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Entry version 212 (13 Feb 2019)
Sequence version 3 (23 Jan 2007)
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Protein

Mitogen-activated protein kinase 14

Gene

Mapk14

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

Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK14 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. RPS6KA5/MSK1 and RPS6KA4/MSK2 can directly phosphorylate and activate transcription factors such as CREB1, ATF1, the NF-kappa-B isoform RELA/NFKB3, STAT1 and STAT3, but can also phosphorylate histone H3 and the nucleosomal protein HMGN1. RPS6KA5/MSK1 and RPS6KA4/MSK2 play important roles in the rapid induction of immediate-early genes in response to stress or mitogenic stimuli, either by inducing chromatin remodeling or by recruiting the transcription machinery. On the other hand, two other kinase targets, MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control of gene expression mostly at the post-transcriptional level, by phosphorylating ZFP36 (tristetraprolin) and ELAVL1, and by regulating EEF2K, which is important for the elongation of mRNA during translation. MKNK1/MNK1 and MKNK2/MNK2, two other kinases activated by p38 MAPKs, regulate protein synthesis by phosphorylating the initiation factor EIF4E2. MAPK14 interacts also with casein kinase II, leading to its activation through autophosphorylation and further phosphorylation of TP53/p53. In the cytoplasm, the p38 MAPK pathway is an important regulator of protein turnover. For example, CFLAR is an inhibitor of TNF-induced apoptosis whose proteasome-mediated degradation is regulated by p38 MAPK phosphorylation. In a similar way, MAPK14 phosphorylates the ubiquitin ligase SIAH2, regulating its activity towards EGLN3. MAPK14 may also inhibit the lysosomal degradation pathway of autophagy by interfering with the intracellular trafficking of the transmembrane protein ATG9. Another function of MAPK14 is to regulate the endocytosis of membrane receptors by different mechanisms that impinge on the small GTPase RAB5A. In addition, clathrin-mediated EGFR internalization induced by inflammatory cytokines and UV irradiation depends on MAPK14-mediated phosphorylation of EGFR itself as well as of RAB5A effectors. Ectodomain shedding of transmembrane proteins is regulated by p38 MAPKs as well. In response to inflammatory stimuli, p38 MAPKs phosphorylate the membrane-associated metalloprotease ADAM17. Such phosphorylation is required for ADAM17-mediated ectodomain shedding of TGF-alpha family ligands, which results in the activation of EGFR signaling and cell proliferation. Another p38 MAPK substrate is FGFR1. FGFR1 can be translocated from the extracellular space into the cytosol and nucleus of target cells, and regulates processes such as rRNA synthesis and cell growth. FGFR1 translocation requires p38 MAPK activation. In the nucleus, many transcription factors are phosphorylated and activated by p38 MAPKs in response to different stimuli. Classical examples include ATF1, ATF2, ATF6, ELK1, PTPRH, DDIT3, TP53/p53 and MEF2C and MEF2A. The p38 MAPKs are emerging as important modulators of gene expression by regulating chromatin modifiers and remodelers. The promoters of several genes involved in the inflammatory response, such as IL6, IL8 and IL12B, display a p38 MAPK-dependent enrichment of histone H3 phosphorylation on 'Ser-10' (H3S10ph) in LPS-stimulated myeloid cells. This phosphorylation enhances the accessibility of the cryptic NF-kappa-B-binding sites marking promoters for increased NF-kappa-B recruitment. Phosphorylates CDC25B and CDC25C which is required for binding to 14-3-3 proteins and leads to initiation of a G2 delay after ultraviolet radiation. Phosphorylates TIAR following DNA damage, releasing TIAR from GADD45A mRNA and preventing mRNA degradation. The p38 MAPKs may also have kinase-independent roles, which are thought to be due to the binding to targets in the absence of phosphorylation. Protein O-Glc-N-acylation catalyzed by the OGT is regulated by MAPK14, and, although OGT does not seem to be phosphorylated by MAPK14, their interaction increases upon MAPK14 activation induced by glucose deprivation. This interaction may regulate OGT activity by recruiting it to specific targets such as neurofilament H, stimulating its O-Glc-N-acylation. Required in mid-fetal development for the growth of embryo-derived blood vessels in the labyrinth layer of the placenta. Also plays an essential role in developmental and stress-induced erythropoiesis, through regulation of EPO gene expression. Phosphorylates S100A9 at 'Thr-113' (By similarity).By similarity4 Publications

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

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

Mg2+

<p>This subsection of the ‘Function’ 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

Activated by cell stresses such as DNA damage, heat shock, osmotic shock, anisomycin and sodium arsenite, as well as pro-inflammatory stimuli such as bacterial lipopolysaccharide (LPS) and interleukin-1. Activation occurs through dual phosphorylation of Thr-180 and Tyr-182 by either of two dual specificity kinases, MAP2K3/MKK3 or MAP2K6/MKK6, and potentially also MAP2K4/MKK4, as well as by TAB1-mediated autophosphorylation. MAPK14 phosphorylated on both Thr-180 and Tyr-182 is 10-20-fold more active than MAPK14 phosphorylated only on Thr-180, whereas MAPK14 phosphorylated on Tyr-182 alone is inactive. whereas Thr-180 is necessary for catalysis, Tyr-182 may be required for auto-activation and substrate recognition. Phosphorylated at Tyr-323 by ZAP70 in an alternative activation pathway in response to TCR signaling in T-cells. This alternative pathway is inhibited by GADD45A. Inhibited by dual specificity phosphatases, such as DUSP1, DUSP10, and DUSP16. Specifically inhibited by the binding of pyridinyl-imidazole compounds, which are cytokine-suppressive anti-inflammatory drugs (CSAID). SB203580 is an inhibitor of MAPK14.3 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

  1. KM=212 µM for ATP (when both Thr-180 and Tyr-182 are phosphorylated)1 Publication
  2. KM=1669 µM for ATP (when only Thr-180 is phosphorylated)1 Publication
  3. KM=656 µM for EGFR peptide as a substrate (when both Thr-180 and Tyr-182 are phosphorylated)1 Publication
  4. KM=2800 µM for EGFR peptide as a substrate (when only Thr-180 is phosphorylated)1 Publication
  5. KM=2.03 µM for ATF2 as a substrate (when both Thr-180 and Tyr-182 are phosphorylated)1 Publication
  6. KM=20.1 µM for ATF2 as a substrate (when only Thr-180 is phosphorylated)1 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 sitei32Inhibitor2 Publications1
    Binding sitei35Inhibitor2 Publications1
    Binding sitei53ATPPROSITE-ProRule annotation1
    Binding sitei53Inhibitor2 Publications1
    Binding sitei71Inhibitor2 Publications1
    Binding sitei109Inhibitor; via amide nitrogen and carbonyl oxygen2 Publications1
    Binding sitei111Inhibitor; via amide nitrogen2 Publications1
    <p>This subsection of the ‘Function’ 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 sitei168Proton acceptorPROSITE-ProRule annotation1
    Binding sitei168Inhibitor2 Publications1
    Binding sitei169Inhibitor; via carbonyl oxygen2 Publications1

    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 bindingi30 – 38ATPPROSITE-ProRule annotation9

    <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 functionKinase, Serine/threonine-protein kinase, Transferase
    Biological processApoptosis, Stress response, Transcription, Transcription regulation
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.7.11.24 3474

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-MMU-168638 NOD1/2 Signaling Pathway
    R-MMU-171007 p38MAPK events
    R-MMU-198753 ERK/MAPK targets
    R-MMU-2559580 Oxidative Stress Induced Senescence
    R-MMU-375170 CDO in myogenesis
    R-MMU-376172 DSCAM interactions
    R-MMU-418592 ADP signalling through P2Y purinoceptor 1
    R-MMU-432142 Platelet sensitization by LDL
    R-MMU-4420097 VEGFA-VEGFR2 Pathway
    R-MMU-450302 activated TAK1 mediates p38 MAPK activation
    R-MMU-450341 Activation of the AP-1 family of transcription factors
    R-MMU-5668599 RHO GTPases Activate NADPH Oxidases
    R-MMU-6798695 Neutrophil degranulation
    R-MMU-6804756 Regulation of TP53 Activity through Phosphorylation

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P47811

    <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:
    Mitogen-activated protein kinase 14 (EC:2.7.11.242 Publications)
    Short name:
    MAP kinase 14
    Short name:
    MAPK 14
    Alternative name(s):
    CRK1
    Mitogen-activated protein kinase p38 alpha
    Short name:
    MAP kinase p38 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:Mapk14
    Synonyms:Crk1, Csbp1, Csbp2
    <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>OrganismiMus musculus (Mouse)
    <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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
    <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
    • UP000000589 <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 17

    Organism-specific databases

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

    More...
    MGIi
    MGI:1346865 Mapk14

    <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

    Cytoplasm, 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>Mutagenesisi180T → A: Phosphorylation blocked. 1 Publication1
    Mutagenesisi182Y → F: Phosphorylation blocked. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL2336

    <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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
    <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_00001862922 – 360Mitogen-activated protein kinase 14Add BLAST359

    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 residuei2N-acetylserineBy similarity1
    Modified residuei2PhosphoserineBy similarity1
    Modified residuei16PhosphothreonineBy similarity1
    Modified residuei53N6-acetyllysineBy similarity1
    Modified residuei152N6-acetyllysineBy similarity1
    Modified residuei180PhosphothreonineCombined sources1 Publication1
    Modified residuei180Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and autocatalysisBy similarity1
    Modified residuei182PhosphotyrosineCombined sources1 Publication1
    Modified residuei182Phosphotyrosine; by MAP2K3, MAP2K4, MAP2K6 and autocatalysisBy similarity1
    Modified residuei323Phosphotyrosine; by ZAP70By similarity1

    <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

    Dually phosphorylated on Thr-180 and Tyr-182 by the MAP2Ks MAP2K3/MKK3, MAP2K4/MKK4 and MAP2K6/MKK6 in response to inflammatory cytokines, environmental stress or growth factors, which activates the enzyme. Dual phosphorylation can also be mediated by TAB1-mediated autophosphorylation. TCR engagement in T-cells also leads to Tyr-323 phosphorylation by ZAP70. Dephosphorylated and inactivated by DUPS1, DUSP10 and DUSP16. PPM1D also mediates dephosphorylation and inactivation of MAPK14 (By similarity).By similarity2 Publications
    Acetylated at Lys-53 and Lys-152 by KAT2B and EP300. Acetylation at Lys-53 increases the affinity for ATP and enhances kinase activity. Lys-53 and Lys-152 are deacetylated by HDAC3 (By similarity).By similarity
    Ubiquitinated. Ubiquitination leads to degradation by the proteasome pathway (By similarity).By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P47811

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P47811

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P47811

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

    More...
    PaxDbi
    P47811

    PeptideAtlas

    More...
    PeptideAtlasi
    P47811

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P47811

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P47811

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

    More...
    PhosphoSitePlusi
    P47811

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

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

    Macrophages, monocytes, T- and B-lymphocytes. Isoform 2 is specifically expressed in kidney and liver.

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSMUSG00000053436 Expressed in 297 organ(s), highest expression level in blood

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P47811 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P47811 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_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

    Component of a signaling complex containing at least AKAP13, PKN1, MAPK14, ZAK and MAP2K3. Within this complex, AKAP13 interacts directly with PKN1, which in turn recruits MAPK14, MAP2K3 and ZAK (By similarity). Binds to a kinase interaction motif within the protein tyrosine phosphatase, PTPRR (By similarity). This interaction retains MAPK14 in the cytoplasm and prevents nuclear accumulation (By similarity). Interacts with SPAG9 and GADD45A (By similarity). Interacts with CDC25B, CDC25C, DUSP1, DUSP10, DUSP16, NP60, SUPT20H and TAB1. Interacts with casein kinase II subunits CSNK2A1 and CSNK2B. Interacts with PPM1D. Interacts with CDK5RAP3; recruits PPM1D to MAPK14 and may regulate its dephosphorylation (By similarity).By similarity6 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    204969, 25 interactors

    Database of interacting proteins

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    DIPi
    DIP-31073N

    The Eukaryotic Linear Motif resource for Functional Sites in Proteins

    More...
    ELMi
    P47811

    Protein interaction database and analysis system

    More...
    IntActi
    P47811, 27 interactors

    Molecular INTeraction database

    More...
    MINTi
    P47811

    STRING: functional protein association networks

    More...
    STRINGi
    10090.ENSMUSP00000004990

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P47811

    <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

    1360
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

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    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1LEWX-ray2.30A1-360[»]
    1LEZX-ray2.30A1-360[»]
    1YW2X-ray2.01A1-360[»]
    1YWRX-ray1.95A1-360[»]
    2EWAX-ray2.10A1-360[»]
    2GHLX-ray2.10A5-352[»]
    2GHMX-ray2.35A5-352[»]
    2GTMX-ray1.90A5-352[»]
    2GTNX-ray1.80A5-352[»]
    2OZAX-ray2.70B2-360[»]
    2PUUX-ray2.50A5-352[»]
    3P4KX-ray2.30A1-360[»]
    3P5KX-ray2.09A2-360[»]
    3P78X-ray2.30A2-360[»]
    3P79X-ray2.10A2-360[»]
    3P7AX-ray2.31A2-360[»]
    3P7BX-ray1.90A2-360[»]
    3P7CX-ray2.30A2-360[»]
    3PY3X-ray2.10A1-360[»]
    3TG1X-ray2.71A1-360[»]
    4KA3X-ray2.71A1-360[»]
    4LOOX-ray1.95A1-360[»]
    4LOPX-ray2.05A/B/C/D1-360[»]
    4LOQX-ray2.32A/B/C/D1-360[»]
    4TYHX-ray3.00B6-353[»]
    5LARX-ray1.50A1-360[»]
    5NZZX-ray2.60E/F/G/H1-360[»]
    5O90X-ray2.49A1-360[»]
    5UOJX-ray2.10A1-360[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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    ProteinModelPortali
    P47811

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

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    SMRi
    P47811

    Database of comparative protein structure models

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    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
    P47811

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini24 – 308Protein kinasePROSITE-ProRule annotationAdd BLAST285

    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>Regioni106 – 111Inhibitor-binding6

    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>Motifi180 – 182TXY3

    <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 TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.

    <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
    KOG0660 Eukaryota
    ENOG410XNY0 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000155325

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG014652

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P47811

    KEGG Orthology (KO)

    More...
    KOi
    K04441

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    EITNRYT

    Database of Orthologous Groups

    More...
    OrthoDBi
    683132at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P47811

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF105100

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd07877 STKc_p38alpha, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR011009 Kinase-like_dom_sf
    IPR003527 MAP_kinase_CS
    IPR008352 MAPK_p38-like
    IPR038784 p38alpha
    IPR000719 Prot_kinase_dom
    IPR017441 Protein_kinase_ATP_BS

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00069 Pkinase, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR01773 P38MAPKINASE

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00220 S_TKc, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF56112 SSF56112, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS01351 MAPK, 1 hit
    PS00107 PROTEIN_KINASE_ATP, 1 hit
    PS50011 PROTEIN_KINASE_DOM, 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 (4+)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.

    <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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 <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 4 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: P47811-1) [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
    MSQERPTFYR QELNKTIWEV PERYQNLSPV GSGAYGSVCA AFDTKTGHRV
    60 70 80 90 100
    AVKKLSRPFQ SIIHAKRTYR ELRLLKHMKH ENVIGLLDVF TPARSLEEFN
    110 120 130 140 150
    DVYLVTHLMG ADLNNIVKCQ KLTDDHVQFL IYQILRGLKY IHSADIIHRD
    160 170 180 190 200
    LKPSNLAVNE DCELKILDFG LARHTDDEMT GYVATRWYRA PEIMLNWMHY
    210 220 230 240 250
    NQTVDIWSVG CIMAELLTGR TLFPGTDHID QLKLILRLVG TPGAELLKKI
    260 270 280 290 300
    SSESARNYIQ SLAQMPKMNF ANVFIGANPL AVDLLEKMLV LDSDKRITAA
    310 320 330 340 350
    QALAHAYFAQ YHDPDDEPVA DPYDQSFESR DLLIDEWKSL TYDEVISFVP
    360
    PPLDQEEMES
    Length:360
    Mass (Da):41,287
    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:iDFB03EBCE97BB51A
    GO
    Isoform 2 (identifier: P47811-2) [UniParc]FASTAAdd to basket
    Also known as: Piccolo

    The sequence of this isoform differs from the canonical sequence as follows:
         255-278: ARNYIQSLAQMPKMNFANVFIGAN → DAKP
         279-360: Missing.

    Show »
    Length:258
    Mass (Da):29,637
    Checksum:iABBBDF65DC32AF03
    GO
    Isoform 3 (identifier: P47811-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         230-254: DQLKLILRLVGTPGAELLKKISSES → NQLQQIMRLTGTPPAYLINRMPSHE

    Show »
    Length:360
    Mass (Da):41,487
    Checksum:iF1F20352F76590BD
    GO
    Isoform 4 (identifier: P47811-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-77: Missing.

    Show »
    Length:283
    Mass (Da):32,327
    Checksum:i895D71CB69550519
    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
    B2KF34B2KF34_MOUSE
    Mitogen-activated protein kinase
    Mapk14
    227Annotation 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>
    B2KF35B2KF35_MOUSE
    Mitogen-activated protein kinase
    Mapk14
    258Annotation 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>
    A0A3B2WB60A0A3B2WB60_MOUSE
    Mitogen-activated protein kinase
    Mapk14
    307Annotation 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>
    A0A3B2WAZ7A0A3B2WAZ7_MOUSE
    Mitogen-activated protein kinase 14
    Mapk14
    50Annotation 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 conflicti98E → G in AAF06348 (Ref. 7) Curated1
    Sequence conflicti107 – 108HL → LS in AAF06348 (Ref. 7) Curated2
    Sequence conflicti115N → R in AAF06348 (Ref. 7) Curated1
    Sequence conflicti124D → G in AAF06348 (Ref. 7) Curated1
    Sequence conflicti159 – 162NEDC → TQVI in AAF06348 (Ref. 7) Curated4
    Sequence conflicti166I → L in AAF06348 (Ref. 7) Curated1
    Sequence conflicti202Q → R in AAF06348 (Ref. 7) Curated1
    Sequence conflicti211 – 212CI → GF in AAF06348 (Ref. 7) Curated2
    Sequence conflicti224P → L in AAF06348 (Ref. 7) Curated1
    Sequence conflicti271A → P in AAF06348 (Ref. 7) Curated1
    Sequence conflicti299A → V in AAF06348 (Ref. 7) Curated1
    Sequence conflicti315D → Y in AAF06348 (Ref. 7) Curated1
    Isoform 3 (identifier: P47811-3)
    Sequence conflicti238L → M in BAA19741 (Ref. 2) 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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0223591 – 77Missing in isoform 4. 1 PublicationAdd BLAST77
    Alternative sequenceiVSP_007544230 – 254DQLKL…ISSES → NQLQQIMRLTGTPPAYLINR MPSHE in isoform 3. 3 PublicationsAdd BLAST25
    Alternative sequenceiVSP_004846255 – 278ARNYI…FIGAN → DAKP in isoform 2. 1 PublicationAdd BLAST24
    Alternative sequenceiVSP_007545279 – 360Missing in isoform 2. 1 PublicationAdd BLAST82

    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
    U10871 mRNA Translation: AAA20888.1
    D83073 mRNA Translation: BAA19741.1
    AF128892 mRNA Translation: AAF34818.1
    AK151348 mRNA Translation: BAE30324.1
    AK153025 mRNA Translation: BAE31659.1
    AK089059 mRNA Translation: BAC40726.1
    AK133684 mRNA Translation: BAE21782.1
    CT009661 Genomic DNA No translation available.
    BC012235 mRNA Translation: AAH12235.1
    AF195850 mRNA Translation: AAF06348.1
    X65067 mRNA Translation: CAA46200.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS28583.1 [P47811-1]
    CCDS50048.1 [P47811-3]
    CCDS50049.1 [P47811-4]

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    I49066

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001161980.1, NM_001168508.1 [P47811-3]
    NP_001161985.1, NM_001168513.1 [P47811-4]
    NP_001161986.1, NM_001168514.1 [P47811-4]
    NP_036081.1, NM_011951.3 [P47811-1]

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Mm.311337

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENSMUST00000004990; ENSMUSP00000004990; ENSMUSG00000053436 [P47811-3]
    ENSMUST00000062694; ENSMUSP00000061958; ENSMUSG00000053436 [P47811-1]
    ENSMUST00000114752; ENSMUSP00000110400; ENSMUSG00000053436 [P47811-4]
    ENSMUST00000114754; ENSMUSP00000110402; ENSMUSG00000053436 [P47811-4]
    ENSMUST00000114758; ENSMUSP00000110406; ENSMUSG00000053436 [P47811-2]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    26416

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    mmu:26416

    UCSC genome browser

    More...
    UCSCi
    uc008brl.2 mouse [P47811-1]

    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
    U10871 mRNA Translation: AAA20888.1
    D83073 mRNA Translation: BAA19741.1
    AF128892 mRNA Translation: AAF34818.1
    AK151348 mRNA Translation: BAE30324.1
    AK153025 mRNA Translation: BAE31659.1
    AK089059 mRNA Translation: BAC40726.1
    AK133684 mRNA Translation: BAE21782.1
    CT009661 Genomic DNA No translation available.
    BC012235 mRNA Translation: AAH12235.1
    AF195850 mRNA Translation: AAF06348.1
    X65067 mRNA Translation: CAA46200.1
    CCDSiCCDS28583.1 [P47811-1]
    CCDS50048.1 [P47811-3]
    CCDS50049.1 [P47811-4]
    PIRiI49066
    RefSeqiNP_001161980.1, NM_001168508.1 [P47811-3]
    NP_001161985.1, NM_001168513.1 [P47811-4]
    NP_001161986.1, NM_001168514.1 [P47811-4]
    NP_036081.1, NM_011951.3 [P47811-1]
    UniGeneiMm.311337

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1LEWX-ray2.30A1-360[»]
    1LEZX-ray2.30A1-360[»]
    1YW2X-ray2.01A1-360[»]
    1YWRX-ray1.95A1-360[»]
    2EWAX-ray2.10A1-360[»]
    2GHLX-ray2.10A5-352[»]
    2GHMX-ray2.35A5-352[»]
    2GTMX-ray1.90A5-352[»]
    2GTNX-ray1.80A5-352[»]
    2OZAX-ray2.70B2-360[»]
    2PUUX-ray2.50A5-352[»]
    3P4KX-ray2.30A1-360[»]
    3P5KX-ray2.09A2-360[»]
    3P78X-ray2.30A2-360[»]
    3P79X-ray2.10A2-360[»]
    3P7AX-ray2.31A2-360[»]
    3P7BX-ray1.90A2-360[»]
    3P7CX-ray2.30A2-360[»]
    3PY3X-ray2.10A1-360[»]
    3TG1X-ray2.71A1-360[»]
    4KA3X-ray2.71A1-360[»]
    4LOOX-ray1.95A1-360[»]
    4LOPX-ray2.05A/B/C/D1-360[»]
    4LOQX-ray2.32A/B/C/D1-360[»]
    4TYHX-ray3.00B6-353[»]
    5LARX-ray1.50A1-360[»]
    5NZZX-ray2.60E/F/G/H1-360[»]
    5O90X-ray2.49A1-360[»]
    5UOJX-ray2.10A1-360[»]
    ProteinModelPortaliP47811
    SMRiP47811
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi204969, 25 interactors
    DIPiDIP-31073N
    ELMiP47811
    IntActiP47811, 27 interactors
    MINTiP47811
    STRINGi10090.ENSMUSP00000004990

    Chemistry databases

    BindingDBiP47811
    ChEMBLiCHEMBL2336

    PTM databases

    iPTMnetiP47811
    PhosphoSitePlusiP47811

    Proteomic databases

    EPDiP47811
    jPOSTiP47811
    MaxQBiP47811
    PaxDbiP47811
    PeptideAtlasiP47811
    PRIDEiP47811

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000004990; ENSMUSP00000004990; ENSMUSG00000053436 [P47811-3]
    ENSMUST00000062694; ENSMUSP00000061958; ENSMUSG00000053436 [P47811-1]
    ENSMUST00000114752; ENSMUSP00000110400; ENSMUSG00000053436 [P47811-4]
    ENSMUST00000114754; ENSMUSP00000110402; ENSMUSG00000053436 [P47811-4]
    ENSMUST00000114758; ENSMUSP00000110406; ENSMUSG00000053436 [P47811-2]
    GeneIDi26416
    KEGGimmu:26416
    UCSCiuc008brl.2 mouse [P47811-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    1432
    MGIiMGI:1346865 Mapk14

    Phylogenomic databases

    eggNOGiKOG0660 Eukaryota
    ENOG410XNY0 LUCA
    GeneTreeiENSGT00940000155325
    HOVERGENiHBG014652
    InParanoidiP47811
    KOiK04441
    OMAiEITNRYT
    OrthoDBi683132at2759
    PhylomeDBiP47811
    TreeFamiTF105100

    Enzyme and pathway databases

    BRENDAi2.7.11.24 3474
    ReactomeiR-MMU-168638 NOD1/2 Signaling Pathway
    R-MMU-171007 p38MAPK events
    R-MMU-198753 ERK/MAPK targets
    R-MMU-2559580 Oxidative Stress Induced Senescence
    R-MMU-375170 CDO in myogenesis
    R-MMU-376172 DSCAM interactions
    R-MMU-418592 ADP signalling through P2Y purinoceptor 1
    R-MMU-432142 Platelet sensitization by LDL
    R-MMU-4420097 VEGFA-VEGFR2 Pathway
    R-MMU-450302 activated TAK1 mediates p38 MAPK activation
    R-MMU-450341 Activation of the AP-1 family of transcription factors
    R-MMU-5668599 RHO GTPases Activate NADPH Oxidases
    R-MMU-6798695 Neutrophil degranulation
    R-MMU-6804756 Regulation of TP53 Activity through Phosphorylation
    SABIO-RKiP47811

    Miscellaneous databases

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

    More...
    ChiTaRSi
    Mapk14 mouse
    EvolutionaryTraceiP47811

    Protein Ontology

    More...
    PROi
    PR:P47811

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSMUSG00000053436 Expressed in 297 organ(s), highest expression level in blood
    ExpressionAtlasiP47811 baseline and differential
    GenevisibleiP47811 MM

    Family and domain databases

    CDDicd07877 STKc_p38alpha, 1 hit
    InterProiView protein in InterPro
    IPR011009 Kinase-like_dom_sf
    IPR003527 MAP_kinase_CS
    IPR008352 MAPK_p38-like
    IPR038784 p38alpha
    IPR000719 Prot_kinase_dom
    IPR017441 Protein_kinase_ATP_BS
    PfamiView protein in Pfam
    PF00069 Pkinase, 1 hit
    PRINTSiPR01773 P38MAPKINASE
    SMARTiView protein in SMART
    SM00220 S_TKc, 1 hit
    SUPFAMiSSF56112 SSF56112, 1 hit
    PROSITEiView protein in PROSITE
    PS01351 MAPK, 1 hit
    PS00107 PROTEIN_KINASE_ATP, 1 hit
    PS50011 PROTEIN_KINASE_DOM, 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 nameiMK14_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: P47811
    Secondary accession number(s): B2KF37
    , B2KF38, O08666, Q3U6R5, Q3UZS3, Q8C289, Q9JLV8, Q9QZ80
    <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: February 1, 1996
    Last sequence update: January 23, 2007
    Last modified: February 13, 2019
    This is version 212 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
    3. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    UniProt is an ELIXIR core data resource
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