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P47811

- MK14_MOUSE

UniProt

P47811 - MK14_MOUSE

Protein

Mitogen-activated protein kinase 14

Gene

Mapk14

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 3 (23 Jan 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. MAPK14 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. RPS6KA5/MSK1 and RPS6KA4/MSK2 can directly phosphorylate and activate transcription factors such as CREB1, ATF1, the NF-kappa-B isoform RELA/NFKB3, STAT1 and STAT3, but can also phosphorylate histone H3 and the nucleosomal protein HMGN1. RPS6KA5/MSK1 and RPS6KA4/MSK2 play important roles in the rapid induction of immediate-early genes in response to stress or mitogenic stimuli, either by inducing chromatin remodeling or by recruiting the transcription machinery. On the other hand, two other kinase targets, MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control of gene expression mostly at the post-transcriptional level, by phosphorylating ZFP36 (tristetraprolin) and ELAVL1, and by regulating EEF2K, which is important for the elongation of mRNA during translation. MKNK1/MNK1 and MKNK2/MNK2, two other kinases activated by p38 MAPKs, regulate protein synthesis by phosphorylating the initiation factor EIF4E2. MAPK14 interacts also with casein kinase II, leading to its activation through autophosphorylation and further phosphorylation of TP53/p53. In the cytoplasm, the p38 MAPK pathway is an important regulator of protein turnover. For example, CFLAR is an inhibitor of TNF-induced apoptosis whose proteasome-mediated degradation is regulated by p38 MAPK phosphorylation. In a similar way, MAPK14 phosphorylates the ubiquitin ligase SIAH2, regulating its activity towards EGLN3. MAPK14 may also inhibit the lysosomal degradation pathway of autophagy by interfering with the intracellular trafficking of the transmembrane protein ATG9. Another function of MAPK14 is to regulate the endocytosis of membrane receptors by different mechanisms that impinge on the small GTPase RAB5A. In addition, clathrin-mediated EGFR internalization induced by inflammatory cytokines and UV irradiation depends on MAPK14-mediated phosphorylation of EGFR itself as well as of RAB5A effectors. Ectodomain shedding of transmembrane proteins is regulated by p38 MAPKs as well. In response to inflammatory stimuli, p38 MAPKs phosphorylate the membrane-associated metalloprotease ADAM17. Such phosphorylation is required for ADAM17-mediated ectodomain shedding of TGF-alpha family ligands, which results in the activation of EGFR signaling and cell proliferation. Another p38 MAPK substrate is FGFR1. FGFR1 can be translocated from the extracellular space into the cytosol and nucleus of target cells, and regulates processes such as rRNA synthesis and cell growth. FGFR1 translocation requires p38 MAPK activation. In the nucleus, many transcription factors are phosphorylated and activated by p38 MAPKs in response to different stimuli. Classical examples include ATF1, ATF2, ATF6, ELK1, PTPRH, DDIT3, TP53/p53 and MEF2C and MEF2A. The p38 MAPKs are emerging as important modulators of gene expression by regulating chromatin modifiers and remodelers. The promoters of several genes involved in the inflammatory response, such as IL6, IL8 and IL12B, display a p38 MAPK-dependent enrichment of histone H3 phosphorylation on 'Ser-10' (H3S10ph) in LPS-stimulated myeloid cells. This phosphorylation enhances the accessibility of the cryptic NF-kappa-B-binding sites marking promoters for increased NF-kappa-B recruitment. Phosphorylates CDC25B and CDC25C which is required for binding to 14-3-3 proteins and leads to initiation of a G2 delay after ultraviolet radiation. Phosphorylates TIAR following DNA damage, releasing TIAR from GADD45A mRNA and preventing mRNA degradation. The p38 MAPKs may also have kinase-independent roles, which are thought to be due to the binding to targets in the absence of phosphorylation. Protein O-Glc-N-acylation catalyzed by the OGT is regulated by MAPK14, and, although OGT does not seem to be phosphorylated by MAPK14, their interaction increases upon MAPK14 activation induced by glucose deprivation. This interaction may regulate OGT activity by recruiting it to specific targets such as neurofilament H, stimulating its O-Glc-N-acylation. Required in mid-fetal development for the growth of embryo-derived blood vessels in the labyrinth layer of the placenta. Also plays an essential role in developmental and stress-induced erythropoiesis, through regulation of EPO gene expression. Phosphorylates S100A9 at 'Thr-113' By similarity.By similarity

    Catalytic activityi

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

    Cofactori

    Magnesium.

    Enzyme regulationi

    Activated by cell stresses such as DNA damage, heat shock, osmotic shock, anisomycin and sodium arsenite, as well as pro-inflammatory stimuli such as bacterial lipopolysaccharide (LPS) and interleukin-1. Activation occurs through dual phosphorylation of Thr-180 and Tyr-182 by either of two dual specificity kinases, MAP2K3/MKK3 or MAP2K6/MKK6, and potentially also MAP2K4/MKK4, as well as by TAB1-mediated autophosphorylation. MAPK14 phosphorylated on both Thr-180 and Tyr-182 is 10-20-fold more active than MAPK14 phosphorylated only on Thr-180, whereas MAPK14 phosphorylated on Tyr-182 alone is inactive. whereas Thr-180 is necessary for catalysis, Tyr-182 may be required for auto-activation and substrate recognition. Phosphorylated at Tyr-323 by ZAP70 in an alternative activation pathway in response to TCR signaling in T-cells. This alternative pathway is inhibited by GADD45A. Inhibited by dual specificity phosphatases, such as DUSP1, DUSP10, and DUSP16. Specifically inhibited by the binding of pyridinyl-imidazole compounds, which are cytokine-suppressive anti-inflammatory drugs (CSAID). SB203580 is an inhibitor of MAPK14.3 Publications

    Kineticsi

    1. KM=212 µM for ATP (when both Thr-180 and Tyr-182 are phosphorylated)1 Publication
    2. KM=1669 µM for ATP (when only Thr-180 is phosphorylated)1 Publication
    3. KM=656 µM for EGFR peptide as a substrate (when both Thr-180 and Tyr-182 are phosphorylated)1 Publication
    4. KM=2800 µM for EGFR peptide as a substrate (when only Thr-180 is phosphorylated)1 Publication
    5. KM=2.03 µM for ATF2 as a substrate (when both Thr-180 and Tyr-182 are phosphorylated)1 Publication
    6. KM=20.1 µM for ATF2 as a substrate (when only Thr-180 is phosphorylated)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei32 – 321Inhibitor2 Publications
    Binding sitei35 – 351Inhibitor2 Publications
    Binding sitei53 – 531ATPPROSITE-ProRule annotation
    Binding sitei53 – 531Inhibitor2 Publications
    Binding sitei71 – 711Inhibitor2 Publications
    Binding sitei109 – 1091Inhibitor; via amide nitrogen and carbonyl oxygen2 Publications
    Binding sitei111 – 1111Inhibitor; via amide nitrogen2 Publications
    Active sitei168 – 1681Proton acceptorPROSITE-ProRule annotation
    Binding sitei168 – 1681Inhibitor2 Publications
    Binding sitei169 – 1691Inhibitor; via carbonyl oxygen2 Publications

    Regions

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

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. kinase activity Source: MGI
    3. MAP kinase activity Source: UniProtKB
    4. NFAT protein binding Source: BHF-UCL
    5. protein binding Source: IntAct
    6. protein kinase activity Source: MGI
    7. protein serine/threonine kinase activity Source: MGI

    GO - Biological processi

    1. angiogenesis Source: MGI
    2. apoptotic process Source: UniProtKB-KW
    3. cartilage condensation Source: AgBase
    4. cell morphogenesis Source: MGI
    5. cellular response to DNA damage stimulus Source: MGI
    6. cellular response to ionizing radiation Source: Ensembl
    7. cellular response to lipopolysaccharide Source: MGI
    8. cellular response to vascular endothelial growth factor stimulus Source: Ensembl
    9. chondrocyte differentiation Source: AgBase
    10. DNA damage checkpoint Source: MGI
    11. fatty acid oxidation Source: MGI
    12. glucose metabolic process Source: MGI
    13. intracellular signal transduction Source: UniProtKB
    14. lipopolysaccharide-mediated signaling pathway Source: MGI
    15. myoblast differentiation involved in skeletal muscle regeneration Source: MGI
    16. negative regulation of canonical Wnt signaling pathway Source: AgBase
    17. osteoclast differentiation Source: BHF-UCL
    18. p38MAPK cascade Source: UniProtKB
    19. peptidyl-serine phosphorylation Source: BHF-UCL
    20. positive regulation of erythrocyte differentiation Source: MGI
    21. positive regulation of myoblast differentiation Source: UniProtKB
    22. positive regulation of myoblast fusion Source: UniProtKB
    23. positive regulation of myotube differentiation Source: UniProtKB
    24. positive regulation of protein import into nucleus Source: MGI
    25. positive regulation of reactive oxygen species metabolic process Source: Ensembl
    26. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    27. protein phosphorylation Source: MGI
    28. regulation of transcription, DNA-templated Source: MGI
    29. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    30. response to lipopolysaccharide Source: MGI
    31. response to muramyl dipeptide Source: MGI
    32. signal transduction in response to DNA damage Source: Ensembl
    33. skeletal muscle tissue development Source: MGI
    34. stress-induced premature senescence Source: Ensembl
    35. striated muscle cell differentiation Source: MGI
    36. transcription, DNA-templated Source: UniProtKB-KW
    37. transmembrane receptor protein serine/threonine kinase signaling pathway Source: MGI
    38. vascular endothelial growth factor receptor signaling pathway Source: Ensembl

    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

    BRENDAi2.7.11.24. 3474.
    ReactomeiREACT_188970. Oxidative Stress Induced Senescence.
    REACT_198696. KSRP destabilizes mRNA.
    REACT_204811. Activation of the AP-1 family of transcription factors.
    REACT_205688. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
    REACT_207601. p38MAPK events.
    REACT_211125. NOD1/2 Signaling Pathway.
    REACT_215063. ERK/MAPK targets.
    SABIO-RKP47811.

    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):
    CRK1
    Mitogen-activated protein kinase p38 alpha
    Short name:
    MAP kinase p38 alpha
    Gene namesi
    Name:Mapk14
    Synonyms:Crk1, Csbp1, Csbp2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:1346865. Mapk14.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cell Source: MGI
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: MGI
    4. mitochondrion Source: MGI
    5. nucleus Source: UniProtKB
    6. spindle pole Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi180 – 1801T → A: Phosphorylation blocked. 1 Publication
    Mutagenesisi182 – 1821Y → F: Phosphorylation blocked. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 360359Mitogen-activated protein kinase 14PRO_0000186292Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei2 – 21PhosphoserineBy similarity
    Modified residuei16 – 161PhosphothreonineBy similarity
    Modified residuei53 – 531N6-acetyllysineBy similarity
    Modified residuei152 – 1521N6-acetyllysineBy similarity
    Modified residuei180 – 1801Phosphothreonine; alternate4 Publications
    Modified residuei180 – 1801Phosphothreonine; by MAP2K3, MAP2K4, MAP2K6 and autocatalysis; alternateBy similarity
    Modified residuei182 – 1821Phosphotyrosine; alternate4 Publications
    Modified residuei182 – 1821Phosphotyrosine; by MAP2K3, MAP2K4, MAP2K6 and autocatalysis; alternateBy similarity
    Modified residuei323 – 3231Phosphotyrosine; by ZAP70By similarity

    Post-translational modificationi

    Dually phosphorylated on Thr-180 and Tyr-182 by the MAP2Ks MAP2K3/MKK3, MAP2K4/MKK4 and MAP2K6/MKK6 in response to inflammatory cytokines, environmental stress or growth factors, which activates the enzyme. Dual phosphorylation can also be mediated by TAB1-mediated autophosphorylation. TCR engagement in T-cells also leads to Tyr-323 phosphorylation by ZAP70. Dephosphorylated and inactivated by DUPS1, DUSP10 and DUSP16.5 Publications
    Acetylated at Lys-53 and Lys-152 by KAT2B and EP300. Acetylation at Lys-53 increases the affinity for ATP and enhances kinase activity. Lys-53 and Lys-152 are deacetylated by HDAC3 By similarity.By similarity
    Ubiquitinated. Ubiquitination leads to degradation by the proteasome pathway By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP47811.
    PaxDbiP47811.
    PRIDEiP47811.

    PTM databases

    PhosphoSiteiP47811.

    Expressioni

    Tissue specificityi

    Macrophages, monocytes, T- and B-lymphocytes. Isoform 2 is specifically expressed in kidney and liver.

    Gene expression databases

    ArrayExpressiP47811.
    BgeeiP47811.
    CleanExiMM_MAPK14.
    GenevestigatoriP47811.

    Interactioni

    Subunit structurei

    Binds to a kinase interaction motif within the protein tyrosine phosphatase, PTPRR. This interaction retains MAPK14 in the cytoplasm and prevents nuclear accumulation. Interacts with SPAG9, SUPT20H and GADD45A. Interacts with CDC25B, CDC25C, DUSP1, DUSP10, DUSP16, NP60 and TAB1 By similarity. Interacts with casein kinase II subunits CSNK2A1 and CSNK2B By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DUSP9Q999562EBI-298727,EBI-3906678From a different organism.
    Lcp1Q612335EBI-298727,EBI-309345
    Mapk11Q9WUI110EBI-298727,EBI-645081
    Mapkapk2P491382EBI-298727,EBI-298776
    Slc12a2P550122EBI-298727,EBI-621078
    Stk39Q9Z1W92EBI-298727,EBI-444764

    Protein-protein interaction databases

    BioGridi204969. 20 interactions.
    DIPiDIP-31073N.
    IntActiP47811. 26 interactions.
    MINTiMINT-1204448.
    STRINGi10090.ENSMUSP00000004990.

    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 – 329
    Beta strandi34 – 4310
    Turni44 – 474
    Beta strandi48 – 5710
    Helixi62 – 7716
    Beta strandi87 – 904
    Helixi96 – 983
    Beta strandi103 – 1075
    Beta strandi111 – 1133
    Helixi114 – 1196
    Helixi124 – 14320
    Helixi153 – 1553
    Beta strandi156 – 1583
    Beta strandi164 – 1663
    Beta strandi172 – 1754
    Beta strandi176 – 1827
    Helixi185 – 1884
    Helixi191 – 1933
    Beta strandi197 – 1993
    Helixi204 – 21815
    Helixi228 – 23912
    Helixi244 – 2474
    Helixi253 – 2608
    Helixi270 – 2734
    Turni274 – 2763
    Helixi279 – 28810
    Turni293 – 2953
    Helixi299 – 3035
    Helixi306 – 3083
    Turni309 – 3113
    Helixi314 – 3163
    Helixi326 – 3294
    Helixi334 – 34613

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LEWX-ray2.30A13-360[»]
    1LEZX-ray2.30A1-360[»]
    1P38X-ray2.10A1-360[»]
    1YW2X-ray2.01A1-360[»]
    1YWRX-ray1.95A1-360[»]
    2EWAX-ray2.10A1-360[»]
    2GHLX-ray2.10A5-352[»]
    2GHMX-ray2.35A5-352[»]
    2GTMX-ray1.90A5-352[»]
    2GTNX-ray1.80A5-352[»]
    2OZAX-ray2.70B2-360[»]
    2PUUX-ray2.50A5-352[»]
    3P4KX-ray2.30A1-360[»]
    3P5KX-ray2.09A2-360[»]
    3P78X-ray2.30A2-360[»]
    3P79X-ray2.10A2-360[»]
    3P7AX-ray2.31A2-360[»]
    3P7BX-ray1.90A2-360[»]
    3P7CX-ray2.30A2-360[»]
    3PY3X-ray2.10A1-360[»]
    3TG1X-ray2.71A1-360[»]
    4KA3X-ray2.71A1-360[»]
    4LOOX-ray1.95A1-360[»]
    4LOPX-ray2.05A/B/C/D1-360[»]
    4LOQX-ray2.32A/B/C/D1-360[»]
    ProteinModelPortaliP47811.
    SMRiP47811. Positions 5-353.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP47811.

    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 – 1116Inhibitor-binding

    Motif

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

    Domaini

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

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00550000074271.
    HOVERGENiHBG014652.
    InParanoidiB2KF38.
    KOiK04441.
    OMAiCSEREKY.
    PhylomeDBiP47811.
    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 1 (identifier: P47811-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSQERPTFYR QELNKTIWEV PERYQNLSPV GSGAYGSVCA AFDTKTGHRV    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 SLAQMPKMNF ANVFIGANPL AVDLLEKMLV LDSDKRITAA 300
    QALAHAYFAQ YHDPDDEPVA DPYDQSFESR DLLIDEWKSL TYDEVISFVP 350
    PPLDQEEMES 360
    Length:360
    Mass (Da):41,287
    Last modified:January 23, 2007 - v3
    Checksum:iDFB03EBCE97BB51A
    GO
    Isoform 2 (identifier: P47811-2) [UniParc]FASTAAdd to Basket

    Also known as: Piccolo

    The sequence of this isoform differs from the canonical sequence as follows:
         255-278: ARNYIQSLAQMPKMNFANVFIGAN → DAK
         279-360: Missing.

    Show »
    Length:257
    Mass (Da):29,540
    Checksum:iABDF65DC32AF0387
    GO
    Isoform 3 (identifier: P47811-3) [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):41,487
    Checksum:iF1F20352F76590BD
    GO
    Isoform 4 (identifier: P47811-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-77: Missing.

    Show »
    Length:284
    Mass (Da):32,458
    Checksum:iEF6828D872F4AC30
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti98 – 981E → G in AAF06348. 1 PublicationCurated
    Sequence conflicti107 – 1082HL → LS in AAF06348. 1 PublicationCurated
    Sequence conflicti115 – 1151N → R in AAF06348. 1 PublicationCurated
    Sequence conflicti124 – 1241D → G in AAF06348. 1 PublicationCurated
    Sequence conflicti159 – 1624NEDC → TQVI in AAF06348. 1 PublicationCurated
    Sequence conflicti166 – 1661I → L in AAF06348. 1 PublicationCurated
    Sequence conflicti202 – 2021Q → R in AAF06348. 1 PublicationCurated
    Sequence conflicti211 – 2122CI → GF in AAF06348. 1 PublicationCurated
    Sequence conflicti224 – 2241P → L in AAF06348. 1 PublicationCurated
    Sequence conflicti271 – 2711A → P in AAF06348. 1 PublicationCurated
    Sequence conflicti299 – 2991A → V in AAF06348. 1 PublicationCurated
    Sequence conflicti315 – 3151D → Y in AAF06348. 1 PublicationCurated
    Isoform 3 (identifier: P47811-3)
    Sequence conflicti238 – 2381L → M in BAA19741. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 7776Missing in isoform 4. 1 PublicationVSP_022359Add
    BLAST
    Alternative sequencei230 – 25425DQLKL…ISSES → NQLQQIMRLTGTPPAYLINR MPSHE in isoform 3. 3 PublicationsVSP_007544Add
    BLAST
    Alternative sequencei255 – 27824ARNYI…FIGAN → DAK in isoform 2. 1 PublicationVSP_004846Add
    BLAST
    Alternative sequencei279 – 36082Missing in isoform 2. 1 PublicationVSP_007545Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10871 mRNA. Translation: AAA20888.1.
    D83073 mRNA. Translation: BAA19741.1.
    AF128892 mRNA. Translation: AAF34818.1.
    AK151348 mRNA. Translation: BAE30324.1.
    AK153025 mRNA. Translation: BAE31659.1.
    AK089059 mRNA. Translation: BAC40726.1.
    AK133684 mRNA. Translation: BAE21782.1.
    CT009661 Genomic DNA. Translation: CAQ52036.1.
    CT009661 Genomic DNA. Translation: CAQ52037.1.
    BC012235 mRNA. Translation: AAH12235.1.
    AF195850 mRNA. Translation: AAF06348.1.
    X65067 mRNA. Translation: CAA46200.1.
    CCDSiCCDS28583.1. [P47811-1]
    CCDS50048.1. [P47811-3]
    PIRiI49066.
    RefSeqiNP_001161980.1. NM_001168508.1. [P47811-3]
    NP_001161985.1. NM_001168513.1.
    NP_001161986.1. NM_001168514.1.
    NP_036081.1. NM_011951.3. [P47811-1]
    UniGeneiMm.311337.

    Genome annotation databases

    EnsembliENSMUST00000004990; ENSMUSP00000004990; ENSMUSG00000053436. [P47811-3]
    ENSMUST00000062694; ENSMUSP00000061958; ENSMUSG00000053436. [P47811-1]
    ENSMUST00000114752; ENSMUSP00000110400; ENSMUSG00000053436.
    ENSMUST00000114754; ENSMUSP00000110402; ENSMUSG00000053436.
    GeneIDi26416.
    KEGGimmu:26416.
    UCSCiuc008brl.2. mouse. [P47811-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U10871 mRNA. Translation: AAA20888.1 .
    D83073 mRNA. Translation: BAA19741.1 .
    AF128892 mRNA. Translation: AAF34818.1 .
    AK151348 mRNA. Translation: BAE30324.1 .
    AK153025 mRNA. Translation: BAE31659.1 .
    AK089059 mRNA. Translation: BAC40726.1 .
    AK133684 mRNA. Translation: BAE21782.1 .
    CT009661 Genomic DNA. Translation: CAQ52036.1 .
    CT009661 Genomic DNA. Translation: CAQ52037.1 .
    BC012235 mRNA. Translation: AAH12235.1 .
    AF195850 mRNA. Translation: AAF06348.1 .
    X65067 mRNA. Translation: CAA46200.1 .
    CCDSi CCDS28583.1. [P47811-1 ]
    CCDS50048.1. [P47811-3 ]
    PIRi I49066.
    RefSeqi NP_001161980.1. NM_001168508.1. [P47811-3 ]
    NP_001161985.1. NM_001168513.1.
    NP_001161986.1. NM_001168514.1.
    NP_036081.1. NM_011951.3. [P47811-1 ]
    UniGenei Mm.311337.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LEW X-ray 2.30 A 13-360 [» ]
    1LEZ X-ray 2.30 A 1-360 [» ]
    1P38 X-ray 2.10 A 1-360 [» ]
    1YW2 X-ray 2.01 A 1-360 [» ]
    1YWR X-ray 1.95 A 1-360 [» ]
    2EWA X-ray 2.10 A 1-360 [» ]
    2GHL X-ray 2.10 A 5-352 [» ]
    2GHM X-ray 2.35 A 5-352 [» ]
    2GTM X-ray 1.90 A 5-352 [» ]
    2GTN X-ray 1.80 A 5-352 [» ]
    2OZA X-ray 2.70 B 2-360 [» ]
    2PUU X-ray 2.50 A 5-352 [» ]
    3P4K X-ray 2.30 A 1-360 [» ]
    3P5K X-ray 2.09 A 2-360 [» ]
    3P78 X-ray 2.30 A 2-360 [» ]
    3P79 X-ray 2.10 A 2-360 [» ]
    3P7A X-ray 2.31 A 2-360 [» ]
    3P7B X-ray 1.90 A 2-360 [» ]
    3P7C X-ray 2.30 A 2-360 [» ]
    3PY3 X-ray 2.10 A 1-360 [» ]
    3TG1 X-ray 2.71 A 1-360 [» ]
    4KA3 X-ray 2.71 A 1-360 [» ]
    4LOO X-ray 1.95 A 1-360 [» ]
    4LOP X-ray 2.05 A/B/C/D 1-360 [» ]
    4LOQ X-ray 2.32 A/B/C/D 1-360 [» ]
    ProteinModelPortali P47811.
    SMRi P47811. Positions 5-353.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204969. 20 interactions.
    DIPi DIP-31073N.
    IntActi P47811. 26 interactions.
    MINTi MINT-1204448.
    STRINGi 10090.ENSMUSP00000004990.

    Chemistry

    BindingDBi P47811.
    ChEMBLi CHEMBL2336.

    PTM databases

    PhosphoSitei P47811.

    Proteomic databases

    MaxQBi P47811.
    PaxDbi P47811.
    PRIDEi P47811.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000004990 ; ENSMUSP00000004990 ; ENSMUSG00000053436 . [P47811-3 ]
    ENSMUST00000062694 ; ENSMUSP00000061958 ; ENSMUSG00000053436 . [P47811-1 ]
    ENSMUST00000114752 ; ENSMUSP00000110400 ; ENSMUSG00000053436 .
    ENSMUST00000114754 ; ENSMUSP00000110402 ; ENSMUSG00000053436 .
    GeneIDi 26416.
    KEGGi mmu:26416.
    UCSCi uc008brl.2. mouse. [P47811-1 ]

    Organism-specific databases

    CTDi 1432.
    MGIi MGI:1346865. Mapk14.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00550000074271.
    HOVERGENi HBG014652.
    InParanoidi B2KF38.
    KOi K04441.
    OMAi CSEREKY.
    PhylomeDBi P47811.
    TreeFami TF105100.

    Enzyme and pathway databases

    BRENDAi 2.7.11.24. 3474.
    Reactomei REACT_188970. Oxidative Stress Induced Senescence.
    REACT_198696. KSRP destabilizes mRNA.
    REACT_204811. Activation of the AP-1 family of transcription factors.
    REACT_205688. Activation of PPARGC1A (PGC-1alpha) by phosphorylation.
    REACT_207601. p38MAPK events.
    REACT_211125. NOD1/2 Signaling Pathway.
    REACT_215063. ERK/MAPK targets.
    SABIO-RK P47811.

    Miscellaneous databases

    EvolutionaryTracei P47811.
    NextBioi 304425.
    PROi P47811.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P47811.
    Bgeei P47811.
    CleanExi MM_MAPK14.
    Genevestigatori P47811.

    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. "A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells."
      Han J., Lee J.-D., Bibbs L., Ulevitch R.J.
      Science 265:808-811(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
      Tissue: Liver.
    2. Higashitsuji H., Fujita J.
      Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Strain: C57BL/6.
      Tissue: Brain.
    3. "Piccolo, a new alternative spliced form of p38/CSBP1/Mxi2 that is specifically expressed in kidney and liver."
      Faccio L., Fusco C., Zervos S.A.
      Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Strain: C57BL/6.
      Tissue: Kidney.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
      Strain: C57BL/6J.
      Tissue: Bone marrow, Pituitary and Thymus.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    6. "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: Liver.
    7. Yin Z., Li J., Sha J., Zhou Z., Lin M., Wang L.
      Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 94-318 (ISOFORM 3).
      Tissue: Testis.
    8. "Novel CDC2-related protein kinases produced in murine hematopoietic stem cells."
      Ershler M.A., Nagorskaya T.V., Visser J.W.M., Belyavsky A.V.
      Gene 124:305-306(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 154-186.
      Strain: CBA.
      Tissue: Bone marrow.
    9. "Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms."
      Derijard B., Raingeaud J., Barrett T., Wu I.-H., Han J., Ulevitch R.J., Davis R.J.
      Science 267:682-685(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    10. "A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase."
      Blanco-Aparicio C., Torres J., Pulido R.
      J. Cell Biol. 147:1129-1136(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTPRR, SUBCELLULAR LOCATION.
    11. "Deficiency of the stress kinase p38alpha results in embryonic lethality: characterization of the kinase dependence of stress responses of enzyme-deficient embryonic stem cells."
      Allen M., Svensson L., Roach M., Hambor J., McNeish J., Gabel C.A.
      J. Exp. Med. 191:859-870(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION.
      Tissue: Embryonic stem cell.
    12. "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, SUBUNIT.
      Strain: C57BL/6J.
    13. "MSK1 and MSK2 are required for the mitogen- and stress-induced phosphorylation of CREB and ATF1 in fibroblasts."
      Wiggin G.R., Soloaga A., Foster J.M., Murray-Tait V., Cohen P., Arthur J.S.
      Mol. Cell. Biol. 22:2871-2881(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ACTIVATION OF RPS6KA5/MSK1 AND RPS6KA4/MSK2.
    14. "JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors."
      Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., Reddy E.P.
      Proc. Natl. Acad. Sci. U.S.A. 99:14189-14194(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SPAG9.
    15. "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 GADD45A, PHOSPHORYLATION AT TYR-323, AUTOPHOSPHORYLATION, ENZYME REGULATION, FUNCTION.
    16. "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.
    17. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND TYR-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND TYR-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    19. "Enzymatic activity and substrate specificity of mitogen-activated protein kinase p38alpha in different phosphorylation states."
      Zhang Y.Y., Mei Z.Q., Wu J.W., Wang Z.X.
      J. Biol. Chem. 283:26591-26601(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-180 AND TYR-182, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    20. "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.
    21. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND TYR-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    22. "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.
    23. "The structure of mitogen-activated protein kinase p38 at 2.1-A resolution."
      Wang Z., Harkins P.C., Ulevitch R.J., Han J., Cobb M.H., Goldsmith E.J.
      Proc. Natl. Acad. Sci. U.S.A. 94:2327-2332(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
    24. "Crystal structures of MAP kinase p38 complexed to the docking sites on its nuclear substrate MEF2A and activator MKK3b."
      Chang C.I., Xu B.E., Akella R., Cobb M.H., Goldsmith E.J.
      Mol. Cell 9:1241-1249(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH MEF2A AND MAP2K3.
    25. Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
    26. Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
    27. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2-360 IN COMPLEX WITH MAPKAPK2.
    28. "A distinct interaction mode revealed by the crystal structure of the kinase p38alpha with the MAPK binding domain of the phosphatase MKP5."
      Zhang Y.Y., Wu J.W., Wang Z.X.
      Sci. Signal. 4:RA88-RA88(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) IN COMPLEX WITH DUSP10, CATALYTIC ACTIVITY, DEPHOSPHORYLATION BY DUSP10, INTERACTION WITH DUSP10.

    Entry informationi

    Entry nameiMK14_MOUSE
    AccessioniPrimary (citable) accession number: P47811
    Secondary accession number(s): B2KF37
    , B2KF38, O08666, Q3U6R5, Q3UZS3, Q8C289, Q9JLV8, Q9QZ80
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 167 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3