
Sequence version 1 (01 Nov 1999)
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Protein

DNA polymerase eta

Gene

POLH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

DNA polymerase specifically involved in the DNA repair by translesion synthesis (TLS) (PubMed:10385124, PubMed:11743006, PubMed:24449906, PubMed:24553286, PubMed:16357261).

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).

9 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 Publication, Mn2+1 PublicationNote: Binds 2 Mg2+ (PubMed:27284197). Prefers Mg2+, but can also use Mn2+ (PubMed:27284197). In vitro, can also utilize other divalent cations such as Ca2+ (PubMed:27284197).1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

The enzyme in complex with the DNA substrate binds a third divalent metal cation (PubMed:27284197). The binding of this third divalent cation, which is coordinated by water molecules and two oxygen atoms from DNA and dNTP, is essential for catalyzing the DNA synthesis (PubMed:27284197).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi13Magnesium 1 or manganese 1Combined sources1 Publication1
Metal bindingi13Magnesium 2 or manganese 2Combined sources1 Publication1
Metal bindingi14Magnesium 1 or manganese 1; via carbonyl oxygenCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei61dNTP1 Publication1
Metal bindingi115Magnesium 1 or manganese 1Combined sources1 Publication1
Metal bindingi115Magnesium 2 or manganese 2Combined sources1 Publication1
Metal bindingi116Magnesium 2 or manganese 2Combined sources1 Publication1
Metal bindingi635ZincCombined sources1 Publication1
Metal bindingi638ZincCombined sources1 Publication1
Metal bindingi650Zinc; via tele nitrogenCombined sources1 Publication1
Metal bindingi654Zinc; via tele nitrogenCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri628 – 662UBZ3-typePROSITE-ProRule annotationAdd BLAST35

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>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, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.7.7, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q9Y253

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-110320, Translesion Synthesis by POLH
R-HSA-5656169, Termination of translesion DNA synthesis
R-HSA-5685942, HDR through Homologous Recombination (HRR)

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		Q9Y253

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q9Y253

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
DNA polymerase eta (EC:2.7.7.71 Publication)
Alternative name(s):
RAD30 homolog A
Xeroderma pigmentosum variant type protein
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:POLH
Synonyms:RAD30, RAD30A, XPV
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:9181, POLH

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		603968, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9Y253

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000170734

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Xeroderma pigmentosum variant type (XPV)6 Publications
The disease is caused by variants 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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 PublicationCorresponds to variant dbSNP:rs1561900151Ensembl.1
Natural variantiVAR_021230263G → V in XPV; impairs translesion synthesis. 1 PublicationCorresponds to variant dbSNP:rs1413703153Ensembl.1
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
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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
Mutagenesisi61R → A: Reduces enzymatic activity by two-thirds. 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
Mutagenesisi324 – 326NFP → AAA: Reduces binding to chromatin and to monoubiquitinated PCNA. Abolishes binding to monoubiquitinated PCNA; when associated with 705-E--H-713 Del. 1 Publication3
Mutagenesisi638C → A: Reduces cell resistance to UV-induced DNA damage. 1 Publication1
Mutagenesisi652D → A: Abolishes ubiquitin binding and localization to nuclear foci after UV-induced DNA damage but does not affect catalytic activity. 1 Publication1
Mutagenesisi705 – 713Missing : Reduces cell resistance to UV-induced DNA damage. Reduces binding to chromatin and to monoubiquitinated PCNA. Abolishes binding to monoubiquitinated PCNA; when associated with 324-A--A-326. 2 Publications9

Keywords - Diseasei

Disease variant, Xeroderma pigmentosum

Organism-specific databases

DisGeNET

More...DisGeNETi		5429

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		POLH

MalaCards human disease database

More...MalaCardsi		POLH
MIMi278750, phenotype

Open Targets

More...OpenTargetsi		ENSG00000170734

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		90342, Xeroderma pigmentosum variant

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA279

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q9Y253, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL5542

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		POLH

Domain mapping of disease mutations (DMDM)

More...DMDMi		59798441

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001739861 – 713DNA polymerase etaAdd BLAST713

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Monoubiquitinated by RCHY1/PIRH2 (PubMed:20159558, PubMed:21791603). Ubiquitination depends on integrity of the UBZ3-type zinc finger domain and is enhanced by TRAIP (PubMed:24553286, PubMed:16357261). Ubiquitination inhibits the ability of PolH to interact with PCNA and to bypass UV-induced lesions (PubMed:20159558, PubMed:21791603, PubMed:24553286).4 Publications

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q9Y253

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q9Y253

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q9Y253

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q9Y253

PeptideAtlas

More...PeptideAtlasi		Q9Y253

PRoteomics IDEntifications database

More...PRIDEi		Q9Y253

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		85655 [Q9Y253-1]
85656 [Q9Y253-2]

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		Q9Y253, 1 site, 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9Y253

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q9Y253

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000170734, Expressed in buccal mucosa cell and 248 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9Y253, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9Y253, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000170734, Low tissue specificity

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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).

Interacts (via C-terminus) with TRAIP (PubMed:24553286).

Interacts with ubiquitin (PubMed:16357261).

Interacts with POLDIP2 (PubMed:20554254).

By similarity6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		111425, 47 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q9Y253

Protein interaction database and analysis system

More...IntActi		Q9Y253, 23 interactors

Molecular INTeraction database

More...MINTi		Q9Y253

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000361310

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q9Y253

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q9Y253, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

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

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		Q9Y253

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q9Y253

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q9Y253

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini9 – 259UmuCPROSITE-ProRule annotationAdd BLAST251

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni441 – 472DisorderedSequence analysisAdd BLAST32
Regioni495 – 527DisorderedSequence analysisAdd BLAST33
Regioni677 – 705DisorderedSequence analysisAdd BLAST29

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi701 – 708PIP-box2 Publications8

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.1 Publication
The UBZ3-type zinc finger domain and the PIP-box mediate the interaction with ubiquitinated PCNA and are both necessary for the enzymatic activity in translesion synthesis.2 Publications

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the DNA polymerase type-Y family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri628 – 662UBZ3-typePROSITE-ProRule annotationAdd BLAST35

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2095, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000157048

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_012348_7_2_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9Y253

Identification of Orthologs from Complete Genome Data

More...OMAi		DYHFAME

Database of Orthologous Groups

More...OrthoDBi		20162at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9Y253

TreeFam database of animal gene trees

More...TreeFami		TF103010

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.1490.100, 1 hit
3.30.70.270, 2 hits

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID00108

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR043502, DNA/RNA_pol_sf
IPR036775, DNA_pol_Y-fam_lit_finger_sf
IPR017961, DNA_pol_Y-fam_little_finger
IPR043128, Rev_trsase/Diguanyl_cyclase
IPR041298, UBZ3
IPR001126, UmuC

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00817, IMS, 1 hit
PF11799, IMS_C, 1 hit
PF18439, zf_UBZ, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF100879, SSF100879, 1 hit
SSF56672, SSF56672, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50173, UMUC, 1 hit
PS51907, ZF_UBZ3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> 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 <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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.

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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>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:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

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 PublicationCorresponds to variant dbSNP:rs1561900151Ensembl.1
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 PublicationCorresponds to variant dbSNP:rs1413703153Ensembl.1
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:rs9296419EnsemblClinVar.1
Natural variantiVAR_021234535K → E in XPV. 1 PublicationCorresponds to variant dbSNP:rs56307355EnsemblClinVar.1
Natural variantiVAR_021235584L → P1 PublicationCorresponds to variant dbSNP:rs9333554EnsemblClinVar.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
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_012799415 – 713Missing in isoform 2. 1 PublicationAdd BLAST299

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

The Consensus CDS (CCDS) project

More...CCDSi		CCDS4902.1 [Q9Y253-1]
CCDS78147.1 [Q9Y253-2]

NCBI Reference Sequences

More...RefSeqi		NP_001278899.1, NM_001291970.1 [Q9Y253-2]
NP_006493.1, NM_006502.2 [Q9Y253-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000372226; ENSP00000361300; ENSG00000170734 [Q9Y253-2]
ENST00000372236; ENSP00000361310; ENSG00000170734 [Q9Y253-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5429

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5429

UCSC genome browser

More...UCSCi		uc003ovq.5, human [Q9Y253-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...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[»]
6MP3X-ray1.91A1-432[»]
6MQ8X-ray1.97A3-432[»]
6MXOX-ray2.04A3-435[»]
6PL7X-ray2.50A1-432[»]
6PL8X-ray2.17A1-432[»]
6PLCX-ray2.50A1-432[»]
6PZ3X-ray2.40A1-432[»]
6Q02X-ray2.09A1-432[»]
6UI2X-ray2.35A1-432[»]
6UQIX-ray2.50A1-432[»]
6V5KX-ray2.69A1-432[»]
6W5XX-ray2.59A1-432[»]
6WK6X-ray2.35A1-432[»]
7M7LX-ray1.58A1-432[»]
7M7MX-ray1.46A1-432[»]
7M7NX-ray1.31A1-432[»]
7M7OX-ray1.80A1-432[»]
7M7PX-ray1.80A1-432[»]
7M7QX-ray2.27A1-432[»]
7M7RX-ray1.81A1-432[»]
7M7SX-ray1.85A1-432[»]
7M7TX-ray1.46A1-432[»]
7M7UX-ray1.94A1-432[»]
7M7YX-ray1.80A1-432[»]
7M7ZX-ray1.82A1-432[»]
7M80X-ray1.98A1-432[»]
7M81X-ray2.05A1-432[»]
7M82X-ray2.07A1-432[»]
7M83X-ray1.55A1-432[»]
7M84X-ray1.47A1-432[»]
7M85X-ray1.75A1-432[»]
7M86X-ray1.55A1-432[»]
7M87X-ray1.85A1-432[»]
7M88X-ray1.66A1-432[»]
7M89X-ray1.83A1-432[»]
7M8AX-ray1.91A1-432[»]
7M8BX-ray1.85A1-432[»]
7M8CX-ray1.85A1-432[»]
7M8DX-ray1.92A1-432[»]
BMRBiQ9Y253
SMRiQ9Y253
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi111425, 47 interactors
CORUMiQ9Y253
IntActiQ9Y253, 23 interactors
MINTiQ9Y253
STRINGi9606.ENSP00000361310

Chemistry databases

BindingDBiQ9Y253
ChEMBLiCHEMBL5542

PTM databases

GlyGeniQ9Y253, 1 site, 1 O-linked glycan (1 site)
iPTMnetiQ9Y253
PhosphoSitePlusiQ9Y253

Genetic variation databases

BioMutaiPOLH
DMDMi59798441

Proteomic databases

EPDiQ9Y253
jPOSTiQ9Y253
MassIVEiQ9Y253
PaxDbiQ9Y253
PeptideAtlasiQ9Y253
PRIDEiQ9Y253
ProteomicsDBi85655 [Q9Y253-1]
85656 [Q9Y253-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		1879, 202 antibodies

The DNASU plasmid repository

More...DNASUi		5429

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5429
DisGeNETi5429

GeneCards: human genes, protein and diseases

More...GeneCardsi		POLH
GeneReviewsiPOLH
HGNCiHGNC:9181, POLH
HPAiENSG00000170734, Low tissue specificity
MalaCardsiPOLH
MIMi278750, phenotype
603968, gene
neXtProtiNX_Q9Y253
OpenTargetsiENSG00000170734
Orphaneti90342, Xeroderma pigmentosum variant
PharmGKBiPA279
VEuPathDBiHostDB:ENSG00000170734

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG2095, Eukaryota
GeneTreeiENSGT00940000157048
HOGENOMiCLU_012348_7_2_1
InParanoidiQ9Y253
OMAiDYHFAME
OrthoDBi20162at2759
PhylomeDBiQ9Y253
TreeFamiTF103010

Enzyme and pathway databases

BRENDAi2.7.7.7, 2681
PathwayCommonsiQ9Y253
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

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		5429, 14 hits in 1021 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		POLH, human
EvolutionaryTraceiQ9Y253

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		DNA_polymerase_eta

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		5429
PharosiQ9Y253, Tchem

Protein Ontology

More...PROi		PR:Q9Y253
RNActiQ9Y253, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000170734, Expressed in buccal mucosa cell and 248 other tissues
ExpressionAtlasiQ9Y253, baseline and differential
GenevisibleiQ9Y253, HS

Family and domain databases

Gene3Di3.30.1490.100, 1 hit
3.30.70.270, 2 hits
IDEALiIID00108
InterProiView protein in InterPro
IPR043502, DNA/RNA_pol_sf
IPR036775, DNA_pol_Y-fam_lit_finger_sf
IPR017961, DNA_pol_Y-fam_little_finger
IPR043128, Rev_trsase/Diguanyl_cyclase
IPR041298, UBZ3
IPR001126, UmuC
PfamiView protein in Pfam
PF00817, IMS, 1 hit
PF11799, IMS_C, 1 hit
PF18439, zf_UBZ, 1 hit
SUPFAMiSSF100879, SSF100879, 1 hit
SSF56672, SSF56672, 1 hit
PROSITEiView protein in PROSITE
PS50173, UMUC, 1 hit
PS51907, ZF_UBZ3, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPOLH_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9Y253
Secondary accession number(s): Q7L8E3, Q96BC4, Q9BX13
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: November 1, 1999
Last modified: September 29, 2021
This is version 181 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, 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 genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  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
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