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P45983

- MK08_HUMAN

UniProt

P45983 - MK08_HUMAN

Protein

Mitogen-activated protein kinase 8

Gene

MAPK8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (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 cell proliferation, differentiation, migration, transformation 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 MAPK8/JNK1. In turn, MAPK8/JNK1 phosphorylates a number of transcription factors, primarily components of AP-1 such as JUN, JDP2 and ATF2 and thus regulates AP-1 transcriptional activity. Phosphorylates the replication licensing factor CDT1, inhibiting the interaction between CDT1 and the histone H4 acetylase HBO1 to replication origins. Loss of this interaction abrogates the acetylation required for replication initiation. Promotes stressed cell apoptosis by phosphorylating key regulatory factors including p53/TP53 and Yes-associates protein YAP1. In T-cells, MAPK8 and MAPK9 are required for polarized differentiation of T-helper cells into Th1 cells. Contributes to the survival of erythroid cells by phosphorylating the antagonist of cell death BAD upon EPO stimulation. Mediates starvation-induced BCL2 phosphorylation, BCL2 dissociation from BECN1, and thus activation of autophagy. Phosphorylates STMN2 and hence regulates microtubule dynamics, controlling neurite elongation in cortical neurons. In the developing brain, through its cytoplasmic activity on STMN2, negatively regulates the rate of exit from multipolar stage and of radial migration from the ventricular zone. Phosphorylates several other substrates including heat shock factor protein 4 (HSF4), the deacetylase SIRT1, ELK1, or the E3 ligase ITCH.
    JNK1 isoforms display different binding patterns: beta-1 preferentially binds to c-Jun, whereas alpha-1, alpha-2, and beta-2 have a similar low level of binding to both c-Jun or ATF2. However, there is no correlation between binding and phosphorylation, which is achieved at about the same efficiency by all isoforms.

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.1 Publication

    Enzyme regulationi

    Activated by threonine and tyrosine phosphorylation by either of two dual specificity kinases, MAP2K4 and MAP2K7. MAP2K4 shows a strong preference for Tyr-185 while MAP2K7 phosphorylates Tyr-183 preferentially. Inhibited by dual specificity phosphatases, such as DUSP1. Inhibited by SERPINB3.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei55 – 551ATPPROSITE-ProRule annotation
    Active sitei151 – 1511Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi32 – 409ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. histone deacetylase binding Source: BHF-UCL
    3. histone deacetylase regulator activity Source: BHF-UCL
    4. JUN kinase activity Source: UniProtKB
    5. protein binding Source: IntAct
    6. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: Reactome
    2. apoptotic signaling pathway Source: Reactome
    3. cellular response to lipopolysaccharide Source: MGI
    4. cellular response to mechanical stimulus Source: UniProtKB
    5. Fc-epsilon receptor signaling pathway Source: Reactome
    6. innate immune response Source: Reactome
    7. intrinsic apoptotic signaling pathway Source: Reactome
    8. JNK cascade Source: UniProtKB
    9. JUN phosphorylation Source: UniProtKB
    10. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    11. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    12. negative regulation of apoptotic process Source: UniProtKB
    13. negative regulation of protein binding Source: UniProtKB
    14. neurotrophin TRK receptor signaling pathway Source: Reactome
    15. ossification Source: Ensembl
    16. peptidyl-serine phosphorylation Source: UniProtKB
    17. peptidyl-threonine phosphorylation Source: UniProtKB
    18. positive regulation of apoptotic process Source: Reactome
    19. positive regulation of apoptotic signaling pathway Source: Ensembl
    20. positive regulation of deacetylase activity Source: BHF-UCL
    21. positive regulation of determination of dorsal identity Source: Ensembl
    22. positive regulation of gene expression Source: BHF-UCL
    23. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
    24. regulation of histone deacetylation Source: GOC
    25. regulation of protein localization Source: BHF-UCL
    26. regulation of sequence-specific DNA binding transcription factor activity Source: Reactome
    27. response to cadmium ion Source: Ensembl
    28. response to stress Source: ProtInc
    29. response to UV Source: MGI
    30. stress-activated MAPK cascade Source: Reactome
    31. toll-like receptor 10 signaling pathway Source: Reactome
    32. toll-like receptor 2 signaling pathway Source: Reactome
    33. toll-like receptor 3 signaling pathway Source: Reactome
    34. toll-like receptor 4 signaling pathway Source: Reactome
    35. toll-like receptor 5 signaling pathway Source: Reactome
    36. toll-like receptor 9 signaling pathway Source: Reactome
    37. toll-like receptor signaling pathway Source: Reactome
    38. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    39. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    40. 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_13638. NRAGE signals death through JNK.
    REACT_13643. NRIF signals cell death from the nucleus.
    REACT_163701. FCERI mediated MAPK activation.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_2100. Activation of BMF and translocation to mitochondria.
    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.
    REACT_25299. DSCAM interactions.
    SignaLinkiP45983.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase 8 (EC:2.7.11.24)
    Short name:
    MAP kinase 8
    Short name:
    MAPK 8
    Alternative name(s):
    JNK-46
    Stress-activated protein kinase 1c
    Short name:
    SAPK1c
    Stress-activated protein kinase JNK1
    c-Jun N-terminal kinase 1
    Gene namesi
    Name:MAPK8
    Synonyms:JNK1, PRKM8, SAPK1, SAPK1C
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:6881. MAPK8.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. mitochondrion Source: Ensembl
    3. nucleoplasm Source: Reactome
    4. nucleus Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi183 – 1831T → A: Phosphorylation blocked. 1 Publication
    Mutagenesisi185 – 1851Y → F: Phosphorylation blocked. 1 Publication

    Organism-specific databases

    PharmGKBiPA283.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 427427Mitogen-activated protein kinase 8PRO_0000186262Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei116 – 1161S-nitrosocysteineBy similarity
    Modified residuei183 – 1831Phosphothreonine; by MAP2K72 Publications
    Modified residuei185 – 1851Phosphotyrosine; by MAP2K42 Publications
    Modified residuei377 – 3771PhosphoserineBy similarity

    Post-translational modificationi

    Dually phosphorylated on Thr-183 and Tyr-185 by MAP2K7 and MAP2K4, which activates the enzyme. Phosphorylated by TAOK2.2 Publications

    Keywords - PTMi

    Phosphoprotein, S-nitrosylation

    Proteomic databases

    MaxQBiP45983.
    PaxDbiP45983.
    PRIDEiP45983.

    PTM databases

    PhosphoSiteiP45983.

    Expressioni

    Gene expression databases

    ArrayExpressiP45983.
    BgeeiP45983.
    CleanExiHS_MAPK8.
    GenevestigatoriP45983.

    Organism-specific databases

    HPAiCAB004463.

    Interactioni

    Subunit structurei

    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 TP53 and WWOX. Interacts with JAMP. Forms a complex with MAPK8IP1 and ARHGEF28 By similarity. Interacts (phosphorylated form) with NFE2; the interaction phosphorylates NFE2 in undifferentiated cells By similarity. Interacts with NFATC4. Interacts with MECOM; regulates JNK signaling. Interacts with PIN1; this interaction mediates MAPK8 conformational changes leading to the binding of MAPK8 to its substrates.By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BADQ929342EBI-286483,EBI-700771
    CBLP226812EBI-286483,EBI-518228
    CRKP461082EBI-286483,EBI-886
    JUNP054124EBI-286483,EBI-852823
    MAP2K7O14733-23EBI-286483,EBI-492627
    MAPK8IP1Q9UQF27EBI-286483,EBI-78404
    Mapk8ip1Q9WVI9-12EBI-286483,EBI-288461From a different organism.
    PIK3R1P279862EBI-286483,EBI-79464

    Protein-protein interaction databases

    BioGridi111585. 143 interactions.
    DIPiDIP-249N.
    IntActiP45983. 54 interactions.
    MINTiMINT-1211982.
    STRINGi9606.ENSP00000353483.

    Structurei

    Secondary structure

    1
    427
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 96
    Beta strandi10 – 156
    Beta strandi18 – 236
    Beta strandi26 – 349
    Beta strandi36 – 4510
    Turni46 – 494
    Beta strandi50 – 589
    Helixi60 – 623
    Helixi64 – 7916
    Beta strandi83 – 853
    Beta strandi88 – 925
    Beta strandi94 – 974
    Turni98 – 1003
    Beta strandi103 – 1097
    Beta strandi112 – 1143
    Helixi115 – 1206
    Helixi125 – 14420
    Helixi154 – 1563
    Beta strandi157 – 1593
    Turni161 – 1633
    Beta strandi165 – 1673
    Beta strandi174 – 1774
    Beta strandi178 – 1803
    Beta strandi182 – 1843
    Beta strandi185 – 1873
    Helixi189 – 1913
    Helixi194 – 1974
    Helixi206 – 22015
    Helixi230 – 24112
    Helixi246 – 2494
    Helixi254 – 2618
    Helixi271 – 2744
    Helixi277 – 2793
    Helixi285 – 30117
    Helixi306 – 3083
    Helixi312 – 3176
    Helixi319 – 3224
    Helixi327 – 3304
    Turni339 – 3424
    Helixi349 – 36315

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UKHX-ray2.35A1-363[»]
    1UKIX-ray2.70A1-363[»]
    2G01X-ray3.50A/B1-364[»]
    2GMXX-ray3.50A/B1-364[»]
    2H96X-ray3.00A/B1-364[»]
    2NO3X-ray3.20A/B1-364[»]
    2XRWX-ray1.33A2-364[»]
    2XS0X-ray2.60A1-379[»]
    3ELJX-ray1.80A1-364[»]
    3O17X-ray3.00A/B1-364[»]
    3O2MX-ray2.70A/B1-364[»]
    3PZEX-ray2.00A7-364[»]
    3V3VX-ray2.70A1-366[»]
    3VUDX-ray3.50A1-364[»]
    3VUGX-ray3.24A1-364[»]
    3VUHX-ray2.70A1-364[»]
    3VUIX-ray2.80A1-364[»]
    3VUKX-ray2.95A1-364[»]
    3VULX-ray2.81A1-364[»]
    3VUMX-ray2.69A1-364[»]
    4AWIX-ray1.91A1-364[»]
    4E73X-ray2.27A1-363[»]
    4G1WX-ray2.45A1-363[»]
    4HYSX-ray2.42A1-363[»]
    4HYUX-ray2.15A1-363[»]
    4IZYX-ray2.30A1-363[»]
    4L7FX-ray1.95A7-362[»]
    ProteinModelPortaliP45983.
    SMRiP45983. Positions 7-364.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP45983.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 321296Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi183 – 1853TXY

    Domaini

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

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG014652.
    InParanoidiP45983.
    KOiK04440.
    OMAiREHTLEQ.
    OrthoDBiEOG7PCJGV.
    PhylomeDBiP45983.
    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 (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 2 (identifier: P45983-1) [UniParc]FASTAAdd to Basket

    Also known as: JNK1-alpha-2

    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

    MSRSKRDNNF YSVEIGDSTF TVLKRYQNLK PIGSGAQGIV CAAYDAILER    50
    NVAIKKLSRP FQNQTHAKRA YRELVLMKCV NHKNIIGLLN VFTPQKSLEE 100
    FQDVYIVMEL MDANLCQVIQ MELDHERMSY LLYQMLCGIK HLHSAGIIHR 150
    DLKPSNIVVK SDCTLKILDF GLARTAGTSF MMTPYVVTRY YRAPEVILGM 200
    GYKENVDLWS VGCIMGEMVC HKILFPGRDY IDQWNKVIEQ LGTPCPEFMK 250
    KLQPTVRTYV ENRPKYAGYS FEKLFPDVLF PADSEHNKLK ASQARDLLSK 300
    MLVIDASKRI SVDEALQHPY INVWYDPSEA EAPPPKIPDK QLDEREHTIE 350
    EWKELIYKEV MDLEERTKNG VIRGQPSPLG AAVINGSQHP SSSSSVNDVS 400
    SMSTDPTLAS DTDSSLEAAA GPLGCCR 427
    Length:427
    Mass (Da):48,296
    Last modified:November 1, 1997 - v2
    Checksum:i94FB6BE0358B9B60
    GO
    Isoform 1 (identifier: P45983-2) [UniParc]FASTAAdd to Basket

    Also known as: JNK1-alpha-1

    The sequence of this isoform differs from the canonical sequence as follows:
         380-427: GAAVINGSQHPSSSSSVNDVSSMSTDPTLASDTDSSLEAAAGPLGCCR → AQVQQ

    Note: Contains a phosphoserine at position 377.

    Show »
    Length:384
    Mass (Da):44,229
    Checksum:iA7320EF933E9CF85
    GO
    Isoform 3 (identifier: P45983-3) [UniParc]FASTAAdd to Basket

    Also known as: JNK1-beta-1

    The sequence of this isoform differs from the canonical sequence as follows:
         208-208: L → I
         219-230: VCHKILFPGRDY → IKGGVLFPGTDH
         380-427: GAAVINGSQHPSSSSSVNDVSSMSTDPTLASDTDSSLEAAAGPLGCCR → AQVQQ

    Note: Contains a phosphoserine at position 377.

    Show »
    Length:384
    Mass (Da):44,022
    Checksum:i76E49A950E64C1A1
    GO
    Isoform 4 (identifier: P45983-4) [UniParc]FASTAAdd to Basket

    Also known as: JNK1-beta-2

    The sequence of this isoform differs from the canonical sequence as follows:
         208-208: L → I
         219-230: VCHKILFPGRDY → IKGGVLFPGTDH

    Show »
    Length:427
    Mass (Da):48,088
    Checksum:i3F5CC3F6A4F3EF2D
    GO
    Isoform 5 (identifier: P45983-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         206-281: Missing.
         380-427: GAAVINGSQHPSSSSSVNDVSSMSTDPTLASDTDSSLEAAAGPLGCCR → AQVQQ

    Show »
    Length:308
    Mass (Da):35,333
    Checksum:i914B803A1223601D
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti171 – 1711G → S in a renal clear cell carcinoma sample; somatic mutation. 1 Publication
    VAR_042258
    Natural varianti177 – 1771G → R in a glioblastoma multiforme sample; somatic mutation. 1 Publication
    VAR_042259
    Natural varianti365 – 3651E → K.
    Corresponds to variant rs45483593 [ dbSNP | Ensembl ].
    VAR_050592

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei206 – 28176Missing in isoform 5. 1 PublicationVSP_054554Add
    BLAST
    Alternative sequencei208 – 2081L → I in isoform 3 and isoform 4. 1 PublicationVSP_004831
    Alternative sequencei219 – 23012VCHKI…PGRDY → IKGGVLFPGTDH in isoform 3 and isoform 4. 1 PublicationVSP_004832Add
    BLAST
    Alternative sequencei380 – 42748GAAVI…LGCCR → AQVQQ in isoform 1, isoform 3 and isoform 5. 3 PublicationsVSP_004833Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L26318 mRNA. Translation: AAA36131.1.
    U34822 mRNA. Translation: AAC50607.1.
    U35004 mRNA. Translation: AAC50610.1.
    U35005 mRNA. Translation: AAC50611.1.
    DQ234352 mRNA. Translation: ABB29981.1.
    AC016397 Genomic DNA. No translation available.
    AC074325 Genomic DNA. No translation available.
    AB451231 mRNA. Translation: BAG70045.1.
    CH471187 Genomic DNA. Translation: EAW93132.1.
    CH471187 Genomic DNA. Translation: EAW93129.1.
    CH471187 Genomic DNA. Translation: EAW93130.1.
    CH471187 Genomic DNA. Translation: EAW93133.1.
    CH471187 Genomic DNA. Translation: EAW93134.1.
    CH471187 Genomic DNA. Translation: EAW93136.1.
    BC144063 mRNA. Translation: AAI44064.1.
    CCDSiCCDS60527.1. [P45983-5]
    CCDS7223.1. [P45983-4]
    CCDS7224.1. [P45983-1]
    CCDS7225.1. [P45983-2]
    CCDS7226.1. [P45983-3]
    PIRiS71097.
    S71099.
    RefSeqiNP_001265476.1. NM_001278547.1. [P45983-4]
    NP_001265477.1. NM_001278548.1. [P45983-5]
    NP_002741.1. NM_002750.3. [P45983-2]
    NP_620634.1. NM_139046.2. [P45983-3]
    NP_620637.1. NM_139049.2. [P45983-1]
    XP_006717980.1. XM_006717917.1. [P45983-1]
    XP_006717981.1. XM_006717918.1. [P45983-3]
    XP_006717982.1. XM_006717919.1. [P45983-2]
    UniGeneiHs.138211.
    Hs.522924.

    Genome annotation databases

    EnsembliENST00000360332; ENSP00000353483; ENSG00000107643. [P45983-1]
    ENST00000374176; ENSP00000363291; ENSG00000107643. [P45983-4]
    ENST00000374179; ENSP00000363294; ENSG00000107643. [P45983-3]
    ENST00000374182; ENSP00000363297; ENSG00000107643. [P45983-2]
    ENST00000374189; ENSP00000363304; ENSG00000107643. [P45983-1]
    ENST00000395611; ENSP00000378974; ENSG00000107643. [P45983-5]
    GeneIDi5599.
    KEGGihsa:5599.
    UCSCiuc001jgo.3. human. [P45983-3]
    uc001jgp.3. human. [P45983-1]
    uc001jgq.3. human. [P45983-2]

    Polymorphism databases

    DMDMi2507195.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    Wikipedia

    C-Jun N-terminal kinases entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L26318 mRNA. Translation: AAA36131.1 .
    U34822 mRNA. Translation: AAC50607.1 .
    U35004 mRNA. Translation: AAC50610.1 .
    U35005 mRNA. Translation: AAC50611.1 .
    DQ234352 mRNA. Translation: ABB29981.1 .
    AC016397 Genomic DNA. No translation available.
    AC074325 Genomic DNA. No translation available.
    AB451231 mRNA. Translation: BAG70045.1 .
    CH471187 Genomic DNA. Translation: EAW93132.1 .
    CH471187 Genomic DNA. Translation: EAW93129.1 .
    CH471187 Genomic DNA. Translation: EAW93130.1 .
    CH471187 Genomic DNA. Translation: EAW93133.1 .
    CH471187 Genomic DNA. Translation: EAW93134.1 .
    CH471187 Genomic DNA. Translation: EAW93136.1 .
    BC144063 mRNA. Translation: AAI44064.1 .
    CCDSi CCDS60527.1. [P45983-5 ]
    CCDS7223.1. [P45983-4 ]
    CCDS7224.1. [P45983-1 ]
    CCDS7225.1. [P45983-2 ]
    CCDS7226.1. [P45983-3 ]
    PIRi S71097.
    S71099.
    RefSeqi NP_001265476.1. NM_001278547.1. [P45983-4 ]
    NP_001265477.1. NM_001278548.1. [P45983-5 ]
    NP_002741.1. NM_002750.3. [P45983-2 ]
    NP_620634.1. NM_139046.2. [P45983-3 ]
    NP_620637.1. NM_139049.2. [P45983-1 ]
    XP_006717980.1. XM_006717917.1. [P45983-1 ]
    XP_006717981.1. XM_006717918.1. [P45983-3 ]
    XP_006717982.1. XM_006717919.1. [P45983-2 ]
    UniGenei Hs.138211.
    Hs.522924.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UKH X-ray 2.35 A 1-363 [» ]
    1UKI X-ray 2.70 A 1-363 [» ]
    2G01 X-ray 3.50 A/B 1-364 [» ]
    2GMX X-ray 3.50 A/B 1-364 [» ]
    2H96 X-ray 3.00 A/B 1-364 [» ]
    2NO3 X-ray 3.20 A/B 1-364 [» ]
    2XRW X-ray 1.33 A 2-364 [» ]
    2XS0 X-ray 2.60 A 1-379 [» ]
    3ELJ X-ray 1.80 A 1-364 [» ]
    3O17 X-ray 3.00 A/B 1-364 [» ]
    3O2M X-ray 2.70 A/B 1-364 [» ]
    3PZE X-ray 2.00 A 7-364 [» ]
    3V3V X-ray 2.70 A 1-366 [» ]
    3VUD X-ray 3.50 A 1-364 [» ]
    3VUG X-ray 3.24 A 1-364 [» ]
    3VUH X-ray 2.70 A 1-364 [» ]
    3VUI X-ray 2.80 A 1-364 [» ]
    3VUK X-ray 2.95 A 1-364 [» ]
    3VUL X-ray 2.81 A 1-364 [» ]
    3VUM X-ray 2.69 A 1-364 [» ]
    4AWI X-ray 1.91 A 1-364 [» ]
    4E73 X-ray 2.27 A 1-363 [» ]
    4G1W X-ray 2.45 A 1-363 [» ]
    4HYS X-ray 2.42 A 1-363 [» ]
    4HYU X-ray 2.15 A 1-363 [» ]
    4IZY X-ray 2.30 A 1-363 [» ]
    4L7F X-ray 1.95 A 7-362 [» ]
    ProteinModelPortali P45983.
    SMRi P45983. Positions 7-364.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111585. 143 interactions.
    DIPi DIP-249N.
    IntActi P45983. 54 interactions.
    MINTi MINT-1211982.
    STRINGi 9606.ENSP00000353483.

    Chemistry

    BindingDBi P45983.
    ChEMBLi CHEMBL2096667.
    GuidetoPHARMACOLOGYi 1496.

    PTM databases

    PhosphoSitei P45983.

    Polymorphism databases

    DMDMi 2507195.

    Proteomic databases

    MaxQBi P45983.
    PaxDbi P45983.
    PRIDEi P45983.

    Protocols and materials databases

    DNASUi 5599.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360332 ; ENSP00000353483 ; ENSG00000107643 . [P45983-1 ]
    ENST00000374176 ; ENSP00000363291 ; ENSG00000107643 . [P45983-4 ]
    ENST00000374179 ; ENSP00000363294 ; ENSG00000107643 . [P45983-3 ]
    ENST00000374182 ; ENSP00000363297 ; ENSG00000107643 . [P45983-2 ]
    ENST00000374189 ; ENSP00000363304 ; ENSG00000107643 . [P45983-1 ]
    ENST00000395611 ; ENSP00000378974 ; ENSG00000107643 . [P45983-5 ]
    GeneIDi 5599.
    KEGGi hsa:5599.
    UCSCi uc001jgo.3. human. [P45983-3 ]
    uc001jgp.3. human. [P45983-1 ]
    uc001jgq.3. human. [P45983-2 ]

    Organism-specific databases

    CTDi 5599.
    GeneCardsi GC10P049514.
    HGNCi HGNC:6881. MAPK8.
    HPAi CAB004463.
    MIMi 601158. gene.
    neXtProti NX_P45983.
    PharmGKBi PA283.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG014652.
    InParanoidi P45983.
    KOi K04440.
    OMAi REHTLEQ.
    OrthoDBi EOG7PCJGV.
    PhylomeDBi P45983.
    TreeFami TF105100.

    Enzyme and pathway databases

    BRENDAi 2.7.11.24. 2681.
    Reactomei REACT_13638. NRAGE signals death through JNK.
    REACT_13643. NRIF signals cell death from the nucleus.
    REACT_163701. FCERI mediated MAPK activation.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_2100. Activation of BMF and translocation to mitochondria.
    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.
    REACT_25299. DSCAM interactions.
    SignaLinki P45983.

    Miscellaneous databases

    EvolutionaryTracei P45983.
    GeneWikii MAPK8.
    GenomeRNAii 5599.
    NextBioi 21738.
    PROi P45983.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P45983.
    Bgeei P45983.
    CleanExi HS_MAPK8.
    Genevestigatori P45983.

    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. "JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain."
      Derijard B., Hibi M., Wu I.-H., Barrett T., Su B., Deng T., Karin M., Davis R.J.
      Cell 76:1025-1037(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetal brain.
    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], ALTERNATIVE SPLICING.
      Tissue: Brain.
    3. Lin L., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M., Tang Z., Huang B., Li H., Yang S.
      Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
    4. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 3).
    8. "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.
    9. "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: PHOSPHORYLATION AT THR-183 AND TYR-185, REGULATION BY MAP2K4 AND MAP2K7, COFACTOR.
    10. "The evi-1 oncoprotein inhibits c-Jun N-terminal kinase and prevents stress-induced cell death."
      Kurokawa M., Mitani K., Yamagata T., Takahashi T., Izutsu K., Ogawa S., Moriguchi T., Nishida E., Yazaki Y., Hirai H.
      EMBO J. 19:2958-2968(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MECOM.
    11. "JNK1 physically interacts with WW domain-containing oxidoreductase (WOX1) and inhibits WOX1-mediated apoptosis."
      Chang N.-S., Doherty J., Ensign A.
      J. Biol. Chem. 278:9195-9202(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WWOX AND TP53.
    12. "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.
    13. "Association and regulation of heat shock transcription factor 4b with both extracellular signal-regulated kinase mitogen-activated protein kinase and dual-specificity tyrosine phosphatase DUSP26."
      Hu Y., Mivechi N.F.
      Mol. Cell. Biol. 26:3282-3294(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HSF4.
    14. "Nuclear factor of activated T3 is a negative regulator of Ras-JNK1/2-AP-1 induced cell transformation."
      Yao K., Cho Y.-Y., Bergen H.R. III, Madden B.J., Choi B.Y., Ma W.-Y., Bode A.M., Dong Z.
      Cancer Res. 67:8725-8735(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NFATC4.
    15. "Prostate-derived sterile 20-like kinase 1-alpha induces apoptosis. JNK-and caspase-dependent nuclear localization is a requirement for membrane blebbing."
      Zihni C., Mitsopoulos C., Tavares I.A., Baum B., Ridley A.J., Morris J.D.
      J. Biol. Chem. 282:6484-6493(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY TAOK2.
    16. "Rev7/MAD2B links c-Jun N-terminal protein kinase pathway signaling to activation of the transcription factor Elk-1."
      Zhang L., Yang S.H., Sharrocks A.D.
      Mol. Cell. Biol. 27:2861-2869(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF ELK1.
    17. "Phosphorylation of two eukaryotic transcription factors, Jun dimerization protein 2 and activation transcription factor 2, in Escherichia coli by Jun N-terminal kinase 1."
      Murata T., Shinozuka Y., Obata Y., Yokoyama K.K.
      Anal. Biochem. 376:115-121(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF JDP2.
    18. "JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy."
      Wei Y., Pattingre S., Sinha S., Bassik M., Levine B.
      Mol. Cell 30:678-688(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF BCL2.
    19. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 (ISOFORMS 1 AND 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "Crystal structure of SCCA1 and insight about the interaction with JNK1."
      Zheng B., Matoba Y., Kumagai T., Katagiri C., Hibino T., Sugiyama M.
      Biochem. Biophys. Res. Commun. 380:143-147(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SERPINB3, ENZYME REGULATION.
    22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 (ISOFORMS 1 AND 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "JNK1 phosphorylates SIRT1 and promotes its enzymatic activity."
      Nasrin N., Kaushik V.K., Fortier E., Wall D., Pearson K.J., de Cabo R., Bordone L.
      PLoS ONE 4:E8414-E8414(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF SIRT1.
    24. "JNK phosphorylates Yes-associated protein (YAP) to regulate apoptosis."
      Tomlinson V., Gudmundsdottir K., Luong P., Leung K.Y., Knebel A., Basu S.
      Cell Death Dis. 1:E29-E29(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF YAP1.
    25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "A critical step for JNK activation: isomerization by the prolyl isomerase Pin1."
      Park J.E., Lee J.A., Park S.G., Lee D.H., Kim S.J., Kim H.J., Uchida C., Uchida T., Park B.C., Cho S.
      Cell Death Differ. 19:153-161(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIN1.
    27. "Phosphorylation of Bcl-associated death protein (Bad) by erythropoietin-activated c-Jun N-terminal protein kinase 1 contributes to survival of erythropoietin-dependent cells."
      Deng H., Zhang J., Yoon T., Song D., Li D., Lin A.
      Int. J. Biochem. Cell Biol. 43:409-415(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF BAD.
    28. "Defective anchoring of JNK1 in the cytoplasm by MKK7 in Jurkat cells is associated with resistance to Fas-mediated apoptosis."
      Wang J., Tang R., Lv M., Wang Q., Zhang X., Guo Y., Chang H., Qiao C., Xiao H., Li X., Li Y., Shen B., Zhang J.
      Mol. Biol. Cell 22:117-127(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    29. "JNK1 phosphorylation of Cdt1 inhibits recruitment of HBO1 histone acetylase and blocks replication licensing in response to stress."
      Miotto B., Struhl K.
      Mol. Cell 44:62-71(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CDT1.
    30. "Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125."
      Heo Y.S., Kim S.K., Seo C.I., Kim Y.K., Sung B.J., Lee H.S., Lee J.I., Park S.Y., Kim J.H., Hwang K.Y., Hyun Y.L., Jeon Y.H., Ro S., Cho J.M., Lee T.G., Yang C.H.
      EMBO J. 23:2185-2195(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-363.
    31. "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] SER-171 AND ARG-177.

    Entry informationi

    Entry nameiMK08_HUMAN
    AccessioniPrimary (citable) accession number: P45983
    Secondary accession number(s): B5BTZ5
    , B7ZLV4, D3DX88, D3DX92, Q15709, Q15712, Q15713, Q308M2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 166 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 10
      Human chromosome 10: 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