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Entry version 149 (07 Apr 2021)
Sequence version 1 (01 Feb 1991)
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Protein

DNA primase small subunit

Gene

Prim1

Organism
Mus musculus (Mouse)
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

Catalytic subunit of the DNA primase complex and component of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex) which play an essential role in the initiation of DNA synthesis (PubMed:8253737, PubMed:8026492). During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1, an accessory subunit POLA2 and two primase subunits, the catalytic subunit PRIM1 and the regulatory subunit PRIM2) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1 (By similarity). The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively (By similarity). In the primase complex, both subunits are necessary for the initial di-nucleotide formation, but the extension of the primer depends only on the catalytic subunit (PubMed:8253737). Can add both ribo- and deoxynucleotides during elongation of the primers (PubMed:8253737). Binds single stranded DNA (PubMed:8253737).By similarity2 Publications

Miscellaneous

The bound zinc ion is not a cofactor. It is bound to a zinc knuckle motif that may be involved in sequence recognition and the binding of ssDNA (By similarity).By similarity

<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 similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 presence of the regulatory subunit PRIM2/p58 accelerates the kinetics of initiation and primer extension.1 Publication

<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

  1. KM=0.25 mM for ATP1 Publication
  2. KM=3 mM for ATP (in presence of the regulatory PRIM2/p58)1 Publication
  3. KM=4.1 µM for oligo(A)-primed poly(dT)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei44Sequence analysis1
    Active sitei109Sequence analysis1
    Active sitei111Sequence analysis1

    <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 replication, Transcription
    LigandMetal-binding, Zinc

    Enzyme and pathway databases

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-MMU-113501, Inhibition of replication initiation of damaged DNA by RB1/E2F1
    R-MMU-174411, Polymerase switching on the C-strand of the telomere
    R-MMU-174430, Telomere C-strand synthesis initiation
    R-MMU-68952, DNA replication initiation
    R-MMU-68962, Activation of the pre-replicative complex
    R-MMU-69091, Polymerase switching
    R-MMU-69166, Removal of the Flap Intermediate
    R-MMU-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 primase small subunit (EC:2.7.7.-2 Publications)
    Alternative name(s):
    DNA primase 49 kDa subunit
    Short name:
    p49
    <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:Prim1
    <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>OrganismiMus musculus (Mouse)
    <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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
    <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
    • UP000000589 <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 10

    Organism-specific databases

    Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

    More...
    MGIi
    MGI:97757, Prim1

    <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

    DNA-directed RNA polymerase, Primosome

    <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_00000467311 – 417DNA primase small subunitAdd BLAST417

    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 residuei1N-acetylmethionineBy similarity1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P20664

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

    More...
    PaxDbi
    P20664

    PeptideAtlas

    More...
    PeptideAtlasi
    P20664

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P20664

    ProteomicsDB: a multi-organism proteome resource

    More...
    ProteomicsDBi
    291558

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P20664

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

    More...
    PhosphoSitePlusi
    P20664

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

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSMUSG00000025395, Expressed in midbrain and 304 other tissues

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P20664, MM

    <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

    Heterodimer of a catalytic subunit PRIM1 and a regulatory subunit PRIM2, also known as the DNA primase complex (PubMed:8253737, PubMed:8026492).

    Interacts with PRIM2/p58 (via C-terminus) (By similarity).

    Component of the alpha DNA polymerase complex (also known as the alpha DNA polymerase-primase complex) consisting of four subunits: the catalytic subunit POLA1, the regulatory subunit POLA2, and the primase complex subunits PRIM1 and PRIM2 respectively (PubMed:8253737). Within the complex, POLA1 directly interacts with PRIM2 (PubMed:8253737).

    By similarity2 Publications

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

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    202361, 7 interactors

    ComplexPortal: manually curated resource of macromolecular complexes

    More...
    ComplexPortali
    CPX-2088, DNA polymerase alpha:primase complex

    CORUM comprehensive resource of mammalian protein complexes

    More...
    CORUMi
    P20664

    Protein interaction database and analysis system

    More...
    IntActi
    P20664, 4 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    10090.ENSMUSP00000026461

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...
    RNActi
    P20664, 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

    3D structure databases

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

    More...
    SMRi
    P20664

    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

    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>Motifi121 – 131Zinc knuckle motifAdd BLAST11

    <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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG2851, Eukaryota

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00390000011466

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P20664

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    NVTRGFN

    Database of Orthologous Groups

    More...
    OrthoDBi
    1346165at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P20664

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF312823

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd04860, AE_Prim_S, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR002755, DNA_primase_S
    IPR014052, DNA_primase_ssu_euk/arc

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR10536, PTHR10536, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01896, DNA_primase_S, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00335, primase_sml, 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>Sequence (1+)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 has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

    P20664-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MEPFDPAELP ELLKLYYRRL FPYAQYYRWL NYGGVTKNYF QHREFSFTLK
    60 70 80 90 100
    DDIYIRYQSF NNQSELEKEM QKMNPYKIDI GAVYSHRPNQ HNTVKLGAFQ
    110 120 130 140 150
    AQEKELVFDI DMTDYDDVRR CCSSADICSK CWTLMTMAMR IIDRALKEDF
    160 170 180 190 200
    GFKHRLWVYS GRRGVHCWVC DESVRKLSSA VRSGIVEYLS LVKGGQDVKK
    210 220 230 240 250
    KVHLNEKVHP FVRKSINIIK KYFEEYALVG QDILENKENW DKILALVPET
    260 270 280 290 300
    IHDELQRGFQ KFHSSPQRWE HLRKVANSSQ NMKNDKCGPW LEWEVMLQYC
    310 320 330 340 350
    FPRLDVNVSK GVNHLLKSPF SVHPKTGRIS VPIDFHKVDQ FDPFTVPTIS
    360 370 380 390 400
    AICRELDMVS THEKEKEENE ADSKHRVRGY KKTSLAPYVK VFEQFLENLD
    410
    KSRKGELLKK SDLQKDF
    Length:417
    Mass (Da):49,295
    Last modified:February 1, 1991 - 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:i54EBF4DA4DE47D8A
    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
    J3QN19J3QN19_MOUSE
    DNA primase
    Prim1
    418Annotation 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 conflicti57Y → I in AAA39880 (PubMed:2925677).Curated1

    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
    J04620 mRNA Translation: AAA39880.1
    D13544 mRNA Translation: BAA02744.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS36086.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A33269

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_032947.1, NM_008921.2

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENSMUST00000026461; ENSMUSP00000026461; ENSMUSG00000025395

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    19075

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    mmu:19075

    UCSC genome browser

    More...
    UCSCi
    uc011xpx.2, mouse

    <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
    J04620 mRNA Translation: AAA39880.1
    D13544 mRNA Translation: BAA02744.1
    CCDSiCCDS36086.1
    PIRiA33269
    RefSeqiNP_032947.1, NM_008921.2

    3D structure databases

    SMRiP20664
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGRIDi202361, 7 interactors
    ComplexPortaliCPX-2088, DNA polymerase alpha:primase complex
    CORUMiP20664
    IntActiP20664, 4 interactors
    STRINGi10090.ENSMUSP00000026461

    PTM databases

    iPTMnetiP20664
    PhosphoSitePlusiP20664

    Proteomic databases

    EPDiP20664
    PaxDbiP20664
    PeptideAtlasiP20664
    PRIDEiP20664
    ProteomicsDBi291558

    Genome annotation databases

    EnsembliENSMUST00000026461; ENSMUSP00000026461; ENSMUSG00000025395
    GeneIDi19075
    KEGGimmu:19075
    UCSCiuc011xpx.2, mouse

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    5557
    MGIiMGI:97757, Prim1

    Phylogenomic databases

    eggNOGiKOG2851, Eukaryota
    GeneTreeiENSGT00390000011466
    InParanoidiP20664
    OMAiNVTRGFN
    OrthoDBi1346165at2759
    PhylomeDBiP20664
    TreeFamiTF312823

    Enzyme and pathway databases

    ReactomeiR-MMU-113501, Inhibition of replication initiation of damaged DNA by RB1/E2F1
    R-MMU-174411, Polymerase switching on the C-strand of the telomere
    R-MMU-174430, Telomere C-strand synthesis initiation
    R-MMU-68952, DNA replication initiation
    R-MMU-68962, Activation of the pre-replicative complex
    R-MMU-69091, Polymerase switching
    R-MMU-69166, Removal of the Flap Intermediate
    R-MMU-69183, Processive synthesis on the lagging strand

    Miscellaneous databases

    BioGRID ORCS database of CRISPR phenotype screens

    More...
    BioGRID-ORCSi
    19075, 18 hits in 52 CRISPR screens

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

    More...
    ChiTaRSi
    Prim1, mouse

    Protein Ontology

    More...
    PROi
    PR:P20664
    RNActiP20664, protein

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSMUSG00000025395, Expressed in midbrain and 304 other tissues
    GenevisibleiP20664, MM

    Family and domain databases

    CDDicd04860, AE_Prim_S, 1 hit
    InterProiView protein in InterPro
    IPR002755, DNA_primase_S
    IPR014052, DNA_primase_ssu_euk/arc
    PANTHERiPTHR10536, PTHR10536, 1 hit
    PfamiView protein in Pfam
    PF01896, DNA_primase_S, 1 hit
    TIGRFAMsiTIGR00335, primase_sml, 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 nameiPRI1_MOUSE
    <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: P20664
    <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: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: April 7, 2021
    This is version 149 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

    <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

    Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families
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