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Protein

Poly(A) polymerase alpha

Gene

PAPOLA

Organism
Bos taurus (Bovine)
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

Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus.By similarity1 Publication

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

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

Mg2+1 Publication, Mn2+1 PublicationNote: Binds 2 magnesium ions. Also active with manganese.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=0.229 mM for ATP1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 sitei109ATP1
    <p>This subsection of the ‘Function’ 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 bindingi113Magnesium 1; catalytic1
    Metal bindingi113Magnesium 2; catalytic1
    Metal bindingi115Magnesium 1; catalytic1
    Metal bindingi115Magnesium 2; catalytic1
    Metal bindingi167Magnesium 2; catalytic1
    Binding sitei167ATP1
    Binding sitei228ATP1
    Binding sitei237ATP1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi100 – 102ATP3
    Nucleotide bindingi113 – 115ATP3
    Nucleotide bindingi246 – 247ATP2

    <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 functionRNA-binding, Transferase
    Biological processmRNA processing
    LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.7.7.19 908

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-BTA-109688 Cleavage of Growing Transcript in the Termination Region
    R-BTA-72163 mRNA Splicing - Major Pathway
    R-BTA-72187 mRNA 3'-end processing
    R-BTA-77595 Processing of Intronless Pre-mRNAs

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P25500

    <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:
    Poly(A) polymerase alpha (EC:2.7.7.19)
    Short name:
    PAP-alpha
    Alternative name(s):
    Polynucleotide adenylyltransferase alpha
    <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:PAPOLA
    Synonyms:PAP
    <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>OrganismiBos taurus (Bovine)
    <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 identifieri9913 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    <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
    • UP000009136 <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 21

    <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; 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_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>Mutagenesisi100F → D: Strongly decreased enzyme activity. Strongly reduced affinity for RNA. 1 Publication1
    Mutagenesisi113 – 115DID → AIA: Abolishes most of the specific and non-specific polyadenylation activity. 3
    Mutagenesisi113D → H: Abolishes most of the specific and non-specific polyadenylation activity. 1 Publication1
    Mutagenesisi115D → H: Abolishes most of the specific and non-specific polyadenylation activity. 1 Publication1
    Mutagenesisi153F → A: Strongly reduced affinity for RNA. 1 Publication1
    Mutagenesisi156V → A: Strongly decreased enzyme activity. Strongly reduced affinity for RNA. 1 Publication1
    Mutagenesisi162 – 163DG → HA: Small decrease in non-specific and specific polyadenylation activity. 1 Publication2
    Mutagenesisi167D → A: Loss of enzyme activity. 2 Publications1
    Mutagenesisi167D → H: Abolishes most of the specific and non-specific polyadenylation activity. 2 Publications1
    Mutagenesisi167D → N: Strongly decreased enzyme activity. Strongly reduced affinity for RNA. 2 Publications1
    Mutagenesisi186D → H: Small decrease in non-specific and specific polyadenylation activity. 1 Publication1
    Mutagenesisi194D → H: No change in non-specific and specific polyadenylation activity. 1 Publication1
    Mutagenesisi199R → A: Strongly reduced affinity for RNA. 1 Publication1
    Mutagenesisi202N → A: Strongly decreased enzyme activity. Strongly reduced affinity for RNA. 1 Publication1
    Mutagenesisi203G → H: Loss of enzyme activity. Strongly reduced affinity for RNA. 1 Publication1
    Mutagenesisi208 – 209DE → AA: Reduces by 60% non-specific and specific polyadenylation activity. 2
    Mutagenesisi208D → A: Reduces by 60% non-specific rf and specific polyadenylation activity. 1 Publication1
    Mutagenesisi208D → H: Reduces by 20% non-specific and specific polyadenylation activity. 1 Publication1
    Mutagenesisi209E → A: No change in non-specific and specific polyadenylation activity. 1 Publication1
    Mutagenesisi228K → A: Strongly decreased affinity for ATP. 1 Publication1
    Mutagenesisi232K → A: Decreased affinity for ATP. 1 Publication1
    Mutagenesisi237Y → A: Strongly decreased affinity for ATP. 1 Publication1
    Mutagenesisi247V → A or R: Strongly reduced affinity for RNA. 1 Publication1
    Mutagenesisi291 – 292EE → AA: Abolishes most of non-specific polyadenylation activity. 2
    Mutagenesisi291E → A: Reduces by 60% non-specific polyadenylation activity. 1 Publication1
    Mutagenesisi292E → A: No change in non-specific polyadenylation activity. 1 Publication1
    Mutagenesisi308D → A: No change in non-specific and specific polyadenylation activity. 1
    Mutagenesisi317T → G: Strongly decreased affinity for ATP. 1
    Mutagenesisi431 – 432EE → AA: No change in non-specific and specific polyadenylation activity. 1 Publication2
    Mutagenesisi455D → A: Reduces by 30% non-specific polyadenylation activity. 1 Publication1
    Mutagenesisi459D → A: No change in non-specific polyadenylation activity. 1 Publication1
    Mutagenesisi465D → A: No change in non-specific and specific polyadenylation activity. 1 Publication1
    Mutagenesisi635K → Q: Weak binding to KPBN1. Cytoplasmic location; when associated with Q-644; Q-730 and Q-734. 1 Publication1
    Mutagenesisi635K → R: Some decrease in acetylation. Binds KPBN1 and localizes to the nucleus; when associated with R-644; R-730 and R-734. 1 Publication1
    Mutagenesisi644K → Q: Weak binding to KPBN1. Cytoplasmic location; when associated with Q-635; Q-730 and Q-734. 1 Publication1
    Mutagenesisi644K → R: Large decrease in acetylation. Binds KPBN1 and localizes to the nucleus; when associated with R-635; R-730 and R-734. 1 Publication1
    Mutagenesisi730K → Q: Weak binding to KPBN1. Cytoplasmic location; when associated with Q-635; Q-644 and Q-734. 1 Publication1
    Mutagenesisi730K → R: Some decrease in acetylation. Binds KPBN1 and localizes to the nucleus; when associated with R-635; R-644 and R-734. 1 Publication1
    Mutagenesisi734K → Q: Weak binding to KPBN1. Cytoplasmic location; when associated with Q-635; Q-644 and Q-730. 1 Publication1
    Mutagenesisi734K → R: Some decrease in acetylation. Binds KPBN1 and localizes to the nucleus; when associated with R-635; R-644 and R-730. 1 Publication1

    <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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000516111 – 739Poly(A) polymerase alphaAdd BLAST739

    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 residuei10PhosphoserineBy similarity1
    Modified residuei24PhosphoserineBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki444Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
    Cross-linki445Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
    Cross-linki506Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
    Cross-linki507Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)Curated
    Modified residuei537Phosphoserine; by MAPKBy similarity1
    Modified residuei558PhosphoserineBy similarity1
    Modified residuei635N6-acetyllysine1 Publication1
    Modified residuei644N6-acetyllysine1 Publication1
    Modified residuei730N6-acetyllysine; alternate1 Publication1
    Cross-linki730Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
    Modified residuei732PhosphoserineBy similarity1
    Modified residuei734N6-acetyllysine; alternate1 Publication1
    Cross-linki734Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity

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

    Polysumoylated. Varying sumolyation depending on tissue- and cell-type. Highly sumoylated in bladder and NIH 3T3 cells. Sumoylation is required for nuclear localization and enhances PAP stability. Desumoylated by SENP1. Inhibits polymerase activity (By similarity).By similarity
    Hyperphosphorylation on multiple CDK2 consensus and non-consensus sites in the C-terminal Ser/Thr-rich region represses PAP activity in late M-phase. Phosphorylation/dephosphorylation may regulate the interaction between PAP and CPSF (By similarity).By similarity
    Acetylated in the C-terminus. Acetylation decreases interaction with NUDT21 and KPNB1, and inhibits nuclear localization through inhibiting binding to the importin alpha/beta complex.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

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

    More...
    PaxDbi
    P25500

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P25500

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P25500

    <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
    ENSBTAG00000004054 Expressed in 10 organ(s), highest expression level in spleen

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P25500 baseline and differential

    <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

    Monomer (PubMed:10944102, PubMed:15328606). Found in a complex with CPSF1, FIP1L1 and PAPOLA. Interacts with AHCYL1 and FIP1L1; the interaction with AHCYL1 seems to increase interaction with FIP1L1 (By similarity). Interacts with NUDT21; the interaction is diminished by acetylation (PubMed:17172643). Interacts with KPNB1; the interaction promotes PAP nuclear import and is inhibited by acetylation of PAP (PubMed:17172643).By similarity3 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei153Interaction with RNABy similarity1
    Sitei158Interaction with RNABy similarity1
    Sitei328Interaction with RNABy similarity1
    Sitei399Interaction with RNABy similarity1
    Sitei524Interaction with RNABy similarity1

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    9913.ENSBTAP00000005300

    <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

    1739
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P25500

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

    More...
    SMRi
    P25500

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P25500

    <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>Regioni508 – 643Ser/Thr-richAdd BLAST136
    Regioni671 – 739Required for interaction with NUDT211 PublicationAdd BLAST69

    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>Motifi490 – 507Nuclear localization signal 1Add BLAST18
    Motifi644 – 659Nuclear localization signal 2Add 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 poly(A) polymerase family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG2245 Eukaryota
    COG5186 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000154598

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000204376

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG053502

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P25500

    KEGG Orthology (KO)

    More...
    KOi
    K14376

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    QLEWCGL

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG091G0571

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF300842

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR011068 NuclTrfase_I-like_C
    IPR007012 PolA_pol_cen_dom
    IPR007010 PolA_pol_RNA-bd_dom
    IPR014492 PolyA_polymerase
    IPR002934 Polymerase_NTP_transf_dom

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR10682 PTHR10682, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01909 NTP_transf_2, 1 hit
    PF04928 PAP_central, 1 hit
    PF04926 PAP_RNA-bind, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF018425 PolyA_polymerase, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF55003 SSF55003, 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>.<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
    Note: Additional isoforms seem to exist.

    This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

    Isoform Long (identifier: P25500-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' 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
    MPFPVTTQGS QQTQPPQKHY GITSPISLAA PKETDCLLTQ KLVETLKPFG
    60 70 80 90 100
    VFEEEEELQR RILILGKLNN LVKEWIREIS ESKNLPQSVI ENVGGKIFTF
    110 120 130 140 150
    GSYRLGVHTK GADIDALCVA PRHVDRSDFF TSFYDKLKLQ EEVKDLRAVE
    160 170 180 190 200
    EAFVPVIKLC FDGIEIDILF ARLALQTIPE DLDLRDDSLL KNLDIRCIRS
    210 220 230 240 250
    LNGCRVTDEI LHLVPNIDNF RLTLRAIKLW AKRHNIYSNI LGFLGGVSWA
    260 270 280 290 300
    MLVARTCQLY PNAIASTLVH KFFLVFSKWE WPNPVLLKQP EECNLNLPVW
    310 320 330 340 350
    DPRVNPSDRY HLMPIITPAY PQQNSTYNVS VSTRMVMVEE FKQGLAITDE
    360 370 380 390 400
    ILLSKAEWSK LFEAPNFFQK YKHYIVLLAS APTEKQRLEW VGLVESKIRI
    410 420 430 440 450
    LVGSLEKNEF ITLAHVNPQS FPAPKENPDK EEFRTMWVIG LVFKKTENSE
    460 470 480 490 500
    NLSVDLTYDI QSFTDTVYRQ AINSKMFEVD MKIAAMHVKR KQLHQLLPSH
    510 520 530 540 550
    VLQKKKKHST EGVKLTPLND SSLDLSMDSD NSMSVPSPTS AMKTSPLNSS
    560 570 580 590 600
    GSSQGRNSPA PAVTAASVTN IQATEVSLPQ INSSESSGGT SSESIPQTAT
    610 620 630 640 650
    QPAISSPPKP TVSRVVSSTR LVNPPPRPSG NAAAKIPNPI VGVKRTSSPH
    660 670 680 690 700
    KEESPKKTKT EEDETSEDAN CLALSGHDKT ETKEQLDTET STTQSETIQT
    710 720 730
    ATSLLASQKT SSTDLSDIPA LPANPIPVIK NSIKLRLNR
    Length:739
    Mass (Da):82,441
    Last modified:January 23, 2007 - 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:i7C89C15E33232CFF
    GO
    Isoform Short (identifier: P25500-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         663-683: Missing.
         709-710: KT → II
         711-739: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:689
    Mass (Da):77,066
    Checksum:i20BECA9A51B9ED1A
    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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    Q3T0A2Q3T0A2_BOVIN
    PAPOLA protein
    PAPOLA
    693Annotation score:

    Annotation score:2 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>
    G3MYA2G3MYA2_BOVIN
    Poly(A) polymerase alpha
    PAPOLA
    718Annotation score:

    Annotation score:2 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 conflicti80S → R in CAA45031 (PubMed:1896071).Curated1

    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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_004524663 – 683Missing in isoform Short. 1 PublicationAdd BLAST21
    Alternative sequenceiVSP_004525709 – 710KT → II in isoform Short. 1 Publication2
    Alternative sequenceiVSP_004526711 – 739Missing in isoform Short. 1 PublicationAdd BLAST29

    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
    X61585 mRNA Translation: CAA43782.1
    X63436 mRNA Translation: CAA45031.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S17875
    S17925
    S18642

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_788820.1, NM_176647.2 [P25500-1]

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Bt.109586

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENSBTAT00000005300; ENSBTAP00000005300; ENSBTAG00000004054 [P25500-1]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    338051

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    bta:338051

    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
    X61585 mRNA Translation: CAA43782.1
    X63436 mRNA Translation: CAA45031.1
    PIRiS17875
    S17925
    S18642
    RefSeqiNP_788820.1, NM_176647.2 [P25500-1]
    UniGeneiBt.109586

    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
    1F5AX-ray2.50A1-513[»]
    1Q78X-ray2.80A1-514[»]
    1Q79X-ray2.15A1-514[»]
    ProteinModelPortaliP25500
    SMRiP25500
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000005300

    PTM databases

    iPTMnetiP25500

    Proteomic databases

    PaxDbiP25500
    PRIDEiP25500

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSBTAT00000005300; ENSBTAP00000005300; ENSBTAG00000004054 [P25500-1]
    GeneIDi338051
    KEGGibta:338051

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    10914

    Phylogenomic databases

    eggNOGiKOG2245 Eukaryota
    COG5186 LUCA
    GeneTreeiENSGT00940000154598
    HOGENOMiHOG000204376
    HOVERGENiHBG053502
    InParanoidiP25500
    KOiK14376
    OMAiQLEWCGL
    OrthoDBiEOG091G0571
    TreeFamiTF300842

    Enzyme and pathway databases

    BRENDAi2.7.7.19 908
    ReactomeiR-BTA-109688 Cleavage of Growing Transcript in the Termination Region
    R-BTA-72163 mRNA Splicing - Major Pathway
    R-BTA-72187 mRNA 3'-end processing
    R-BTA-77595 Processing of Intronless Pre-mRNAs
    SABIO-RKiP25500

    Miscellaneous databases

    EvolutionaryTraceiP25500

    Gene expression databases

    BgeeiENSBTAG00000004054 Expressed in 10 organ(s), highest expression level in spleen
    ExpressionAtlasiP25500 baseline and differential

    Family and domain databases

    InterProiView protein in InterPro
    IPR011068 NuclTrfase_I-like_C
    IPR007012 PolA_pol_cen_dom
    IPR007010 PolA_pol_RNA-bd_dom
    IPR014492 PolyA_polymerase
    IPR002934 Polymerase_NTP_transf_dom
    PANTHERiPTHR10682 PTHR10682, 1 hit
    PfamiView protein in Pfam
    PF01909 NTP_transf_2, 1 hit
    PF04928 PAP_central, 1 hit
    PF04926 PAP_RNA-bind, 1 hit
    PIRSFiPIRSF018425 PolyA_polymerase, 1 hit
    SUPFAMiSSF55003 SSF55003, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    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 nameiPAPOA_BOVIN
    <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: P25500
    <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: May 1, 1992
    Last sequence update: January 23, 2007
    Last modified: December 5, 2018
    This is version 161 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

    <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, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
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