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Q15759

- MK11_HUMAN

UniProt

Q15759 - MK11_HUMAN

Protein

Mitogen-activated protein kinase 11

Gene

MAPK11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 2 (20 Mar 2007)
      Previous versions | rss
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    Functioni

    Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK11 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. MAPK11 functions are mostly redundant with those of MAPK14. 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. 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. 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. Additional examples of p38 MAPK substrates are the 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.5 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by phosphorylation on threonine and tyrosine by MAP2K3/MKK3, MAP2K4/MKK4 and MAP2K6/MKK6. MAP2K3/MKK3 and MAP2K6/MKK6 are both essential for the activation of MAPK11 induced by environmental stress. HDAC3 interacts directly and selectively with MAPK11 to repress ATF2 transcriptional activity, and regulate TNF gene expression in LPS-stimulated cells. Inhibited by SB203580 and pyridinyl-imidazole related compounds.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei53 – 531ATPPROSITE-ProRule annotation
    Binding sitei71 – 711Nilotinib
    Active sitei150 – 1501Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi30 – 389ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. MAP kinase activity Source: UniProtKB
    3. protein binding Source: IntAct
    4. protein serine/threonine kinase activity Source: Reactome

    GO - Biological processi

    1. activation of MAPK activity Source: Reactome
    2. gene expression Source: Reactome
    3. innate immune response Source: Reactome
    4. intracellular signal transduction Source: UniProtKB
    5. mRNA metabolic process Source: Reactome
    6. muscle cell differentiation Source: Reactome
    7. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    8. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    9. neurotrophin TRK receptor signaling pathway Source: Reactome
    10. positive regulation of muscle cell differentiation Source: Reactome
    11. Ras protein signal transduction Source: Reactome
    12. regulation of sequence-specific DNA binding transcription factor activity Source: Reactome
    13. response to stress Source: UniProtKB
    14. RNA metabolic process Source: Reactome
    15. signal transduction Source: ProtInc
    16. stress-activated MAPK cascade Source: Reactome
    17. toll-like receptor 10 signaling pathway Source: Reactome
    18. toll-like receptor 2 signaling pathway Source: Reactome
    19. toll-like receptor 3 signaling pathway Source: Reactome
    20. toll-like receptor 4 signaling pathway Source: Reactome
    21. toll-like receptor 5 signaling pathway Source: Reactome
    22. toll-like receptor 9 signaling pathway Source: Reactome
    23. toll-like receptor signaling pathway Source: Reactome
    24. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    25. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    26. transcription, DNA-templated Source: UniProtKB-KW
    27. TRIF-dependent toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Stress response, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.24. 2681.
    ReactomeiREACT_12065. p38MAPK events.
    REACT_12599. ERK/MAPK targets.
    REACT_169436. Oxidative Stress Induced Senescence.
    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_25042. KSRP destabilizes mRNA.
    REACT_25299. DSCAM interactions.
    REACT_75776. NOD1/2 Signaling Pathway.
    SignaLinkiQ15759.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase 11 (EC:2.7.11.24)
    Short name:
    MAP kinase 11
    Short name:
    MAPK 11
    Alternative name(s):
    Mitogen-activated protein kinase p38 beta
    Short name:
    MAP kinase p38 beta
    Short name:
    p38b
    Stress-activated protein kinase 2b
    Short name:
    SAPK2b
    p38-2
    Gene namesi
    Name:MAPK11
    Synonyms:PRKM11, SAPK2, SAPK2B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:6873. MAPK11.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi180 – 1801T → A: Inactivation.
    Mutagenesisi182 – 1821Y → F: Inactivation.

    Organism-specific databases

    PharmGKBiPA30618.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 364364Mitogen-activated protein kinase 11PRO_0000186280Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei180 – 1801Phosphothreonine; by MAP2K3, MAP2K4 and MAP2K61 Publication
    Modified residuei182 – 1821Phosphotyrosine; by MAP2K3, MAP2K4 and MAP2K61 Publication
    Modified residuei323 – 3231Phosphotyrosine; by ZAP70By similarity

    Post-translational modificationi

    Dually phosphorylated on Thr-180 and Tyr-182 by MAP2K3/MKK3, MAP2K4/MKK4 and MAP2K6/MKK6, which activates the enzyme.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ15759.
    PRIDEiQ15759.

    PTM databases

    PhosphoSiteiQ15759.

    Expressioni

    Tissue specificityi

    Highest levels in the brain and heart. Also expressed in the placenta, lung, liver, skeletal muscle, kidney and pancreas.

    Gene expression databases

    ArrayExpressiQ15759.
    BgeeiQ15759.
    CleanExiHS_MAPK11.
    GenevestigatoriQ15759.

    Organism-specific databases

    HPAiCAB012961.

    Interactioni

    Subunit structurei

    Interacts with HDAC3 and DUSP16.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TP53P046372EBI-298304,EBI-366083
    ZNHIT1O432572EBI-298304,EBI-347522

    Protein-protein interaction databases

    BioGridi111586. 28 interactions.
    IntActiQ15759. 21 interactions.
    MINTiMINT-3032032.
    STRINGi9606.ENSP00000333685.

    Structurei

    Secondary structure

    1
    364
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 158
    Beta strandi17 – 215
    Beta strandi24 – 296
    Beta strandi31 – 333
    Turni34 – 374
    Beta strandi38 – 436
    Turni44 – 474
    Beta strandi48 – 547
    Helixi62 – 7716
    Beta strandi86 – 905
    Helixi96 – 983
    Beta strandi103 – 1075
    Beta strandi110 – 1123
    Helixi113 – 1197
    Helixi124 – 14320
    Helixi153 – 1553
    Beta strandi156 – 1583
    Beta strandi164 – 1663
    Helixi179 – 1824
    Helixi185 – 1884
    Helixi191 – 1944
    Helixi203 – 21816
    Helixi228 – 23912
    Helixi244 – 2496
    Turni253 – 2553
    Helixi256 – 2605
    Helixi270 – 2734
    Turni274 – 2763
    Helixi279 – 2857
    Turni286 – 2883
    Helixi293 – 2953
    Helixi299 – 3024
    Helixi306 – 3083
    Turni309 – 3113
    Helixi314 – 3163
    Helixi326 – 3294
    Helixi334 – 34714

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3GC8X-ray2.40A/B1-364[»]
    3GC9X-ray2.05A/B1-364[»]
    3GP0X-ray1.90A5-350[»]
    ProteinModelPortaliQ15759.
    SMRiQ15759. Positions 3-349.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15759.

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    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.
    HOGENOMiHOG000233024.
    HOVERGENiHBG014652.
    InParanoidiQ15759.
    KOiK04441.
    OMAiETIGGCE.
    OrthoDBiEOG7PCJGV.
    PhylomeDBiQ15759.
    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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15759-1) [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

    MSGPRAGFYR QELNKTVWEV PQRLQGLRPV GSGAYGSVCS AYDARLRQKV    50
    AVKKLSRPFQ SLIHARRTYR ELRLLKHLKH ENVIGLLDVF TPATSIEDFS 100
    EVYLVTTLMG ADLNNIVKCQ ALSDEHVQFL VYQLLRGLKY IHSAGIIHRD 150
    LKPSNVAVNE DCELRILDFG LARQADEEMT GYVATRWYRA PEIMLNWMHY 200
    NQTVDIWSVG CIMAELLQGK ALFPGSDYID QLKRIMEVVG TPSPEVLAKI 250
    SSEHARTYIQ SLPPMPQKDL SSIFRGANPL AIDLLGRMLV LDSDQRVSAA 300
    EALAHAYFSQ YHDPEDEPEA EPYDESVEAK ERTLEEWKEL TYQEVLSFKP 350
    PEPPKPPGSL EIEQ 364
    Length:364
    Mass (Da):41,357
    Last modified:March 20, 2007 - v2
    Checksum:i68DA4C7B7C721475
    GO
    Isoform 2 (identifier: Q15759-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-108: Missing.
         204-321: VDIWSVGCIM...HDPEDEPEAE → GAGGRPWGDE...GYLVRGLHHG
         322-364: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:213
    Mass (Da):23,603
    Checksum:iE3466E25BE1D27A3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti98 – 981D → V in BAF84534. (PubMed:14702039)Curated
    Sequence conflicti122 – 1232LS → GAHQGARLAL in AAB05036. (PubMed:8663524)Curated
    Sequence conflicti326 – 3261S → G in AAB66313. (PubMed:9235954)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti221 – 2211A → V in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication
    VAR_042264
    Natural varianti275 – 2751R → H.2 Publications
    Corresponds to variant rs33932986 [ dbSNP | Ensembl ].
    VAR_025176

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 108108Missing in isoform 2. 1 PublicationVSP_055221Add
    BLAST
    Alternative sequencei204 – 321118VDIWS…EPEAE → GAGGRPWGDEGQGPRLALDW LCMPGLRGQARSPRMWDPHS KVALQRPLEHDGCWPPLAVQ LWTSPCLGGLGMAEEGVCPS WGLDVTVGLLEEGRGVGTLM EVPSPSHSGYLVRGLHHG in isoform 2. 1 PublicationVSP_055222Add
    BLAST
    Alternative sequencei322 – 36443Missing in isoform 2. 1 PublicationVSP_055223Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U53442 mRNA. Translation: AAB05036.1.
    AF001008 mRNA. Translation: AAC51250.1.
    AF001174 mRNA. Translation: AAC51373.1.
    AF031135 mRNA. Translation: AAC12714.1.
    Y14440 mRNA. Translation: CAA74792.1.
    U92268 mRNA. Translation: AAB66313.1.
    CR456514 mRNA. Translation: CAG30400.1.
    DQ279722 Genomic DNA. Translation: ABB72677.1.
    AK291845 mRNA. Translation: BAF84534.1.
    AK299745 mRNA. Translation: BAH13116.1.
    EU332851 Genomic DNA. Translation: ABY87540.1.
    JX512451 Genomic DNA. Translation: AGC09598.1.
    AL022328 Genomic DNA. No translation available.
    CH471138 Genomic DNA. Translation: EAW73524.1.
    CH471138 Genomic DNA. Translation: EAW73525.1.
    CH471138 Genomic DNA. Translation: EAW73526.1.
    BC027933 mRNA. Translation: AAH27933.1.
    CCDSiCCDS14090.1. [Q15759-1]
    PIRiG02524.
    JC5529.
    RefSeqiNP_002742.3. NM_002751.6.
    UniGeneiHs.57732.

    Genome annotation databases

    EnsembliENST00000330651; ENSP00000333685; ENSG00000185386. [Q15759-1]
    ENST00000395764; ENSP00000379113; ENSG00000185386. [Q15759-1]
    GeneIDi5600.
    KEGGihsa:5600.
    UCSCiuc003bkr.3. human. [Q15759-1]

    Polymorphism databases

    DMDMi134047835.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U53442 mRNA. Translation: AAB05036.1 .
    AF001008 mRNA. Translation: AAC51250.1 .
    AF001174 mRNA. Translation: AAC51373.1 .
    AF031135 mRNA. Translation: AAC12714.1 .
    Y14440 mRNA. Translation: CAA74792.1 .
    U92268 mRNA. Translation: AAB66313.1 .
    CR456514 mRNA. Translation: CAG30400.1 .
    DQ279722 Genomic DNA. Translation: ABB72677.1 .
    AK291845 mRNA. Translation: BAF84534.1 .
    AK299745 mRNA. Translation: BAH13116.1 .
    EU332851 Genomic DNA. Translation: ABY87540.1 .
    JX512451 Genomic DNA. Translation: AGC09598.1 .
    AL022328 Genomic DNA. No translation available.
    CH471138 Genomic DNA. Translation: EAW73524.1 .
    CH471138 Genomic DNA. Translation: EAW73525.1 .
    CH471138 Genomic DNA. Translation: EAW73526.1 .
    BC027933 mRNA. Translation: AAH27933.1 .
    CCDSi CCDS14090.1. [Q15759-1 ]
    PIRi G02524.
    JC5529.
    RefSeqi NP_002742.3. NM_002751.6.
    UniGenei Hs.57732.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3GC8 X-ray 2.40 A/B 1-364 [» ]
    3GC9 X-ray 2.05 A/B 1-364 [» ]
    3GP0 X-ray 1.90 A 5-350 [» ]
    ProteinModelPortali Q15759.
    SMRi Q15759. Positions 3-349.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111586. 28 interactions.
    IntActi Q15759. 21 interactions.
    MINTi MINT-3032032.
    STRINGi 9606.ENSP00000333685.

    Chemistry

    BindingDBi Q15759.
    ChEMBLi CHEMBL3961.
    GuidetoPHARMACOLOGYi 1500.

    PTM databases

    PhosphoSitei Q15759.

    Polymorphism databases

    DMDMi 134047835.

    Proteomic databases

    PaxDbi Q15759.
    PRIDEi Q15759.

    Protocols and materials databases

    DNASUi 5600.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000330651 ; ENSP00000333685 ; ENSG00000185386 . [Q15759-1 ]
    ENST00000395764 ; ENSP00000379113 ; ENSG00000185386 . [Q15759-1 ]
    GeneIDi 5600.
    KEGGi hsa:5600.
    UCSCi uc003bkr.3. human. [Q15759-1 ]

    Organism-specific databases

    CTDi 5600.
    GeneCardsi GC22M050702.
    HGNCi HGNC:6873. MAPK11.
    HPAi CAB012961.
    MIMi 602898. gene.
    neXtProti NX_Q15759.
    PharmGKBi PA30618.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233024.
    HOVERGENi HBG014652.
    InParanoidi Q15759.
    KOi K04441.
    OMAi ETIGGCE.
    OrthoDBi EOG7PCJGV.
    PhylomeDBi Q15759.
    TreeFami TF105100.

    Enzyme and pathway databases

    BRENDAi 2.7.11.24. 2681.
    Reactomei REACT_12065. p38MAPK events.
    REACT_12599. ERK/MAPK targets.
    REACT_169436. Oxidative Stress Induced Senescence.
    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_25042. KSRP destabilizes mRNA.
    REACT_25299. DSCAM interactions.
    REACT_75776. NOD1/2 Signaling Pathway.
    SignaLinki Q15759.

    Miscellaneous databases

    EvolutionaryTracei Q15759.
    GeneWikii MAPK11.
    GenomeRNAii 5600.
    NextBioi 21748.
    PROi Q15759.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15759.
    Bgeei Q15759.
    CleanExi HS_MAPK11.
    Genevestigatori Q15759.

    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. "Characterization of the structure and function of a new mitogen-activated protein kinase (p38beta)."
      Jiang Y., Chen C., Li Z., Guo W., Gegner J.A., Lin S., Han J.
      J. Biol. Chem. 271:17920-17926(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. Jiang Y., Han J.
      Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Novel homologues of CSBP/p38 MAP kinase: activation, substrate specificity and sensitivity to inhibition by pyridinyl imidazoles."
      Kumar S., McDonnell P.C., Gum R.J., Hand A.T., Lee J.C., Young P.R.
      Biochem. Biophys. Res. Commun. 235:533-538(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    4. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN PHOSPHORYLATION OF ATF2; ELK1 AND MBP, ENZYME REGULATION.
      Tissue: Brain.
    5. "Activation of the novel stress-activated protein kinase SAPK4 by cytokines and cellular stresses is mediated by SKK3 (MKK6); comparison of its substrate specificity with that of other SAP kinases."
      Goedert M., Cuenda A., Craxton M., Jakes R., Cohen P.
      EMBO J. 16:3563-3571(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME REGULATION.
    6. "p38-2, a novel mitogen-activated protein kinase with distinct properties."
      Stein B., Yang M.X., Young D.B., Janknecht R., Hunter T., Murray B.W., Barbosa M.S.
      J. Biol. Chem. 272:19509-19517(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    8. "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] (ISOFORMS 1 AND 2).
      Tissue: Brain.
    9. NIEHS SNPs program
      Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-275.
    10. NHLBI resequencing and genotyping service (RS&G)
      Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    11. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [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 1).
      Tissue: Brain.
    14. "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.
    15. "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.
    16. "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.
    17. "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.
    18. "Histone deacetylase 3, a class I histone deacetylase, suppresses MAPK11-mediated activating transcription factor-2 activation and represses TNF gene expression."
      Mahlknecht U., Will J., Varin A., Hoelzer D., Herbein G.
      J. Immunol. 173:3979-3990(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HDAC3, PHOSPHORYLATION, ENZYME REGULATION, FUNCTION IN ATF2 ACTIVATION.
    19. "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.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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.
    22. "The three-dimensional structure of MAP kinase p38beta: different features of the ATP-binding site in p38beta compared with p38alpha."
      Patel S.B., Cameron P.M., O'Keefe S.J., Frantz-Wattley B., Thompson J., O'Neill E.A., Tennis T., Liu L., Becker J.W., Scapin G.
      Acta Crystallogr. D 65:777-785(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
    23. "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-221 AND HIS-275.

    Entry informationi

    Entry nameiMK11_HUMAN
    AccessioniPrimary (citable) accession number: Q15759
    Secondary accession number(s): A8K730
    , B0LPG1, B7Z630, E7ETQ1, L7RT27, O00284, O15472, Q2XNF2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: March 20, 2007
    Last modified: October 1, 2014
    This is version 159 of the entry and version 2 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, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: 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