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Entry version 139 (29 Sep 2021)
Sequence version 3 (28 Mar 2018)
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Protein

DNA-directed primase/polymerase protein

Gene

PRIMPOL

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 primase and DNA polymerase required to tolerate replication-stalling lesions by bypassing them (PubMed:24126761, PubMed:24207056, PubMed:24240614, PubMed:24267451, PubMed:25255211, PubMed:24682820, PubMed:25262353, PubMed:25746449, PubMed:25550423, PubMed:27989484, PubMed:29608762, PubMed:30889508, PubMed:28534480).

Required to facilitate mitochondrial and nuclear replication fork progression by initiating de novo DNA synthesis using dNTPs and acting as an error-prone DNA polymerase able to bypass certain DNA lesions (PubMed:24126761, PubMed:24207056, PubMed:24240614, PubMed:24267451, PubMed:25255211, PubMed:24682820, PubMed:25262353, PubMed:25746449, PubMed:25550423, PubMed:27989484, PubMed:29608762, PubMed:30889508, PubMed:30633872, PubMed:28534480).

Shows a high capacity to tolerate DNA damage lesions such as 8oxoG and abasic sites in DNA (PubMed:24126761, PubMed:24207056, PubMed:24240614, PubMed:24267451, PubMed:25746449).

Provides different translesion synthesis alternatives when DNA replication is stalled: able to synthesize DNA primers downstream of lesions, such as ultraviolet (UV) lesions, R-loops and G-quadruplexes, to allow DNA replication to continue (PubMed:24240614, PubMed:26626482, PubMed:28534480, PubMed:30478192).

Can also realign primers ahead of 'unreadable lesions' such as abasic sites and 6-4 photoproduct (6-4 pyrimidine-pyrimidinone), thereby skipping the lesion (PubMed:25746449).

Also able to incorporate nucleotides opposite DNA lesions such as 8oxoG, like a regular translesion synthesis DNA polymerase (PubMed:24207056, PubMed:25255211, PubMed:25746449).

Also required for reinitiating stalled forks after UV damage during nuclear DNA replication (PubMed:24240614).

Required for mitochondrial DNA (mtDNA) synthesis and replication, by reinitiating synthesis after UV damage or in the presence of chain-terminating nucleotides (PubMed:24207056).

Prevents APOBEC family-mediated DNA mutagenesis by repriming downstream of abasic site to prohibit error-prone translesion synthesis (By similarity).

Has non-overlapping function with POLH (PubMed:24240614).

In addition to its role in DNA damage response, also required to maintain efficient nuclear and mitochondrial DNA replication in unperturbed cells (PubMed:30715459).

By similarity17 Publications

Involved in adaptive response to cisplatin, a chemotherapeutic that causes reversal of replication forks, in cancer cells: reinitiates DNA synthesis past DNA lesions in BRCA1-deficient cancer cells treated with cisplatin via its de novo priming activity (PubMed:31676232).

Repriming rescues fork degradation while leading to accumulation of internal ssDNA gaps behind the forks (PubMed:31676232).

ATR regulates adaptive response to cisplatin (PubMed:31676232).

1 Publication

Caution

According to a report, the association between the variant Asp-89 and high myopia MYP22 is unclear as this variant is found in control populations (PubMed:25680975). The paper also questions the relevance of functional study on this variant (PubMed:25680975). Authors of the functional characterization study replied that their analysis clearly shows that Asp-89 variant affects the DNA polymerase and primase activities, regardless of its association with high myopia MYP22 (PubMed:25680976). Additional studies are therefore required to confirm the link between this variant and high myopia MYP22.Curated2 Publications

<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

Mn2+1 Publication5 PublicationsNote: Can act both with Mn2+ and Mg2+ as cofactor in vitro, but Mn2+ is the preferred cofactor in vivo (PubMed:25255211, PubMed:25746449, PubMed:27989484, PubMed:30889508, PubMed:30633872). The polymerase activity incorporates correct dNTPs with much higher efficiency with Mn2+ than with Mg2+ (PubMed:25255211, PubMed:30889508). The fidelity is slightly more accurate when Mg2+ is the cofactor compared to Mn2+ (PubMed:25255211, PubMed:30889508). In the presence of Mn2+, a conformational transition step from non-productive to productive PRIMPOL:DNA complexes limits the enzymatic turnover, whereas in the presence of Mg2+, the chemical step becomes rate limiting (PubMed:30633872).5 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Kcat is 0.05 sec(-1) for dTTP (in presence of 2 mM of Mn2+. Kcat is 0.02 sec(-1) for dTTP (in presence of 50 µM of Mn2+. Kcat is 0.01 sec(-1) for dTTP (in presence of 2 mM of Mg2+.
  1. KM=14 µM for dTTP (in presence of 2 mM of Mn2+1 Publication
  2. KM=24 µM for dTTP (in presence of 50 µM of Mn2+1 Publication
  3. KM=430 µM for dTTP (in presence of 2 mM of Mg2+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 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 sitei76SubstrateCombined sources1 Publication1
<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 bindingi114Manganese; catalyticCombined sources2 Publications1
Metal bindingi116Manganese; catalyticCombined sources1 Publication1
Binding sitei297SubstrateCombined sources1 Publication1
Metal bindingi419Zinc1 Publication1
Metal bindingi426Zinc1 Publication1
Metal bindingi446Zinc1 Publication1
Metal bindingi451Zinc1 Publication1

<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 functionDNA-directed DNA polymerase, Nucleotidyltransferase, Transferase
Biological processDNA damage, DNA repair, Transcription
LigandManganese, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.7.102, 2681

Pathway Commons web resource for biological pathway data

More...
PathwayCommonsi
Q96LW4

<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-directed primase/polymerase protein1 Publication (EC:2.7.7.-6 Publications)
Short name:
hPrimpol11 Publication
Alternative name(s):
Coiled-coil domain-containing protein 1111 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:PRIMPOL1 PublicationImported
Synonyms:CCDC1111 Publication
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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 4

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:26575, PRIMPOL

Online Mendelian Inheritance in Man (OMIM)

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MIMi
615421, gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q96LW4

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
HostDB:ENSG00000164306

<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

Chromosome, DNA-directed RNA polymerase, Mitochondrion, 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

Myopia 22, autosomal dominant (MYP22)2 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA refractive error of the eye, in which parallel rays from a distant object come to focus in front of the retina, vision being better for near objects than for far.
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_07012089Y → D in MYP22; unknown pathological significance; reduced DNA polymerase and DNA primase activities; reduced DNA-binding. 2 PublicationsCorresponds to variant dbSNP:rs200857997EnsemblClinVar.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>Mutagenesisi89Y → F: Does not affect DNA primase activity. 1 Publication1
Mutagenesisi89Y → S: Reduced DNA primase activity. 1 Publication1
Mutagenesisi114 – 116DLE → ALA in AxA; abolished DNA primase and polymerase activities. 7 Publications3
Mutagenesisi114D → A: Abolishes DNA primase and polymerase activities. 1 Publication1
Mutagenesisi169H → N: Abolishes DNA primase and polymerase activities. 1 Publication1
Mutagenesisi280D → A: Abolished Mn(2+) DNA primase activity. 1 Publication1
Mutagenesisi419C → A: Abolished zinc-binding, leading to altered translesion synthesis; when associated with A-426. 3 Publications1
Mutagenesisi419C → G in mutant CH; abolished DNA primase activity and impaired ability to restart stalled forks; when associated with Y-426. 1 Publication1
Mutagenesisi426H → A: Abolished zinc-binding, leading to altered translesion synthesis; when associated with A-419. 3 Publications1
Mutagenesisi426H → D: Abolishes DNA primase activity, while it increases DNA polymerase activity. 2 Publications1
Mutagenesisi426H → Y in mutant CH; abolished DNA primase activity and impaired ability to restart stalled forks; when associated with G-419. 2 Publications1
Mutagenesisi519 – 522DAYF → RAYA: Abolished interaction with RPA1, impairing recruitment to chromatin and reducing DNA primase activity; when associated with 551-R--A-554. 1 Publication4
Mutagenesisi551 – 554DELI → RELA: Abolished interaction with RPA1, impairing recruitment to chromatin and reducing DNA primase activity; when associated with 519-R--A-522. 1 Publication4

Keywords - Diseasei

Disease variant

Organism-specific databases

DisGeNET

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DisGeNETi
201973

MalaCards human disease database

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MalaCardsi
PRIMPOL
MIMi615420, phenotype

Open Targets

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OpenTargetsi
ENSG00000164306

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA145008751

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
Q96LW4, Tbio

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
PRIMPOL

Domain mapping of disease mutations (DMDM)

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DMDMi
296434425

<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_00002793951 – 560DNA-directed primase/polymerase proteinAdd BLAST560

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei255PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q96LW4

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q96LW4

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

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PaxDbi
Q96LW4

PeptideAtlas

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PeptideAtlasi
Q96LW4

PRoteomics IDEntifications database

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PRIDEi
Q96LW4

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
14139
77258 [Q96LW4-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q96LW4

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

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PhosphoSitePlusi
Q96LW4

<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

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Bgeei
ENSG00000164306, Expressed in zone of skin and 209 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q96LW4, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q96LW4, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000164306, 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 RPA1; leading to recruitment to chromatin and stimulate DNA primase activity (PubMed:24126761, PubMed:25550423, PubMed:28396594, PubMed:28534480).

Interacts with SSBP1 (PubMed:25550423).

Interacts with POLDIP2; leading to enhance DNA polymerase activity (PubMed:26984527).

5 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

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Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
128410, 20 interactors

Protein interaction database and analysis system

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IntActi
Q96LW4, 18 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000313816

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
Q96LW4, 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

1560
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

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SMRi
Q96LW4

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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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

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>Regioni114 – 116Substrate bindingCombined sources1 Publication3
Regioni165 – 169Substrate bindingCombined sources1 Publication5
Regioni203 – 223DisorderedSequence analysisAdd BLAST21
Regioni288 – 291Substrate bindingCombined sources1 Publication4
Regioni480 – 507DisorderedSequence analysisAdd BLAST28
Regioni481 – 560Interaction with RPA11 PublicationAdd BLAST80

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili1 – 22Sequence analysisAdd BLAST22

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>Motifi419 – 452Zinc knuckle motif1 PublicationAdd BLAST34
Motifi513 – 527RPA1-binding motif 11 PublicationAdd BLAST15
Motifi548 – 556RPA1-binding motif 21 Publication9

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 biasi493 – 507Polar residuesSequence analysisAdd BLAST15

<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 zinc knuckle motif binds zinc and is required for the DNA primase activity (PubMed:24682820, PubMed:29608762). It facilitates the binding and selection of the 5'-nucleotide of the newly synthesized primer and the recognition of preferred initiation sites (PubMed:29608762).2 Publications
The RPA1-binding motifs (RBM) mediate interaction with RPA1 and are essential for recruitment to chromatin (PubMed:28534480). The interaction is primarily mediated by RPA1-binding motif 1, which binds to the basic cleft of RPA1, with motif 2 plays a supporting role in RPA1-binding (PubMed:28534480).1 Publication
The presence of an Asp-Aaa-Glu (DxE) motif in the metal-binding active site favors the use of Mn2+ ions to achieve optimal incoming nucleotide stabilization, especially required during primer synthesis (PubMed:30889508). Glu-116 is required to stabilize the incoming nucleotide at the 3'-site (PubMed:30889508).1 Publication

<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

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG502QS1Q, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00390000003901

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q96LW4

Identification of Orthologs from Complete Genome Data

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OMAi
ADWWMDA

Database of Orthologous Groups

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OrthoDBi
1373896at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q96LW4

TreeFam database of animal gene trees

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TreeFami
TF328961

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR002755, DNA_primase_S

Pfam protein domain database

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Pfami
View protein in Pfam
PF01896, DNA_primase_S, 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 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q96LW4-1) [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
MNRKWEAKLK QIEERASHYE RKPLSSVYRP RLSKPEEPPS IWRLFHRQAQ
60 70 80 90 100
AFNFVKSCKE DVHVFALECK VGDGQRIYLV TTYAEFWFYY KSRKNLLHCY
110 120 130 140 150
EVIPENAVCK LYFDLEFNKP ANPGADGKKM VALLIEYVCK ALQELYGVNC
160 170 180 190 200
SAEDVLNLDS STDEKFSRHL IFQLHDVAFK DNIHVGNFLR KILQPALDLL
210 220 230 240 250
GSEDDDSAPE TTGHGFPHFS EAPARQGFSF NKMFTEKATE ESWTSNSKKL
260 270 280 290 300
ERLGSAEQSS PDLSFLVVKN NMGEKHLFVD LGVYTRNRNF RLYKSSKIGK
310 320 330 340 350
RVALEVTEDN KFFPIQSKDV SDEYQYFLSS LVSNVRFSDT LRILTCEPSQ
360 370 380 390 400
NKQKGVGYFN SIGTSVETIE GFQCSPYPEV DHFVLSLVNK DGIKGGIRRW
410 420 430 440 450
NYFFPEELLV YDICKYRWCE NIGRAHKSNN IMILVDLKNE VWYQKCHDPV
460 470 480 490 500
CKAENFKSDC FPLPAEVCLL FLFKEEEEFT TDEADETRSN ETQNPHKPSP
510 520 530 540 550
SRLSTGASAD AVWDNGIDDA YFLEATEDAE LAEAAENSLL SYNSEVDEIP
560
DELIIEVLQE
Length:560
Mass (Da):64,412
Last modified:March 28, 2018 - v3
<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:i2B58D2B57F51DD4E
GO
Isoform 2 (identifier: Q96LW4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     366-366: Missing.

Show »
Length:559
Mass (Da):64,312
Checksum:iB5544871BEBB0508
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 are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A5S6SZ32A0A5S6SZ32_HUMAN
DNA-directed primase/polymerase pro...
PRIMPOL FLJ33167, hCG_1786938
431Annotation 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>
D6R971D6R971_HUMAN
DNA-directed primase/polymerase pro...
PRIMPOL
93Annotation 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>
D6R908D6R908_HUMAN
DNA-directed primase/polymerase pro...
PRIMPOL
112Annotation 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>
H0Y9N8H0Y9N8_HUMAN
DNA-directed primase/polymerase pro...
PRIMPOL
172Annotation 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>

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 conflicti322D → G in CAI46079 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07012089Y → D in MYP22; unknown pathological significance; reduced DNA polymerase and DNA primase activities; reduced DNA-binding. 2 PublicationsCorresponds to variant dbSNP:rs200857997EnsemblClinVar.1
Natural variantiVAR_030878168R → Q. Corresponds to variant dbSNP:rs2463447Ensembl.1
Natural variantiVAR_030879505T → K. Corresponds to variant dbSNP:rs14969Ensembl.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_053600366Missing in isoform 2. 1 Publication1

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
AK057729 mRNA Translation: BAB71553.1
BX647575 mRNA Translation: CAI46079.1
AC079257 Genomic DNA No translation available.
KF459591 Genomic DNA No translation available.
CH471056 Genomic DNA Translation: EAX04667.1
CH471056 Genomic DNA Translation: EAX04669.1
CH471056 Genomic DNA Translation: EAX04670.1
BC064600 mRNA Translation: AAH64600.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS3837.1 [Q96LW4-1]
CCDS75211.1 [Q96LW4-2]

NCBI Reference Sequences

More...
RefSeqi
NP_001287696.1, NM_001300767.1
NP_001287697.1, NM_001300768.1 [Q96LW4-2]
NP_001332824.1, NM_001345895.1 [Q96LW4-1]
NP_001332825.1, NM_001345896.1 [Q96LW4-2]
NP_689896.1, NM_152683.3 [Q96LW4-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000314970; ENSP00000313816; ENSG00000164306 [Q96LW4-1]
ENST00000503752; ENSP00000420860; ENSG00000164306 [Q96LW4-1]
ENST00000512834; ENSP00000425316; ENSG00000164306 [Q96LW4-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
201973

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:201973

UCSC genome browser

More...
UCSCi
uc003iwj.3, human
uc003iwk.3, human [Q96LW4-1]

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK057729 mRNA Translation: BAB71553.1
BX647575 mRNA Translation: CAI46079.1
AC079257 Genomic DNA No translation available.
KF459591 Genomic DNA No translation available.
CH471056 Genomic DNA Translation: EAX04667.1
CH471056 Genomic DNA Translation: EAX04669.1
CH471056 Genomic DNA Translation: EAX04670.1
BC064600 mRNA Translation: AAH64600.1
CCDSiCCDS3837.1 [Q96LW4-1]
CCDS75211.1 [Q96LW4-2]
RefSeqiNP_001287696.1, NM_001300767.1
NP_001287697.1, NM_001300768.1 [Q96LW4-2]
NP_001332824.1, NM_001345895.1 [Q96LW4-1]
NP_001332825.1, NM_001345896.1 [Q96LW4-2]
NP_689896.1, NM_152683.3 [Q96LW4-1]

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
5L2XX-ray2.20A/B1-353[»]
5N85X-ray2.00B514-528[»]
5N8AX-ray1.28X480-560[»]
7JK1X-ray2.62A/B1-354[»]
7JKLX-ray2.38A/B1-354[»]
7JKPX-ray2.59A/B1-354[»]
7JL8X-ray2.10A/B1-354[»]
7JLGX-ray2.07A/B1-354[»]
SMRiQ96LW4
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi128410, 20 interactors
IntActiQ96LW4, 18 interactors
STRINGi9606.ENSP00000313816

PTM databases

iPTMnetiQ96LW4
PhosphoSitePlusiQ96LW4

Genetic variation databases

BioMutaiPRIMPOL
DMDMi296434425

Proteomic databases

jPOSTiQ96LW4
MassIVEiQ96LW4
PaxDbiQ96LW4
PeptideAtlasiQ96LW4
PRIDEiQ96LW4
ProteomicsDBi14139
77258 [Q96LW4-1]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
66503, 36 antibodies

The DNASU plasmid repository

More...
DNASUi
201973

Genome annotation databases

EnsembliENST00000314970; ENSP00000313816; ENSG00000164306 [Q96LW4-1]
ENST00000503752; ENSP00000420860; ENSG00000164306 [Q96LW4-1]
ENST00000512834; ENSP00000425316; ENSG00000164306 [Q96LW4-2]
GeneIDi201973
KEGGihsa:201973
UCSCiuc003iwj.3, human
uc003iwk.3, human [Q96LW4-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
201973
DisGeNETi201973

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PRIMPOL
HGNCiHGNC:26575, PRIMPOL
HPAiENSG00000164306, Low tissue specificity
MalaCardsiPRIMPOL
MIMi615420, phenotype
615421, gene
neXtProtiNX_Q96LW4
OpenTargetsiENSG00000164306
PharmGKBiPA145008751
VEuPathDBiHostDB:ENSG00000164306

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG502QS1Q, Eukaryota
GeneTreeiENSGT00390000003901
InParanoidiQ96LW4
OMAiADWWMDA
OrthoDBi1373896at2759
PhylomeDBiQ96LW4
TreeFamiTF328961

Enzyme and pathway databases

BRENDAi2.7.7.102, 2681
PathwayCommonsiQ96LW4

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
201973, 6 hits in 1002 CRISPR screens

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

More...
ChiTaRSi
PRIMPOL, human

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

More...
GenomeRNAii
201973
PharosiQ96LW4, Tbio

Protein Ontology

More...
PROi
PR:Q96LW4
RNActiQ96LW4, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000164306, Expressed in zone of skin and 209 other tissues
ExpressionAtlasiQ96LW4, baseline and differential
GenevisibleiQ96LW4, HS

Family and domain databases

InterProiView protein in InterPro
IPR002755, DNA_primase_S
PfamiView protein in Pfam
PF01896, DNA_primase_S, 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 nameiPRIPO_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: Q96LW4
Secondary accession number(s): A0A0A0MTC0
, D3DP55, D6RDM1, Q5HYJ9
<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: March 6, 2007
Last sequence update: March 28, 2018
Last modified: September 29, 2021
This is version 139 of the entry and version 3 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. Human chromosome 4
    Human chromosome 4: 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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