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P53779

- MK10_HUMAN

UniProt

P53779 - MK10_HUMAN

Protein

Mitogen-activated protein kinase 10

Gene

MAPK10

Organism
Homo sapiens (Human)
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 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Serine/threonine-protein kinase involved in various processes such as neuronal proliferation, differentiation, migration and programmed cell death. Extracellular stimuli such as proinflammatory cytokines or physical stress stimulate the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. In this cascade, two dual specificity kinases MAP2K4/MKK4 and MAP2K7/MKK7 phosphorylate and activate MAPK10/JNK3. In turn, MAPK10/JNK3 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN and ATF2 and thus regulates AP-1 transcriptional activity. Plays regulatory roles in the signaling pathways during neuronal apoptosis. Phosphorylates the neuronal microtubule regulator STMN2. Acts in the regulation of the beta-amyloid precursor protein/APP signaling during neuronal differentiation by phosphorylating APP. Participates also in neurite growth in spiral ganglion neurons.1 Publication

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.1 Publication

    Enzyme regulationi

    Activated by threonine and tyrosine phosphorylation by two dual specificity kinases, MAP2K4 and MAP2K7. MAP2K7 phosphorylates MAPK10 on Thr-221 causing a conformational change and a large increase in Vmax. MAP2K4 then phosphorylates Tyr-223 resulting in a further increase in Vmax. Inhibited by dual specificity phosphatases, such as DUSP1. Inhibited by HDAC9.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei93 – 931ATP
    Active sitei189 – 1891Proton acceptor

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi70 – 789ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. JUN kinase activity Source: UniProtKB
    3. MAP kinase kinase activity Source: ProtInc
    4. protein binding Source: IntAct

    GO - Biological processi

    1. activation of MAPK activity Source: GOC
    2. Fc-epsilon receptor signaling pathway Source: Reactome
    3. innate immune response Source: Reactome
    4. JNK cascade Source: UniProtKB
    5. JUN phosphorylation Source: GOC
    6. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    7. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    8. regulation of sequence-specific DNA binding transcription factor activity Source: Reactome
    9. signal transduction Source: ProtInc
    10. stress-activated MAPK cascade Source: Reactome
    11. toll-like receptor 10 signaling pathway Source: Reactome
    12. toll-like receptor 2 signaling pathway Source: Reactome
    13. toll-like receptor 3 signaling pathway Source: Reactome
    14. toll-like receptor 4 signaling pathway Source: Reactome
    15. toll-like receptor 5 signaling pathway Source: Reactome
    16. toll-like receptor 9 signaling pathway Source: Reactome
    17. toll-like receptor signaling pathway Source: Reactome
    18. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    19. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    20. TRIF-dependent toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.24. 2681.
    ReactomeiREACT_163701. FCERI mediated MAPK activation.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_21326. Activation of the AP-1 family of transcription factors.
    REACT_21368. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
    SignaLinkiP53779.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase 10 (EC:2.7.11.24)
    Short name:
    MAP kinase 10
    Short name:
    MAPK 10
    Alternative name(s):
    MAP kinase p49 3F12
    Stress-activated protein kinase 1b
    Short name:
    SAPK1b
    Stress-activated protein kinase JNK3
    c-Jun N-terminal kinase 3
    Gene namesi
    Name:MAPK10
    Synonyms:JNK3, JNK3A, PRKM10, SAPK1B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:6872. MAPK10.

    Subcellular locationi

    Cytoplasm 1 Publication. Membrane 1 Publication; Lipid-anchor 1 Publication. Nucleus 1 Publication. Mitochondrion 1 Publication
    Note: Palmitoylation regulates MAPK10 trafficking to cytoskeleton. Recruited to the mitochondria in the presence of SARM1 By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. mitochondrion Source: UniProtKB
    4. nucleoplasm Source: Reactome
    5. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving MAPK10 has been found in a single patient with pharmacoresistant epileptic encephalopathy. Translocation t(Y;4)(q11.2;q21) which causes MAPK10 truncation.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi462 – 4621C → S: Loss of palmitoylation. 1 Publication
    Mutagenesisi463 – 4631C → S: Loss of palmitoylation. 1 Publication

    Keywords - Diseasei

    Epilepsy, Mental retardation

    Organism-specific databases

    Orphaneti2382. Lennox-Gastaut syndrome.
    PharmGKBiPA30617.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 464464Mitogen-activated protein kinase 10PRO_0000186277Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei154 – 1541S-nitrosocysteineBy similarity
    Modified residuei221 – 2211Phosphothreonine; by MAP2K71 Publication
    Modified residuei223 – 2231Phosphotyrosine; by MAP2K41 Publication
    Lipidationi462 – 4621S-palmitoyl cysteine1 Publication
    Lipidationi463 – 4631S-palmitoyl cysteine1 Publication

    Post-translational modificationi

    Dually phosphorylated on Thr-221 and Tyr-223 by MAP2K4 and MAP2K7, which activates the enzyme. MAP2K7 shows a strong preference for Thr-221 while MAP2K4 phosphorylates Tyr-223 preferentially. Weakly autophosphorylated on threonine and tyrosine residues in vitro.1 Publication
    Palmitoylation regulates subcellular location and axonal development.1 Publication

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein, S-nitrosylation

    Proteomic databases

    MaxQBiP53779.
    PaxDbiP53779.
    PRIDEiP53779.

    PTM databases

    PhosphoSiteiP53779.

    Expressioni

    Tissue specificityi

    Specific to a subset of neurons in the nervous system. Present in the hippocampus and areas, cerebellum, striatum, brain stem, and weakly in the spinal cord. Very weak expression in testis and kidney.

    Gene expression databases

    ArrayExpressiP53779.
    BgeeiP53779.
    CleanExiHS_MAPK10.
    GenevestigatoriP53779.

    Organism-specific databases

    HPAiCAB022625.

    Interactioni

    Subunit structurei

    Interacts with MAPKBP1 By similarity. Binds to at least four scaffolding proteins, MAPK8IP1/JIP-1, MAPK8IP2/JIP-2, MAPK8IP3/JIP-3/JSAP1 and SPAG9/MAPK8IP4/JIP-4. These proteins also bind other components of the JNK signaling pathway. Interacts with HDAC9. Interacts with ARRB2; the interaction enhances MAPK10 activation by MAP3K5. Interacts with SARM1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARRB1P494072EBI-713543,EBI-743313
    JUNP054122EBI-713543,EBI-852823
    RELAQ042062EBI-713543,EBI-73886

    Protein-protein interaction databases

    BioGridi111588. 42 interactions.
    DIPiDIP-1015N.
    IntActiP53779. 18 interactions.
    MINTiMINT-1373516.
    STRINGi9606.ENSP00000352157.

    Structurei

    Secondary structure

    1
    464
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi48 – 536
    Beta strandi56 – 616
    Beta strandi64 – 696
    Beta strandi77 – 837
    Turni84 – 874
    Beta strandi88 – 9710
    Helixi98 – 1003
    Helixi102 – 11413
    Turni115 – 1173
    Beta strandi121 – 1233
    Beta strandi127 – 1304
    Turni136 – 1383
    Beta strandi142 – 1476
    Beta strandi150 – 1523
    Helixi153 – 1575
    Helixi163 – 18220
    Helixi192 – 1943
    Beta strandi195 – 1973
    Beta strandi199 – 2013
    Beta strandi203 – 2053
    Beta strandi207 – 2093
    Turni212 – 2143
    Helixi216 – 2194
    Beta strandi220 – 2223
    Helixi227 – 2293
    Helixi232 – 2354
    Helixi244 – 25815
    Helixi268 – 27912
    Helixi284 – 2874
    Helixi292 – 2998
    Helixi309 – 3124
    Helixi315 – 3173
    Helixi323 – 33917
    Turni344 – 3463
    Helixi350 – 3556
    Turni357 – 3615
    Helixi365 – 3684
    Helixi378 – 3825
    Helixi387 – 39913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JNKX-ray2.30A1-423[»]
    1PMNX-ray2.20A40-401[»]
    1PMQX-ray2.20A40-401[»]
    1PMUX-ray2.70A40-401[»]
    1PMVX-ray2.50A40-401[»]
    2B1PX-ray1.90A46-400[»]
    2EXCX-ray2.75X45-400[»]
    2O0UX-ray2.10A39-402[»]
    2O2UX-ray2.45A39-402[»]
    2OK1X-ray2.40A40-402[»]
    2P33X-ray2.40A40-402[»]
    2R9SX-ray2.40A/B46-401[»]
    2WAJX-ray2.40A39-402[»]
    2ZDTX-ray2.00A39-402[»]
    2ZDUX-ray2.50A39-402[»]
    3CGFX-ray3.00A40-402[»]
    3CGOX-ray3.00A40-402[»]
    3DA6X-ray2.00A39-402[»]
    3FI2X-ray2.28A39-402[»]
    3FI3X-ray2.20A39-402[»]
    3FV8X-ray2.28A39-402[»]
    3G90X-ray2.40X40-402[»]
    3G9LX-ray2.20X40-402[»]
    3G9NX-ray2.80A40-402[»]
    3KVXX-ray2.40A39-402[»]
    3OXIX-ray2.20A40-401[»]
    3OY1X-ray1.70A40-401[»]
    3PTGX-ray2.43A40-401[»]
    3RTPX-ray2.40A40-401[»]
    3TTIX-ray2.20A1-464[»]
    3TTJX-ray2.10A1-464[»]
    3V6RX-ray2.60A/B39-402[»]
    3V6SX-ray2.97A/B39-402[»]
    4H36X-ray3.00A46-400[»]
    4H39X-ray1.99A46-400[»]
    4H3BX-ray2.08A/C46-400[»]
    4KKEX-ray2.20A40-402[»]
    4KKGX-ray2.40A40-402[»]
    4KKHX-ray2.00A40-402[»]
    ProteinModelPortaliP53779.
    SMRiP53779. Positions 11-429.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP53779.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini64 – 359296Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi221 – 2233TXY

    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.
    InParanoidiP53779.
    KOiK04440.
    OMAiEVMNFEE.
    OrthoDBiEOG7PCJGV.
    PhylomeDBiP53779.
    TreeFamiTF105100.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR008351. MAPK_JNK.
    IPR000719. Prot_kinase_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    PRINTSiPR01772. JNKMAPKINASE.
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS01351. MAPK. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Note: A similar low level of binding to substrates is observed for isoform alpha-1 and isoform alpha-2. However, there is no correlation between binding and phosphorylation, which is achieved about at the same efficiency by all isoforms.

    Isoform Alpha-2 (identifier: P53779-1) [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

    MSLHFLYYCS EPTLDVKIAF CQGFDKQVDV SYIAKHYNMS KSKVDNQFYS    50
    VEVGDSTFTV LKRYQNLKPI GSGAQGIVCA AYDAVLDRNV AIKKLSRPFQ 100
    NQTHAKRAYR ELVLMKCVNH KNIISLLNVF TPQKTLEEFQ DVYLVMELMD 150
    ANLCQVIQME LDHERMSYLL YQMLCGIKHL HSAGIIHRDL KPSNIVVKSD 200
    CTLKILDFGL ARTAGTSFMM TPYVVTRYYR APEVILGMGY KENVDIWSVG 250
    CIMGEMVRHK ILFPGRDYID QWNKVIEQLG TPCPEFMKKL QPTVRNYVEN 300
    RPKYAGLTFP KLFPDSLFPA DSEHNKLKAS QARDLLSKML VIDPAKRISV 350
    DDALQHPYIN VWYDPAEVEA PPPQIYDKQL DEREHTIEEW KELIYKEVMN 400
    SEEKTKNGVV KGQPSPSGAA VNSSESLPPS SSVNDISSMS TDQTLASDTD 450
    SSLEASAGPL GCCR 464
    Length:464
    Mass (Da):52,585
    Last modified:November 1, 1997 - v2
    Checksum:i2E20C05EB89CDA66
    GO
    Isoform Alpha-1 (identifier: P53779-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         418-464: GAAVNSSESLPPSSSVNDISSMSTDQTLASDTDSSLEASAGPLGCCR → AQVQQ

    Show »
    Length:422
    Mass (Da):48,554
    Checksum:iFCC8C11954481C04
    GO
    Isoform 3 (identifier: P53779-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-38: Missing.

    Show »
    Length:426
    Mass (Da):48,128
    Checksum:i1022B6AC7774A666
    GO
    Isoform 4 (identifier: P53779-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-145: Missing.
         418-464: GAAVNSSESLPPSSSVNDISSMSTDQTLASDTDSSLEASAGPLGCCR → AQVQQ

    Show »
    Length:277
    Mass (Da):31,933
    Checksum:i5C2FA3CFC85C1FF8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti162 – 1621D → G in BAG51956. (PubMed:14702039)Curated

    Mass spectrometryi

    Molecular mass is 44070 Da from positions 1 - 464. Determined by ESI. 1 Publication

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 145145Missing in isoform 4. 1 PublicationVSP_041910Add
    BLAST
    Alternative sequencei1 – 3838Missing in isoform 3. 1 PublicationVSP_041911Add
    BLAST
    Alternative sequencei418 – 46447GAAVN…LGCCR → AQVQQ in isoform Alpha-1 and isoform 4. 3 PublicationsVSP_004839Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07620 mRNA. Translation: AAC50101.1.
    U34819 mRNA. Translation: AAC50604.1.
    U34820 mRNA. Translation: AAC50605.1.
    AK057723 mRNA. Translation: BAG51956.1.
    AK124791 mRNA. Translation: BAG54096.1.
    AC096953 Genomic DNA. No translation available.
    AC104059 Genomic DNA. No translation available.
    AC104827 Genomic DNA. No translation available.
    AC108054 Genomic DNA. No translation available.
    AC110076 Genomic DNA. No translation available.
    CH471057 Genomic DNA. Translation: EAX05963.1.
    BC035057 mRNA. Translation: AAH35057.1.
    CCDSiCCDS34026.1. [P53779-1]
    CCDS3612.1. [P53779-3]
    CCDS3613.1. [P53779-4]
    CCDS43247.1. [P53779-2]
    PIRiS71104.
    RefSeqiNP_002744.1. NM_002753.3. [P53779-2]
    NP_620446.1. NM_138980.2. [P53779-3]
    NP_620447.1. NM_138981.2. [P53779-4]
    NP_620448.1. NM_138982.2. [P53779-1]
    XP_005263186.1. XM_005263129.1. [P53779-1]
    XP_005263187.1. XM_005263130.1. [P53779-1]
    XP_005263192.1. XM_005263135.2. [P53779-2]
    XP_006714330.1. XM_006714267.1. [P53779-1]
    XP_006714331.1. XM_006714268.1. [P53779-3]
    UniGeneiHs.125503.
    Hs.13438.

    Genome annotation databases

    EnsembliENST00000359221; ENSP00000352157; ENSG00000109339. [P53779-1]
    ENST00000361569; ENSP00000355297; ENSG00000109339. [P53779-2]
    ENST00000395160; ENSP00000378589; ENSG00000109339. [P53779-4]
    ENST00000395161; ENSP00000378590; ENSG00000109339. [P53779-2]
    ENST00000395166; ENSP00000378595; ENSG00000109339. [P53779-3]
    ENST00000395169; ENSP00000378598; ENSG00000109339. [P53779-3]
    GeneIDi5602.
    KEGGihsa:5602.
    UCSCiuc003hpo.3. human. [P53779-1]
    uc003hpp.3. human. [P53779-4]
    uc003hpt.3. human. [P53779-2]

    Polymorphism databases

    DMDMi2507196.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07620 mRNA. Translation: AAC50101.1 .
    U34819 mRNA. Translation: AAC50604.1 .
    U34820 mRNA. Translation: AAC50605.1 .
    AK057723 mRNA. Translation: BAG51956.1 .
    AK124791 mRNA. Translation: BAG54096.1 .
    AC096953 Genomic DNA. No translation available.
    AC104059 Genomic DNA. No translation available.
    AC104827 Genomic DNA. No translation available.
    AC108054 Genomic DNA. No translation available.
    AC110076 Genomic DNA. No translation available.
    CH471057 Genomic DNA. Translation: EAX05963.1 .
    BC035057 mRNA. Translation: AAH35057.1 .
    CCDSi CCDS34026.1. [P53779-1 ]
    CCDS3612.1. [P53779-3 ]
    CCDS3613.1. [P53779-4 ]
    CCDS43247.1. [P53779-2 ]
    PIRi S71104.
    RefSeqi NP_002744.1. NM_002753.3. [P53779-2 ]
    NP_620446.1. NM_138980.2. [P53779-3 ]
    NP_620447.1. NM_138981.2. [P53779-4 ]
    NP_620448.1. NM_138982.2. [P53779-1 ]
    XP_005263186.1. XM_005263129.1. [P53779-1 ]
    XP_005263187.1. XM_005263130.1. [P53779-1 ]
    XP_005263192.1. XM_005263135.2. [P53779-2 ]
    XP_006714330.1. XM_006714267.1. [P53779-1 ]
    XP_006714331.1. XM_006714268.1. [P53779-3 ]
    UniGenei Hs.125503.
    Hs.13438.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JNK X-ray 2.30 A 1-423 [» ]
    1PMN X-ray 2.20 A 40-401 [» ]
    1PMQ X-ray 2.20 A 40-401 [» ]
    1PMU X-ray 2.70 A 40-401 [» ]
    1PMV X-ray 2.50 A 40-401 [» ]
    2B1P X-ray 1.90 A 46-400 [» ]
    2EXC X-ray 2.75 X 45-400 [» ]
    2O0U X-ray 2.10 A 39-402 [» ]
    2O2U X-ray 2.45 A 39-402 [» ]
    2OK1 X-ray 2.40 A 40-402 [» ]
    2P33 X-ray 2.40 A 40-402 [» ]
    2R9S X-ray 2.40 A/B 46-401 [» ]
    2WAJ X-ray 2.40 A 39-402 [» ]
    2ZDT X-ray 2.00 A 39-402 [» ]
    2ZDU X-ray 2.50 A 39-402 [» ]
    3CGF X-ray 3.00 A 40-402 [» ]
    3CGO X-ray 3.00 A 40-402 [» ]
    3DA6 X-ray 2.00 A 39-402 [» ]
    3FI2 X-ray 2.28 A 39-402 [» ]
    3FI3 X-ray 2.20 A 39-402 [» ]
    3FV8 X-ray 2.28 A 39-402 [» ]
    3G90 X-ray 2.40 X 40-402 [» ]
    3G9L X-ray 2.20 X 40-402 [» ]
    3G9N X-ray 2.80 A 40-402 [» ]
    3KVX X-ray 2.40 A 39-402 [» ]
    3OXI X-ray 2.20 A 40-401 [» ]
    3OY1 X-ray 1.70 A 40-401 [» ]
    3PTG X-ray 2.43 A 40-401 [» ]
    3RTP X-ray 2.40 A 40-401 [» ]
    3TTI X-ray 2.20 A 1-464 [» ]
    3TTJ X-ray 2.10 A 1-464 [» ]
    3V6R X-ray 2.60 A/B 39-402 [» ]
    3V6S X-ray 2.97 A/B 39-402 [» ]
    4H36 X-ray 3.00 A 46-400 [» ]
    4H39 X-ray 1.99 A 46-400 [» ]
    4H3B X-ray 2.08 A/C 46-400 [» ]
    4KKE X-ray 2.20 A 40-402 [» ]
    4KKG X-ray 2.40 A 40-402 [» ]
    4KKH X-ray 2.00 A 40-402 [» ]
    ProteinModelPortali P53779.
    SMRi P53779. Positions 11-429.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111588. 42 interactions.
    DIPi DIP-1015N.
    IntActi P53779. 18 interactions.
    MINTi MINT-1373516.
    STRINGi 9606.ENSP00000352157.

    Chemistry

    BindingDBi P53779.
    ChEMBLi CHEMBL3038502.
    GuidetoPHARMACOLOGYi 1498.

    PTM databases

    PhosphoSitei P53779.

    Polymorphism databases

    DMDMi 2507196.

    Proteomic databases

    MaxQBi P53779.
    PaxDbi P53779.
    PRIDEi P53779.

    Protocols and materials databases

    DNASUi 5602.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359221 ; ENSP00000352157 ; ENSG00000109339 . [P53779-1 ]
    ENST00000361569 ; ENSP00000355297 ; ENSG00000109339 . [P53779-2 ]
    ENST00000395160 ; ENSP00000378589 ; ENSG00000109339 . [P53779-4 ]
    ENST00000395161 ; ENSP00000378590 ; ENSG00000109339 . [P53779-2 ]
    ENST00000395166 ; ENSP00000378595 ; ENSG00000109339 . [P53779-3 ]
    ENST00000395169 ; ENSP00000378598 ; ENSG00000109339 . [P53779-3 ]
    GeneIDi 5602.
    KEGGi hsa:5602.
    UCSCi uc003hpo.3. human. [P53779-1 ]
    uc003hpp.3. human. [P53779-4 ]
    uc003hpt.3. human. [P53779-2 ]

    Organism-specific databases

    CTDi 5602.
    GeneCardsi GC04M086878.
    H-InvDB HIX0163985.
    HGNCi HGNC:6872. MAPK10.
    HPAi CAB022625.
    MIMi 602897. gene.
    neXtProti NX_P53779.
    Orphaneti 2382. Lennox-Gastaut syndrome.
    PharmGKBi PA30617.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233024.
    HOVERGENi HBG014652.
    InParanoidi P53779.
    KOi K04440.
    OMAi EVMNFEE.
    OrthoDBi EOG7PCJGV.
    PhylomeDBi P53779.
    TreeFami TF105100.

    Enzyme and pathway databases

    BRENDAi 2.7.11.24. 2681.
    Reactomei REACT_163701. FCERI mediated MAPK activation.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_21326. Activation of the AP-1 family of transcription factors.
    REACT_21368. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
    SignaLinki P53779.

    Miscellaneous databases

    ChiTaRSi MAPK10. human.
    EvolutionaryTracei P53779.
    GeneWikii MAPK10.
    GenomeRNAii 5602.
    NextBioi 21762.
    PROi P53779.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P53779.
    Bgeei P53779.
    CleanExi HS_MAPK10.
    Genevestigatori P53779.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR003527. MAP_kinase_CS.
    IPR008351. MAPK_JNK.
    IPR000719. Prot_kinase_dom.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    PRINTSi PR01772. JNKMAPKINASE.
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS01351. MAPK. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "p493F12 kinase: a novel MAP kinase expressed in a subset of neurons in the human nervous system."
      Mohit A.A., Martin J.H., Miller C.A.
      Neuron 14:67-78(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1).
      Tissue: Hippocampus.
    2. "Selective interaction of JNK protein kinase isoforms with transcription factors."
      Gupta S., Barrett T., Whitmarsh A.J., Cavanagh J., Sluss H.K., Derijard B., Davis R.J.
      EMBO J. 15:2760-2770(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1 AND ALPHA-2).
      Tissue: Brain.
    3. "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 3 AND 4).
      Tissue: Caudate nucleus.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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 ALPHA-2).
      Tissue: Brain.
    7. "Activation of JNK3 alpha 1 requires both MKK4 and MKK7: kinetic characterization of in vitro phosphorylated JNK3 alpha 1."
      Lisnock J., Griffin P., Calaycay J., Frantz B., Parsons J., O'Keefe S.J., LoGrasso P.
      Biochemistry 39:3141-3148(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, REGULATION BY MAP2K4 AND MAP2K7, PHOSPHORYLATION AT THR-221 AND TYR-223, COFACTOR, MASS SPECTROMETRY.
    8. "Synergistic activation of stress-activated protein kinase 1/c-Jun N-terminal kinase (SAPK1/JNK) isoforms by mitogen-activated protein kinase kinase 4 (MKK4) and MKK7."
      Fleming Y., Armstrong C.G., Morrice N., Paterson A., Goedert M., Cohen P.
      Biochem. J. 352:145-154(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    9. "c-Jun N-terminal kinase-3 (JNK3)/stress-activated protein kinase-beta (SAPKbeta) binds and phosphorylates the neuronal microtubule regulator SCG10."
      Neidhart S., Antonsson B., Gillieron C., Vilbois F., Grenningloh G., Arkinstall S.
      FEBS Lett. 508:259-264(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF STMN2.
    10. "Characterization of a novel human sperm-associated antigen 9 (SPAG9) having structural homology with c-Jun N-terminal kinase-interacting protein."
      Jagadish N., Rana R., Selvi R., Mishra D., Garg M., Yadav S., Herr J.C., Okumura K., Hasegawa A., Koyama K., Suri A.
      Biochem. J. 389:73-82(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SPAG9.
    11. "Truncation of the CNS-expressed JNK3 in a patient with a severe developmental epileptic encephalopathy."
      Shoichet S.A., Duprez L., Hagens O., Waetzig V., Menzel C., Herdegen T., Schweiger S., Dan B., Vamos E., Ropers H.-H., Kalscheuer V.M.
      Hum. Genet. 118:559-567(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL REARRANGEMENT, DISEASE.
    12. "Visual and both non-visual arrestins in their 'inactive' conformation bind JNK3 and Mdm2 and relocalize them from the nucleus to the cytoplasm."
      Song X., Raman D., Gurevich E.V., Vishnivetskiy S.A., Gurevich V.V.
      J. Biol. Chem. 281:21491-21499(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    13. Cited for: INTERACTION WITH HDAC9, ENZYME REGULATION.
    14. "Mutations of beta-arrestin 2 that limit self-association also interfere with interactions with the beta2-adrenoceptor and the ERK1/2 MAPKs: implications for beta2-adrenoceptor signalling via the ERK1/2 MAPKs."
      Xu T.-R., Baillie G.S., Bhari N., Houslay T.M., Pitt A.M., Adams D.R., Kolch W., Houslay M.D., Milligan G.
      Biochem. J. 413:51-60(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARRB2.
    15. "Isoform-specific palmitoylation of JNK regulates axonal development."
      Yang G., Liu Y., Yang K., Liu R., Zhu S., Coquinco A., Wen W., Kojic L., Jia W., Cynader M.
      Cell Death Differ. 19:553-561(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-462 AND CYS-463, MUTAGENESIS OF CYS-462 AND CYS-463.
    16. "Crystal structure of JNK3: a kinase implicated in neuronal apoptosis."
      Xie X., Gu Y., Fox T., Coll J.T., Fleming M.A., Markland W., Caron P.R., Wilson K.P., Su M.S.-S.
      Structure 6:983-991(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 40-402.

    Entry informationi

    Entry nameiMK10_HUMAN
    AccessioniPrimary (citable) accession number: P53779
    Secondary accession number(s): A6NFS3
    , A6NG28, B3KQ94, Q15707, Q49AP1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 167 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, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3