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Protein

Mitogen-activated protein kinase 14

Gene

MAPK14

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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. Isoform MXI2 activation is stimulated by mitogens and oxidative stress and only poorly phosphorylates ELK1 and ATF2. Isoform EXIP may play a role in the early onset of apoptosis. Phosphorylates S100A9 at 'Thr-113'.16 Publications
(Microbial infection) Activated by phosphorylation by M.tuberculosis EsxA in T-cells leading to inhibition of IFN-gamma production; phosphorylation is apparent within 15 minute and is inhibited by kinase-specific inhibitors SB203580 and siRNA (PubMed:21586573).1 Publication

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

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

Mg2+1 Publication

<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). Isoform Mxi2 is 100-fold less sensitive to these agents than the other isoforms and is not inhibited by DUSP1. Isoform Exip is not activated by MAP2K6. SB203580 is an inhibitor of MAPK14.18 Publications

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 sitei35Inhibitor3 Publications1
Binding sitei53ATP1
Binding sitei53Inhibitor3 Publications1
Binding sitei71Inhibitor3 Publications1
Binding sitei109Inhibitor; via amide nitrogen and carbonyl oxygen3 Publications1
Binding sitei154Inhibitor; via carbonyl oxygen3 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 acceptor1
Binding sitei168Inhibitor; via amide nitrogen and carbonyl oxygen3 Publications1
Binding sitei197Inhibitor3 Publications1
Binding sitei252Inhibitor; via amide nitrogen3 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 – 38ATP9

<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

  • ATP binding Source: UniProtKB-KW
  • enzyme binding Source: BHF-UCL
  • MAP kinase activity Source: UniProtKB
  • MAP kinase kinase activity Source: ProtInc
  • mitogen-activated protein kinase p38 binding Source: UniProtKB
  • NFAT protein binding Source: BHF-UCL
  • protein phosphatase binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: Reactome

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

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS03507-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.7.11.24 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-168638 NOD1/2 Signaling Pathway
R-HSA-171007 p38MAPK events
R-HSA-198753 ERK/MAPK targets
R-HSA-2151209 Activation of PPARGC1A (PGC-1alpha) by phosphorylation
R-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-375170 CDO in myogenesis
R-HSA-376172 DSCAM interactions
R-HSA-418592 ADP signalling through P2Y purinoceptor 1
R-HSA-432142 Platelet sensitization by LDL
R-HSA-4420097 VEGFA-VEGFR2 Pathway
R-HSA-450302 activated TAK1 mediates p38 MAPK activation
R-HSA-450341 Activation of the AP-1 family of transcription factors
R-HSA-450604 KSRP (KHSRP) binds and destabilizes mRNA
R-HSA-6798695 Neutrophil degranulation
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q16539

SIGNOR Signaling Network Open Resource

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SIGNORi
Q16539

<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:2.7.11.243 Publications)
Short name:
MAP kinase 14
Short name:
MAPK 14
Alternative name(s):
Cytokine suppressive anti-inflammatory drug-binding protein
Short name:
CSAID-binding protein
Short name:
CSBP
MAP kinase MXI2
MAX-interacting protein 2
Mitogen-activated protein kinase p38 alpha
Short name:
MAP kinase p38 alpha
Stress-activated protein kinase 2a
Short name:
SAPK2a
<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:CSBP, CSBP1, CSBP2, CSPB1, MXI2, SAPK2A
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000112062.10

Human Gene Nomenclature Database

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HGNCi
HGNC:6876 MAPK14

Online Mendelian Inheritance in Man (OMIM)

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MIMi
600289 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q16539

<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>Mutagenesisi34A → V: Lowered kinase activity. 1 Publication1
Mutagenesisi53K → R: Loss of kinase activity. 1 Publication1
Mutagenesisi54K → R: Impairs MAP2K6/MKK6-dependent autophosphorylation. 1 Publication1
Mutagenesisi69Y → H: Lowered kinase activity. 1 Publication1
Mutagenesisi168D → A: Loss of kinase activity. 1 Publication1
Mutagenesisi175T → A: No effect on either the kinase activity or tyrosine phosphorylation. 1 Publication1
Mutagenesisi176D → A: Emulation of the active state. Increase in activity; when associated with S-327 or L-327. 1 Publication1
Mutagenesisi177D → A: Loss of kinase activity. 1 Publication1
Mutagenesisi180T → E: Loss of kinase activity. 1 Publication1
Mutagenesisi182Y → F: Loss of kinase activity. 1 Publication1
Mutagenesisi320A → T: Lowered kinase activity. 1 Publication1
Mutagenesisi327F → L: Emulation of the active state. Increase in activity; when associated with A-176. 1 Publication1
Mutagenesisi327F → S: Emulation of the active state. Increase in activity; when associated with A-176. 1 Publication1
Mutagenesisi337W → R: Loss of kinase activity. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
1432

Open Targets

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OpenTargetsi
ENSG00000112062

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA30621

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL260

Drug and drug target database

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DrugBanki
DB02277 1-(5-Tert-Butyl-2-Methyl-2h-Pyrazol-3-Yl)-3-(4-Chloro-Phenyl)-Urea
DB03044 1-(5-Tert-Butyl-2-P-Tolyl-2h-Pyrazol-3-Yl)-3-[4-(2-Morpholin-4-Yl-Ethoxy)-Naphthalen-1-Yl]-Urea
DB06882 1-[1-(3-aminophenyl)-3-tert-butyl-1H-pyrazol-5-yl]-3-naphthalen-1-ylurea
DB08395 2-(ETHOXYMETHYL)-4-(4-FLUOROPHENYL)-3-[2-(2-HYDROXYPHENOXY)PYRIMIDIN-4-YL]ISOXAZOL-5(2H)-ONE
DB03110 2-Chlorophenol
DB07942 2-fluoro-4-[4-(4-fluorophenyl)-1H-pyrazol-3-yl]pyridine
DB07943 2-{4-[5-(4-chlorophenyl)-4-pyrimidin-4-yl-1H-pyrazol-3-yl]piperidin-1-yl}-2-oxoethanol
DB08093 3-(1-NAPHTHYLMETHOXY)PYRIDIN-2-AMINE
DB02352 3-(Benzyloxy)Pyridin-2-Amine
DB08730 3-FLUORO-5-MORPHOLIN-4-YL-N-[1-(2-PYRIDIN-4-YLETHYL)-1H-INDOL-6-YL]BENZAMIDE
DB08091 3-FLUORO-5-MORPHOLIN-4-YL-N-[3-(2-PYRIDIN-4-YLETHYL)-1H-INDOL-5-YL]BENZAMIDE
DB08092 3-fluoro-N-1H-indol-5-yl-5-morpholin-4-ylbenzamide
DB04632 4-(2-HYDROXYBENZYLAMINO)-N-(3-(4-FLUOROPHENOXY)PHENYL)PIPERIDINE-1-SULFONAMIDE
DB08522 4-(4-FLUOROPHENYL)-1-CYCLOROPROPYLMETHYL-5-(4-PYRIDYL)-IMIDAZOLE
DB03980 4-(Fluorophenyl)-1-Cyclopropylmethyl-5-(2-Amino-4-Pyrimidinyl)Imidazole
DB07829 4-[3-(4-FLUOROPHENYL)-1H-PYRAZOL-4-YL]PYRIDINE
DB07607 4-[5-(3-IODO-PHENYL)-2-(4-METHANESULFINYL-PHENYL)-1H-IMIDAZOL-4-YL]-PYRIDINE
DB08521 4-[5-(4-FLUORO-PHENYL)-2-(4-METHANESULFINYL-PHENYL)-3H-IMIDAZOL-4-YL]-PYRIDINE
DB01761 4-[5-[2-(1-Phenyl-Ethylamino)-Pyrimidin-4-Yl]-1-Methyl-4-(3-Trifluoromethylphenyl)-1h-Imidazol-2-Yl]-Piperidine
DB07459 4-PHENOXY-N-(PYRIDIN-2-YLMETHYL)BENZAMIDE
DB01988 6((S)-3-Benzylpiperazin-1-Yl)-3-(Naphthalen-2-Yl)-4-(Pyridin-4-Yl)Pyrazine
DB08423 [5-AMINO-1-(4-FLUOROPHENYL)-1H-PYRAZOL-4-YL][3-(PIPERIDIN-4-YLOXY)PHENYL]METHANONE
DB01953 Inhibitor of P38 Kinase
DB05157 KC706
DB08064 N-(3-TERT-BUTYL-1H-PYRAZOL-5-YL)-N'-{4-CHLORO-3-[(PYRIDIN-3-YLOXY)METHYL]PHENYL}UREA
DB08068 N-[4-CHLORO-3-(PYRIDIN-3-YLOXYMETHYL)-PHENYL]-3-FLUORO-
DB07307 N-cyclopropyl-4-methyl-3-[1-(2-methylphenyl)phthalazin-6-yl]benzamide
DB08351 N-cyclopropyl-4-methyl-3-{2-[(2-morpholin-4-ylethyl)amino]quinazolin-6-yl}benzamide
DB04338 SB220025
DB05412 SCIO-469
DB04797 Triazolopyridine
DB05470 VX-702

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1499

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
MAPK14

<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 methionineiRemovedCombined sources1 Publication
<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_00001862912 – 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-acetylserineCombined sources1
Modified residuei2PhosphoserineCombined sources1
Modified residuei16PhosphothreonineCombined sources1
Modified residuei53N6-acetyllysine1 Publication1
Modified residuei152N6-acetyllysine1 Publication1
Modified residuei180Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and autocatalysisCombined sources1 Publication1
Modified residuei182Phosphotyrosine; by MAP2K3, MAP2K4, MAP2K6 and autocatalysisCombined sources1 Publication1
Modified residuei263PhosphothreonineCombined sources1
Modified residuei323Phosphotyrosine; by ZAP701 Publication1

<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 citokines, 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 (PubMed:21283629).6 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 HDAC3.1 Publication
Ubiquitinated. Ubiquitination leads to degradation by the proteasome pathway.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q16539

MaxQB - The MaxQuant DataBase

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MaxQBi
Q16539

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

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PaxDbi
Q16539

PeptideAtlas

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PeptideAtlasi
Q16539

PRoteomics IDEntifications database

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PRIDEi
Q16539

ProteomicsDB human proteome resource

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ProteomicsDBi
60901
60902 [Q16539-2]
60903 [Q16539-3]
60904 [Q16539-4]

2D gel databases

USC-OGP 2-DE database

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OGPi
Q16539

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q16539

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

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PhosphoSitePlusi
Q16539

<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

Brain, heart, placenta, pancreas and skeletal muscle. Expressed to a lesser extent in lung, liver and kidney.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000112062 Expressed in 228 organ(s), highest expression level in blood

CleanEx database of gene expression profiles

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CleanExi
HS_MAPK14

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q16539 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q16539 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB010285
CAB040578
HPA051825

<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 (PubMed:21224381). 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 (PubMed:21283629).By similarity18 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)

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BioGridi
107819, 233 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q16539

Database of interacting proteins

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DIPi
DIP-30987N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
Q16539

Protein interaction database and analysis system

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IntActi
Q16539, 104 interactors

Molecular INTeraction database

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MINTi
Q16539

STRING: functional protein association networks

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STRINGi
9606.ENSP00000229794

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q16539

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q16539

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

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SMRi
Q16539

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q16539

<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>Regioni70 – 71Inhibitor-binding2
Regioni106 – 110Inhibitor-binding5
Regioni168 – 169Inhibitor-binding2

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
ENOG410XNY0 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155325

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000233024

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG014652

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q16539

KEGG Orthology (KO)

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KOi
K04441

Identification of Orthologs from Complete Genome Data

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OMAi
EITNRYT

Database of Orthologous Groups

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OrthoDBi
EOG091G08QL

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q16539

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

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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 (5+)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 5 <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 5 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform CSBP2 (identifier: Q16539-1) [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 AFDTKTGLRV
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 SLTQMPKMNF ANVFIGANPL AVDLLEKMLV LDSDKRITAA
310 320 330 340 350
QALAHAYFAQ YHDPDDEPVA DPYDQSFESR DLLIDEWKSL TYDEVISFVP
360
PPLDQEEMES
Length:360
Mass (Da):41,293
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:i286C81D0487618B3
GO
Isoform CSBP1 (identifier: Q16539-2) [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):41,493
Checksum:i062EBC3E56683D14
GO
Isoform Mxi2 (identifier: Q16539-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     281-360: AVDLLEKMLV...PPLDQEEMES → GKLTIYPHLMDIELVMI

Show »
Length:297
Mass (Da):34,092
Checksum:iC17A753943B49F56
GO
Isoform Exip (identifier: Q16539-4) [UniParc]FASTAAdd to basket
Also known as: Exon skip

The sequence of this isoform differs from the canonical sequence as follows:
     255-307: ARNYIQSLTQ...TAAQALAHAY → LSTCWRRCLY...ISPLKAGTSL
     308-360: Missing.

Show »
Length:307
Mass (Da):35,453
Checksum:i9297934FF4AC6F94
GO
Isoform 5 (identifier: Q16539-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     255-360: ARNYIQSLTQ...PPLDQEEMES → VS

Show »
Length:256
Mass (Da):29,388
Checksum:i847356DB686D6E5B
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
B4E0K5B4E0K5_HUMAN
Mitogen-activated protein kinase
MAPK14
283Annotation 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>
B5TY33B5TY33_HUMAN
Mitogen-activated protein kinase
MAPK14
173Annotation 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>
E7EX54E7EX54_HUMAN
Mitogen-activated protein kinase 14
MAPK14
132Annotation 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>
H7C4E2H7C4E2_HUMAN
Mitogen-activated protein kinase 14
MAPK14
90Annotation 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 conflicti67R → G in BAF84398 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_04227051A → V in a gastric adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042271322P → R in a lung adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042272343D → G1 PublicationCorresponds to variant dbSNP:rs45496794Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_004842230 – 254DQLKL…ISSES → NQLQQIMRLTGTPPAYLINR MPSHE in isoform CSBP1. 1 PublicationAdd BLAST25
Alternative sequenceiVSP_057194255 – 360ARNYI…EEMES → VS in isoform 5. 1 PublicationAdd BLAST106
Alternative sequenceiVSP_004843255 – 307ARNYI…LAHAY → LSTCWRRCLYWTQIRELQRP KPLHMPTLLSTTILMMNQWP ILMISPLKAGTSL in isoform Exip. 1 PublicationAdd BLAST53
Alternative sequenceiVSP_004844281 – 360AVDLL…EEMES → GKLTIYPHLMDIELVMI in isoform Mxi2. 1 PublicationAdd BLAST80
Alternative sequenceiVSP_004845308 – 360Missing in isoform Exip. 1 PublicationAdd BLAST53

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
L35263 mRNA Translation: AAA57455.1
L35264 mRNA Translation: AAA57456.1
L35253 mRNA Translation: AAA74301.1
U19775 mRNA Translation: AAC50329.1
AF100544 mRNA Translation: AAF36770.1
AB074150 mRNA Translation: BAB85654.1
FJ032367 mRNA Translation: ACI00233.1
AK291709 mRNA Translation: BAF84398.1
BT006933 mRNA Translation: AAP35579.1
CR536505 mRNA Translation: CAG38743.1
EU332860 Genomic DNA Translation: ABY87549.1
Z95152 Genomic DNA No translation available.
CH471081 Genomic DNA Translation: EAX03869.1
BC000092 mRNA Translation: AAH00092.1
BC031574 mRNA Translation: AAH31574.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS4815.1 [Q16539-2]
CCDS4816.1 [Q16539-1]
CCDS4817.1 [Q16539-4]

Protein sequence database of the Protein Information Resource

More...
PIRi
S53536

NCBI Reference Sequences

More...
RefSeqi
NP_001306.1, NM_001315.2 [Q16539-2]
NP_620581.1, NM_139012.2 [Q16539-1]
NP_620582.1, NM_139013.2 [Q16539-3]
NP_620583.1, NM_139014.2 [Q16539-4]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.485233

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000229794; ENSP00000229794; ENSG00000112062 [Q16539-1]
ENST00000229795; ENSP00000229795; ENSG00000112062 [Q16539-2]
ENST00000310795; ENSP00000308669; ENSG00000112062 [Q16539-4]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1432

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:1432

UCSC genome browser

More...
UCSCi
uc003olp.4 human [Q16539-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

P38 mitogen-activated protein kinases entry

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35263 mRNA Translation: AAA57455.1
L35264 mRNA Translation: AAA57456.1
L35253 mRNA Translation: AAA74301.1
U19775 mRNA Translation: AAC50329.1
AF100544 mRNA Translation: AAF36770.1
AB074150 mRNA Translation: BAB85654.1
FJ032367 mRNA Translation: ACI00233.1
AK291709 mRNA Translation: BAF84398.1
BT006933 mRNA Translation: AAP35579.1
CR536505 mRNA Translation: CAG38743.1
EU332860 Genomic DNA Translation: ABY87549.1
Z95152 Genomic DNA No translation available.
CH471081 Genomic DNA Translation: EAX03869.1
BC000092 mRNA Translation: AAH00092.1
BC031574 mRNA Translation: AAH31574.1
CCDSiCCDS4815.1 [Q16539-2]
CCDS4816.1 [Q16539-1]
CCDS4817.1 [Q16539-4]
PIRiS53536
RefSeqiNP_001306.1, NM_001315.2 [Q16539-2]
NP_620581.1, NM_139012.2 [Q16539-1]
NP_620582.1, NM_139013.2 [Q16539-3]
NP_620583.1, NM_139014.2 [Q16539-4]
UniGeneiHs.485233

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
1A9UX-ray2.50A1-360[»]
1BL6X-ray2.50A1-360[»]
1BL7X-ray2.50A1-360[»]
1BMKX-ray2.40A1-360[»]
1DI9X-ray2.60A1-360[»]
1IANX-ray2.00A2-360[»]
1KV1X-ray2.50A1-360[»]
1KV2X-ray2.80A1-360[»]
1M7QX-ray2.40A1-360[»]
1OUKX-ray2.50A1-360[»]
1OUYX-ray2.50A1-360[»]
1OVEX-ray2.10A1-360[»]
1OZ1X-ray2.10A1-360[»]
1R39X-ray2.30A1-360[»]
1R3CX-ray2.00A1-360[»]
1W7HX-ray2.21A2-360[»]
1W82X-ray2.20A2-360[»]
1W83X-ray2.50A2-360[»]
1W84X-ray2.20A2-360[»]
1WBNX-ray2.40A2-360[»]
1WBOX-ray2.16A2-360[»]
1WBSX-ray1.80A2-360[»]
1WBTX-ray2.00A2-360[»]
1WBVX-ray2.00A2-360[»]
1WBWX-ray2.41A2-360[»]
1WFCX-ray2.30A1-360[»]
1YQJX-ray2.00A2-360[»]
1ZYJX-ray2.00A1-360[»]
1ZZ2X-ray2.00A1-360[»]
1ZZLX-ray2.00A4-354[»]
2BAJX-ray2.25A2-360[»]
2BAKX-ray2.20A2-360[»]
2BALX-ray2.10A2-360[»]
2BAQX-ray2.80A2-360[»]
2FSLX-ray1.70X2-360[»]
2FSMX-ray1.86X2-360[»]
2FSOX-ray1.83X2-360[»]
2FSTX-ray1.45X2-360[»]
2GFSX-ray1.75A2-360[»]
2I0HX-ray2.00A1-360[»]
2LGCNMR-A2-354[»]
2NPQX-ray1.80A2-360[»]
2OKRX-ray2.00A/D2-360[»]
2ONLX-ray4.00A/B2-360[»]
2QD9X-ray1.70A2-360[»]
2RG5X-ray2.40A2-360[»]
2RG6X-ray1.72A2-360[»]
2Y8OX-ray1.95A1-360[»]
2YISX-ray2.00A2-360[»]
2YIWX-ray2.00A2-360[»]
2YIXX-ray2.30A4-354[»]
2ZAZX-ray1.80A1-360[»]
2ZB0X-ray2.10A1-360[»]
2ZB1X-ray2.50A1-360[»]
3BV2X-ray2.40A2-360[»]
3BV3X-ray2.59A2-360[»]
3BX5X-ray2.40A2-360[»]
3C5UX-ray2.80A2-360[»]
3CTQX-ray1.95A5-352[»]
3D7ZX-ray2.10A1-360[»]
3D83X-ray1.90A1-360[»]
3DS6X-ray2.90A/B/C/D1-360[»]
3DT1X-ray2.80A1-360[»]
3E92X-ray2.00A1-360[»]
3E93X-ray2.00A1-360[»]
3FC1X-ray2.40X1-360[»]
3FI4X-ray2.20A1-360[»]
3FKLX-ray2.00A1-360[»]
3FKNX-ray2.00A1-360[»]
3FKOX-ray2.00A1-360[»]
3FL4X-ray1.80A1-360[»]
3FLNX-ray1.90C1-360[»]
3FLQX-ray1.90A1-360[»]
3FLSX-ray2.30A1-360[»]
3FLWX-ray2.10A1-360[»]
3FLYX-ray1.80A1-360[»]
3FLZX-ray2.23A1-360[»]
3FMHX-ray1.90A1-360[»]
3FMJX-ray2.00A1-360[»]
3FMKX-ray1.70A1-360[»]
3FMLX-ray2.10A1-360[»]
3FMMX-ray2.00A1-360[»]
3FMNX-ray1.90A1-360[»]
3FSFX-ray2.10A1-360[»]
3FSKX-ray2.00A1-360[»]
3GC7X-ray1.80A1-360[»]
3GCPX-ray2.25A2-360[»]
3GCQX-ray2.00A2-360[»]
3GCSX-ray2.10A2-360[»]
3GCUX-ray2.10A/B2-360[»]
3GCVX-ray2.30A2-360[»]
3GFEX-ray2.10A1-360[»]
3GI3X-ray2.40A1-360[»]
3HA8X-ray2.48A1-360[»]
3HECX-ray2.50A5-352[»]
3HEGX-ray2.20A5-352[»]
3HL7X-ray1.88A1-360[»]
3HLLX-ray1.95A1-360[»]
3HP2X-ray2.15A1-360[»]
3HP5X-ray2.30A1-360[»]
3HRBX-ray2.20A2-360[»]
3HUBX-ray2.25A2-360[»]
3HUCX-ray1.80A2-360[»]
3HV3X-ray2.00A2-360[»]
3HV4X-ray2.60A/B2-360[»]
3HV5X-ray2.25A/B2-360[»]
3HV6X-ray1.95A2-360[»]
3HV7X-ray2.40A2-360[»]
3HVCX-ray2.10A1-360[»]
3IPHX-ray2.10A1-360[»]
3ITZX-ray2.25A1-360[»]
3IW5X-ray2.50A2-360[»]
3IW6X-ray2.10A2-360[»]
3IW7X-ray2.40A2-360[»]
3IW8X-ray2.00A2-360[»]
3K3IX-ray1.70A5-352[»]
3K3JX-ray2.00A1-360[»]
3KF7X-ray2.00A1-360[»]
3KQ7X-ray1.80A1-360[»]
3L8SX-ray2.35A2-360[»]
3L8XX-ray2.15A2-360[»]
3LFAX-ray2.10A2-360[»]
3LFBX-ray2.60A2-360[»]
3LFCX-ray2.80A2-360[»]
3LFDX-ray3.40A2-360[»]
3LFEX-ray2.30A2-360[»]
3LFFX-ray1.50A2-360[»]
3LHJX-ray3.31A1-360[»]
3MGYX-ray2.10A1-360[»]
3MH0X-ray2.00A1-360[»]
3MH1X-ray2.20A1-360[»]
3MH2X-ray2.30A1-360[»]
3MH3X-ray2.20A1-360[»]
3MPAX-ray2.10A1-360[»]
3MPTX-ray1.89A1-360[»]
3MVLX-ray2.80A/B2-360[»]
3MVMX-ray2.00A/B2-360[»]
3MW1X-ray2.80A2-360[»]
3NEWX-ray2.51A1-360[»]
3NNUX-ray2.40A1-354[»]
3NNVX-ray2.10A1-354[»]
3NNWX-ray1.89A1-354[»]
3NNXX-ray2.28A1-354[»]
3NWWX-ray2.09A2-360[»]
3O8PX-ray2.10A1-360[»]
3O8TX-ray2.00A1-360[»]
3O8UX-ray2.10A1-360[»]
3OBGX-ray2.80A1-360[»]
3OBJX-ray2.40A1-360[»]
3OC1X-ray2.59A1-360[»]
3OCGX-ray2.21A2-360[»]
3OD6X-ray2.68X1-360[»]
3ODYX-ray2.20X1-360[»]
3ODZX-ray2.30X1-360[»]
3OEFX-ray1.60X1-360[»]
3PG3X-ray2.00A2-360[»]
3QUDX-ray2.00A2-360[»]
3QUEX-ray2.70A2-360[»]
3RINX-ray2.20A1-360[»]
3ROCX-ray1.70A1-360[»]
3S3IX-ray1.80A4-352[»]
3S4QX-ray2.27A2-360[»]
3U8WX-ray2.15A1-360[»]
3UVPX-ray2.40A2-360[»]
3UVQX-ray2.20A2-360[»]
3UVRX-ray2.10A2-360[»]
3ZS5X-ray1.60A2-360[»]
3ZSGX-ray1.89A2-360[»]
3ZSHX-ray2.05A2-360[»]
3ZSIX-ray2.40A2-360[»]
3ZYAX-ray1.90A1-360[»]
4A9YX-ray2.20A2-360[»]
4AA0X-ray1.80A2-360[»]
4AA4X-ray2.30A2-360[»]
4AA5X-ray2.38A2-360[»]
4AACX-ray2.50A2-360[»]
4DLIX-ray1.91A2-360[»]
4DLJX-ray2.60A2-360[»]
4E5AX-ray1.87X1-360[»]
4E5BX-ray2.00A1-360[»]
4E6AX-ray2.09A1-360[»]
4E6CX-ray2.39A1-360[»]
4E8AX-ray2.70A1-360[»]
4EH2X-ray2.00A2-360[»]
4EH3X-ray2.40A2-360[»]
4EH4X-ray2.50A2-360[»]
4EH5X-ray2.00A2-360[»]
4EH6X-ray2.10A2-360[»]
4EH7X-ray2.10A2-360[»]
4EH8X-ray2.20A2-360[»]
4EH9X-ray2.10A2-360[»]
4EHVX-ray1.60A2-360[»]
4EWQX-ray2.10A2-360[»]
4F9WX-ray2.00A2-360[»]
4F9YX-ray1.85A2-360[»]
4FA2X-ray2.00A2-360[»]
4GEOX-ray1.66A2-360[»]
4KINX-ray1.97A/B/C/D2-360[»]
4KIPX-ray2.27A/B2-360[»]
4KIQX-ray2.50A/B/C/D2-360[»]
4L8MX-ray2.10A2-360[»]
4R3CX-ray2.06A2-360[»]
4ZTHX-ray2.15A2-360[»]
5ETAX-ray2.80A/B1-360[»]
5ETCX-ray2.42A1-360[»]
5ETFX-ray2.40A1-360[»]
5ETIX-ray2.80A1-360[»]
5ML5X-ray1.90A1-360[»]
5MTXX-ray1.80A1-360[»]
5MTYX-ray2.31A1-360[»]
5MZ3X-ray2.15A1-360[»]
5N63X-ray2.40A1-360[»]
5N64X-ray2.40A1-360[»]
5N65X-ray2.00A1-360[»]
5N66X-ray2.40A1-360[»]
5N67X-ray1.90A1-360[»]
5N68X-ray1.85A1-360[»]
5O8UX-ray2.00A1-360[»]
5O8VX-ray2.00A1-360[»]
5TBEX-ray2.44A1-360[»]
5TCOX-ray2.10A2-360[»]
5WJJX-ray1.60A1-360[»]
5XYXX-ray2.61A1-360[»]
5XYYX-ray1.70A1-360[»]
6ANLX-ray2.00A1-360[»]
ProteinModelPortaliQ16539
SMRiQ16539
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107819, 233 interactors
CORUMiQ16539
DIPiDIP-30987N
ELMiQ16539
IntActiQ16539, 104 interactors
MINTiQ16539
STRINGi9606.ENSP00000229794

Chemistry databases

BindingDBiQ16539
ChEMBLiCHEMBL260
DrugBankiDB02277 1-(5-Tert-Butyl-2-Methyl-2h-Pyrazol-3-Yl)-3-(4-Chloro-Phenyl)-Urea
DB03044 1-(5-Tert-Butyl-2-P-Tolyl-2h-Pyrazol-3-Yl)-3-[4-(2-Morpholin-4-Yl-Ethoxy)-Naphthalen-1-Yl]-Urea
DB06882 1-[1-(3-aminophenyl)-3-tert-butyl-1H-pyrazol-5-yl]-3-naphthalen-1-ylurea
DB08395 2-(ETHOXYMETHYL)-4-(4-FLUOROPHENYL)-3-[2-(2-HYDROXYPHENOXY)PYRIMIDIN-4-YL]ISOXAZOL-5(2H)-ONE
DB03110 2-Chlorophenol
DB07942 2-fluoro-4-[4-(4-fluorophenyl)-1H-pyrazol-3-yl]pyridine
DB07943 2-{4-[5-(4-chlorophenyl)-4-pyrimidin-4-yl-1H-pyrazol-3-yl]piperidin-1-yl}-2-oxoethanol
DB08093 3-(1-NAPHTHYLMETHOXY)PYRIDIN-2-AMINE
DB02352 3-(Benzyloxy)Pyridin-2-Amine
DB08730 3-FLUORO-5-MORPHOLIN-4-YL-N-[1-(2-PYRIDIN-4-YLETHYL)-1H-INDOL-6-YL]BENZAMIDE
DB08091 3-FLUORO-5-MORPHOLIN-4-YL-N-[3-(2-PYRIDIN-4-YLETHYL)-1H-INDOL-5-YL]BENZAMIDE
DB08092 3-fluoro-N-1H-indol-5-yl-5-morpholin-4-ylbenzamide
DB04632 4-(2-HYDROXYBENZYLAMINO)-N-(3-(4-FLUOROPHENOXY)PHENYL)PIPERIDINE-1-SULFONAMIDE
DB08522 4-(4-FLUOROPHENYL)-1-CYCLOROPROPYLMETHYL-5-(4-PYRIDYL)-IMIDAZOLE
DB03980 4-(Fluorophenyl)-1-Cyclopropylmethyl-5-(2-Amino-4-Pyrimidinyl)Imidazole
DB07829 4-[3-(4-FLUOROPHENYL)-1H-PYRAZOL-4-YL]PYRIDINE
DB07607 4-[5-(3-IODO-PHENYL)-2-(4-METHANESULFINYL-PHENYL)-1H-IMIDAZOL-4-YL]-PYRIDINE
DB08521 4-[5-(4-FLUORO-PHENYL)-2-(4-METHANESULFINYL-PHENYL)-3H-IMIDAZOL-4-YL]-PYRIDINE
DB01761 4-[5-[2-(1-Phenyl-Ethylamino)-Pyrimidin-4-Yl]-1-Methyl-4-(3-Trifluoromethylphenyl)-1h-Imidazol-2-Yl]-Piperidine
DB07459 4-PHENOXY-N-(PYRIDIN-2-YLMETHYL)BENZAMIDE
DB01988 6((S)-3-Benzylpiperazin-1-Yl)-3-(Naphthalen-2-Yl)-4-(Pyridin-4-Yl)Pyrazine
DB08423 [5-AMINO-1-(4-FLUOROPHENYL)-1H-PYRAZOL-4-YL][3-(PIPERIDIN-4-YLOXY)PHENYL]METHANONE
DB01953 Inhibitor of P38 Kinase
DB05157 KC706
DB08064 N-(3-TERT-BUTYL-1H-PYRAZOL-5-YL)-N'-{4-CHLORO-3-[(PYRIDIN-3-YLOXY)METHYL]PHENYL}UREA
DB08068 N-[4-CHLORO-3-(PYRIDIN-3-YLOXYMETHYL)-PHENYL]-3-FLUORO-
DB07307 N-cyclopropyl-4-methyl-3-[1-(2-methylphenyl)phthalazin-6-yl]benzamide
DB08351 N-cyclopropyl-4-methyl-3-{2-[(2-morpholin-4-ylethyl)amino]quinazolin-6-yl}benzamide
DB04338 SB220025
DB05412 SCIO-469
DB04797 Triazolopyridine
DB05470 VX-702
GuidetoPHARMACOLOGYi1499

PTM databases

iPTMnetiQ16539
PhosphoSitePlusiQ16539

Polymorphism and mutation databases

BioMutaiMAPK14

2D gel databases

OGPiQ16539

Proteomic databases

EPDiQ16539
MaxQBiQ16539
PaxDbiQ16539
PeptideAtlasiQ16539
PRIDEiQ16539
ProteomicsDBi60901
60902 [Q16539-2]
60903 [Q16539-3]
60904 [Q16539-4]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
1432
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000229794; ENSP00000229794; ENSG00000112062 [Q16539-1]
ENST00000229795; ENSP00000229795; ENSG00000112062 [Q16539-2]
ENST00000310795; ENSP00000308669; ENSG00000112062 [Q16539-4]
GeneIDi1432
KEGGihsa:1432
UCSCiuc003olp.4 human [Q16539-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1432
DisGeNETi1432
EuPathDBiHostDB:ENSG00000112062.10

GeneCards: human genes, protein and diseases

More...
GeneCardsi
MAPK14
HGNCiHGNC:6876 MAPK14
HPAiCAB010285
CAB040578
HPA051825
MIMi600289 gene
neXtProtiNX_Q16539
OpenTargetsiENSG00000112062
PharmGKBiPA30621

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0660 Eukaryota
ENOG410XNY0 LUCA
GeneTreeiENSGT00940000155325
HOGENOMiHOG000233024
HOVERGENiHBG014652
InParanoidiQ16539
KOiK04441
OMAiEITNRYT
OrthoDBiEOG091G08QL
PhylomeDBiQ16539
TreeFamiTF105100

Enzyme and pathway databases

BioCyciMetaCyc:HS03507-MONOMER
BRENDAi2.7.11.24 2681
ReactomeiR-HSA-168638 NOD1/2 Signaling Pathway
R-HSA-171007 p38MAPK events
R-HSA-198753 ERK/MAPK targets
R-HSA-2151209 Activation of PPARGC1A (PGC-1alpha) by phosphorylation
R-HSA-2559580 Oxidative Stress Induced Senescence
R-HSA-375170 CDO in myogenesis
R-HSA-376172 DSCAM interactions
R-HSA-418592 ADP signalling through P2Y purinoceptor 1
R-HSA-432142 Platelet sensitization by LDL
R-HSA-4420097 VEGFA-VEGFR2 Pathway
R-HSA-450302 activated TAK1 mediates p38 MAPK activation
R-HSA-450341 Activation of the AP-1 family of transcription factors
R-HSA-450604 KSRP (KHSRP) binds and destabilizes mRNA
R-HSA-6798695 Neutrophil degranulation
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
SignaLinkiQ16539
SIGNORiQ16539

Miscellaneous databases

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

More...
ChiTaRSi
MAPK14 human
EvolutionaryTraceiQ16539

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
MAPK14

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

More...
GenomeRNAii
1432

Protein Ontology

More...
PROi
PR:Q16539

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000112062 Expressed in 228 organ(s), highest expression level in blood
CleanExiHS_MAPK14
ExpressionAtlasiQ16539 baseline and differential
GenevisibleiQ16539 HS

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_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q16539
Secondary accession number(s): A6ZJ92
, A8K6P4, B0LPH0, B5TY32, O60776, Q13083, Q14084, Q8TDX0
<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: November 1, 1997
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 226 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, 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 chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
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