Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q16539

- MK14_HUMAN

UniProt

Q16539 - MK14_HUMAN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 181 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Magnesium.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 binding Source: IntAct
    6. 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. negative regulation of canonical Wnt signaling pathway Source: Ensembl
    27. neurotrophin TRK receptor signaling pathway Source: Reactome
    28. osteoclast differentiation Source: BHF-UCL
    29. p38MAPK cascade Source: UniProtKB
    30. peptidyl-serine phosphorylation Source: BHF-UCL
    31. platelet activation Source: Reactome
    32. positive regulation of erythrocyte differentiation Source: Ensembl
    33. positive regulation of muscle cell differentiation Source: Reactome
    34. positive regulation of myoblast differentiation Source: UniProtKB
    35. positive regulation of myoblast fusion Source: UniProtKB
    36. positive regulation of myotube differentiation Source: UniProtKB
    37. positive regulation of protein import into nucleus Source: Ensembl
    38. positive regulation of reactive oxygen species metabolic process Source: BHF-UCL
    39. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    40. Ras protein signal transduction Source: Reactome
    41. regulation of sequence-specific DNA binding transcription factor activity Source: Reactome
    42. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    43. response to muramyl dipeptide Source: Ensembl
    44. RNA metabolic process Source: Reactome
    45. signal transduction Source: ProtInc
    46. signal transduction in response to DNA damage Source: BHF-UCL
    47. skeletal muscle tissue development Source: Ensembl
    48. stress-activated MAPK cascade Source: Reactome
    49. stress-induced premature senescence Source: BHF-UCL
    50. striated muscle cell differentiation Source: Ensembl
    51. toll-like receptor 10 signaling pathway Source: Reactome
    52. toll-like receptor 2 signaling pathway Source: Reactome
    53. toll-like receptor 3 signaling pathway Source: Reactome
    54. toll-like receptor 4 signaling pathway Source: Reactome
    55. toll-like receptor 5 signaling pathway Source: Reactome
    56. toll-like receptor 9 signaling pathway Source: Reactome
    57. toll-like receptor signaling pathway Source: Reactome
    58. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    59. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    60. transcription, DNA-templated Source: UniProtKB-KW
    61. transmembrane receptor protein serine/threonine kinase signaling pathway Source: Ensembl
    62. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
    63. vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL

    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_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

    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

    ArrayExpressiQ16539.
    BgeeiQ16539.
    CleanExiHS_MAPK14.
    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. 149 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 – 136
    Beta strandi16 – 216
    Beta strandi24 – 296
    Helixi31 – 333
    Turni34 – 363
    Beta strandi38 – 436
    Turni44 – 474
    Beta strandi48 – 547
    Helixi62 – 7716
    Beta strandi87 – 904
    Helixi96 – 983
    Beta strandi103 – 1075
    Beta strandi110 – 1123
    Turni113 – 1153
    Turni116 – 1194
    Helixi124 – 14320
    Helixi153 – 1553
    Beta strandi156 – 1583
    Turni160 – 1623
    Beta strandi164 – 1663
    Beta strandi168 – 1703
    Helixi173 – 1753
    Helixi177 – 1793
    Beta strandi180 – 1823
    Turni185 – 1884
    Helixi191 – 1944
    Beta strandi197 – 1993
    Helixi204 – 21815
    Helixi228 – 23912
    Helixi244 – 2474
    Helixi253 – 2608
    Helixi270 – 2734
    Turni274 – 2763
    Helixi279 – 28810
    Helixi293 – 2953
    Helixi299 – 3035
    Helixi306 – 3083
    Turni309 – 3113
    Helixi314 – 3163
    Helixi325 – 3273
    Helixi334 – 34714

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOVERGENiHBG014652.
    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_dom.
    [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 (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 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

    MSQERPTFYR QELNKTIWEV PERYQNLSPV GSGAYGSVCA AFDTKTGLRV    50
    AVKKLSRPFQ SIIHAKRTYR ELRLLKHMKH ENVIGLLDVF TPARSLEEFN 100
    DVYLVTHLMG ADLNNIVKCQ KLTDDHVQFL IYQILRGLKY IHSADIIHRD 150
    LKPSNLAVNE DCELKILDFG LARHTDDEMT GYVATRWYRA PEIMLNWMHY 200
    NQTVDIWSVG CIMAELLTGR TLFPGTDHID QLKLILRLVG TPGAELLKKI 250
    SSESARNYIQ SLTQMPKMNF ANVFIGANPL AVDLLEKMLV LDSDKRITAA 300
    QALAHAYFAQ YHDPDDEPVA DPYDQSFESR DLLIDEWKSL TYDEVISFVP 350
    PPLDQEEMES 360
    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

    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 – 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:
    EMBL
    GenBank
    DDBJ
    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.
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 149 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.
    HOVERGENi HBG014652.
    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_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

    ArrayExpressi Q16539.
    Bgeei Q16539.
    CleanExi HS_MAPK14.
    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_dom.
    [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

    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. "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].
    7. "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).
    8. "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).
    9. NHLBI resequencing and genotyping service (RS&G)
      Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    10. "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].
    11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. "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.
    13. "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.
    14. "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.
    15. "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.
    16. "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.
    17. "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.
    18. "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.
    19. "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.
    20. "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.
    21. "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.
    22. "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.
    23. "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.
    24. "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.
    25. "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.
    26. "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.
    27. "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.
    28. "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.
    29. "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.
    30. "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.
    31. "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.
    32. "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.
    33. "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.
    34. "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.
    35. "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].
    36. "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.
    37. "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.
    38. "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.
    39. "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.
    40. Cited for: FUNCTION IN PHOSPHORYLATION OF SIAH2, ENZYME REGULATION.
    41. "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.
    42. "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.
    43. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    44. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    45. "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.
    46. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND TYR-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    47. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    48. "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.
    49. "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.
    50. "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.
    51. "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.
    52. "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.
    53. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    54. "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.
    55. "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.
    56. "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.
    57. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
    58. "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).
    59. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    60. "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).
    61. Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS), ENZYME REGULATION.
    62. Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), ENZYME REGULATION.
    63. Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS), ENZYME REGULATION.
    64. "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.
    65. "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.
    66. Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-359 IN COMPLEX WITH INHIBITOR.
    67. Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-359, ENZYME REGULATION.
    68. Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), ENZYME REGULATION.
    69. Cited for: X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) OF 2-359 IN COMPLEX WITH INHIBITOR.
    70. "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.
    71. Erratum
      ter Haar E., Prabhakar P., Liu X., Lepre C.
      J. Biol. Chem. 282:14684-14684(2007)
    72. "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, O60776, Q13083, Q14084, Q8TDX0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 181 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