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Q9BUB5

- MKNK1_HUMAN

UniProt

Q9BUB5 - MKNK1_HUMAN

Protein

MAP kinase-interacting serine/threonine-protein kinase 1

Gene

MKNK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    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.4 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.2 Publications

    Cofactori

    Magnesium.2 Publications

    Enzyme regulationi

    Phosphorylated and activated by the p38 kinases and kinases in the Erk pathway.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei78 – 781ATP1 PublicationPROSITE-ProRule annotation
    Active sitei211 – 2111Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi55 – 639ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
    2. fibroblast growth factor receptor signaling pathway Source: Reactome
    3. intracellular signal transduction Source: UniProtKB
    4. peptidyl-serine phosphorylation Source: BHF-UCL
    5. protein phosphorylation Source: UniProtKB
    6. regulation of translation Source: UniProtKB-KW
    7. response to salt stress Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Translation regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_111080. Spry regulation of FGF signaling.
    SignaLinkiQ9BUB5.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    MAP kinase-interacting serine/threonine-protein kinase 1 (EC:2.7.11.1)
    Alternative name(s):
    MAP kinase signal-integrating kinase 1
    Short name:
    MAPK signal-integrating kinase 1
    Short name:
    Mnk1
    Gene namesi
    Name:MKNK1
    Synonyms:MNK1
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:7110. MKNK1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi78 – 781K → M: Loss of kinase activity; when associated with D-232. 1 Publication
    Mutagenesisi232 – 2321D → A: Loss of kinase activity; when associated with K-78. 1 Publication
    Mutagenesisi250 – 2501T → A: Loss of kinase activity; when associated with T-255. 1 Publication
    Mutagenesisi255 – 2551T → A: Loss of kinase activity; when associated with T-250. 1 Publication
    Mutagenesisi385 – 3851T → D: Constitutively active. 1 Publication

    Organism-specific databases

    PharmGKBiPA30829.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 465465MAP kinase-interacting serine/threonine-protein kinase 1PRO_0000086334Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei39 – 391Phosphoserine; by PAK2By similarity
    Modified residuei250 – 2501Phosphothreonine1 Publication
    Modified residuei255 – 2551Phosphothreonine1 Publication
    Modified residuei385 – 3851Phosphothreonine1 Publication
    Modified residuei460 – 4601Phosphoserine1 Publication

    Post-translational modificationi

    Dual phosphorylation of Thr-250 and Thr-255 activates the kinase. Phosphorylation of Thr-385 activates the kinase. MAPK3/ERK1 is one of the kinases which activate MKNK1/MNK1. Phosphorylation by PAK2 leads to a reduced phosphorylation of EIF4G1.5 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9BUB5.
    PaxDbiQ9BUB5.
    PRIDEiQ9BUB5.

    PTM databases

    PhosphoSiteiQ9BUB5.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiQ9BUB5.
    BgeeiQ9BUB5.
    CleanExiHS_MKNK1.
    GenevestigatoriQ9BUB5.

    Interactioni

    Subunit structurei

    Interacts with the C-terminal regions of EIF4G1 and EIF4G2. Also binds to dephosphorylated ERK1 and ERK2, and to the p38 kinases.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MAPK14Q165393EBI-73837,EBI-73946

    Protein-protein interaction databases

    BioGridi114138. 24 interactions.
    IntActiQ9BUB5. 17 interactions.
    MINTiMINT-85533.
    STRINGi9606.ENSP00000361014.

    Structurei

    Secondary structure

    1
    465
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi44 – 463
    Beta strandi48 – 5710
    Beta strandi59 – 6810
    Turni69 – 713
    Beta strandi74 – 818
    Helixi87 – 10115
    Beta strandi110 – 1156
    Beta strandi117 – 1259
    Helixi132 – 1398
    Helixi144 – 16320
    Helixi214 – 2163
    Beta strandi217 – 2204
    Beta strandi227 – 2304
    Beta strandi271 – 2744
    Helixi277 – 29620
    Helixi337 – 3404
    Helixi345 – 35410
    Turni359 – 3613
    Helixi365 – 3706
    Turni372 – 3754
    Helixi439 – 4413
    Helixi443 – 4497

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HW6X-ray2.50A/B37-382[»]
    2Y9QX-ray1.55B434-451[»]
    ProteinModelPortaliQ9BUB5.
    SMRiQ9BUB5. Positions 39-407.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BUB5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini49 – 374326Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG106949.
    InParanoidiQ9BUB5.
    KOiK04372.
    OMAiASFYDKR.
    PhylomeDBiQ9BUB5.
    TreeFamiTF314050.

    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. 2 hits.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q9BUB5-1) [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

    MVSSQKLEKP IEMGSSEPLP IADGDRRRKK KRRGRATDSL PGKFEDMYKL    50
    TSELLGEGAY AKVQGAVSLQ NGKEYAVKII EKQAGHSRSR VFREVETLYQ 100
    CQGNKNILEL IEFFEDDTRF YLVFEKLQGG SILAHIQKQK HFNEREASRV 150
    VRDVAAALDF LHTKDKVSLC HLGWSAMAPS GLTAAPTSLG SSDPPTSASQ 200
    VAGTTGIAHR DLKPENILCE SPEKVSPVKI CDFDLGSGMK LNNSCTPITT 250
    PELTTPCGSA EYMAPEVVEV FTDQATFYDK RCDLWSLGVV LYIMLSGYPP 300
    FVGHCGADCG WDRGEVCRVC QNKLFESIQE GKYEFPDKDW AHISSEAKDL 350
    ISKLLVRDAK QRLSAAQVLQ HPWVQGQAPE KGLPTPQVLQ RNSSTMDLTL 400
    FAAEAIALNR QLSQHEENEL AEEPEALADG LCSMKLSPPC KSRLARRRAL 450
    AQAGRGEDRS PPTAL 465
    Length:465
    Mass (Da):51,342
    Last modified:June 1, 2001 - v1
    Checksum:iCAE225C35DCB2B43
    GO
    Isoform 21 Publication (identifier: Q9BUB5-2) [UniParc]FASTAAdd to Basket

    Also known as: MNK1a

    The sequence of this isoform differs from the canonical sequence as follows:
         165-205: Missing.

    Show »
    Length:424
    Mass (Da):47,402
    Checksum:iDB39E49EC0BED990
    GO
    Isoform 3 (identifier: Q9BUB5-3) [UniParc]FASTAAdd to Basket

    Also known as: MNK1b

    The sequence of this isoform differs from the canonical sequence as follows:
         165-205: Missing.
         377-465: QAPEKGLPTP...GEDRSPPTAL → EQQHNGPDALRS

    Show »
    Length:347
    Mass (Da):39,104
    Checksum:i1CCA03B12D39641F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti49 – 491K → Q.1 Publication
    Corresponds to variant rs56351860 [ dbSNP | Ensembl ].
    VAR_040801
    Natural varianti158 – 1581L → V.1 Publication
    Corresponds to variant rs56408722 [ dbSNP | Ensembl ].
    VAR_040802
    Natural varianti308 – 3081D → N.1 Publication
    Corresponds to variant rs55791614 [ dbSNP | Ensembl ].
    VAR_040803
    Natural varianti446 – 4461R → Q.1 Publication
    Corresponds to variant rs34881418 [ dbSNP | Ensembl ].
    VAR_040804

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei165 – 20541Missing in isoform 2 and isoform 3. 2 PublicationsVSP_007352Add
    BLAST
    Alternative sequencei377 – 46589QAPEK…PPTAL → EQQHNGPDALRS in isoform 3. 1 PublicationVSP_017515Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB000409 mRNA. Translation: BAA19885.1.
    AY355461 mRNA. Translation: AAQ84219.1.
    AL136373 Genomic DNA. Translation: CAI14764.1.
    AL136373 Genomic DNA. Translation: CAI14765.1.
    CH471059 Genomic DNA. Translation: EAX06900.1.
    CH471059 Genomic DNA. Translation: EAX06902.1.
    CH471059 Genomic DNA. Translation: EAX06904.1.
    CH471059 Genomic DNA. Translation: EAX06905.1.
    BC002755 mRNA. Translation: AAH02755.1.
    CCDSiCCDS30705.1. [Q9BUB5-3]
    CCDS44134.1. [Q9BUB5-2]
    CCDS538.1. [Q9BUB5-1]
    RefSeqiNP_001129025.1. NM_001135553.2. [Q9BUB5-2]
    NP_003675.2. NM_003684.5. [Q9BUB5-1]
    NP_945324.1. NM_198973.3. [Q9BUB5-3]
    XP_006711063.1. XM_006711000.1. [Q9BUB5-2]
    XP_006711075.1. XM_006711012.1. [Q9BUB5-3]
    UniGeneiHs.371594.

    Genome annotation databases

    EnsembliENST00000341183; ENSP00000339573; ENSG00000079277. [Q9BUB5-3]
    ENST00000371945; ENSP00000361013; ENSG00000079277. [Q9BUB5-2]
    ENST00000371946; ENSP00000361014; ENSG00000079277. [Q9BUB5-1]
    ENST00000428112; ENSP00000411135; ENSG00000079277. [Q9BUB5-3]
    GeneIDi8569.
    KEGGihsa:8569.
    UCSCiuc001cqb.4. human. [Q9BUB5-1]
    uc001cqc.4. human. [Q9BUB5-2]
    uc009vyi.4. human. [Q9BUB5-3]

    Polymorphism databases

    DMDMi30316115.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB000409 mRNA. Translation: BAA19885.1 .
    AY355461 mRNA. Translation: AAQ84219.1 .
    AL136373 Genomic DNA. Translation: CAI14764.1 .
    AL136373 Genomic DNA. Translation: CAI14765.1 .
    CH471059 Genomic DNA. Translation: EAX06900.1 .
    CH471059 Genomic DNA. Translation: EAX06902.1 .
    CH471059 Genomic DNA. Translation: EAX06904.1 .
    CH471059 Genomic DNA. Translation: EAX06905.1 .
    BC002755 mRNA. Translation: AAH02755.1 .
    CCDSi CCDS30705.1. [Q9BUB5-3 ]
    CCDS44134.1. [Q9BUB5-2 ]
    CCDS538.1. [Q9BUB5-1 ]
    RefSeqi NP_001129025.1. NM_001135553.2. [Q9BUB5-2 ]
    NP_003675.2. NM_003684.5. [Q9BUB5-1 ]
    NP_945324.1. NM_198973.3. [Q9BUB5-3 ]
    XP_006711063.1. XM_006711000.1. [Q9BUB5-2 ]
    XP_006711075.1. XM_006711012.1. [Q9BUB5-3 ]
    UniGenei Hs.371594.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HW6 X-ray 2.50 A/B 37-382 [» ]
    2Y9Q X-ray 1.55 B 434-451 [» ]
    ProteinModelPortali Q9BUB5.
    SMRi Q9BUB5. Positions 39-407.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114138. 24 interactions.
    IntActi Q9BUB5. 17 interactions.
    MINTi MINT-85533.
    STRINGi 9606.ENSP00000361014.

    Chemistry

    BindingDBi Q9BUB5.
    ChEMBLi CHEMBL4718.
    GuidetoPHARMACOLOGYi 2104.

    PTM databases

    PhosphoSitei Q9BUB5.

    Polymorphism databases

    DMDMi 30316115.

    Proteomic databases

    MaxQBi Q9BUB5.
    PaxDbi Q9BUB5.
    PRIDEi Q9BUB5.

    Protocols and materials databases

    DNASUi 8569.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000341183 ; ENSP00000339573 ; ENSG00000079277 . [Q9BUB5-3 ]
    ENST00000371945 ; ENSP00000361013 ; ENSG00000079277 . [Q9BUB5-2 ]
    ENST00000371946 ; ENSP00000361014 ; ENSG00000079277 . [Q9BUB5-1 ]
    ENST00000428112 ; ENSP00000411135 ; ENSG00000079277 . [Q9BUB5-3 ]
    GeneIDi 8569.
    KEGGi hsa:8569.
    UCSCi uc001cqb.4. human. [Q9BUB5-1 ]
    uc001cqc.4. human. [Q9BUB5-2 ]
    uc009vyi.4. human. [Q9BUB5-3 ]

    Organism-specific databases

    CTDi 8569.
    GeneCardsi GC01M047023.
    HGNCi HGNC:7110. MKNK1.
    MIMi 606724. gene.
    neXtProti NX_Q9BUB5.
    PharmGKBi PA30829.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG106949.
    InParanoidi Q9BUB5.
    KOi K04372.
    OMAi ASFYDKR.
    PhylomeDBi Q9BUB5.
    TreeFami TF314050.

    Enzyme and pathway databases

    Reactomei REACT_111080. Spry regulation of FGF signaling.
    SignaLinki Q9BUB5.

    Miscellaneous databases

    EvolutionaryTracei Q9BUB5.
    GeneWikii MKNK1.
    GenomeRNAii 8569.
    NextBioi 32143.
    PROi Q9BUB5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BUB5.
    Bgeei Q9BUB5.
    CleanExi HS_MKNK1.
    Genevestigatori Q9BUB5.

    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. 2 hits.
    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. "MNK1, a new MAP kinase-activated protein kinase, isolated by a novel expression screening method for identifying protein kinase substrates."
      Fukunaga R., Hunter T.
      EMBO J. 16:1921-1933(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, PHOSPHORYLATION BY MAPK3/ERK1, ENZYME REGULATION.
      Tissue: Cervix carcinoma.
    2. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, PHOSPHORYLATION AT THR-250; THR-255 AND THR-385, MUTAGENESIS OF LYS-78; ASP-232; THR-250; THR-255 AND THR-385.
      Tissue: T-cell.
    3. "Identification and molecular characterization of Mnk1b, a splice variant of human MAP kinase-interacting kinase Mnk1."
      O'Loghlen A., Gonzalez V.M., Pineiro D., Perez-Morgado M.I., Salinas M., Martin M.E.
      Exp. Cell Res. 299:343-355(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, SUBCELLULAR LOCATION.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [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 1).
      Tissue: Placenta.
    7. "Human eukaryotic translation initiation factor 4G (eIF4G) recruits mnk1 to phosphorylate eIF4E."
      Pyronnet S., Imataka H., Gingras A.-C., Fukunaga R., Hunter T., Sonenberg N.
      EMBO J. 18:270-279(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EIF4G1 AND EIF4G2.
    8. "Phosphorylation of Mnk1 by caspase-activated Pak2/gamma-PAK inhibits phosphorylation and interaction of eIF4G with Mnk."
      Orton K.C., Ling J., Waskiewicz A.J., Cooper J.A., Merrick W.C., Korneeva N.L., Rhoads R.E., Sonenberg N., Traugh J.A.
      J. Biol. Chem. 279:38649-38657(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY PAK2.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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] GLN-49; VAL-158; ASN-308 AND GLN-446.

    Entry informationi

    Entry nameiMKNK1_HUMAN
    AccessioniPrimary (citable) accession number: Q9BUB5
    Secondary accession number(s): D3DQ20
    , D3DQ21, O00312, Q5TC06, Q5TC07, Q6V0N6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 30, 2003
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 136 of the entry and version 1 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 1
      Human chromosome 1: 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