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Q16584

- M3K11_HUMAN

UniProt

Q16584 - M3K11_HUMAN

Protein

Mitogen-activated protein kinase kinase kinase 11

Gene

MAP3K11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Activates the JUN N-terminal pathway. Required for serum-stimulated cell proliferation and for mitogen and cytokine activation of MAPK14 (p38), MAPK3 (ERK) and MAPK8 (JNK1) through phosphorylation and activation of MAP2K4/MKK4 and MAP2K7/MKK7. Plays a role in mitogen-stimulated phosphorylation and activation of BRAF, but does not phosphorylate BRAF directly. Influences microtubule organization during the cell cycle.4 Publications

    Catalytic activityi

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

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Homodimerization via the leucine zipper domains is required for autophosphorylation and subsequent activation.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei144 – 1441ATP2 PublicationsPROSITE-ProRule annotation
    Active sitei241 – 2411Proton acceptorBy similarityPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi123 – 1319ATPBy similarityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. identical protein binding Source: UniProtKB
    3. JUN kinase kinase kinase activity Source: UniProtKB
    4. mitogen-activated protein kinase kinase kinase binding Source: UniProtKB
    5. protein binding Source: IntAct
    6. protein homodimerization activity Source: UniProtKB
    7. protein kinase activity Source: ProtInc
    8. protein serine/threonine kinase activity Source: UniProtKB
    9. protein tyrosine kinase activity Source: InterPro

    GO - Biological processi

    1. activation of JUN kinase activity Source: UniProtKB
    2. activation of MAPK activity Source: UniProtKB
    3. cell death Source: Ensembl
    4. cell proliferation Source: UniProtKB
    5. JNK cascade Source: ProtInc
    6. microtubule-based process Source: UniProtKB
    7. mitotic G1 phase Source: UniProtKB
    8. positive regulation of JNK cascade Source: UniProtKB
    9. positive regulation of JUN kinase activity Source: UniProtKB
    10. positive regulation of neuron apoptotic process Source: Ensembl
    11. protein autophosphorylation Source: UniProtKB
    12. protein phosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ16584.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase kinase kinase 11 (EC:2.7.11.25)
    Alternative name(s):
    Mixed lineage kinase 3
    Src-homology 3 domain-containing proline-rich kinase
    Gene namesi
    Name:MAP3K11Imported
    Synonyms:MLK31 Publication, PTK1, SPRKImported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:6850. MAP3K11.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication
    Note: Location is cell cycle dependent.

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytoplasm Source: UniProtKB-KW
    3. membrane Source: UniProtKB
    4. microtubule Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi144 – 1441K → A: Greatly reduced autophosphorylation activity. 2 Publications
    Mutagenesisi144 – 1441K → R: Loss of kinase activity. Prevents activation of SAPK and MAPK14. 2 Publications
    Mutagenesisi164 – 1641E → A: Greatly reduced autophosphorylation activity. 1 Publication
    Mutagenesisi277 – 2771T → A: Severely reduced autophosphorylation activity. Prevents phosphorylation of SAPK and MAPK14. 1 Publication
    Mutagenesisi277 – 2771T → E: No effect on SAPK activation. 1 Publication
    Mutagenesisi278 – 2781T → A: No effect on autophosphorylation activity or activation of SAPK and MAPK14. 1 Publication
    Mutagenesisi281 – 2811S → A: Reduced autophosphorylation activity. Reduced activation of SAPK and MAPK14. 1 Publication
    Mutagenesisi281 – 2811S → E: No effect on SAPK activation. 1 Publication

    Organism-specific databases

    PharmGKBiPA30594.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 847847Mitogen-activated protein kinase kinase kinase 11PRO_0000086260Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei11 – 111Phosphoserine1 Publication
    Modified residuei277 – 2771Phosphothreonine; by autocatalysis1 Publication
    Modified residuei281 – 2811Phosphoserine; by autocatalysis and MAP4K11 Publication
    Modified residuei394 – 3941Phosphoserine1 Publication
    Modified residuei507 – 5071Phosphoserine3 Publications
    Modified residuei524 – 5241Phosphoserine1 Publication
    Modified residuei548 – 5481Phosphoserine2 Publications
    Modified residuei555 – 5551Phosphoserine1 Publication
    Modified residuei556 – 5561Phosphoserine1 Publication
    Modified residuei654 – 6541Phosphoserine1 Publication
    Modified residuei693 – 6931Phosphoserine1 Publication
    Modified residuei705 – 7051Phosphoserine3 Publications
    Modified residuei708 – 7081Phosphothreonine1 Publication
    Modified residuei724 – 7241Phosphoserine1 Publication
    Modified residuei727 – 7271Phosphoserine1 Publication
    Modified residuei740 – 7401Phosphoserine1 Publication
    Modified residuei748 – 7481Phosphoserine2 Publications
    Modified residuei758 – 7581Phosphoserine3 Publications
    Modified residuei770 – 7701Phosphoserine1 Publication
    Modified residuei789 – 7891Phosphoserine3 Publications
    Modified residuei793 – 7931Phosphoserine5 Publications
    Modified residuei815 – 8151Phosphoserine1 Publication

    Post-translational modificationi

    Autophosphorylation on serine and threonine residues within the activation loop plays a role in enzyme activation. Thr-277 is likely to be the main autophosphorylation site. Phosphorylation of Ser-555 and Ser-556 is induced by CDC42.8 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ16584.
    PaxDbiQ16584.
    PRIDEiQ16584.

    PTM databases

    PhosphoSiteiQ16584.

    Expressioni

    Tissue specificityi

    Expressed in a wide variety of normal and neoplastic tissues including fetal lung, liver, heart and kidney, and adult lung, liver, heart, kidney, placenta, skeletal muscle, pancreas and brain.2 Publications

    Gene expression databases

    ArrayExpressiQ16584.
    BgeeiQ16584.
    CleanExiHS_MAP3K11.
    GenevestigatoriQ16584.

    Organism-specific databases

    HPAiCAB010165.

    Interactioni

    Subunit structurei

    Homodimer; undergoes dimerization during activation. Interacts with MAP2K4/MKK4. Interacts with MAP2K7/MKK7 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q99IB85EBI-49961,EBI-6927873From a different organism.
    CDC42P609533EBI-49961,EBI-81752
    Map4k1P702183EBI-49961,EBI-2906801From a different organism.
    NF2P352404EBI-49961,EBI-1014472

    Protein-protein interaction databases

    BioGridi110442. 36 interactions.
    IntActiQ16584. 15 interactions.
    MINTiMINT-2836851.
    STRINGi9606.ENSP00000309597.

    Structurei

    3D structure databases

    ProteinModelPortaliQ16584.
    SMRiQ16584. Positions 44-101, 114-465.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini41 – 10565SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini117 – 379263Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni403 – 42422Leucine-zipper 1Add
    BLAST
    Regioni438 – 45922Leucine-zipper 2Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi14 – 138125Gly-richSequence AnalysisAdd
    BLAST
    Compositional biasi18 – 3013Poly-GlySequence AnalysisAdd
    BLAST
    Compositional biasi426 – 51489Arg-richSequence AnalysisAdd
    BLAST
    Compositional biasi599 – 825227Pro-richSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH3 domain

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000060081.
    HOVERGENiHBG067662.
    InParanoidiQ16584.
    KOiK04419.
    OMAiAWGRQSP.
    PhylomeDBiQ16584.
    TreeFamiTF105118.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR016231. MAPKKK9/10/11.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR001452. SH3_domain.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view]
    PfamiPF07714. Pkinase_Tyr. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000556. MAPKKK9_11. 1 hit.
    PRINTSiPR00452. SH3DOMAIN.
    PR00109. TYRKINASE.
    SMARTiSM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q16584-1) [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

    MEPLKSLFLK SPLGSWNGSG SGGGGGGGGG RPEGSPKAAG YANPVWTALF    50
    DYEPSGQDEL ALRKGDRVEV LSRDAAISGD EGWWAGQVGG QVGIFPSNYV 100
    SRGGGPPPCE VASFQELRLE EVIGIGGFGK VYRGSWRGEL VAVKAARQDP 150
    DEDISVTAES VRQEARLFAM LAHPNIIALK AVCLEEPNLC LVMEYAAGGP 200
    LSRALAGRRV PPHVLVNWAV QIARGMHYLH CEALVPVIHR DLKSNNILLL 250
    QPIESDDMEH KTLKITDFGL AREWHKTTQM SAAGTYAWMA PEVIKASTFS 300
    KGSDVWSFGV LLWELLTGEV PYRGIDCLAV AYGVAVNKLT LPIPSTCPEP 350
    FAQLMADCWA QDPHRRPDFA SILQQLEALE AQVLREMPRD SFHSMQEGWK 400
    REIQGLFDEL RAKEKELLSR EEELTRAARE QRSQAEQLRR REHLLAQWEL 450
    EVFERELTLL LQQVDRERPH VRRRRGTFKR SKLRARDGGE RISMPLDFKH 500
    RITVQASPGL DRRRNVFEVG PGDSPTFPRF RAIQLEPAEP GQAWGRQSPR 550
    RLEDSSNGER RACWAWGPSS PKPGEAQNGR RRSRMDEATW YLDSDDSSPL 600
    GSPSTPPALN GNPPRPSLEP EEPKRPVPAE RGSSSGTPKL IQRALLRGTA 650
    LLASLGLGRD LQPPGGPGRE RGESPTTPPT PTPAPCPTEP PPSPLICFSL 700
    KTPDSPPTPA PLLLDLGIPV GQRSAKSPRR EEEPRGGTVS PPPGTSRSAP 750
    GTPGTPRSPP LGLISRPRPS PLRSRIDPWS FVSAGPRPSP LPSPQPAPRR 800
    APWTLFPDSD PFWDSPPANP FQGGPQDCRA QTKDMGAQAP WVPEAGP 847
    Length:847
    Mass (Da):92,688
    Last modified:November 1, 1996 - v1
    Checksum:iAFB6E930EA281C15
    GO
    Isoform 2 (identifier: Q16584-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-257: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:590
    Mass (Da):65,344
    Checksum:iC7C24CA0C053133D
    GO

    Sequence cautioni

    The sequence BAD92892.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti247 – 27226ILLLQ…FGLAR → SEFLGAWLGVAWLWYTPAPN LPLSLA in BAD92892. 1 PublicationCuratedAdd
    BLAST
    Sequence conflicti791 – 7911L → P in BAD96501. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti151 – 1511D → V.1 Publication
    Corresponds to variant rs34178129 [ dbSNP | Ensembl ].
    VAR_040703
    Natural varianti252 – 2521P → H.1 Publication
    Corresponds to variant rs17855912 [ dbSNP | Ensembl ].
    VAR_030604
    Natural varianti282 – 2821A → G.1 Publication
    Corresponds to variant rs34594252 [ dbSNP | Ensembl ].
    VAR_040704

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 257257Missing in isoform 2. 1 PublicationVSP_056183Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07747 mRNA. Translation: AAA19647.1.
    L32976 mRNA. Translation: AAA59859.1.
    AB209655 mRNA. Translation: BAD92892.1. Different initiation.
    AK299609 mRNA. Translation: BAG61538.1.
    AK316032 mRNA. Translation: BAH14403.1.
    AK222781 mRNA. Translation: BAD96501.1.
    AP001362 Genomic DNA. No translation available.
    BC011263 mRNA. Translation: AAH11263.1.
    BC064543 mRNA. Translation: AAH64543.1.
    CCDSiCCDS8107.1.
    PIRiA53800.
    RefSeqiNP_002410.1. NM_002419.3.
    UniGeneiHs.502872.

    Genome annotation databases

    EnsembliENST00000309100; ENSP00000309597; ENSG00000173327.
    ENST00000530153; ENSP00000433886; ENSG00000173327.
    GeneIDi4296.
    KEGGihsa:4296.
    UCSCiuc001oew.3. human.

    Polymorphism databases

    DMDMi71153819.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07747 mRNA. Translation: AAA19647.1 .
    L32976 mRNA. Translation: AAA59859.1 .
    AB209655 mRNA. Translation: BAD92892.1 . Different initiation.
    AK299609 mRNA. Translation: BAG61538.1 .
    AK316032 mRNA. Translation: BAH14403.1 .
    AK222781 mRNA. Translation: BAD96501.1 .
    AP001362 Genomic DNA. No translation available.
    BC011263 mRNA. Translation: AAH11263.1 .
    BC064543 mRNA. Translation: AAH64543.1 .
    CCDSi CCDS8107.1.
    PIRi A53800.
    RefSeqi NP_002410.1. NM_002419.3.
    UniGenei Hs.502872.

    3D structure databases

    ProteinModelPortali Q16584.
    SMRi Q16584. Positions 44-101, 114-465.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110442. 36 interactions.
    IntActi Q16584. 15 interactions.
    MINTi MINT-2836851.
    STRINGi 9606.ENSP00000309597.

    Chemistry

    BindingDBi Q16584.
    ChEMBLi CHEMBL2708.
    GuidetoPHARMACOLOGYi 2071.

    PTM databases

    PhosphoSitei Q16584.

    Polymorphism databases

    DMDMi 71153819.

    Proteomic databases

    MaxQBi Q16584.
    PaxDbi Q16584.
    PRIDEi Q16584.

    Protocols and materials databases

    DNASUi 4296.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000309100 ; ENSP00000309597 ; ENSG00000173327 .
    ENST00000530153 ; ENSP00000433886 ; ENSG00000173327 .
    GeneIDi 4296.
    KEGGi hsa:4296.
    UCSCi uc001oew.3. human.

    Organism-specific databases

    CTDi 4296.
    GeneCardsi GC11M065365.
    HGNCi HGNC:6850. MAP3K11.
    HPAi CAB010165.
    MIMi 600050. gene.
    neXtProti NX_Q16584.
    PharmGKBi PA30594.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000060081.
    HOVERGENi HBG067662.
    InParanoidi Q16584.
    KOi K04419.
    OMAi AWGRQSP.
    PhylomeDBi Q16584.
    TreeFami TF105118.

    Enzyme and pathway databases

    SignaLinki Q16584.

    Miscellaneous databases

    GeneWikii MAP3K11.
    GenomeRNAii 4296.
    NextBioi 16911.
    PROi Q16584.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16584.
    Bgeei Q16584.
    CleanExi HS_MAP3K11.
    Genevestigatori Q16584.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR016231. MAPKKK9/10/11.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR001452. SH3_domain.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view ]
    Pfami PF07714. Pkinase_Tyr. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000556. MAPKKK9_11. 1 hit.
    PRINTSi PR00452. SH3DOMAIN.
    PR00109. TYRKINASE.
    SMARTi SM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of SPRK, a novel src-homology 3 domain-containing proline-rich kinase with serine/threonine kinase activity."
      Gallo K.A., Mark M.R., Scadden D.T., Wang Z., Gu Q., Godowski P.J.
      J. Biol. Chem. 269:15092-15100(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-144 AND GLU-164.
      Tissue: Megakaryocyte.
    2. "MLK-3: identification of a widely-expressed protein kinase bearing an SH3 domain and a leucine zipper-basic region domain."
      Ing Y.L., Leung I.W.L., Heng H.H.Q., Tsui L.-C., Lassam N.J.
      Oncogene 9:1745-1750(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: ThymusImported.
    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] (ISOFORM 2).
      Tissue: Brain.
    4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Liver and Spleen.
    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), VARIANT HIS-252.
      Tissue: BrainImported and Hippocampus1 Publication.
    7. "MLK-3 activates the SAPK/JNK and p38/RK pathways via SEK1 and MKK3/6."
      Tibbles L.A., Ing Y.L., Kiefer F., Chan J., Iscove N., Woodgett J.R., Lassam N.J.
      EMBO J. 15:7026-7035(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP2K4/MKK4, FUNCTION IN PHOSPHORYLATION OF MAP2K4/MKK4.
    8. "Dimerization via tandem leucine zippers is essential for the activation of the mitogen-activated protein kinase kinase kinase, MLK-3."
      Leung I.W.L., Lassam N.J.
      J. Biol. Chem. 273:32408-32415(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, HOMODIMERIZATION.
    9. "The kinase activation loop is the key to mixed lineage kinase-3 activation via both autophosphorylation and hematopoietic progenitor kinase 1 phosphorylation."
      Leung I.W.L., Lassam N.J.
      J. Biol. Chem. 276:1961-1967(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, PHOSPHORYLATION AT THR-277 AND SER-281, MUTAGENESIS OF LYS-144; THR-277; THR-278 AND SER-281.
    10. "Identification of in vivo phosphorylation sites of MLK3 by mass spectrometry and phosphopeptide mapping."
      Vacratsis P.O., Phinney B.S., Gage D.A., Gallo K.A.
      Biochemistry 41:5613-5624(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-524; SER-555; SER-556; SER-654; SER-705; SER-724; SER-727; SER-740; SER-758; SER-770 AND SER-793.
    11. "A new identity for MLK3 as an NIMA-related, cell cycle-regulated kinase that is localized near centrosomes and influences microtubule organization."
      Swenson K.I., Winkler K.E., Means A.R.
      Mol. Biol. Cell 14:156-172(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    12. "MLK3 is required for mitogen activation of B-Raf, ERK and cell proliferation."
      Chadee D.N., Kyriakis J.M.
      Nat. Cell Biol. 6:770-776(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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-11; SER-507; SER-548; SER-705; THR-708; SER-748; SER-758; SER-793 AND SER-815, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-789 AND SER-793, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-507; SER-548; SER-693; SER-705; SER-748; SER-758; SER-789 AND SER-793, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-789 AND SER-793, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "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] VAL-151 AND GLY-282.

    Entry informationi

    Entry nameiM3K11_HUMAN
    AccessioniPrimary (citable) accession number: Q16584
    Secondary accession number(s): B4DS76
    , Q53H00, Q59F06, Q6P2G4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 142 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3