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Q16539

- MK14_HUMAN

UniProt

Q16539 - MK14_HUMAN

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Protein

Mitogen-activated protein kinase 14

Gene

MAPK14

Organism
Homo sapiens (Human)
Status
Reviewed - 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

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei35 – 351Inhibitor3 Publications
Binding sitei53 – 531ATP
Binding sitei53 – 531Inhibitor3 Publications
Binding sitei71 – 711Inhibitor3 Publications
Binding sitei109 – 1091Inhibitor; via amide nitrogen and carbonyl oxygen3 Publications
Binding sitei154 – 1541Inhibitor; via carbonyl oxygen3 Publications
Active sitei168 – 1681Proton acceptor
Binding sitei168 – 1681Inhibitor; via amide nitrogen and carbonyl oxygen3 Publications
Binding sitei197 – 1971Inhibitor3 Publications
Binding sitei252 – 2521Inhibitor; via amide nitrogen3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi30 – 389ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. MAP kinase activity Source: UniProtKB
  3. MAP kinase kinase activity Source: ProtInc
  4. NFAT protein binding Source: BHF-UCL
  5. protein serine/threonine kinase activity Source: Reactome

GO - Biological processi

  1. 3'-UTR-mediated mRNA stabilization Source: UniProtKB
  2. activation of MAPK activity Source: Reactome
  3. angiogenesis Source: Ensembl
  4. apoptotic process Source: UniProtKB-KW
  5. blood coagulation Source: Reactome
  6. cartilage condensation Source: Ensembl
  7. cell morphogenesis Source: Ensembl
  8. cell surface receptor signaling pathway Source: ProtInc
  9. cellular component movement Source: ProtInc
  10. cellular response to ionizing radiation Source: BHF-UCL
  11. cellular response to lipopolysaccharide Source: MGI
  12. cellular response to vascular endothelial growth factor stimulus Source: BHF-UCL
  13. chemotaxis Source: ProtInc
  14. chondrocyte differentiation Source: Ensembl
  15. DNA damage checkpoint Source: Ensembl
  16. fatty acid oxidation Source: Ensembl
  17. gene expression Source: Reactome
  18. glucose metabolic process Source: Ensembl
  19. innate immune response Source: Reactome
  20. intracellular signal transduction Source: UniProtKB
  21. lipopolysaccharide-mediated signaling pathway Source: Ensembl
  22. mRNA metabolic process Source: Reactome
  23. muscle cell differentiation Source: Reactome
  24. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  25. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  26. myoblast differentiation involved in skeletal muscle regeneration Source: Ensembl
  27. negative regulation of canonical Wnt signaling pathway Source: Ensembl
  28. neurotrophin TRK receptor signaling pathway Source: Reactome
  29. osteoclast differentiation Source: BHF-UCL
  30. p38MAPK cascade Source: UniProtKB
  31. peptidyl-serine phosphorylation Source: BHF-UCL
  32. platelet activation Source: Reactome
  33. positive regulation of erythrocyte differentiation Source: Ensembl
  34. positive regulation of muscle cell differentiation Source: Reactome
  35. positive regulation of myoblast differentiation Source: UniProtKB
  36. positive regulation of myoblast fusion Source: UniProtKB
  37. positive regulation of myotube differentiation Source: UniProtKB
  38. positive regulation of protein import into nucleus Source: Ensembl
  39. positive regulation of reactive oxygen species metabolic process Source: BHF-UCL
  40. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  41. Ras protein signal transduction Source: Reactome
  42. regulation of sequence-specific DNA binding transcription factor activity Source: Reactome
  43. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  44. response to muramyl dipeptide Source: Ensembl
  45. RNA metabolic process Source: Reactome
  46. signal transduction Source: ProtInc
  47. signal transduction in response to DNA damage Source: BHF-UCL
  48. skeletal muscle tissue development Source: Ensembl
  49. stress-activated MAPK cascade Source: Reactome
  50. stress-induced premature senescence Source: BHF-UCL
  51. striated muscle cell differentiation Source: Ensembl
  52. toll-like receptor 10 signaling pathway Source: Reactome
  53. toll-like receptor 2 signaling pathway Source: Reactome
  54. toll-like receptor 3 signaling pathway Source: Reactome
  55. toll-like receptor 4 signaling pathway Source: Reactome
  56. toll-like receptor 5 signaling pathway Source: Reactome
  57. toll-like receptor 9 signaling pathway Source: Reactome
  58. toll-like receptor signaling pathway Source: Reactome
  59. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  60. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  61. transcription, DNA-templated Source: UniProtKB-KW
  62. transmembrane receptor protein serine/threonine kinase signaling pathway Source: Ensembl
  63. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
  64. vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
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.
ReactomeiREACT_12065. p38MAPK events.
REACT_12599. ERK/MAPK targets.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_19140. ADP signalling through P2Y purinoceptor 1.
REACT_200686. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_21326. Activation of the AP-1 family of transcription factors.
REACT_21399. activated TAK1 mediates p38 MAPK activation.
REACT_21402. CDO in myogenesis.
REACT_228166. VEGFA-VEGFR2 Pathway.
REACT_23879. Platelet sensitization by LDL.
REACT_25042. KSRP destabilizes mRNA.
REACT_25299. DSCAM interactions.
REACT_75776. NOD1/2 Signaling Pathway.
SignaLinkiQ16539.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitogen-activated protein kinase 14 (EC:2.7.11.24)
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
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:6876. MAPK14.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. mitochondrion Source: Ensembl
  5. nucleoplasm Source: Reactome
  6. nucleus Source: UniProtKB
  7. spindle pole Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi34 – 341A → V: Lowered kinase activity. 1 Publication
Mutagenesisi53 – 531K → R: Loss of kinase activity. 1 Publication
Mutagenesisi54 – 541K → R: Impairs MAP2K6/MKK6-dependent autophosphorylation. 1 Publication
Mutagenesisi69 – 691Y → H: Lowered kinase activity. 1 Publication
Mutagenesisi168 – 1681D → A: Loss of kinase activity. 1 Publication
Mutagenesisi175 – 1751T → A: Loss of kinase activity. 1 Publication
Mutagenesisi176 – 1761D → A: Emulation of the active state. Increase in activity; when associated with S-327 or L-327. 1 Publication
Mutagenesisi177 – 1771D → A: Loss of kinase activity. 1 Publication
Mutagenesisi180 – 1801T → E: Loss of kinase activity. 1 Publication
Mutagenesisi182 – 1821Y → F: Loss of kinase activity. 1 Publication
Mutagenesisi320 – 3201A → T: Lowered kinase activity. 1 Publication
Mutagenesisi327 – 3271F → L: Emulation of the active state. Increase in activity; when associated with A-176. 1 Publication
Mutagenesisi327 – 3271F → S: Emulation of the active state. Increase in activity; when associated with A-176. 1 Publication
Mutagenesisi337 – 3371W → R: Loss of kinase activity. 1 Publication

Organism-specific databases

PharmGKBiPA30621.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 360359Mitogen-activated protein kinase 14PRO_0000186291Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei2 – 21Phosphoserine1 Publication
Modified residuei16 – 161Phosphothreonine1 Publication
Modified residuei53 – 531N6-acetyllysine1 Publication
Modified residuei152 – 1521N6-acetyllysine1 Publication
Modified residuei180 – 1801Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and autocatalysis4 Publications
Modified residuei182 – 1821Phosphotyrosine; by MAP2K3, MAP2K4, MAP2K6 and autocatalysis4 Publications
Modified residuei263 – 2631Phosphothreonine1 Publication
Modified residuei323 – 3231Phosphotyrosine; by ZAP701 Publication

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 DUSP16.10 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 HDAC3.2 Publications
Ubiquitinated. Ubiquitination leads to degradation by the proteasome pathway.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ16539.
PaxDbiQ16539.
PRIDEiQ16539.

2D gel databases

OGPiQ16539.

PTM databases

PhosphoSiteiQ16539.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ16539.
CleanExiHS_MAPK14.
ExpressionAtlasiQ16539. baseline and differential.
GenevestigatoriQ16539.

Organism-specific databases

HPAiCAB010285.
CAB040578.

Interactioni

Subunit structurei

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.By similarity16 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
MAPKAPK2P491375EBI-73946,EBI-993299
MAPKAPK3Q166443EBI-73946,EBI-1384657
MKNK1Q9BUB53EBI-73946,EBI-73837
MKNK2Q9HBH93EBI-73946,EBI-2864341
NUP153P497902EBI-6932370,EBI-286779
PPM1AP358132EBI-73946,EBI-989143
PTPN7P352362EBI-73946,EBI-2265723
PTPRRQ152563EBI-73946,EBI-2265659
RB1P064004EBI-73946,EBI-491274
RPS6KA4O756763EBI-73946,EBI-73933
SUPT20HQ8NEM75EBI-73946,EBI-946984
TAB1Q157502EBI-73946,EBI-358643
TSC1Q925742EBI-73946,EBI-1047085
ZFP36L1Q073522EBI-73946,EBI-721823
ZNHIT1O432577EBI-73946,EBI-347522

Protein-protein interaction databases

BioGridi107819. 179 interactions.
DIPiDIP-30987N.
IntActiQ16539. 97 interactions.
MINTiMINT-126546.
STRINGi9606.ENSP00000229794.

Structurei

Secondary structure

1
360
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 136Combined sources
Beta strandi16 – 216Combined sources
Beta strandi24 – 296Combined sources
Helixi31 – 333Combined sources
Turni34 – 363Combined sources
Beta strandi38 – 436Combined sources
Turni44 – 474Combined sources
Beta strandi48 – 547Combined sources
Helixi62 – 7716Combined sources
Beta strandi87 – 904Combined sources
Helixi96 – 983Combined sources
Beta strandi103 – 1075Combined sources
Beta strandi110 – 1123Combined sources
Turni113 – 1153Combined sources
Turni116 – 1194Combined sources
Helixi124 – 14320Combined sources
Helixi153 – 1553Combined sources
Beta strandi156 – 1583Combined sources
Turni160 – 1623Combined sources
Beta strandi164 – 1663Combined sources
Beta strandi168 – 1703Combined sources
Helixi173 – 1753Combined sources
Helixi177 – 1793Combined sources
Beta strandi180 – 1823Combined sources
Turni185 – 1884Combined sources
Helixi191 – 1944Combined sources
Beta strandi197 – 1993Combined sources
Helixi204 – 21815Combined sources
Helixi228 – 23912Combined sources
Helixi244 – 2474Combined sources
Helixi253 – 2608Combined sources
Helixi270 – 2734Combined sources
Turni274 – 2763Combined sources
Helixi279 – 28810Combined sources
Helixi293 – 2953Combined sources
Helixi299 – 3035Combined sources
Helixi306 – 3083Combined sources
Turni309 – 3113Combined sources
Helixi314 – 3163Combined sources
Helixi325 – 3273Combined sources
Helixi334 – 34714Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ16539.
SMRiQ16539. Positions 4-354.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16539.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 308285Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni70 – 712Inhibitor-binding
Regioni106 – 1105Inhibitor-binding
Regioni168 – 1692Inhibitor-binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi180 – 1823TXY

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

eggNOGiCOG0515.
GeneTreeiENSGT00550000074271.
HOVERGENiHBG014652.
InParanoidiQ16539.
KOiK04441.
OMAiDIFRGAN.
OrthoDBiEOG7PCJGV.
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.
IPR002290. Ser/Thr_dual-sp_kinase.
[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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 671R → G in BAF84398. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti51 – 511A → V in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042270
Natural varianti322 – 3221P → R in a lung adenocarcinoma sample; somatic mutation. 1 Publication
VAR_042271
Natural varianti343 – 3431D → G.1 Publication
Corresponds to variant rs45496794 [ dbSNP | Ensembl ].
VAR_042272

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei230 – 25425DQLKL…ISSES → NQLQQIMRLTGTPPAYLINR MPSHE in isoform CSBP1. 1 PublicationVSP_004842Add
BLAST
Alternative sequencei255 – 360106ARNYI…EEMES → VS in isoform 5. 1 PublicationVSP_057194Add
BLAST
Alternative sequencei255 – 30753ARNYI…LAHAY → LSTCWRRCLYWTQIRELQRP KPLHMPTLLSTTILMMNQWP ILMISPLKAGTSL in isoform Exip. 1 PublicationVSP_004843Add
BLAST
Alternative sequencei281 – 36080AVDLL…EEMES → GKLTIYPHLMDIELVMI in isoform Mxi2. 1 PublicationVSP_004844Add
BLAST
Alternative sequencei308 – 36053Missing in isoform Exip. 1 PublicationVSP_004845Add
BLAST

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.
UCSCiuc003olo.3. human. [Q16539-3]
uc003olp.3. human. [Q16539-2]
uc003olq.3. human. [Q16539-1]
uc003olr.3. human. [Q16539-4]

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 .
CCDSi CCDS4815.1. [Q16539-2 ]
CCDS4816.1. [Q16539-1 ]
CCDS4817.1. [Q16539-4 ]
PIRi S53536.
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 ]
UniGenei Hs.485233.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A9U X-ray 2.50 A 1-360 [» ]
1BL6 X-ray 2.50 A 1-360 [» ]
1BL7 X-ray 2.50 A 1-360 [» ]
1BMK X-ray 2.40 A 1-360 [» ]
1DI9 X-ray 2.60 A 1-360 [» ]
1IAN X-ray 2.00 A 2-360 [» ]
1KV1 X-ray 2.50 A 1-360 [» ]
1KV2 X-ray 2.80 A 1-360 [» ]
1M7Q X-ray 2.40 A 1-360 [» ]
1OUK X-ray 2.50 A 1-360 [» ]
1OUY X-ray 2.50 A 1-360 [» ]
1OVE X-ray 2.10 A 1-360 [» ]
1OZ1 X-ray 2.10 A 1-360 [» ]
1R39 X-ray 2.30 A 1-360 [» ]
1R3C X-ray 2.00 A 1-360 [» ]
1W7H X-ray 2.21 A 2-360 [» ]
1W82 X-ray 2.20 A 2-360 [» ]
1W83 X-ray 2.50 A 2-360 [» ]
1W84 X-ray 2.20 A 2-360 [» ]
1WBN X-ray 2.40 A 2-360 [» ]
1WBO X-ray 2.16 A 2-360 [» ]
1WBS X-ray 1.80 A 2-360 [» ]
1WBT X-ray 2.00 A 2-360 [» ]
1WBV X-ray 2.00 A 2-360 [» ]
1WBW X-ray 2.41 A 2-360 [» ]
1WFC X-ray 2.30 A 1-360 [» ]
1YQJ X-ray 2.00 A 2-360 [» ]
1ZYJ X-ray 2.00 A 1-360 [» ]
1ZZ2 X-ray 2.00 A 1-360 [» ]
1ZZL X-ray 2.00 A 4-354 [» ]
2BAJ X-ray 2.25 A 2-360 [» ]
2BAK X-ray 2.20 A 2-360 [» ]
2BAL X-ray 2.10 A 2-360 [» ]
2BAQ X-ray 2.80 A 2-360 [» ]
2FSL X-ray 1.70 X 2-360 [» ]
2FSM X-ray 1.86 X 2-360 [» ]
2FSO X-ray 1.83 X 2-360 [» ]
2FST X-ray 1.45 X 2-360 [» ]
2GFS X-ray 1.75 A 2-360 [» ]
2I0H X-ray 2.00 A 1-360 [» ]
2LGC NMR - A 2-354 [» ]
2NPQ X-ray 1.80 A 2-360 [» ]
2OKR X-ray 2.00 A/D 2-360 [» ]
2ONL X-ray 4.00 A/B 2-360 [» ]
2QD9 X-ray 1.70 A 2-360 [» ]
2RG5 X-ray 2.40 A 2-360 [» ]
2RG6 X-ray 1.72 A 2-360 [» ]
2Y8O X-ray 1.95 A 1-360 [» ]
2YIS X-ray 2.00 A 2-360 [» ]
2YIW X-ray 2.00 A 2-360 [» ]
2YIX X-ray 2.30 A 4-354 [» ]
2ZAZ X-ray 1.80 A 1-360 [» ]
2ZB0 X-ray 2.10 A 1-360 [» ]
2ZB1 X-ray 2.50 A 1-360 [» ]
3BV2 X-ray 2.40 A 2-360 [» ]
3BV3 X-ray 2.59 A 2-360 [» ]
3BX5 X-ray 2.40 A 2-360 [» ]
3C5U X-ray 2.80 A 2-360 [» ]
3CTQ X-ray 1.95 A 5-352 [» ]
3D7Z X-ray 2.10 A 1-360 [» ]
3D83 X-ray 1.90 A 1-360 [» ]
3DS6 X-ray 2.90 A/B/C/D 1-360 [» ]
3DT1 X-ray 2.80 A 1-360 [» ]
3E92 X-ray 2.00 A 1-360 [» ]
3E93 X-ray 2.00 A 1-360 [» ]
3FC1 X-ray 2.40 X 1-360 [» ]
3FI4 X-ray 2.20 A 1-360 [» ]
3FKL X-ray 2.00 A 1-360 [» ]
3FKN X-ray 2.00 A 1-360 [» ]
3FKO X-ray 2.00 A 1-360 [» ]
3FL4 X-ray 1.80 A 1-360 [» ]
3FLN X-ray 1.90 C 1-360 [» ]
3FLQ X-ray 1.90 A 1-360 [» ]
3FLS X-ray 2.30 A 1-360 [» ]
3FLW X-ray 2.10 A 1-360 [» ]
3FLY X-ray 1.80 A 1-360 [» ]
3FLZ X-ray 2.23 A 1-360 [» ]
3FMH X-ray 1.90 A 1-360 [» ]
3FMJ X-ray 2.00 A 1-360 [» ]
3FMK X-ray 1.70 A 1-360 [» ]
3FML X-ray 2.10 A 1-360 [» ]
3FMM X-ray 2.00 A 1-360 [» ]
3FMN X-ray 1.90 A 1-360 [» ]
3FSF X-ray 2.10 A 1-360 [» ]
3FSK X-ray 2.00 A 1-360 [» ]
3GC7 X-ray 1.80 A 1-360 [» ]
3GCP X-ray 2.25 A 2-360 [» ]
3GCQ X-ray 2.00 A 2-360 [» ]
3GCS X-ray 2.10 A 2-360 [» ]
3GCU X-ray 2.10 A/B 2-360 [» ]
3GCV X-ray 2.30 A 2-360 [» ]
3GFE X-ray 2.10 A 1-360 [» ]
3GI3 X-ray 2.40 A 1-360 [» ]
3HA8 X-ray 2.48 A 1-360 [» ]
3HEC X-ray 2.50 A 5-352 [» ]
3HEG X-ray 2.20 A 5-352 [» ]
3HL7 X-ray 1.88 A 1-360 [» ]
3HLL X-ray 1.95 A 1-360 [» ]
3HP2 X-ray 2.15 A 1-360 [» ]
3HP5 X-ray 2.30 A 1-360 [» ]
3HRB X-ray 2.20 A 2-360 [» ]
3HUB X-ray 2.25 A 2-360 [» ]
3HUC X-ray 1.80 A 2-360 [» ]
3HV3 X-ray 2.00 A 2-360 [» ]
3HV4 X-ray 2.60 A/B 2-360 [» ]
3HV5 X-ray 2.25 A/B 2-360 [» ]
3HV6 X-ray 1.95 A 2-360 [» ]
3HV7 X-ray 2.40 A 2-360 [» ]
3HVC X-ray 2.10 A 1-360 [» ]
3IPH X-ray 2.10 A 1-360 [» ]
3ITZ X-ray 2.25 A 1-360 [» ]
3IW5 X-ray 2.50 A 2-360 [» ]
3IW6 X-ray 2.10 A 2-360 [» ]
3IW7 X-ray 2.40 A 2-360 [» ]
3IW8 X-ray 2.00 A 2-360 [» ]
3K3I X-ray 1.70 A 5-352 [» ]
3K3J X-ray 2.00 A 1-360 [» ]
3KF7 X-ray 2.00 A 1-360 [» ]
3KQ7 X-ray 1.80 A 1-360 [» ]
3L8S X-ray 2.35 A 2-360 [» ]
3L8X X-ray 2.15 A 2-360 [» ]
3LFA X-ray 2.10 A 2-360 [» ]
3LFB X-ray 2.60 A 2-360 [» ]
3LFC X-ray 2.80 A 2-360 [» ]
3LFD X-ray 3.40 A 2-360 [» ]
3LFE X-ray 2.30 A 2-360 [» ]
3LFF X-ray 1.50 A 2-360 [» ]
3LHJ X-ray 3.31 A 1-360 [» ]
3MGY X-ray 2.10 A 1-360 [» ]
3MH0 X-ray 2.00 A 1-360 [» ]
3MH1 X-ray 2.20 A 1-360 [» ]
3MH2 X-ray 2.30 A 1-360 [» ]
3MH3 X-ray 2.20 A 1-360 [» ]
3MPA X-ray 2.10 A 1-360 [» ]
3MPT X-ray 1.89 A 1-360 [» ]
3MVL X-ray 2.80 A/B 2-360 [» ]
3MVM X-ray 2.00 A/B 2-360 [» ]
3MW1 X-ray 2.80 A 2-360 [» ]
3NEW X-ray 2.51 A 1-360 [» ]
3NNU X-ray 2.40 A 1-354 [» ]
3NNV X-ray 2.10 A 1-354 [» ]
3NNW X-ray 1.89 A 1-354 [» ]
3NNX X-ray 2.28 A 1-354 [» ]
3NWW X-ray 2.09 A 2-360 [» ]
3O8P X-ray 2.10 A 1-360 [» ]
3O8T X-ray 2.00 A 1-360 [» ]
3O8U X-ray 2.10 A 1-360 [» ]
3OBG X-ray 2.80 A 1-360 [» ]
3OBJ X-ray 2.40 A 1-360 [» ]
3OC1 X-ray 2.59 A 1-360 [» ]
3OCG X-ray 2.21 A 2-360 [» ]
3OD6 X-ray 2.68 X 1-360 [» ]
3ODY X-ray 2.20 X 1-360 [» ]
3ODZ X-ray 2.30 X 1-360 [» ]
3OEF X-ray 1.60 X 1-360 [» ]
3PG3 X-ray 2.00 A 2-360 [» ]
3QUD X-ray 2.00 A 2-360 [» ]
3QUE X-ray 2.70 A 2-360 [» ]
3RIN X-ray 2.20 A 1-360 [» ]
3ROC X-ray 1.70 A 1-360 [» ]
3S3I X-ray 1.80 A 4-352 [» ]
3S4Q X-ray 2.27 A 2-360 [» ]
3U8W X-ray 2.15 A 1-360 [» ]
3UVP X-ray 2.40 A 2-360 [» ]
3UVQ X-ray 2.20 A 2-360 [» ]
3UVR X-ray 2.10 A 2-360 [» ]
3ZS5 X-ray 1.60 A 2-360 [» ]
3ZSG X-ray 1.89 A 2-360 [» ]
3ZSH X-ray 2.05 A 2-360 [» ]
3ZSI X-ray 2.40 A 2-360 [» ]
3ZYA X-ray 1.90 A 1-360 [» ]
4A9Y X-ray 2.20 A 2-360 [» ]
4AA0 X-ray 1.80 A 2-360 [» ]
4AA4 X-ray 2.30 A 2-360 [» ]
4AA5 X-ray 2.38 A 2-360 [» ]
4AAC X-ray 2.50 A 2-360 [» ]
4DLI X-ray 1.91 A 2-360 [» ]
4DLJ X-ray 2.60 A 2-360 [» ]
4E5A X-ray 1.87 X 1-360 [» ]
4E5B X-ray 2.00 A 1-360 [» ]
4E6A X-ray 2.09 A 1-360 [» ]
4E6C X-ray 2.39 A 1-360 [» ]
4E8A X-ray 2.70 A 1-360 [» ]
4EH2 X-ray 2.00 A 2-360 [» ]
4EH3 X-ray 2.40 A 2-360 [» ]
4EH4 X-ray 2.50 A 2-360 [» ]
4EH5 X-ray 2.00 A 2-360 [» ]
4EH6 X-ray 2.10 A 2-360 [» ]
4EH7 X-ray 2.10 A 2-360 [» ]
4EH8 X-ray 2.20 A 2-360 [» ]
4EH9 X-ray 2.10 A 2-360 [» ]
4EHV X-ray 1.60 A 2-360 [» ]
4EWQ X-ray 2.10 A 2-360 [» ]
4F9W X-ray 2.00 A 2-360 [» ]
4F9Y X-ray 1.85 A 2-360 [» ]
4FA2 X-ray 2.00 A 2-360 [» ]
4GEO X-ray 1.66 A 2-360 [» ]
4KIN X-ray 1.97 A/B/C/D 2-360 [» ]
4KIP X-ray 2.27 A/B 2-360 [» ]
4KIQ X-ray 2.50 A/B/C/D 2-360 [» ]
4L8M X-ray 2.10 A 2-360 [» ]
ProteinModelPortali Q16539.
SMRi Q16539. Positions 4-354.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107819. 179 interactions.
DIPi DIP-30987N.
IntActi Q16539. 97 interactions.
MINTi MINT-126546.
STRINGi 9606.ENSP00000229794.

Chemistry

BindingDBi Q16539.
ChEMBLi CHEMBL2094115.
GuidetoPHARMACOLOGYi 1499.

PTM databases

PhosphoSitei Q16539.

2D gel databases

OGPi Q16539.

Proteomic databases

MaxQBi Q16539.
PaxDbi Q16539.
PRIDEi Q16539.

Protocols and materials databases

DNASUi 1432.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000229794 ; ENSP00000229794 ; ENSG00000112062 . [Q16539-1 ]
ENST00000229795 ; ENSP00000229795 ; ENSG00000112062 . [Q16539-2 ]
ENST00000310795 ; ENSP00000308669 ; ENSG00000112062 . [Q16539-4 ]
GeneIDi 1432.
KEGGi hsa:1432.
UCSCi uc003olo.3. human. [Q16539-3 ]
uc003olp.3. human. [Q16539-2 ]
uc003olq.3. human. [Q16539-1 ]
uc003olr.3. human. [Q16539-4 ]

Organism-specific databases

CTDi 1432.
GeneCardsi GC06P035995.
HGNCi HGNC:6876. MAPK14.
HPAi CAB010285.
CAB040578.
MIMi 600289. gene.
neXtProti NX_Q16539.
PharmGKBi PA30621.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00550000074271.
HOVERGENi HBG014652.
InParanoidi Q16539.
KOi K04441.
OMAi DIFRGAN.
OrthoDBi EOG7PCJGV.
PhylomeDBi Q16539.
TreeFami TF105100.

Enzyme and pathway databases

BioCyci MetaCyc:HS03507-MONOMER.
Reactomei REACT_12065. p38MAPK events.
REACT_12599. ERK/MAPK targets.
REACT_169436. Oxidative Stress Induced Senescence.
REACT_19140. ADP signalling through P2Y purinoceptor 1.
REACT_200686. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
REACT_21326. Activation of the AP-1 family of transcription factors.
REACT_21399. activated TAK1 mediates p38 MAPK activation.
REACT_21402. CDO in myogenesis.
REACT_228166. VEGFA-VEGFR2 Pathway.
REACT_23879. Platelet sensitization by LDL.
REACT_25042. KSRP destabilizes mRNA.
REACT_25299. DSCAM interactions.
REACT_75776. NOD1/2 Signaling Pathway.
SignaLinki Q16539.

Miscellaneous databases

ChiTaRSi MAPK14. human.
EvolutionaryTracei Q16539.
GeneWikii MAPK14.
GenomeRNAii 1432.
NextBioi 5841.
PROi Q16539.
SOURCEi Search...

Gene expression databases

Bgeei Q16539.
CleanExi HS_MAPK14.
ExpressionAtlasi Q16539. baseline and differential.
Genevestigatori Q16539.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR003527. MAP_kinase_CS.
IPR008352. MAPK_p38.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
PRINTSi PR01773. P38MAPKINASE.
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS01351. MAPK. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CSBP1 AND CSBP2), PARTIAL PROTEIN SEQUENCE.
    Tissue: Peripheral blood.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CSBP2).
    Tissue: Liver.
  3. "Mxi2, a mitogen-activated protein kinase that recognizes and phosphorylates Max protein."
    Zervos A.S., Faccio L., Gatto J.P., Kyriakis J.M., Brent R.
    Proc. Natl. Acad. Sci. U.S.A. 92:10531-10534(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MXI2).
  4. "Structure and polymorphism of two stress-activated protein kinase genes centromeric of the MHC: SAPK2a and SAPK4."
    Herbison C.E., Sayer D.C., Bellgard M., Allcock R.J.N., Christiansen F.T., Price P.
    DNA Seq. 10:229-243(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CSBP2).
    Tissue: B-cell.
  5. "Exip, a new alternative splicing variant of p38 alpha, can induce an earlier onset of apoptosis in HeLa cells."
    Sudo T., Yagasaki Y., Hama H., Watanabe N., Osada H.
    Biochem. Biophys. Res. Commun. 291:838-843(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM EXIP), ENZYME REGULATION.
    Tissue: Renal cell carcinoma.
  6. "Discovery of novel human transcript variants by analysis of intronic single-block EST with polyadenylation site."
    Wang P., Yu P., Gao P., Shi T., Ma D.
    BMC Genomics 10:518-518(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
  7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  8. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CSBP2).
  9. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CSBP2).
  10. NHLBI resequencing and genotyping service (RS&G)
    Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  11. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  13. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CSBP2).
    Tissue: Placenta.
  14. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-10.
    Tissue: Platelet.
  15. "Interleukin-1 activates a novel protein kinase cascade that results in the phosphorylation of Hsp27."
    Freshney N.W., Rawlinson L., Guesdon F., Jones E., Cowley S., Hsuan J., Saklatvala J.
    Cell 78:1039-1049(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 174-186.
  16. "Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine."
    Raingeaud J., Gupta S., Rogers J.S., Dickens M., Han J., Ulevitch R.J., Davis R.J.
    J. Biol. Chem. 270:7420-7426(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-180 AND TYR-182, ENZYME REGULATION, SUBCELLULAR LOCATION.
  17. "Human mitogen-activated protein kinase CSBP1, but not CSBP2, complements a hog1 deletion in yeast."
    Kumar S., McLaughlin M.M., McDonnell P.C., Lee J.C., Livi G.P., Young P.R.
    J. Biol. Chem. 270:29043-29046(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ALA-34; LYS-53; ASP-168; THR-175; THR-180 AND TYR-182.
  18. "MKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen-activated protein kinase signal transduction pathway."
    Raingeaud J., Whitmarsh A.J., Barrett T., Derijard B., Davis R.J.
    Mol. Cell. Biol. 16:1247-1255(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY MAP2K3/MKK3 AND MAP2K6/MKK6, ENZYME REGULATION.
  19. "Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB."
    Deak M., Clifton A.D., Lucocq J.M., Alessi D.R.
    EMBO J. 17:4426-4441(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ACTIVATION OF RPS6KA5/MSK1.
  20. "Selective activation of p38 mitogen-activated protein (MAP) kinase isoforms by the MAP kinase kinases MKK3 and MKK6."
    Enslen H., Raingeaud J., Davis R.J.
    J. Biol. Chem. 273:1741-1748(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF ATF2; ELK1 AND MBP, ENZYME REGULATION.
  21. "RSK-B, a novel ribosomal S6 kinase family member, is a CREB kinase under dominant control of p38alpha mitogen-activated protein kinase (p38alphaMAPK)."
    Pierrat B., Correia J.D.S., Mary J.L., Tomas-Zuber M., Lesslauer W.
    J. Biol. Chem. 273:29661-29671(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPS6KA4, FUNCTION IN PHOSPHORYLATION OF RPS6KA4, SUBCELLULAR LOCATION.
  22. "Molecular cloning and characterization of a novel dual specificity phosphatase, MKP-5."
    Tanoue T., Moriguchi T., Nishida E.
    J. Biol. Chem. 274:19949-19956(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DUSP10, ENZYME REGULATION.
  23. "Regulation of the MEF2 family of transcription factors by p38."
    Zhao M., New L., Kravchenko V.V., Kato Y., Gram H., di Padova F., Olson E.N., Ulevitch R.J., Han J.-D.
    Mol. Cell. Biol. 19:21-30(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MEF2A.
  24. "Targeting of p38 mitogen-activated protein kinases to MEF2 transcription factors."
    Yang S.-H., Galanis A., Sharrocks A.D.
    Mol. Cell. Biol. 19:4028-4038(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MEF2A AND MEF2C.
  25. "Requirement for p38alpha in erythropoietin expression: a role for stress kinases in erythropoiesis."
    Tamura K., Sudo T., Senftleben U., Dadak A.M., Johnson R., Karin M.
    Cell 102:221-231(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Tissue: Hepatoma.
  26. "Distinct carboxy-termini confer divergent characteristics to the mitogen-activated protein kinase p38alpha and its splice isoform Mxi2."
    Sanz V., Arozarena I., Crespo P.
    FEBS Lett. 474:169-174(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM MXI2), COFACTOR, ENZYME REGULATION.
  27. "Stress-induced activation of protein kinase CK2 by direct interaction with p38 mitogen-activated protein kinase."
    Sayed M., Kim S.O., Salh B.S., Issinger O.G., Pelech S.L.
    J. Biol. Chem. 275:16569-16573(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSNK2A1 AND CSNK2B, FUNCTION IN ACTIVATION OF CASEIN KINASE II.
  28. "Differential activation of p38 mitogen-activated protein kinase isoforms depending on signal strength."
    Alonso G., Ambrosino C., Jones M., Nebreda A.R.
    J. Biol. Chem. 275:40641-40648(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MA2PK6/MKK6, PHOSPHORYLATION BY MAP2K6/MKK6, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-54.
  29. "Distinct binding determinants for ERK2/p38alpha and JNK map kinases mediate catalytic activation and substrate selectivity of map kinase phosphatase-1."
    Slack D.N., Seternes O.M., Gabrielsen M., Keyse S.M.
    J. Biol. Chem. 276:16491-16500(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DUSP1, ENZYME REGULATION.
  30. "A Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and p38 alpha and beta MAPKs."
    Tanoue T., Yamamoto T., Maeda R., Nishida E.
    J. Biol. Chem. 276:26629-26639(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DUSP16, ENZYME REGULATION.
  31. "The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a eukaryotic initiation factor 4E kinase with high levels of basal activity in mammalian cells."
    Scheper G.C., Morrice N.A., Kleijn M., Proud C.G.
    Mol. Cell. Biol. 21:743-754(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS MKNK2 KINASE.
  32. "Initiation of a G2/M checkpoint after ultraviolet radiation requires p38 kinase."
    Bulavin D.V., Higashimoto Y., Popoff I.J., Gaarde W.A., Basrur V., Potapova O., Appella E., Fornace A.J. Jr.
    Nature 411:102-107(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDC25B AND CDC25C, FUNCTION IN PHOSPHORYLATION OF CDC25B AND CDC25C.
  33. "MAPKK-independent activation of p38alpha mediated by TAB1-dependent autophosphorylation of p38alpha."
    Ge B., Gram H., Di Padova F., Huang B., New L., Ulevitch R.J., Luo Y., Han J.
    Science 295:1291-1294(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAB1, AUTOPHOSPHORYLATION, ENZYME REGULATION.
  34. "Active mutants of the human p38alpha mitogen-activated protein kinase."
    Diskin R., Askari N., Capone R., Engelberg D., Livnah O.
    J. Biol. Chem. 279:47040-47049(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-69; ASP-176; ASP-177; ALA-320; PHE-327 AND TRP-337.
  35. "Myeloid-related protein-14 is a p38 MAPK substrate in human neutrophils."
    Lominadze G., Rane M.J., Merchant M., Cai J., Ward R.A., McLeish K.R.
    J. Immunol. 174:7257-7267(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF S100A9.
  36. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  37. "Alternative p38 activation pathway mediated by T cell receptor-proximal tyrosine kinases."
    Salvador J.M., Mittelstadt P.R., Guszczynski T., Copeland T.D., Yamaguchi H., Appella E., Fornace A.J. Jr., Ashwell J.D.
    Nat. Immunol. 6:390-395(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-323, ENZYME REGULATION.
  38. "The autoimmune suppressor Gadd45alpha inhibits the T cell alternative p38 activation pathway."
    Salvador J.M., Mittelstadt P.R., Belova G.I., Fornace A.J. Jr., Ashwell J.D.
    Nat. Immunol. 6:396-402(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAB1, AUTOPHOSPHORYLATION, ENZYME REGULATION.
  39. "p38 and a p38-interacting protein are critical for downregulation of E-cadherin during mouse gastrulation."
    Zohn I.E., Li Y., Skolnik E.Y., Anderson K.V., Han J., Niswander L.
    Cell 125:957-969(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SUPT20H.
  40. "p38 MAP kinase mediates stress-induced internalization of EGFR: implications for cancer chemotherapy."
    Zwang Y., Yarden Y.
    EMBO J. 25:4195-4206(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN STRESS-INDUCED INTERNALIZATION OF EGFR.
  41. Cited for: FUNCTION IN PHOSPHORYLATION OF SIAH2, ENZYME REGULATION.
  42. "Nuclear protein NP60 regulates p38 MAPK activity."
    Fu J., Yang Z., Wei J., Han J., Gu J.
    J. Cell Sci. 119:115-123(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NP60.
  43. "p38alpha antagonizes p38gamma activity through c-Jun-dependent ubiquitin-proteasome pathways in regulating Ras transformation and stress response."
    Qi X., Pohl N.M., Loesch M., Hou S., Li R., Qin J.Z., Cuenda A., Chen G.
    J. Biol. Chem. 282:31398-31408(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, UBIQUITINATION.
  44. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  45. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  46. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  47. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND TYR-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  48. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  49. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND TYR-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  50. "Coordinated regulation of autophagy by p38alpha MAPK through mAtg9 and p38IP."
    Webber J.L., Tooze S.A.
    EMBO J. 29:27-40(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INHIBITION OF AUTOPHAGY.
  51. "DNA damage activates a spatially distinct late cytoplasmic cell-cycle checkpoint network controlled by MK2-mediated RNA stabilization."
    Reinhardt H.C., Hasskamp P., Schmedding I., Morandell S., van Vugt M.A., Wang X., Linding R., Ong S.E., Weaver D., Carr S.A., Yaffe M.B.
    Mol. Cell 40:34-49(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF TIAR.
  52. "Direct activation of TACE-mediated ectodomain shedding by p38 MAP kinase regulates EGF receptor-dependent cell proliferation."
    Xu P., Derynck R.
    Mol. Cell 37:551-566(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ADAM17, FUNCTION IN PHOSPHORYLATION OF ADAM17.
  53. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-180 AND TYR-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  54. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  55. "Acetylation of a conserved lysine residue in the ATP binding pocket of p38 augments its kinase activity during hypertrophy of cardiomyocytes."
    Pillai V.B., Sundaresan N.R., Samant S.A., Wolfgeher D., Trivedi C.M., Gupta M.P.
    Mol. Cell. Biol. 31:2349-2363(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-53 AND LYS-152 BY KAT2B/PCAF AND EP300, DEACETYLATION BY HDAC3.
  56. "In the cellular garden of forking paths: how p38 MAPKs signal for downstream assistance."
    Shi Y., Gaestel M.
    Biol. Chem. 383:1519-1536(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  57. "Mechanisms and functions of p38 MAPK signalling."
    Cuadrado A., Nebreda A.R.
    Biochem. J. 429:403-417(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ENZYME REGULATION, REVIEW ON FUNCTION.
  58. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  59. "A highly specific inhibitor of human p38 MAP kinase binds in the ATP pocket."
    Tong L., Pav S., White D.M., Rogers S., Crane K.M., Cywin C.L., Brown M.L., Pargellis C.A.
    Nat. Struct. Biol. 4:311-316(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  60. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  61. "Binding mode of the 4-anilinoquinazoline class of protein kinase inhibitor: X-ray crystallographic studies of 4-anilinoquinazolines bound to cyclin-dependent kinase 2 and p38 kinase."
    Shewchuk L., Hassell A., Wisely B., Rocque W., Holmes W., Veal J., Kuyper L.F.
    J. Med. Chem. 43:133-138(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS).
  62. Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), ENZYME REGULATION.
  63. Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), ENZYME REGULATION.
  64. Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), ENZYME REGULATION.
  65. "Structural basis for p38alpha MAP kinase quinazolinone and pyridol-pyrimidine inhibitor specificity."
    Fitzgerald C.E., Patel S.B., Becker J.W., Cameron P.M., Zaller D., Pikounis V.B., O'Keefe S.J., Scapin G.
    Nat. Struct. Biol. 10:764-769(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
  66. "Lattice stabilization and enhanced diffraction in human p38 alpha crystals by protein engineering."
    Patel S.B., Cameron P.M., Frantz-Wattley B., O'Neill E., Becker J.W., Scapin G.
    Biochim. Biophys. Acta 1696:67-73(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), ENZYME REGULATION.
  67. Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-359 IN COMPLEX WITH INHIBITOR.
  68. Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-359, ENZYME REGULATION.
  69. Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), ENZYME REGULATION.
  70. Cited for: X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 2-359 IN COMPLEX WITH INHIBITOR.
  71. "Crystal structure of the p38 alpha-MAPKAP kinase 2 heterodimer."
    ter Haar E., Prabhakar P., Liu X., Lepre C.
    J. Biol. Chem. 282:9733-9739(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 2-359 IN COMPLEX WITH MAPKAPK2.
  72. Erratum
    ter Haar E., Prabhakar P., Liu X., Lepre C.
    J. Biol. Chem. 282:14684-14684(2007)
  73. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-51; ARG-322 AND GLY-343.

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 26, 2014
This is version 183 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

External Data

Dasty 3