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Entry version 229 (23 Feb 2022)
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%5Fsection">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 <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

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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei354-(4-fluorophenyl)-1-methyl-5-(2-{[(1s)-1-phenylethyl]amino}pyrimidin-4-yl)-2-piperidin-4-yl-1,2-dihydro-3H-pyrazol-3-one; inhibitorCombined sources1
Binding sitei534-(4-fluorophenyl)-1-methyl-5-(2-{[(1s)-1-phenylethyl]amino}pyrimidin-4-yl)-2-piperidin-4-yl-1,2-dihydro-3H-pyrazol-3-one; inhibitorCombined sources1
Binding sitei53ATPPROSITE-ProRule annotation1
Binding sitei1094-(4-fluorophenyl)-1-methyl-5-(2-{[(1s)-1-phenylethyl]amino}pyrimidin-4-yl)-2-piperidin-4-yl-1,2-dihydro-3H-pyrazol-3-one; inhibitor; via amide nitrogen and carbonyl oxygenCombined sources1
<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 sitei168Proton acceptorPROSITE-ProRule annotation1
Binding sitei1684-(4-fluorophenyl)-1-methyl-5-(2-{[(1s)-1-phenylethyl]amino}pyrimidin-4-yl)-2-piperidin-4-yl-1,2-dihydro-3H-pyrazol-3-one; inhibitorCombined sources1

Regions

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

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BRENDAi
2.7.11.24, 3474

Reactome - a knowledgebase of biological pathways and processes

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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-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-525793, Myogenesis
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

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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%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:
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%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:Mapk14
Synonyms:Crk1, Csbp1, Csbp2
<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 17

Organism-specific databases

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

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MGIi
MGI:1346865, Mapk14

Eukaryotic Pathogen, Vector and Host Database Resources

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VEuPathDBi
HostDB:ENSMUSG00000053436

<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

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%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi180T → A: Phosphorylation blocked. 1 Publication1
Mutagenesisi182Y → F: Phosphorylation blocked. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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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%5Fprocessing%5Fsection">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 or proteolytic cleavage.<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%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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

The CPTAC Assay portal

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CPTACi
non-CPTAC-3479

Encyclopedia of Proteome Dynamics

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EPDi
P47811

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P47811

MaxQB - The MaxQuant DataBase

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MaxQBi
P47811

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

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PaxDbi
P47811

PeptideAtlas

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PeptideAtlasi
P47811

PRoteomics IDEntifications database

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PRIDEi
P47811

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
295631 [P47811-1]
295632 [P47811-2]
295633 [P47811-3]
295634 [P47811-4]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P47811

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

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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

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Bgeei
ENSMUSG00000053436, Expressed in granulocyte and 319 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P47811, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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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%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of 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%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

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GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
204969, 180 interactors

Database of interacting proteins

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DIPi
DIP-31073N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P47811

Protein interaction database and analysis system

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IntActi
P47811, 27 interactors

Molecular INTeraction database

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MINTi
P47811

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000004990

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P47811

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
P47811, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

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

3D structure databases

Biological Magnetic Resonance Data Bank

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BMRBi
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...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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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%5Fand%5Fdomains%5Fsection">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

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

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eggNOGi
KOG0660, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000155325

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P47811

Identification of Orthologs from Complete Genome Data

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OMAi
YTDLNPV

Database of Orthologous Groups

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OrthoDBi
683132at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P47811

TreeFam database of animal gene trees

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TreeFami
TF105100

Family and domain databases

Conserved Domains Database

More...
CDDi
cd07877, STKc_p38alpha, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...
IDEALi
IID50045

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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)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.

<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 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 3 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 <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
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 3 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>
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]

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]

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
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[»]
5R8UX-ray1.48A1-360[»]
5R8VX-ray1.48A1-360[»]
5R8WX-ray1.50A1-360[»]
5R8XX-ray1.73A1-360[»]
5R8YX-ray1.68A1-360[»]
5R8ZX-ray1.65A1-360[»]
5R90X-ray1.62A1-360[»]
5R91X-ray1.73A1-360[»]
5R92X-ray1.66A1-360[»]
5R93X-ray1.49A1-360[»]
5R94X-ray1.45A1-360[»]
5R95X-ray1.59A1-360[»]
5R96X-ray1.77A1-360[»]
5R97X-ray1.44A1-360[»]
5R98X-ray1.68A1-360[»]
5R99X-ray1.89A1-360[»]
5R9AX-ray1.53A1-360[»]
5R9BX-ray1.66A1-360[»]
5R9CX-ray1.74A1-360[»]
5R9DX-ray1.69A1-360[»]
5R9EX-ray1.77A1-360[»]
5R9FX-ray1.99A1-360[»]
5R9GX-ray1.73A1-360[»]
5R9HX-ray1.49A1-360[»]
5R9IX-ray1.81A1-360[»]
5R9JX-ray1.52A1-360[»]
5R9KX-ray1.50A1-360[»]
5R9LX-ray1.47A1-360[»]
5R9MX-ray1.81A1-360[»]
5R9NX-ray1.69A1-360[»]
5R9OX-ray1.60A1-360[»]
5R9PX-ray1.72A1-360[»]
5R9QX-ray1.65A1-360[»]
5R9RX-ray1.76A1-360[»]
5R9SX-ray1.70A1-360[»]
5R9TX-ray1.80A1-360[»]
5R9UX-ray1.67A1-360[»]
5R9VX-ray1.45A1-360[»]
5R9WX-ray1.89A1-360[»]
5R9XX-ray1.72A1-360[»]
5R9YX-ray1.57A1-360[»]
5R9ZX-ray1.66A1-360[»]
5RA0X-ray1.91A1-360[»]
5RA1X-ray1.61A1-360[»]
5RA2X-ray1.57A1-360[»]
5RA3X-ray1.57A1-360[»]
5RA4X-ray1.59A1-360[»]
5RA5X-ray1.54A1-360[»]
5RA6X-ray1.86A1-360[»]
5RA7X-ray1.92A1-360[»]
5RA8X-ray1.78A1-360[»]
5RA9X-ray1.68A1-360[»]
5UOJX-ray2.10A1-360[»]
6SO1X-ray1.66A1-360[»]
6SO2X-ray1.60A1-360[»]
6SO4X-ray1.51A1-360[»]
6SODX-ray1.87A1-360[»]
6SOIX-ray1.55A1-359[»]
6SOTX-ray1.54A1-360[»]
6SOUX-ray1.50A1-360[»]
6SOVX-ray1.31A1-360[»]
6SP9X-ray1.22A1-360[»]
6SPLX-ray1.38A1-360[»]
6Y4TX-ray1.98A1-360[»]
6Y4UX-ray1.86A1-360[»]
6Y4VX-ray1.75A1-360[»]
6Y4WX-ray1.86A1-360[»]
6Y4XX-ray1.60A1-360[»]
6Y6VX-ray2.10A1-360[»]
6Y7WX-ray1.39A1-360[»]
6Y7XX-ray1.45A1-360[»]
6Y7YX-ray1.51A1-360[»]
6Y7ZX-ray1.35A1-360[»]
6Y80X-ray1.24A1-360[»]
6Y81X-ray1.54A1-360[»]
6Y82X-ray1.44A1-360[»]
6Y85X-ray1.58A1-360[»]
6Y8HX-ray1.37A1-360[»]
6YCUX-ray1.35A1-360[»]
6YCWX-ray1.34A1-360[»]
6YJCX-ray1.74A1-360[»]
6YK7X-ray1.90A1-360[»]
6ZWRX-ray1.90A1-360[»]
7BDOX-ray2.70A1-360[»]
7BDQX-ray2.75A1-360[»]
7BE4X-ray2.10A1-360[»]
7BE5X-ray1.80A1-360[»]
BMRBiP47811
SMRiP47811
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi204969, 180 interactors
DIPiDIP-31073N
ELMiP47811
IntActiP47811, 27 interactors
MINTiP47811
STRINGi10090.ENSMUSP00000004990

Chemistry databases

BindingDBiP47811
ChEMBLiCHEMBL2336

PTM databases

iPTMnetiP47811
PhosphoSitePlusiP47811

Proteomic databases

CPTACinon-CPTAC-3479
EPDiP47811
jPOSTiP47811
MaxQBiP47811
PaxDbiP47811
PeptideAtlasiP47811
PRIDEiP47811
ProteomicsDBi295631 [P47811-1]
295632 [P47811-2]
295633 [P47811-3]
295634 [P47811-4]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
4142, 2283 antibodies from 53 providers

The DNASU plasmid repository

More...
DNASUi
26416

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
VEuPathDBiHostDB:ENSMUSG00000053436

Phylogenomic databases

eggNOGiKOG0660, Eukaryota
GeneTreeiENSGT00940000155325
InParanoidiP47811
OMAiYTDLNPV
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-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-525793, Myogenesis
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

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
26416, 8 hits in 66 CRISPR screens

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
RNActiP47811, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000053436, Expressed in granulocyte and 319 other tissues
ExpressionAtlasiP47811, baseline and differential
GenevisibleiP47811, MM

Family and domain databases

CDDicd07877, STKc_p38alpha, 1 hit
IDEALiIID50045
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

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 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%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, 1996
Last sequence update: January 23, 2007
Last modified: February 23, 2022
This is version 229 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, Direct protein sequencing, Reference proteome

Documents

  1. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
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