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Entry version 156 (29 Sep 2021)
Sequence version 1 (01 May 2000)
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Protein

DNApol-eta

Gene

DNApol-eta

Organism
Drosophila melanogaster (Fruit fly)
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:11297519).

Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls (PubMed:11297519).

Inserts one or 2 nucleotide(s) opposite the lesion (PubMed:11297519).

During homologous recombination (HR) repair, has a overlapping role with the error-prone translesion polymerase DNApol-zeta/DNApolZ1 to initiate repair synthesis that is completed by end joining or another polymerase that can bind and reinitiate synthesis (PubMed:22532806).

Particularly important for the repair of UV-induced pyrimidine dimers and for hydroxyurea (HU)-induced DNA damage (PubMed:22532806, PubMed:24553286).

Although inserts the correct base, may cause base transitions and transversions depending upon the context (By similarity).

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 (By similarity).

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 (By similarity).

By similarity3 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+By similarity, Mn2+By similarityNote: Binds 2 Mg2+. Prefers Mg2+, but can also use Mn2+. In vitro, can also utilize other divalent cations such as Ca2+.By similarity

<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. This binding is essential for catalyzing the DNA synthesis.By similarity

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 bindingi22Magnesium 1 or manganese 1By similarity1
Metal bindingi22Magnesium 2 or manganese 2By similarity1
Metal bindingi23Magnesium 1 or manganese 1; via carbonyl oxygenBy similarity1
<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 sitei70dNTPBy similarity1
Metal bindingi125Magnesium 1 or manganese 1By similarity1
Metal bindingi125Magnesium 2 or manganese 2By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei126PROSITE-ProRule annotation1
Metal bindingi126Magnesium 2 or manganese 2By similarity1
Metal bindingi805ZincBy similarity1
Metal bindingi808ZincBy similarity1
Metal bindingi820Zinc; via tele nitrogenBy similarity1
Metal bindingi824Zinc; via tele nitrogenBy similarity1

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 fingeri701 – 737UBZ3-type 1PROSITE-ProRule annotationAdd BLAST37
Zinc fingeri798 – 832UBZ3-type 2PROSITE-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

GO - Biological processi

<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 functionNucleotidyltransferase, Transferase
Biological processDNA damage, DNA repair
LigandMagnesium, Manganese, Metal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-DME-110320, Translesion Synthesis by POLH

<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:
DNApol-etaImported (EC:2.7.7.71 Publication)
<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:DNApol-etaImported
Synonyms:DNApolHCurated, dPoletaImported, drad30A1 PublicationImported, POLHImported
ORF Names:CG7143Imported
<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>OrganismiDrosophila melanogaster (Fruit fly)Imported
<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 identifieri7227 [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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
<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
  • UP000000803 <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 3L

Organism-specific databases

Drosophila genome database

More...
FlyBasei
FBgn0037141, DNApol-eta

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
VectorBase:FBgn0037141

<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 describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Viable and fertile (PubMed:24553286). Results in spindle defects (PubMed:24553286). Results in severe sensitivity of third-instar larvae to ultraviolet radiation (UV) (PubMed:22532806, PubMed:24553286). Exhibits a significant reduction in survival after hydroxyurea (HU)-induced DNA damage (PubMed:24553286). Decreases homologous recombination (HR) (PubMed:22532806). Simultaneous knockout of DNApol-eta/DNApolH and DNApol-zeta/DNApolZ1 does not show any difference in the frequency of full HR repair compared to the single knockouts suggesting they have overlapping roles (PubMed:22532806).2 Publications

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>Mutagenesisi125 – 126DE → AA: Loss of catalytic activity. 1 Publication2

<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_00004486861 – 885DNApol-etaAdd BLAST885

<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

Ubiquitination enhanced by nopo.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

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

More...
PaxDbi
Q9VNX1

<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

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in ovaries and testes.1 Publication

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed most highly in 0-2 hour embryos then at lower levels in larvae and pupae.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
FBgn0037141, Expressed in adult abdomen (Drosophila) and 32 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q9VNX1, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9VNX1, DM

<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 (via C-terminus) with nopo.

1 Publication

<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

Protein-protein interaction databases

Protein interaction database and analysis system

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IntActi
Q9VNX1, 6 interactors

STRING: functional protein association networks

More...
STRINGi
7227.FBpp0078142

<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

3D structure databases

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

More...
SMRi
Q9VNX1

Database of comparative protein structure models

More...
ModBasei
Search...

<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>Domaini18 – 274UmuCPROSITE-ProRule annotationAdd BLAST257

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>Regioni599 – 653DisorderedSequence analysisAdd BLAST55
Regioni658 – 677DisorderedSequence analysisAdd BLAST20
Regioni722 – 783DisorderedSequence analysisAdd BLAST62
Regioni846 – 870DisorderedSequence analysisAdd BLAST25

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi599 – 617Acidic residuesSequence analysisAdd BLAST19
Compositional biasi623 – 651Polar residuesSequence analysisAdd BLAST29
Compositional biasi722 – 751Basic and acidic residuesSequence analysisAdd BLAST30
Compositional biasi764 – 783Polar residuesSequence analysisAdd BLAST20
Compositional biasi852 – 870Polar residuesSequence analysisAdd BLAST19

<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.By similarity

<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 fingeri701 – 737UBZ3-type 1PROSITE-ProRule annotationAdd BLAST37
Zinc fingeri798 – 832UBZ3-type 2PROSITE-ProRule annotationAdd BLAST35

Keywords - Domaini

Repeat, 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

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InParanoidi
Q9VNX1

Identification of Orthologs from Complete Genome Data

More...
OMAi
MQNKYDR

Database of Orthologous Groups

More...
OrthoDBi
1593931at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9VNX1

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.1490.100, 1 hit

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
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, 2 hits

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, 2 hits

<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>Sequencei

<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.

Q9VNX1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSARSHVSM QNKYDRVVLL VDMDCFFCQV EEKQHPEYRN RPLAVVQYNP
60 70 80 90 100
WRGGGIIAVN YAARAKGVTR HMRGDEAKDL CPEIVLCQVP NIREKADTSK
110 120 130 140 150
YRDAGKEVAN VLQRFTQLLE RASVDEAYLD ITETVNHRMQ QMQSGAFALQ
160 170 180 190 200
PQELVNTFAV GYPSIGDYVN KITNRFANPY MDDERYQMSY DQNDLPAVRQ
210 220 230 240 250
SDIRLLIGAS VAGEVRAAVK KETGYECSAG IAHNKILAKL AAGMNKPNKQ
260 270 280 290 300
TILPLTETAS LFDSLPVGKI KGLGGKFGEV VCETLGIKFM GQVVKFSEVD
310 320 330 340 350
LQRKFDEKNG TWLFNISRGI DLEAVTPRFY SKSIGCCKKF PGRNNITGLK
360 370 380 390 400
TLQHWLGELS SEINDRLEKD FIENNRRAKH MVVQYVQDID GEEVASSRST
410 420 430 440 450
ALRDYDQESI VRLSLDLIKA NTKTFLRPGS ESALNNAIKF LGISVGKFET
460 470 480 490 500
VSSGQNKLQE MFANQAAKKR RVSGDEPGQL PKVEMEKKQK QTDEFKMKSF
510 520 530 540 550
FANYLQGAKK EDAKADGISA NPLAAAAGAP NKNFVEEYKH KLHAAVRTEG
560 570 580 590 600
TVLTSTPAEF KESFFSQYLK QQKKTGQQGS VTSREDSLDV QELAEELDAI
610 620 630 640 650
EADNSKDFEE DTEEETELTS DTHMSKPEGQ SSDAGQEQDP NTLNDSTGND
660 670 680 690 700
LYVETGIVPP TLTEDELKPS TSKRKFDEIE SSVSNYKECY VEFAVPNLRT
710 720 730 740 750
DILPTIKCDQ CGANIPDEVK SLQTHRDHHF AQELSRTLRS TEREERTQSR
760 770 780 790 800
QKISLKPTPP KKSKKTAGSG SSSYSTAPPS NSITKFFRAK PTQEQAPSDP
810 820 830 840 850
QMNQCPECKA FIKCVDMPEH LDYHVARNLQ RELNQQDLRT RTAALNKEKI
860 870 880
SPVQPKKQSQ KKLNSTISAS SSGTKTIAQF FSQSN
Length:885
Mass (Da):99,026
Last modified:May 1, 2000 - 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:i79AD667CA651AC68
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AGW25604 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti827R → K in AAL14000 (PubMed:12537569).Curated1
Sequence conflicti827R → K in BAB15799 (PubMed:11297519).Curated1
Sequence conflicti827R → K in BAB20905 (Ref. 2) Curated1
Sequence conflicti850I → T in AAL14000 (PubMed:12537569).Curated1
Sequence conflicti850I → T in BAB15799 (PubMed:11297519).Curated1
Sequence conflicti850I → T in BAB20905 (Ref. 2) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AB049433 mRNA Translation: BAB15799.1
AB036766 mRNA Translation: BAB20905.1
AE014296 Genomic DNA Translation: AAF51794.1
AY058771 mRNA Translation: AAL14000.1
BT150322 mRNA Translation: AGW25604.1 Different initiation.

NCBI Reference Sequences

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RefSeqi
NP_649371.2, NM_141114.3

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
FBtr0078489; FBpp0078142; FBgn0037141

Database of genes from NCBI RefSeq genomes

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GeneIDi
40438

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
dme:Dmel_CG7143

UCSC genome browser

More...
UCSCi
CG7143-RA, d. melanogaster

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB049433 mRNA Translation: BAB15799.1
AB036766 mRNA Translation: BAB20905.1
AE014296 Genomic DNA Translation: AAF51794.1
AY058771 mRNA Translation: AAL14000.1
BT150322 mRNA Translation: AGW25604.1 Different initiation.
RefSeqiNP_649371.2, NM_141114.3

3D structure databases

SMRiQ9VNX1
ModBaseiSearch...

Protein-protein interaction databases

IntActiQ9VNX1, 6 interactors
STRINGi7227.FBpp0078142

Proteomic databases

PaxDbiQ9VNX1

Genome annotation databases

EnsemblMetazoaiFBtr0078489; FBpp0078142; FBgn0037141
GeneIDi40438
KEGGidme:Dmel_CG7143
UCSCiCG7143-RA, d. melanogaster

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
40438
FlyBaseiFBgn0037141, DNApol-eta
VEuPathDBiVectorBase:FBgn0037141

Phylogenomic databases

eggNOGiKOG2095, Eukaryota
GeneTreeiENSGT00940000157048
HOGENOMiCLU_012348_7_2_1
InParanoidiQ9VNX1
OMAiMQNKYDR
OrthoDBi1593931at2759
PhylomeDBiQ9VNX1

Enzyme and pathway databases

ReactomeiR-DME-110320, Translesion Synthesis by POLH

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
40438, 0 hits in 1 CRISPR screen

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

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GenomeRNAii
40438

Protein Ontology

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PROi
PR:Q9VNX1

Gene expression databases

BgeeiFBgn0037141, Expressed in adult abdomen (Drosophila) and 32 other tissues
ExpressionAtlasiQ9VNX1, baseline and differential
GenevisibleiQ9VNX1, DM

Family and domain databases

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

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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_DROME
<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: Q9VNX1
Secondary accession number(s): Q9GNC0, T2GGD2
<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: December 11, 2019
Last sequence update: May 1, 2000
Last modified: September 29, 2021
This is version 156 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 programDrosophila annotation project

<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

Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families
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