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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-Experimental evidence at protein leveli

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

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Mg2+1 Publication

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). 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
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
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
Nucleotide bindingi30 – 38ATP9

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Stress response, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS03507-MONOMER.
ZFISH: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.

Names & Taxonomyi

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
Gene namesi
Name:MAPK14
Synonyms:CSBP, CSBP1, CSBP2, CSPB1, MXI2, SAPK2A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:6876. MAPK14.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • mitochondrion Source: Ensembl
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • spindle pole Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

DisGeNETi1432.
OpenTargetsiENSG00000112062.
PharmGKBiPA30621.

Chemistry databases

ChEMBLiCHEMBL260.
GuidetoPHARMACOLOGYi1499.

Polymorphism and mutation databases

BioMutaiMAPK14.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001862912 – 360Mitogen-activated protein kinase 14Add BLAST359

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

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

EPDiQ16539.
MaxQBiQ16539.
PaxDbiQ16539.
PeptideAtlasiQ16539.
PRIDEiQ16539.

2D gel databases

OGPiQ16539.

PTM databases

iPTMnetiQ16539.
PhosphoSitePlusiQ16539.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000112062.
CleanExiHS_MAPK14.
ExpressionAtlasiQ16539. baseline and differential.
GenevisibleiQ16539. HS.

Organism-specific databases

HPAiCAB010285.
CAB040578.
HPA051825.

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 (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

Binary interactionsi

WithEntry#Exp.IntActNotes
AKT1P317492EBI-73946,EBI-296087
DUSP1P285624EBI-73946,EBI-975493
DUSP9Q999563EBI-73946,EBI-3906678
MAP2K3P467342EBI-73946,EBI-602462
MAPK1P284825EBI-6932370,EBI-959949
MAPK3P273615EBI-73946,EBI-73995
MAPKAPK2P491377EBI-73946,EBI-993299
MAPKAPK3Q166445EBI-73946,EBI-1384657
MKNK1Q9BUB53EBI-73946,EBI-73837
MKNK2Q9HBH93EBI-73946,EBI-2864341
NUP153P497902EBI-6932370,EBI-286779
PPM1AP358132EBI-73946,EBI-989143
PTPRRQ152563EBI-73946,EBI-2265659
RB1P064004EBI-73946,EBI-491274
RPS6KA4O756764EBI-73946,EBI-73933
SUPT20HQ8NEM75EBI-73946,EBI-946984
TAB1Q157502EBI-73946,EBI-358643
TSC1Q925742EBI-73946,EBI-1047085
ZFP36L1Q073522EBI-73946,EBI-721823
ZNHIT1O432577EBI-73946,EBI-347522

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL
  • NFAT protein binding Source: BHF-UCL
  • protein phosphatase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107819. 199 interactors.
DIPiDIP-30987N.
IntActiQ16539. 100 interactors.
MINTiMINT-126546.
STRINGi9606.ENSP00000229794.

Chemistry databases

BindingDBiQ16539.

Structurei

Secondary structure

1360
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 13Combined sources6
Beta strandi16 – 21Combined sources6
Beta strandi24 – 29Combined sources6
Helixi31 – 33Combined sources3
Turni34 – 36Combined sources3
Beta strandi38 – 43Combined sources6
Turni44 – 47Combined sources4
Beta strandi48 – 54Combined sources7
Helixi62 – 77Combined sources16
Beta strandi87 – 90Combined sources4
Helixi96 – 98Combined sources3
Beta strandi103 – 107Combined sources5
Beta strandi110 – 112Combined sources3
Turni113 – 115Combined sources3
Turni116 – 119Combined sources4
Helixi124 – 143Combined sources20
Helixi153 – 155Combined sources3
Beta strandi156 – 158Combined sources3
Turni160 – 162Combined sources3
Beta strandi164 – 166Combined sources3
Beta strandi168 – 170Combined sources3
Helixi173 – 175Combined sources3
Helixi177 – 179Combined sources3
Beta strandi180 – 182Combined sources3
Turni185 – 188Combined sources4
Helixi191 – 194Combined sources4
Beta strandi197 – 199Combined sources3
Helixi204 – 218Combined sources15
Helixi228 – 239Combined sources12
Helixi244 – 247Combined sources4
Helixi253 – 260Combined sources8
Helixi270 – 273Combined sources4
Turni274 – 276Combined sources3
Helixi279 – 288Combined sources10
Helixi293 – 295Combined sources3
Helixi299 – 303Combined sources5
Helixi306 – 308Combined sources3
Turni309 – 311Combined sources3
Helixi314 – 316Combined sources3
Helixi325 – 327Combined sources3
Helixi334 – 347Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
5ETCX-ray2.42A1-360[»]
5ETIX-ray2.80A1-360[»]
ProteinModelPortaliQ16539.
SMRiQ16539.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16539.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 308Protein kinasePROSITE-ProRule annotationAdd BLAST285

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni70 – 71Inhibitor-binding2
Regioni106 – 110Inhibitor-binding5
Regioni168 – 169Inhibitor-binding2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi180 – 182TXY3

Domaini

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

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0660. Eukaryota.
ENOG410XNY0. LUCA.
GeneTreeiENSGT00550000074271.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiQ16539.
KOiK04441.
OMAiIQSLAQM.
OrthoDBiEOG091G08QL.
PhylomeDBiQ16539.
TreeFamiTF105100.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01773. P38MAPKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

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
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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti67R → G in BAF84398 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 → G.1 PublicationCorresponds to variant rs45496794dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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:
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.

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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

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:
PDBei
RCSB PDBi
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[»]
5ETCX-ray2.42A1-360[»]
5ETIX-ray2.80A1-360[»]
ProteinModelPortaliQ16539.
SMRiQ16539.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107819. 199 interactors.
DIPiDIP-30987N.
IntActiQ16539. 100 interactors.
MINTiMINT-126546.
STRINGi9606.ENSP00000229794.

Chemistry databases

BindingDBiQ16539.
ChEMBLiCHEMBL260.
GuidetoPHARMACOLOGYi1499.

PTM databases

iPTMnetiQ16539.
PhosphoSitePlusiQ16539.

Polymorphism and mutation databases

BioMutaiMAPK14.

2D gel databases

OGPiQ16539.

Proteomic databases

EPDiQ16539.
MaxQBiQ16539.
PaxDbiQ16539.
PeptideAtlasiQ16539.
PRIDEiQ16539.

Protocols and materials databases

DNASUi1432.
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

CTDi1432.
DisGeNETi1432.
GeneCardsiMAPK14.
HGNCiHGNC:6876. MAPK14.
HPAiCAB010285.
CAB040578.
HPA051825.
MIMi600289. gene.
neXtProtiNX_Q16539.
OpenTargetsiENSG00000112062.
PharmGKBiPA30621.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0660. Eukaryota.
ENOG410XNY0. LUCA.
GeneTreeiENSGT00550000074271.
HOGENOMiHOG000233024.
HOVERGENiHBG014652.
InParanoidiQ16539.
KOiK04441.
OMAiIQSLAQM.
OrthoDBiEOG091G08QL.
PhylomeDBiQ16539.
TreeFamiTF105100.

Enzyme and pathway databases

BioCyciMetaCyc:HS03507-MONOMER.
ZFISH: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

ChiTaRSiMAPK14. human.
EvolutionaryTraceiQ16539.
GeneWikiiMAPK14.
GenomeRNAii1432.
PROiQ16539.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000112062.
CleanExiHS_MAPK14.
ExpressionAtlasiQ16539. baseline and differential.
GenevisibleiQ16539. HS.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSiPR01773. P38MAPKINASE.
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMK14_HUMAN
AccessioniPrimary (citable) accession number: Q16539
Secondary accession number(s): A6ZJ92
, A8K6P4, B0LPH0, B5TY32, O60776, Q13083, Q14084, Q8TDX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 206 of the entry and version 3 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.