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UniProtKB - Q9HCU8 (DPOD4_HUMAN)

Entry version 154 (17 Jun 2020)
Sequence version 1 (01 Mar 2001)
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Protein

DNA polymerase delta subunit 4

Gene

POLD4

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

As a component of the tetrameric DNA polymerase delta complex (Pol-delta4), plays a role in high fidelity genome replication and repair. Within this complex, increases the rate of DNA synthesis and decreases fidelity by regulating POLD1 polymerase and proofreading 3' to 5' exonuclease activity (PubMed:16510448, PubMed:19074196, PubMed:20334433). Pol-delta4 participates in Okazaki fragment processing, through both the short flap pathway, as well as a nick translation system (PubMed:24035200). Under conditions of DNA replication stress, required for the repair of broken replication forks through break-induced replication (BIR), a mechanism that may induce segmental genomic duplications of up to 200 kb (PubMed:24310611). Involved in Pol-delta4 translesion synthesis (TLS) of templates carrying O6-methylguanine or abasic sites (PubMed:19074196). Its degradation in response to DNA damage is required for the inhibition of fork progression and cell survival (PubMed:24022480).6 Publications

<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 - 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

Biological processDNA damage, DNA excision, DNA repair, DNA replication

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-110314 Recognition of DNA damage by PCNA-containing replication complex
R-HSA-174411 Polymerase switching on the C-strand of the telomere
R-HSA-174414 Processive synthesis on the C-strand of the telomere
R-HSA-174417 Telomere C-strand (Lagging Strand) Synthesis
R-HSA-174437 Removal of the Flap Intermediate from the C-strand
R-HSA-5358565 Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)
R-HSA-5358606 Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta)
R-HSA-5651801 PCNA-Dependent Long Patch Base Excision Repair
R-HSA-5656169 Termination of translesion DNA synthesis
R-HSA-5685942 HDR through Homologous Recombination (HRR)
R-HSA-5696397 Gap-filling DNA repair synthesis and ligation in GG-NER
R-HSA-5696400 Dual Incision in GG-NER
R-HSA-6782135 Dual incision in TC-NER
R-HSA-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-HSA-69091 Polymerase switching
R-HSA-69166 Removal of the Flap Intermediate
R-HSA-69183 Processive synthesis on the lagging strand

<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%5Fand%5Ftaxonomy%5Fsection">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 delta subunit 4
Alternative name(s):
DNA polymerase delta subunit p12
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:POLD4
Synonyms:POLDS
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 11

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000175482.8

Human Gene Nomenclature Database

More...HGNCi		HGNC:14106 POLD4

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		611525 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9HCU8

<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

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

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi1 – 16Missing : Complete loss of PCNA binding and of degradation after UV irradiation. 1 PublicationAdd BLAST16
Mutagenesisi4K → A: No effect on PCNA binding. 1 Publication1
Mutagenesisi4K → Q: No effect on PCNA binding, nor on degradation after UV irradiation; when associated with Y-10. No effect on PCNA binding, but normal degradation after UV irradiation; when associated with Y-10 and A-15. 1 Publication1
Mutagenesisi4K → R: No effect on ubiquitination. Loss of ubiquitination, when associated with R-15, R-25, R-74 and R-89. 1 Publication1
Mutagenesisi7I → A: Complete loss of PCNA binding; when associated with 10-AA-11. 1 Publication1
Mutagenesisi8T → A: Strongly increased stability following UV irradiation; when associated with A-9. 1 Publication1
Mutagenesisi8T → D: Complete loss of PCNA binding. 1 Publication1
Mutagenesisi9D → A: Strongly increased stability following UV irradiation; when associated with A-8. 1 Publication1
Mutagenesisi10 – 11SY → AA: Complete loss of PCNA binding; when associated with A-7. 1 Publication2
Mutagenesisi10S → Y: No effect on PCNA binding, nor on degradation after UV irradiation; when associated with Q-4. No effect on PCNA binding, but normal degradation after UV irradiation with Q-4 and A-15. 1 Publication1
Mutagenesisi15K → A: Decreased PCNA binding. No effect on PCNA binding, but normal degradation after UV irradiation; when associated with Q-4 and Y-10. Increased stability following UV irradiation and no trough during S phase; when associated with A-16 and A-17. 2 Publications1
Mutagenesisi15K → R: No effect on ubiquitination. Loss of ubiquitination; when associated with R-4, R-25, R-74 and R-89. 1 Publication1
Mutagenesisi16R → A: Increased stability following UV irradiation and no trough during S phase; when associated with A-15 and A-17. 1 Publication1
Mutagenesisi17R → A: Increased stability following UV irradiation and no trough during S phase; when associated with A-15 and A-16. 1 Publication1
Mutagenesisi25K → R: No effect on ubiquitination. Loss of ubiquitination; when associated with R-4, R-15, R-74 and R-89. 1 Publication1
Mutagenesisi74K → R: No effect on ubiquitination. Loss of ubiquitination; when associated with R-4, R-15, R-25 and R-89. 1 Publication1
Mutagenesisi89K → R: No effect on ubiquitination. Loss of ubiquitination; when associated with R-4, R-15, R-25 and R-74. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		57804

Open Targets

More...OpenTargetsi		ENSG00000175482

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33498

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q9HCU8 Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2363042

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		POLD4

<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_00001860511 – 107DNA polymerase delta subunit 4Add BLAST107

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Ubiquitinated; undergoes 'Lys-48'-linked ubiquitination in response to UV irradiation, leading to proteasomal degradation (PubMed:17317665, PubMed:16934752, PubMed:23233665, PubMed:23913683). This modification is partly mediated by RNF8 and by the DCX(DTL) E3 ubiquitin ligase complex (also called CRL4(CDT2)) (PubMed:23233665, PubMed:24022480). Efficient degradation requires the presence of PCNA and is required for the inhibition of fork progression after DNA damage (PubMed:24022480).5 Publications

Keywords - PTMi

Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q9HCU8

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q9HCU8

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q9HCU8

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q9HCU8

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

More...PaxDbi		Q9HCU8

PeptideAtlas

More...PeptideAtlasi		Q9HCU8

PRoteomics IDEntifications database

More...PRIDEi		Q9HCU8

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		26732
81802 [Q9HCU8-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9HCU8

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

More...PhosphoSitePlusi		Q9HCU8

<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 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

Expression is cell cycle-dependent, with highest levels in G2/M phase and a drastic drop in S phase (PubMed:22801543, PubMed:23913683). This trough may be mediated by DCX(DTL) E3 ubiquitin ligase complex (also called CRL4(CDT2))-mediated proteasomal degradation (PubMed:23913683).2 Publications

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

In response to DNA damage, genotoxic stress and replication stress, following UV irradiation, ionizing radiation, treatment with methyl methanesulfonate, hydroxyurea, or with aphidicolin, protein expression drops to undetectable levels, due to proteasomal degradation (PubMed:17317665, PubMed:22801543, PubMed:23233665, PubMed:23913683, PubMed:24300032). This down-regulation is ATR-dependent (PubMed:17317665).5 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000175482 Expressed in mucosa of transverse colon and 87 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9HCU8 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9HCU8 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000175482 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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the tetrameric DNA polymerase delta complex (Pol-delta4), which consists of POLD1/p125, POLD2/p50, POLD3/p66/p68 and POLD4/p12, with POLD1 bearing DNA polymerase and 3' to 5' proofreading exonuclease activities (PubMed:16510448, PubMed:17317665, PubMed:22801543). Within this complex, directly interacts with POLD1 and POLD2 (PubMed:12403614, PubMed:16510448). Directly interacts with PCNA, as do POLD1 and POLD3; this interaction stimulates Pol-delta4 polymerase activity (PubMed:24022480). As POLD1 and POLD2, directly interacts with WRNIP1; this interaction stimulates DNA polymerase delta-mediated DNA synthesis, independently of the presence of PCNA. This stimulation may be due predominantly to an increase of initiation frequency and also to increased processivity (PubMed:15670210). Upon genotoxic stress induced by DNA damaging agents or by replication stress, POLD4 is proteolytically degraded and Pol-delta4 is converted into a trimeric form of the complex (Pol-delta3) which has an increased proofreading activity (PubMed:22801543, PubMed:17317665). The DNA polymerase delta complex interacts with POLDIP2; this interaction is probably mediated through direct binding to POLD2 (PubMed:12522211).

7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">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		121774, 9 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-2097 Delta DNA polymerase complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q9HCU8

Protein interaction database and analysis system

More...IntActi		Q9HCU8, 7 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000311368

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q9HCU8 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

1107
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		Q9HCU8

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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

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>Motifi1 – 16PCNA-interaction protein motif (PIP box)2 PublicationsAdd BLAST16

<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 delta subunit 4 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG410J65P Eukaryota
ENOG410XUCX LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00390000005096

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_132157_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9HCU8

KEGG Orthology (KO)

More...KOi		K03505

Identification of Orthologs from Complete Genome Data

More...OMAi		WEYGPCT

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9HCU8

TreeFam database of animal gene trees

More...TreeFami		TF103004

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR007218 DNA_pol_delta_4

The PANTHER Classification System

More...PANTHERi		PTHR14303 PTHR14303, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF04081 DNA_pol_delta_4, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<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: Q9HCU8-1) [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
MGRKRLITDS YPVVKRREGP AGHSKGELAP ELGEEPQPRD EEEAELELLR 
        60         70         80         90        100
QFDLAWQYGP CTGITRLQRW CRAKQMGLEP PPEVWQVLKT HPGDPRFQCS 

LWHLYPL
Length:107
Mass (Da):12,433
Last modified:March 1, 2001 - 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:i6F412738E4D9A19C
GO
Isoform 2 (identifier: Q9HCU8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     63-107: GITRLQRWCRAKQMGLEPPPEVWQVLKTHPGDPRFQCSLWHLYPL → VSGISIPYEAPRKTSCP

Show »
Length:79
Mass (Da):8,868
Checksum:iC8CD845791BE8759
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
E9PL15E9PL15_HUMAN
DNA polymerase delta subunit 4
POLD4
32Annotation 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
<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_02226939R → P1 PublicationCorresponds to variant dbSNP:rs28364240Ensembl.1
Natural variantiVAR_05752659G → R. Corresponds to variant dbSNP:rs34136263Ensembl.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_04686463 – 107GITRL…HLYPL → VSGISIPYEAPRKTSCP in isoform 2. 1 PublicationAdd BLAST45

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
AF179890 mRNA Translation: AAG08966.1
AY928482 Genomic DNA Translation: AAX09676.1
AP003419 Genomic DNA No translation available.
BG403692 mRNA No translation available.

The Consensus CDS (CCDS) project

More...CCDSi		CCDS58149.1 [Q9HCU8-2]
CCDS8158.1 [Q9HCU8-1]

NCBI Reference Sequences

More...RefSeqi		NP_001243799.1, NM_001256870.1 [Q9HCU8-2]
NP_066996.3, NM_021173.4 [Q9HCU8-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000312419; ENSP00000311368; ENSG00000175482 [Q9HCU8-1]
ENST00000539074; ENSP00000444780; ENSG00000175482 [Q9HCU8-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		57804

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:57804

UCSC genome browser

More...UCSCi		uc001okm.5 human [Q9HCU8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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%5Freferences%5Fsection">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

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF179890 mRNA Translation: AAG08966.1
AY928482 Genomic DNA Translation: AAX09676.1
AP003419 Genomic DNA No translation available.
BG403692 mRNA No translation available.
CCDSiCCDS58149.1 [Q9HCU8-2]
CCDS8158.1 [Q9HCU8-1]
RefSeqiNP_001243799.1, NM_001256870.1 [Q9HCU8-2]
NP_066996.3, NM_021173.4 [Q9HCU8-1]

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
6HVOX-ray2.10D/E/F1-19[»]
6S1Melectron microscopy4.27D2-107[»]
6S1Nelectron microscopy4.86D2-107[»]
6S1Oelectron microscopy8.10D2-107[»]
6TNYelectron microscopy3.08D2-107[»]
6TNZelectron microscopy4.05D2-107[»]
SMRiQ9HCU8
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi121774, 9 interactors
ComplexPortaliCPX-2097 Delta DNA polymerase complex
CORUMiQ9HCU8
IntActiQ9HCU8, 7 interactors
STRINGi9606.ENSP00000311368

Chemistry databases

ChEMBLiCHEMBL2363042

PTM databases

iPTMnetiQ9HCU8
PhosphoSitePlusiQ9HCU8

Polymorphism and mutation databases

BioMutaiPOLD4

Proteomic databases

EPDiQ9HCU8
jPOSTiQ9HCU8
MassIVEiQ9HCU8
MaxQBiQ9HCU8
PaxDbiQ9HCU8
PeptideAtlasiQ9HCU8
PRIDEiQ9HCU8
ProteomicsDBi26732
81802 [Q9HCU8-1]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		30343 48 antibodies

The DNASU plasmid repository

More...DNASUi		57804

Genome annotation databases

EnsembliENST00000312419; ENSP00000311368; ENSG00000175482 [Q9HCU8-1]
ENST00000539074; ENSP00000444780; ENSG00000175482 [Q9HCU8-2]
GeneIDi57804
KEGGihsa:57804
UCSCiuc001okm.5 human [Q9HCU8-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		57804
DisGeNETi57804
EuPathDBiHostDB:ENSG00000175482.8

GeneCards: human genes, protein and diseases

More...GeneCardsi		POLD4
HGNCiHGNC:14106 POLD4
HPAiENSG00000175482 Low tissue specificity
MIMi611525 gene
neXtProtiNX_Q9HCU8
OpenTargetsiENSG00000175482
PharmGKBiPA33498

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG410J65P Eukaryota
ENOG410XUCX LUCA
GeneTreeiENSGT00390000005096
HOGENOMiCLU_132157_0_0_1
InParanoidiQ9HCU8
KOiK03505
OMAiWEYGPCT
PhylomeDBiQ9HCU8
TreeFamiTF103004

Enzyme and pathway databases

ReactomeiR-HSA-110314 Recognition of DNA damage by PCNA-containing replication complex
R-HSA-174411 Polymerase switching on the C-strand of the telomere
R-HSA-174414 Processive synthesis on the C-strand of the telomere
R-HSA-174417 Telomere C-strand (Lagging Strand) Synthesis
R-HSA-174437 Removal of the Flap Intermediate from the C-strand
R-HSA-5358565 Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha)
R-HSA-5358606 Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta)
R-HSA-5651801 PCNA-Dependent Long Patch Base Excision Repair
R-HSA-5656169 Termination of translesion DNA synthesis
R-HSA-5685942 HDR through Homologous Recombination (HRR)
R-HSA-5696397 Gap-filling DNA repair synthesis and ligation in GG-NER
R-HSA-5696400 Dual Incision in GG-NER
R-HSA-6782135 Dual incision in TC-NER
R-HSA-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-HSA-69091 Polymerase switching
R-HSA-69166 Removal of the Flap Intermediate
R-HSA-69183 Processive synthesis on the lagging strand

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		57804 11 hits in 791 CRISPR screens

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

More...ChiTaRSi		POLD4 human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		POLD4

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

More...GenomeRNAii		57804
PharosiQ9HCU8 Tbio

Protein Ontology

More...PROi		PR:Q9HCU8
RNActiQ9HCU8 protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000175482 Expressed in mucosa of transverse colon and 87 other tissues
ExpressionAtlasiQ9HCU8 baseline and differential
GenevisibleiQ9HCU8 HS

Family and domain databases

InterProiView protein in InterPro
IPR007218 DNA_pol_delta_4
PANTHERiPTHR14303 PTHR14303, 1 hit
PfamiView protein in Pfam
PF04081 DNA_pol_delta_4, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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 nameiDPOD4_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: Q9HCU8
Secondary accession number(s): F5H506
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: March 1, 2001
Last modified: June 17, 2020
This is version 154 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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