UniProtKB - P47811 (MK14_MOUSE)
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Protein
Mitogen-activated protein kinase 14
Gene
Mapk14
Organism
Mus musculus (Mouse)
Status
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
Catalytic activityi
ATP + a protein = ADP + a phosphoprotein.2 Publications
Cofactori
Enzyme 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
Kineticsi
- KM=212 µM for ATP (when both Thr-180 and Tyr-182 are phosphorylated)1 Publication
- KM=1669 µM for ATP (when only Thr-180 is phosphorylated)1 Publication
- KM=656 µM for EGFR peptide as a substrate (when both Thr-180 and Tyr-182 are phosphorylated)1 Publication
- KM=2800 µM for EGFR peptide as a substrate (when only Thr-180 is phosphorylated)1 Publication
- KM=2.03 µM for ATF2 as a substrate (when both Thr-180 and Tyr-182 are phosphorylated)1 Publication
- KM=20.1 µM for ATF2 as a substrate (when only Thr-180 is phosphorylated)1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 32 | Inhibitor2 Publications | 1 | |
Binding sitei | 35 | Inhibitor2 Publications | 1 | |
Binding sitei | 53 | ATPPROSITE-ProRule annotation | 1 | |
Binding sitei | 53 | Inhibitor2 Publications | 1 | |
Binding sitei | 71 | Inhibitor2 Publications | 1 | |
Binding sitei | 109 | Inhibitor; via amide nitrogen and carbonyl oxygen2 Publications | 1 | |
Binding sitei | 111 | Inhibitor; via amide nitrogen2 Publications | 1 | |
Active sitei | 168 | Proton acceptorPROSITE-ProRule annotation | 1 | |
Binding sitei | 168 | Inhibitor2 Publications | 1 | |
Binding sitei | 169 | Inhibitor; via carbonyl oxygen2 Publications | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 30 – 38 | ATPPROSITE-ProRule annotation | 9 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- enzyme binding Source: MGI
- kinase activity Source: MGI
- MAP kinase activity Source: UniProtKB
- mitogen-activated protein kinase p38 binding Source: MGI
- NFAT protein binding Source: BHF-UCL
- protein kinase activity Source: MGI
- protein phosphatase binding Source: MGI
- protein serine/threonine kinase activity Source: MGI
GO - Biological processi
- angiogenesis Source: MGI
- apoptotic process Source: UniProtKB-KW
- cartilage condensation Source: AgBase
- cell morphogenesis Source: MGI
- cellular response to DNA damage stimulus Source: MGI
- cellular response to ionizing radiation Source: MGI
- cellular response to lipopolysaccharide Source: MGI
- cellular response to lipoteichoic acid Source: MGI
- cellular response to tumor necrosis factor Source: MGI
- cellular response to vascular endothelial growth factor stimulus Source: MGI
- cellular response to virus Source: MGI
- chondrocyte differentiation Source: MGI
- DNA damage checkpoint Source: MGI
- fatty acid oxidation Source: MGI
- glucose metabolic process Source: MGI
- intracellular signal transduction Source: UniProtKB
- lipopolysaccharide-mediated signaling pathway Source: MGI
- myoblast differentiation involved in skeletal muscle regeneration Source: MGI
- negative regulation of canonical Wnt signaling pathway Source: AgBase
- osteoclast differentiation Source: BHF-UCL
- p38MAPK cascade Source: UniProtKB
- peptidyl-serine phosphorylation Source: BHF-UCL
- placenta development Source: MGI
- positive regulation of brown fat cell differentiation Source: MGI
- positive regulation of cardiac muscle cell proliferation Source: MGI
- positive regulation of cyclase activity Source: MGI
- positive regulation of cytokine secretion involved in immune response Source: CAFA
- positive regulation of erythrocyte differentiation Source: MGI
- positive regulation of gene expression Source: MGI
- positive regulation of glucose import Source: MGI
- positive regulation of interleukin-12 secretion Source: MGI
- positive regulation of macrophage chemotaxis Source: CAFA
- positive regulation of metallopeptidase activity Source: CAFA
- positive regulation of myoblast differentiation Source: UniProtKB
- positive regulation of myoblast fusion Source: UniProtKB
- positive regulation of myotube differentiation Source: UniProtKB
- positive regulation of protein import into nucleus Source: MGI
- positive regulation of reactive oxygen species metabolic process Source: MGI
- positive regulation of transcription by RNA polymerase II Source: MGI
- protein phosphorylation Source: MGI
- regulation of cytokine production involved in inflammatory response Source: MGI
- regulation of ossification Source: MGI
- regulation of transcription, DNA-templated Source: MGI
- regulation of transcription by RNA polymerase II Source: UniProtKB
- response to lipopolysaccharide Source: MGI
- response to muramyl dipeptide Source: MGI
- response to muscle stretch Source: MGI
- signal transduction in response to DNA damage Source: MGI
- skeletal muscle tissue development Source: MGI
- stress-induced premature senescence Source: MGI
- striated muscle cell differentiation Source: MGI
- transcription, DNA-templated Source: UniProtKB-KW
- transmembrane receptor protein serine/threonine kinase signaling pathway Source: MGI
- vascular endothelial growth factor receptor signaling pathway Source: MGI
Keywordsi
Molecular function | Kinase, Serine/threonine-protein kinase, Transferase |
Biological process | Apoptosis, Stress response, Transcription, Transcription regulation |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 2.7.11.24. 3474. |
Reactomei | R-MMU-168638. NOD1/2 Signaling Pathway. R-MMU-171007. p38MAPK events. R-MMU-198753. ERK/MAPK targets. R-MMU-2559580. Oxidative Stress Induced Senescence. R-MMU-375170. CDO in myogenesis. R-MMU-376172. DSCAM interactions. R-MMU-418592. ADP signalling through P2Y purinoceptor 1. R-MMU-432142. Platelet sensitization by LDL. R-MMU-4420097. VEGFA-VEGFR2 Pathway. R-MMU-450302. activated TAK1 mediates p38 MAPK activation. R-MMU-450341. Activation of the AP-1 family of transcription factors. R-MMU-6798695. Neutrophil degranulation. R-MMU-6804756. Regulation of TP53 Activity through Phosphorylation. |
SABIO-RKi | P47811. |
Names & Taxonomyi
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 |
Gene namesi | Name:Mapk14 Synonyms:Crk1, Csbp1, Csbp2 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:1346865. Mapk14. |
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 180 | T → A: Phosphorylation blocked. 1 Publication | 1 | |
Mutagenesisi | 182 | Y → F: Phosphorylation blocked. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL2336. |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedBy similarity | |||
ChainiPRO_0000186292 | 2 – 360 | Mitogen-activated protein kinase 14Add BLAST | 359 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserineBy similarity | 1 | |
Modified residuei | 2 | PhosphoserineBy similarity | 1 | |
Modified residuei | 16 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 53 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 152 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 180 | PhosphothreonineCombined sources1 Publication | 1 | |
Modified residuei | 180 | Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and autocatalysisBy similarity | 1 | |
Modified residuei | 182 | PhosphotyrosineCombined sources1 Publication | 1 | |
Modified residuei | 182 | Phosphotyrosine; by MAP2K3, MAP2K4, MAP2K6 and autocatalysisBy similarity | 1 | |
Modified residuei | 323 | Phosphotyrosine; by ZAP70By similarity | 1 |
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 conjugationProteomic databases
EPDi | P47811. |
MaxQBi | P47811. |
PaxDbi | P47811. |
PeptideAtlasi | P47811. |
PRIDEi | P47811. |
PTM databases
iPTMneti | P47811. |
PhosphoSitePlusi | P47811. |
Expressioni
Tissue specificityi
Macrophages, monocytes, T- and B-lymphocytes. Isoform 2 is specifically expressed in kidney and liver.
Gene expression databases
Bgeei | ENSMUSG00000053436. |
CleanExi | MM_MAPK14. |
ExpressionAtlasi | P47811. baseline and differential. |
Genevisiblei | P47811. MM. |
Interactioni
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
Binary interactionsi
GO - Molecular functioni
- enzyme binding Source: MGI
- mitogen-activated protein kinase p38 binding Source: MGI
- NFAT protein binding Source: BHF-UCL
- protein phosphatase binding Source: MGI
Protein-protein interaction databases
BioGridi | 204969. 25 interactors. |
DIPi | DIP-31073N. |
ELMi | P47811. |
IntActi | P47811. 29 interactors. |
MINTi | P47811. |
STRINGi | 10090.ENSMUSP00000004990. |
Chemistry databases
BindingDBi | P47811. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsFeature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Beta strandi | 8 – 13 | Combined sources | 6 | |
Beta strandi | 16 – 21 | Combined sources | 6 | |
Beta strandi | 24 – 30 | Combined sources | 7 | |
Helixi | 31 – 33 | Combined sources | 3 | |
Beta strandi | 34 – 43 | Combined sources | 10 | |
Turni | 44 – 46 | Combined sources | 3 | |
Beta strandi | 49 – 54 | Combined sources | 6 | |
Helixi | 62 – 77 | Combined sources | 16 | |
Beta strandi | 87 – 90 | Combined sources | 4 | |
Helixi | 96 – 98 | Combined sources | 3 | |
Beta strandi | 103 – 107 | Combined sources | 5 | |
Beta strandi | 110 – 112 | Combined sources | 3 | |
Helixi | 113 – 117 | Combined sources | 5 | |
Helixi | 124 – 143 | Combined sources | 20 | |
Helixi | 153 – 155 | Combined sources | 3 | |
Beta strandi | 156 – 158 | Combined sources | 3 | |
Beta strandi | 164 – 166 | Combined sources | 3 | |
Beta strandi | 172 – 175 | Combined sources | 4 | |
Helixi | 176 – 180 | Combined sources | 5 | |
Beta strandi | 182 – 184 | Combined sources | 3 | |
Helixi | 185 – 188 | Combined sources | 4 | |
Helixi | 191 – 194 | Combined sources | 4 | |
Beta strandi | 197 – 199 | Combined sources | 3 | |
Helixi | 203 – 218 | Combined sources | 16 | |
Helixi | 228 – 239 | Combined sources | 12 | |
Helixi | 244 – 247 | Combined sources | 4 | |
Helixi | 253 – 261 | Combined sources | 9 | |
Helixi | 270 – 272 | Combined sources | 3 | |
Turni | 274 – 276 | Combined sources | 3 | |
Helixi | 279 – 288 | Combined sources | 10 | |
Helixi | 293 – 295 | Combined sources | 3 | |
Helixi | 299 – 303 | Combined sources | 5 | |
Helixi | 306 – 308 | Combined sources | 3 | |
Turni | 309 – 311 | Combined sources | 3 | |
Helixi | 314 – 316 | Combined sources | 3 | |
Helixi | 326 – 329 | Combined sources | 4 | |
Helixi | 334 – 346 | Combined sources | 13 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1LEW | X-ray | 2.30 | A | 1-360 | [»] | |
1LEZ | X-ray | 2.30 | A | 1-360 | [»] | |
1YW2 | X-ray | 2.01 | A | 1-360 | [»] | |
1YWR | X-ray | 1.95 | A | 1-360 | [»] | |
2EWA | X-ray | 2.10 | A | 1-360 | [»] | |
2GHL | X-ray | 2.10 | A | 5-352 | [»] | |
2GHM | X-ray | 2.35 | A | 5-352 | [»] | |
2GTM | X-ray | 1.90 | A | 5-352 | [»] | |
2GTN | X-ray | 1.80 | A | 5-352 | [»] | |
2OZA | X-ray | 2.70 | B | 2-360 | [»] | |
2PUU | X-ray | 2.50 | A | 5-352 | [»] | |
3P4K | X-ray | 2.30 | A | 1-360 | [»] | |
3P5K | X-ray | 2.09 | A | 2-360 | [»] | |
3P78 | X-ray | 2.30 | A | 2-360 | [»] | |
3P79 | X-ray | 2.10 | A | 2-360 | [»] | |
3P7A | X-ray | 2.31 | A | 2-360 | [»] | |
3P7B | X-ray | 1.90 | A | 2-360 | [»] | |
3P7C | X-ray | 2.30 | A | 2-360 | [»] | |
3PY3 | X-ray | 2.10 | A | 1-360 | [»] | |
3TG1 | X-ray | 2.71 | A | 1-360 | [»] | |
4KA3 | X-ray | 2.71 | A | 1-360 | [»] | |
4LOO | X-ray | 1.95 | A | 1-360 | [»] | |
4LOP | X-ray | 2.05 | A/B/C/D | 1-360 | [»] | |
4LOQ | X-ray | 2.32 | A/B/C/D | 1-360 | [»] | |
4TYH | X-ray | 3.00 | B | 6-353 | [»] | |
5LAR | X-ray | 1.50 | A | 1-360 | [»] | |
5O90 | X-ray | 2.49 | A | 1-360 | [»] | |
5UOJ | X-ray | 2.10 | A | 1-360 | [»] | |
ProteinModelPortali | P47811. | |||||
SMRi | P47811. | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P47811. |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 24 – 308 | Protein kinasePROSITE-ProRule annotationAdd BLAST | 285 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 106 – 111 | Inhibitor-binding | 6 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 180 – 182 | TXY | 3 |
Domaini
The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
Sequence similaritiesi
Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. MAP kinase subfamily.Curated
Phylogenomic databases
eggNOGi | KOG0660. Eukaryota. ENOG410XNY0. LUCA. |
GeneTreei | ENSGT00550000074271. |
HOVERGENi | HBG014652. |
InParanoidi | P47811. |
KOi | K04441. |
OMAi | DVIDTIC. |
OrthoDBi | EOG091G08QL. |
PhylomeDBi | P47811. |
TreeFami | TF105100. |
Family and domain databases
InterProi | View protein in InterPro IPR011009. Kinase-like_dom_sf. IPR003527. MAP_kinase_CS. IPR008352. MAPK_p38. IPR000719. Prot_kinase_dom. IPR017441. Protein_kinase_ATP_BS. |
Pfami | View protein in Pfam PF00069. Pkinase. 1 hit. |
PRINTSi | PR01773. P38MAPKINASE. |
SMARTi | View protein in SMART SM00220. S_TKc. 1 hit. |
SUPFAMi | SSF56112. SSF56112. 1 hit. |
PROSITEi | View protein in PROSITE PS01351. MAPK. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. |
s (4)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 4 produced by isoformsialternative splicing. AlignAdd to basket
Isoform 1 (identifier: P47811-1) [UniParc]FASTAAdd to basket
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length | |
---|---|---|---|---|---|
Sequence conflicti | 98 | E → G in AAF06348 (Ref. 7) Curated | 1 | ||
Sequence conflicti | 107 – 108 | HL → LS in AAF06348 (Ref. 7) Curated | 2 | ||
Sequence conflicti | 115 | N → R in AAF06348 (Ref. 7) Curated | 1 | ||
Sequence conflicti | 124 | D → G in AAF06348 (Ref. 7) Curated | 1 | ||
Sequence conflicti | 159 – 162 | NEDC → TQVI in AAF06348 (Ref. 7) Curated | 4 | ||
Sequence conflicti | 166 | I → L in AAF06348 (Ref. 7) Curated | 1 | ||
Sequence conflicti | 202 | Q → R in AAF06348 (Ref. 7) Curated | 1 | ||
Sequence conflicti | 211 – 212 | CI → GF in AAF06348 (Ref. 7) Curated | 2 | ||
Sequence conflicti | 224 | P → L in AAF06348 (Ref. 7) Curated | 1 | ||
Sequence conflicti | 271 | A → P in AAF06348 (Ref. 7) Curated | 1 | ||
Sequence conflicti | 299 | A → V in AAF06348 (Ref. 7) Curated | 1 | ||
Sequence conflicti | 315 | D → Y in AAF06348 (Ref. 7) Curated | 1 | ||
Isoform 3 (identifier: P47811-3) | |||||
Sequence conflicti | 238 | L → M in BAA19741 (Ref. 2) Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_022359 | 1 – 77 | Missing in isoform 4. 1 PublicationAdd BLAST | 77 | |
Alternative sequenceiVSP_007544 | 230 – 254 | DQLKL…ISSES → NQLQQIMRLTGTPPAYLINR MPSHE in isoform 3. 3 PublicationsAdd BLAST | 25 | |
Alternative sequenceiVSP_004846 | 255 – 278 | ARNYI…FIGAN → DAK in isoform 2. 1 PublicationAdd BLAST | 24 | |
Alternative sequenceiVSP_007545 | 279 – 360 | Missing in isoform 2. 1 PublicationAdd BLAST | 82 |
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. Translation: CAQ52036.1. CT009661 Genomic DNA. Translation: CAQ52037.1. BC012235 mRNA. Translation: AAH12235.1. AF195850 mRNA. Translation: AAF06348.1. X65067 mRNA. Translation: CAA46200.1. |
CCDSi | CCDS28583.1. [P47811-1] CCDS50048.1. [P47811-3] CCDS50049.1. [P47811-4] |
PIRi | I49066. |
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] |
UniGenei | Mm.311337. |
Genome annotation databases
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Entry informationi
Entry namei | MK14_MOUSE | |
Accessioni | P47811Primary (citable) accession number: P47811 Secondary accession number(s): B2KF37 Q9QZ80 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1996 |
Last sequence update: | January 23, 2007 | |
Last modified: | March 28, 2018 | |
This is version 204 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |