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Q9HBH9

- MKNK2_HUMAN

UniProt

Q9HBH9 - MKNK2_HUMAN

Protein

MAP kinase-interacting serine/threonine-protein kinase 2

Gene

MKNK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 3 (07 Mar 2006)
      Previous versions | rss
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    Functioni

    Serine/threonine-protein kinase that phosphorylates SFPQ/PSF, HNRNPA1 and EIF4E. May play a role in the response to environmental stress and cytokines. Appears to regulate translation by phosphorylating EIF4E, thus increasing the affinity of this protein for the 7-methylguanosine-containing mRNA cap. Required for mediating PP2A-inhibition-induced EIF4E phosphorylation. Triggers EIF4E shuttling from cytoplasm to nucleus. Isoform 1 displays a high basal kinase activity, but isoform 2 exhibits a very low kinase activity. Acts as a mediator of the suppressive effects of IFNgamma on hematopoiesis. Negative regulator for signals that control generation of arsenic trioxide As2O(3)-dependent apoptosis and anti-leukemic responses. Involved in anti-apoptotic signaling in response to serum withdrawal.9 Publications

    Catalytic activityi

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

    Cofactori

    Magnesium.1 Publication
    Binds 1 zinc ion per subunit.

    Enzyme regulationi

    Inhibited by CGP57380 and staurosporine. Activated by phosphorylation in a negative-feedback regulatory manner in response to chemotherapy (e.g. cytarabine) and thus impairs the generation of antileukemic responses.6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei113 – 1131ATPPROSITE-ProRule annotation
    Active sitei205 – 2051Proton acceptorPROSITE-ProRule annotation
    Binding sitei209 – 2091Staurosporine1 Publication
    Metal bindingi299 – 2991Zinc2 Publications
    Metal bindingi311 – 3111Zinc2 Publications
    Metal bindingi314 – 3141Zinc2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi90 – 989ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. cell surface receptor signaling pathway Source: ProtInc
    2. cellular response to arsenic-containing substance Source: UniProtKB
    3. extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
    4. hemopoiesis Source: UniProtKB
    5. intracellular signal transduction Source: UniProtKB
    6. protein phosphorylation Source: UniProtKB
    7. regulation of translation Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Translation regulation

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ9HBH9.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    MAP kinase-interacting serine/threonine-protein kinase 2 (EC:2.7.11.1)
    Alternative name(s):
    MAP kinase signal-integrating kinase 2
    Short name:
    MAPK signal-integrating kinase 2
    Short name:
    Mnk2
    Gene namesi
    Name:MKNK2
    Synonyms:GPRK7, MNK2
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:7111. MKNK2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleolus Source: HPA
    3. nucleus Source: HPA
    4. PML body Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi228 – 2281D → G: Reduced phosphorylation. 1 Publication
    Mutagenesisi244 – 2441T → A: Loss of kinase activity; when associated with T-249. 1 Publication
    Mutagenesisi249 – 2491T → A: Loss of kinase activity; when associated with T-244. 1 Publication
    Mutagenesisi379 – 3791T → D: Constitutively active. 1 Publication

    Organism-specific databases

    PharmGKBiPA30830.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 465465MAP kinase-interacting serine/threonine-protein kinase 2PRO_0000086336Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei74 – 741PhosphoserineBy similarity
    Modified residuei244 – 2441Phosphothreonine1 Publication
    Modified residuei249 – 2491Phosphothreonine1 Publication
    Modified residuei379 – 3791Phosphothreonine1 Publication
    Modified residuei437 – 4371PhosphoserineBy similarity
    Modified residuei440 – 4401PhosphoserineBy similarity
    Modified residuei452 – 4521PhosphoserineBy similarity

    Post-translational modificationi

    Dual phosphorylation of Thr-244 and Thr-249 activates the kinase. Phosphorylation of Thr-379 activates the kinase. Phosphorylated upon arsenic trioxide As2O3 treatment. Phosphorylated by MAPK1/ERK2, MAPK11 and MAPK14. Dephosphorylated by PP2A.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9HBH9.
    PaxDbiQ9HBH9.
    PRIDEiQ9HBH9.

    PTM databases

    PhosphoSiteiQ9HBH9.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed in all tissues examined. Isoform 2 is expressed at higher levels in the ovary than is isoform 1.1 Publication

    Gene expression databases

    ArrayExpressiQ9HBH9.
    BgeeiQ9HBH9.
    CleanExiHS_MKNK2.
    GenevestigatoriQ9HBH9.

    Organism-specific databases

    HPAiCAB037253.
    HPA021875.
    HPA053989.

    Interactioni

    Subunit structurei

    Monomer. Interacts with the C-terminal regions of EIF4G1 and EIF4G2; this interaction is promoted when MAPK pathways are repressed but repressed upon ERK proteins activation. Also binds to dephosphorylated MAPK3/ERK1 and MAPK1/ERK2. Isoform 1 interaction with phosphorylated MAPK3/ERK1 and MAPK1/ERK2 protects it from dephosphorylation and inactivation. Isoform 2 interacts with ESR2 and EIF4E in the nucleus.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MAPK14Q165393EBI-2864341,EBI-73946

    Protein-protein interaction databases

    BioGridi109130. 13 interactions.
    IntActiQ9HBH9. 6 interactions.
    STRINGi9606.ENSP00000250896.

    Structurei

    Secondary structure

    1
    465
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi74 – 763
    Turni79 – 813
    Beta strandi83 – 853
    Beta strandi94 – 1029
    Beta strandi104 – 1063
    Beta strandi109 – 1168
    Helixi123 – 13513
    Beta strandi145 – 1517
    Beta strandi154 – 1607
    Helixi167 – 1748
    Helixi179 – 19820
    Helixi208 – 2103
    Beta strandi211 – 2144
    Beta strandi216 – 2194
    Beta strandi221 – 2244
    Helixi254 – 2563
    Helixi259 – 2646
    Helixi267 – 2726
    Helixi273 – 2753
    Helixi276 – 29015
    Helixi312 – 32413
    Helixi331 – 3344
    Helixi339 – 34810
    Turni353 – 3553
    Helixi359 – 3646
    Turni366 – 3683

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AC3X-ray2.10A72-385[»]
    2AC5X-ray3.20A72-385[»]
    2HW7X-ray2.71A72-385[»]
    ProteinModelPortaliQ9HBH9.
    SMRiQ9HBH9. Positions 71-413.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9HBH9.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini84 – 388305Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni160 – 1623Staurosporine binding

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi60 – 667Nuclear localization signal
    Motifi444 – 4485MAP kinase bindingBy similarity

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG106949.
    InParanoidiQ9HBH9.
    KOiK04372.
    OMAiVQKKTAE.
    PhylomeDBiQ9HBH9.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 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 11 Publication (identifier: Q9HBH9-1) [UniParc]FASTAAdd to Basket

    Also known as: 2a1 Publication

    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

    MVQKKPAELQ GFHRSFKGQN PFELAFSLDQ PDHGDSDFGL QCSARPDMPA    50
    SQPIDIPDAK KRGKKKKRGR ATDSFSGRFE DVYQLQEDVL GEGAHARVQT 100
    CINLITSQEY AVKIIEKQPG HIRSRVFREV EMLYQCQGHR NVLELIEFFE 150
    EEDRFYLVFE KMRGGSILSH IHKRRHFNEL EASVVVQDVA SALDFLHNKG 200
    IAHRDLKPEN ILCEHPNQVS PVKICDFDLG SGIKLNGDCS PISTPELLTP 250
    CGSAEYMAPE VVEAFSEEAS IYDKRCDLWS LGVILYILLS GYPPFVGRCG 300
    SDCGWDRGEA CPACQNMLFE SIQEGKYEFP DKDWAHISCA AKDLISKLLV 350
    RDAKQRLSAA QVLQHPWVQG CAPENTLPTP MVLQRNSCAK DLTSFAAEAI 400
    AMNRQLAQHD EDLAEEEAAG QGQPVLVRAT SRCLQLSPPS QSKLAQRRQR 450
    ASLSSAPVVL VGDHA 465
    Length:465
    Mass (Da):51,875
    Last modified:March 7, 2006 - v3
    Checksum:iD6D4BE6C541012B1
    GO
    Isoform 21 Publication (identifier: Q9HBH9-2) [UniParc]FASTAAdd to Basket

    Also known as: 2b1 Publication

    The sequence of this isoform differs from the canonical sequence as follows:
         386-414: NSCAKDLTSFAAEAIAMNRQLAQHDEDLA → WDSHFLLPPHPCRIHVRPGGLVRTVTVNE
         415-465: Missing.

    Show »
    Length:414
    Mass (Da):46,711
    Checksum:iBA5E7C107CB3FD43
    GO
    Isoform 31 Publication (identifier: Q9HBH9-3)

    Sequence is not available
    Length:
    Mass (Da):
    Isoform 41 Publication (identifier: Q9HBH9-4)

    Sequence is not available
    Length:
    Mass (Da):
    Isoform 51 Publication (identifier: Q9HBH9-5)

    Sequence is not available
    Length:
    Mass (Da):

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti261 – 2611V → L in AAF17226. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti10 – 101Q → K.
    Corresponds to variant rs3746101 [ dbSNP | Ensembl ].
    VAR_051648
    Natural varianti73 – 731D → N.1 Publication
    Corresponds to variant rs56158214 [ dbSNP | Ensembl ].
    VAR_040805
    Natural varianti428 – 4281R → Q.
    Corresponds to variant rs34475638 [ dbSNP | Ensembl ].
    VAR_051649

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei386 – 41429NSCAK…DEDLA → WDSHFLLPPHPCRIHVRPGG LVRTVTVNE in isoform 2. 3 PublicationsVSP_007353Add
    BLAST
    Alternative sequencei415 – 46551Missing in isoform 2. 3 PublicationsVSP_007354Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF237775 mRNA. Translation: AAG26336.1.
    AF237776 mRNA. Translation: AAG26337.1.
    AF125532 mRNA. Translation: AAF17226.1.
    BC073140 mRNA. Translation: AAH73140.1.
    CCDSiCCDS12079.1. [Q9HBH9-2]
    CCDS12080.1. [Q9HBH9-1]
    RefSeqiNP_060042.2. NM_017572.3. [Q9HBH9-2]
    NP_951009.1. NM_199054.2. [Q9HBH9-1]
    UniGeneiHs.515032.

    Genome annotation databases

    EnsembliENST00000250896; ENSP00000250896; ENSG00000099875. [Q9HBH9-1]
    ENST00000309340; ENSP00000309485; ENSG00000099875. [Q9HBH9-2]
    ENST00000591601; ENSP00000467811; ENSG00000099875. [Q9HBH9-1]
    GeneIDi2872.
    KEGGihsa:2872.
    UCSCiuc002lur.2. human. [Q9HBH9-2]
    uc002lus.2. human. [Q9HBH9-1]

    Polymorphism databases

    DMDMi90102033.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF237775 mRNA. Translation: AAG26336.1 .
    AF237776 mRNA. Translation: AAG26337.1 .
    AF125532 mRNA. Translation: AAF17226.1 .
    BC073140 mRNA. Translation: AAH73140.1 .
    CCDSi CCDS12079.1. [Q9HBH9-2 ]
    CCDS12080.1. [Q9HBH9-1 ]
    RefSeqi NP_060042.2. NM_017572.3. [Q9HBH9-2 ]
    NP_951009.1. NM_199054.2. [Q9HBH9-1 ]
    UniGenei Hs.515032.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AC3 X-ray 2.10 A 72-385 [» ]
    2AC5 X-ray 3.20 A 72-385 [» ]
    2HW7 X-ray 2.71 A 72-385 [» ]
    ProteinModelPortali Q9HBH9.
    SMRi Q9HBH9. Positions 71-413.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109130. 13 interactions.
    IntActi Q9HBH9. 6 interactions.
    STRINGi 9606.ENSP00000250896.

    Chemistry

    BindingDBi Q9HBH9.
    ChEMBLi CHEMBL4204.
    GuidetoPHARMACOLOGYi 2105.

    PTM databases

    PhosphoSitei Q9HBH9.

    Polymorphism databases

    DMDMi 90102033.

    Proteomic databases

    MaxQBi Q9HBH9.
    PaxDbi Q9HBH9.
    PRIDEi Q9HBH9.

    Protocols and materials databases

    DNASUi 2872.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000250896 ; ENSP00000250896 ; ENSG00000099875 . [Q9HBH9-1 ]
    ENST00000309340 ; ENSP00000309485 ; ENSG00000099875 . [Q9HBH9-2 ]
    ENST00000591601 ; ENSP00000467811 ; ENSG00000099875 . [Q9HBH9-1 ]
    GeneIDi 2872.
    KEGGi hsa:2872.
    UCSCi uc002lur.2. human. [Q9HBH9-2 ]
    uc002lus.2. human. [Q9HBH9-1 ]

    Organism-specific databases

    CTDi 2872.
    GeneCardsi GC19M002037.
    HGNCi HGNC:7111. MKNK2.
    HPAi CAB037253.
    HPA021875.
    HPA053989.
    MIMi 605069. gene.
    neXtProti NX_Q9HBH9.
    PharmGKBi PA30830.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG106949.
    InParanoidi Q9HBH9.
    KOi K04372.
    OMAi VQKKTAE.
    PhylomeDBi Q9HBH9.

    Enzyme and pathway databases

    SignaLinki Q9HBH9.

    Miscellaneous databases

    EvolutionaryTracei Q9HBH9.
    GeneWikii MKNK2.
    GenomeRNAii 2872.
    NextBioi 11333.
    PROi Q9HBH9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HBH9.
    Bgeei Q9HBH9.
    CleanExi HS_MKNK2.
    Genevestigatori Q9HBH9.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of the human Mnk2 gene (MKNK2) through protein interaction with estrogen receptor beta."
      Slentz-Kesler K., Moore J.T., Lombard M., Zhang J., Hollingsworth R., Weiner M.P.
      Genomics 69:63-71(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), TISSUE SPECIFICITY, INTERACTION WITH ESR2.
      Tissue: Fetal brain.
    2. "A novel gene expressed in human adrenal gland."
      Li Y., Shi J., Huang C., Ren S., Fu S., Zhou J., Yu Y., Xu S., Wang Y., Fu G., Chen Z., Han Z.
      Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Adrenal gland.
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 2).
      Tissue: Uterus.
    5. "The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a eukaryotic initiation factor 4E kinase with high levels of basal activity in mammalian cells."
      Scheper G.C., Morrice N.A., Kleijn M., Proud C.G.
      Mol. Cell. Biol. 21:743-754(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS EIF4E KINASE, ENZYME REGULATION, ALTERNATIVE SPLICING, PHOSPHORYLATION BY MAPK1/ERK2; MAPK11 AND MAPK14, INTERACTION WITH EIF4G PROTEINS.
    6. "Negative regulation of protein translation by mitogen-activated protein kinase-interacting kinases 1 and 2."
      Knauf U., Tschopp C., Gram H.
      Mol. Cell. Biol. 21:5500-5511(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT THR-244; THR-249 AND THR-379, MUTAGENESIS OF THR-244; THR-249 AND THR-379.
      Tissue: Leukocyte.
    7. "The N and C termini of the splice variants of the human mitogen-activated protein kinase-interacting kinase Mnk2 determine activity and localization."
      Scheper G.C., Parra J.L., Wilson M., Van Kollenburg B., Vertegaal A.C.O., Han Z.-G., Proud C.G.
      Mol. Cell. Biol. 23:5692-5705(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS EIF4E KINASE, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH EIF4E; EIF4G1 AND EIF4G2.
    8. "The Mnks are novel components in the control of TNF alpha biosynthesis and phosphorylate and regulate hnRNP A1."
      Buxade M., Parra J.L., Rousseau S., Shpiro N., Marquez R., Morrice N., Bain J., Espel E., Proud C.G.
      Immunity 23:177-189(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS HNRNPA1 KINASE, ENZYME REGULATION.
    9. "The PSF.p54nrb complex is a novel Mnk substrate that binds the mRNA for tumor necrosis factor alpha."
      Buxade M., Morrice N., Krebs D.L., Proud C.G.
      J. Biol. Chem. 283:57-65(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS SFPQ/PSF KINASE.
    10. Cited for: FUNCTION IN ARSENIC TRIOXIDE SIGNALING, PHOSPHORYLATION IN RESPONSE TO ARSENIC TRIOXIDE.
    11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "Discovery of mitogen-activated protein kinase-interacting kinase 1 inhibitors by a comprehensive fragment-oriented virtual screening approach."
      Oyarzabal J., Zarich N., Albarran M.I., Palacios I., Urbano-Cuadrado M., Mateos G., Reymundo I., Rabal O., Salgado A., Corrionero A., Fominaya J., Pastor J., Bischoff J.R.
      J. Med. Chem. 53:6618-6628(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    15. "Regulation of eukaryotic initiation factor 4E (eIF4E) phosphorylation by mitogen-activated protein kinase occurs through modulation of Mnk1-eIF4G interaction."
      Shveygert M., Kaiser C., Bradrick S.S., Gromeier M.
      Mol. Cell. Biol. 30:5160-5167(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS EIF4E KINASE, INTERACTION WITH EIF4G1.
    16. "Negative regulatory effects of Mnk kinases in the generation of chemotherapy-induced antileukemic responses."
      Altman J.K., Glaser H., Sassano A., Joshi S., Ueda T., Watanabe-Fukunaga R., Fukunaga R., Tallman M.S., Platanias L.C.
      Mol. Pharmacol. 78:778-784(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    17. "Protein phosphatase 2A negatively regulates eukaryotic initiation factor 4E phosphorylation and eIF4F assembly through direct dephosphorylation of Mnk and eIF4E."
      Li Y., Yue P., Deng X., Ueda T., Fukunaga R., Khuri F.R., Sun S.-Y.
      Neoplasia 12:848-855(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN EIF4E PHOSPHORYLATION REGULATION, DEPHOSPHORYLATION BY PP2A, ENZYME REGULATION.
    18. "Essential role for Mnk kinases in type II interferon (IFNgamma) signaling and its suppressive effects on normal hematopoiesis."
      Joshi S., Sharma B., Kaur S., Majchrzak B., Ueda T., Fukunaga R., Verma A.K., Fish E.N., Platanias L.C.
      J. Biol. Chem. 286:6017-6026(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN IFNGAMMA SIGNALING.
    19. "The Mnks: MAP kinase-interacting kinases (MAP kinase signal-integrating kinases)."
      Buxade M., Parra-Palau J.L., Proud C.G.
      Front. Biosci. 13:5359-5373(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    20. "Crystal structures of the Mnk2 kinase domain reveal an inhibitory conformation and a zinc binding site."
      Jauch R., Jaekel S., Netter C., Schreiter K., Aicher B., Jaeckle H., Wahl M.C.
      Structure 13:1559-1568(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 72-385 IN COMPLEX WITH ZINC, SUBUNIT.
    21. "Mitogen-activated protein kinases interacting kinases are autoinhibited by a reprogrammed activation segment."
      Jauch R., Cho M.-K., Jaekel S., Netter C., Schreiter K., Aicher B., Zweckstetter M., Jaeckle H., Wahl M.C.
      EMBO J. 25:4020-4032(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 72-385 IN COMPLEX WITH ZINC AND STAUROSPORINE, ENZYME REGULATION, MUTAGENESIS OF ASP-228.
    22. "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: VARIANT [LARGE SCALE ANALYSIS] ASN-73.

    Entry informationi

    Entry nameiMKNK2_HUMAN
    AccessioniPrimary (citable) accession number: Q9HBH9
    Secondary accession number(s): Q6GPI3
    , Q9HBH8, Q9UHR0, Q9Y2N6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 30, 2003
    Last sequence update: March 7, 2006
    Last modified: October 1, 2014
    This is version 138 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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