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Protein

Mitogen-activated protein kinase kinase kinase 9

Gene

MAP3K9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade through the phosphorylation of MAP2K4/MKK4 and MAP2K7/MKK7 which in turn activate the JNKs. The MKK/JNK signaling pathway regulates stress response via activator protein-1 (JUN) and GATA4 transcription factors. Plays also a role in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Enzyme regulationi

Homodimerization via the leucine zipper domains is required for autophosphorylation of multiple sites in the activation loop and subsequent activation. Autophosphorylation at Thr-312 is the key step in activation of MAP3K9/MLK1 and is required for full phosphorylation. Autophosphorylation at Thr-304 and Ser-308 have been shown to be of secondary importance in the activation of MAP3K9/MLK1. CEP-1347 and many indolocarbazole analogs have been shown to act as inhibitors of MAP3K9/MLK1 activity.3 Publications

Kineticsi

  1. KM=62 µM for ATP1 Publication
  2. KM=7 µM for myelin basic protein (MBP) as substrate1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei171 – 1711ATP
    Active sitei268 – 2681Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi150 – 1589ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • JUN kinase kinase kinase activity Source: UniProtKB
    • MAP kinase kinase activity Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB
    • protein serine/threonine kinase activity Source: UniProtKB
    • protein tyrosine kinase activity Source: InterPro

    GO - Biological processi

    • activation of JNKK activity Source: GOC
    • activation of JUN kinase activity Source: UniProtKB
    • apoptotic process Source: UniProtKB-KW
    • positive regulation of apoptotic process Source: Ensembl
    • protein autophosphorylation Source: UniProtKB
    • protein phosphorylation Source: UniProtKB
    • regulation of transcription, DNA-templated Source: UniProtKB-KW
    • transcription, DNA-templated Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Stress response, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiP80192.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase kinase kinase 9 (EC:2.7.11.25)
    Alternative name(s):
    Mixed lineage kinase 1
    Gene namesi
    Name:MAP3K9
    Synonyms:MLK1, PRKE1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:6861. MAP3K9.

    Subcellular locationi

    GO - Cellular componenti

    • intracellular Source: GOC
    Complete GO annotation...

    Pathology & Biotechi

    Involvement in diseasei

    May play a role in esophageal cancer susceptibility and/or development.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi171 – 1711K → A: Loss of kinase activity and threonine phosphorylation. 1 Publication
    Mutagenesisi304 – 3041T → A: Reduces threonine phosphorylation. Impairs JNK activation. 1 Publication
    Mutagenesisi305 – 3051T → A: Little effect on threonine phosphorylation. Mildly impairs JNK activation. 1 Publication
    Mutagenesisi308 – 3081S → A: Impairs JNK activation. 1 Publication
    Mutagenesisi312 – 3121T → A: Loss of threonine phosphorylation. Strongly impairs JNK activation. 1 Publication

    Organism-specific databases

    PharmGKBiPA30607.

    Polymorphism and mutation databases

    DMDMi116242625.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11041104Mitogen-activated protein kinase kinase kinase 9PRO_0000086258Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei304 – 3041Phosphothreonine; by autocatalysis1 Publication
    Modified residuei305 – 3051Phosphothreonine; by autocatalysis1 Publication
    Modified residuei308 – 3081Phosphoserine; by autocatalysis1 Publication
    Modified residuei312 – 3121Phosphothreonine; by autocatalysis1 Publication

    Post-translational modificationi

    Autophosphorylation on serine and threonine residues within the activation loop plays a role in enzyme activation. Thr-312 is likely to be the main autophosphorylation site. Autophosphorylation also occurs on Thr-304 and Ser-308.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP80192.
    PRIDEiP80192.

    PTM databases

    PhosphoSiteiP80192.

    Expressioni

    Tissue specificityi

    Expressed in epithelial tumor cell lines of colonic, breast and esophageal origin.1 Publication

    Gene expression databases

    BgeeiP80192.
    CleanExiHS_MAP3K9.
    ExpressionAtlasiP80192. baseline and differential.
    GenevisibleiP80192. HS.

    Organism-specific databases

    HPAiHPA000942.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HSP90AB1P082382EBI-3951604,EBI-352572

    Protein-protein interaction databases

    BioGridi110439. 1 interaction.
    IntActiP80192. 1 interaction.
    STRINGi9606.ENSP00000451263.

    Structurei

    Secondary structure

    1
    1104
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi143 – 15311Combined sources
    Beta strandi156 – 1638Combined sources
    Beta strandi166 – 1727Combined sources
    Helixi185 – 19713Combined sources
    Beta strandi206 – 2105Combined sources
    Beta strandi217 – 2215Combined sources
    Helixi228 – 2325Combined sources
    Helixi239 – 25820Combined sources
    Beta strandi259 – 2624Combined sources
    Helixi271 – 2733Combined sources
    Beta strandi274 – 2785Combined sources
    Beta strandi281 – 2833Combined sources
    Beta strandi290 – 2923Combined sources
    Helixi313 – 3153Combined sources
    Helixi318 – 3236Combined sources
    Helixi328 – 34417Combined sources
    Turni348 – 3514Combined sources
    Helixi354 – 3629Combined sources
    Helixi376 – 38510Combined sources
    Helixi390 – 3923Combined sources
    Helixi396 – 4049Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3DTCX-ray2.60A136-406[»]
    ProteinModelPortaliP80192.
    SMRiP80192. Positions 55-113, 136-405.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP80192.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini52 – 11665SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini144 – 412269Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni430 – 45122Leucine-zipper 1Add
    BLAST
    Regioni465 – 48622Leucine-zipper 2Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi12 – 4231Ala-richAdd
    BLAST
    Compositional biasi30 – 389Poly-Glu
    Compositional biasi495 – 50915Arg/Lys-rich (basic)Add
    BLAST
    Compositional biasi863 – 972110Pro-richAdd
    BLAST
    Compositional biasi1011 – 104131Ser-richAdd
    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.
    GeneTreeiENSGT00760000118807.
    HOGENOMiHOG000060081.
    HOVERGENiHBG067662.
    InParanoidiP80192.
    KOiK04417.
    OMAiHHRRCEV.
    OrthoDBiEOG7D85VN.
    PhylomeDBiP80192.
    TreeFamiTF105118.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR016231. MLK1/MLK2/MLK4.
    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]
    PfamiPF00069. Pkinase. 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. AlignAdd to basket

    Isoform 1 (identifier: P80192-1) [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

            10         20         30         40         50
    MEPSRALLGC LASAAAAAPP GEDGAGAGAE EEEEEEEEAA AAVGPGELGC
    60 70 80 90 100
    DAPLPYWTAV FEYEAAGEDE LTLRLGDVVE VLSKDSQVSG DEGWWTGQLN
    110 120 130 140 150
    QRVGIFPSNY VTPRSAFSSR CQPGGEDPSC YPPIQLLEID FAELTLEEII
    160 170 180 190 200
    GIGGFGKVYR AFWIGDEVAV KAARHDPDED ISQTIENVRQ EAKLFAMLKH
    210 220 230 240 250
    PNIIALRGVC LKEPNLCLVM EFARGGPLNR VLSGKRIPPD ILVNWAVQIA
    260 270 280 290 300
    RGMNYLHDEA IVPIIHRDLK SSNILILQKV ENGDLSNKIL KITDFGLARE
    310 320 330 340 350
    WHRTTKMSAA GTYAWMAPEV IRASMFSKGS DVWSYGVLLW ELLTGEVPFR
    360 370 380 390 400
    GIDGLAVAYG VAMNKLALPI PSTCPEPFAK LMEDCWNPDP HSRPSFTNIL
    410 420 430 440 450
    DQLTTIEESG FFEMPKDSFH CLQDNWKHEI QEMFDQLRAK EKELRTWEEE
    460 470 480 490 500
    LTRAALQQKN QEELLRRREQ ELAEREIDIL ERELNIIIHQ LCQEKPRVKK
    510 520 530 540 550
    RKGKFRKSRL KLKDGNRISL PSDFQHKFTV QASPTMDKRK SLINSRSSPP
    560 570 580 590 600
    ASPTIIPRLR AIQLTPGESS KTWGRSSVVP KEEGEEEEKR APKKKGRTWG
    610 620 630 640 650
    PGTLGQKELA SGDEGSPQRR EKANGLSTPS ESPHFHLGLK SLVDGYKQWS
    660 670 680 690 700
    SSAPNLVKGP RSSPALPGFT SLMEMEDEDS EGPGSGESRL QHSPSQSYLC
    710 720 730 740 750
    IPFPRGEDGD GPSSDGIHEE PTPVNSATST PQLTPTNSLK RGGAHHRRCE
    760 770 780 790 800
    VALLGCGAVL AATGLGFDLL EAGKCQLLPL EEPEPPAREE KKRREGLFQR
    810 820 830 840 850
    SSRPRRSTSP PSRKLFKKEE PMLLLGDPSA SLTLLSLSSI SECNSTRSLL
    860 870 880 890 900
    RSDSDEIVVY EMPVSPVEAP PLSPCTHNPL VNVRVERFKR DPNQSLTPTH
    910 920 930 940 950
    VTLTTPSQPS SHRRTPSDGA LKPETLLASR SPSSNGLSPS PGAGMLKTPS
    960 970 980 990 1000
    PSRDPGEFPR LPDPNVVFPP TPRRWNTQQD STLERPKTLE FLPRPRPSAN
    1010 1020 1030 1040 1050
    RQRLDPWWFV SPSHARSTSP ANSSSTETPS NLDSCFASSS STVEERPGLP
    1060 1070 1080 1090 1100
    ALLPFQAGPL PPTERTLLDL DAEGQSQDST VPLCRAELNT HRPAPYEIQQ

    EFWS
    Length:1,104
    Mass (Da):121,895
    Last modified:October 17, 2006 - v3
    Checksum:i0F059C867FCE7276
    GO
    Isoform 2 (identifier: P80192-4) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         675-675: M → MALLAASWVVPIDIE

    Show »
    Length:1,118
    Mass (Da):123,373
    Checksum:i608E5BDC00DC09B8
    GO

    Sequence cautioni

    The sequence AAI11408.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti356 – 3561A → R (PubMed:8477742).Curated
    Sequence conflicti433 – 4331M → T in AAQ23054 (PubMed:15610029).Curated
    Sequence conflicti511 – 53525KLKDG…QASPT → AQPVLPFPHGHSRCPGGTGS SWGGQ (PubMed:8477742).CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti246 – 2461A → V in a metastatic melanoma sample; somatic mutation. 1 Publication
    VAR_040698
    Natural varianti467 – 4671R → C in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_040699
    Natural varianti497 – 4971R → Q.1 Publication
    Corresponds to variant rs56196343 [ dbSNP | Ensembl ].
    VAR_040700
    Natural varianti646 – 6461Y → C.1 Publication
    Corresponds to variant rs34322726 [ dbSNP | Ensembl ].
    VAR_040701

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei675 – 6751M → MALLAASWVVPIDIE in isoform 2. 1 PublicationVSP_013765

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY327900 mRNA. Translation: AAQ23054.1.
    BC111407 mRNA. Translation: AAI11408.1. Different initiation.
    BC133706 mRNA. Translation: AAI33707.1.
    AF251442 mRNA. Translation: AAG44591.1.
    CCDSiCCDS32112.1. [P80192-4]
    CCDS61488.1. [P80192-1]
    PIRiS32467. JU0229.
    RefSeqiNP_001271159.1. NM_001284230.1. [P80192-1]
    NP_149132.2. NM_033141.3. [P80192-4]
    UniGeneiHs.445496.
    Hs.593542.

    Genome annotation databases

    EnsembliENST00000554752; ENSP00000451612; ENSG00000006432.
    ENST00000555993; ENSP00000451263; ENSG00000006432. [P80192-4]
    GeneIDi4293.
    KEGGihsa:4293.
    UCSCiuc001xml.3. human. [P80192-4]
    uc001xmm.3. human. [P80192-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AY327900 mRNA. Translation: AAQ23054.1.
    BC111407 mRNA. Translation: AAI11408.1. Different initiation.
    BC133706 mRNA. Translation: AAI33707.1.
    AF251442 mRNA. Translation: AAG44591.1.
    CCDSiCCDS32112.1. [P80192-4]
    CCDS61488.1. [P80192-1]
    PIRiS32467. JU0229.
    RefSeqiNP_001271159.1. NM_001284230.1. [P80192-1]
    NP_149132.2. NM_033141.3. [P80192-4]
    UniGeneiHs.445496.
    Hs.593542.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3DTCX-ray2.60A136-406[»]
    ProteinModelPortaliP80192.
    SMRiP80192. Positions 55-113, 136-405.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi110439. 1 interaction.
    IntActiP80192. 1 interaction.
    STRINGi9606.ENSP00000451263.

    Chemistry

    BindingDBiP80192.
    ChEMBLiCHEMBL2872.
    GuidetoPHARMACOLOGYi2084.

    PTM databases

    PhosphoSiteiP80192.

    Polymorphism and mutation databases

    DMDMi116242625.

    Proteomic databases

    PaxDbiP80192.
    PRIDEiP80192.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000554752; ENSP00000451612; ENSG00000006432.
    ENST00000555993; ENSP00000451263; ENSG00000006432. [P80192-4]
    GeneIDi4293.
    KEGGihsa:4293.
    UCSCiuc001xml.3. human. [P80192-4]
    uc001xmm.3. human. [P80192-1]

    Organism-specific databases

    CTDi4293.
    GeneCardsiGC14M071189.
    H-InvDBHIX0011779.
    HGNCiHGNC:6861. MAP3K9.
    HPAiHPA000942.
    MIMi600136. gene.
    neXtProtiNX_P80192.
    PharmGKBiPA30607.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00760000118807.
    HOGENOMiHOG000060081.
    HOVERGENiHBG067662.
    InParanoidiP80192.
    KOiK04417.
    OMAiHHRRCEV.
    OrthoDBiEOG7D85VN.
    PhylomeDBiP80192.
    TreeFamiTF105118.

    Enzyme and pathway databases

    SignaLinkiP80192.

    Miscellaneous databases

    ChiTaRSiMAP3K9. human.
    EvolutionaryTraceiP80192.
    GeneWikiiMAP3K9.
    GenomeRNAii4293.
    NextBioi16897.
    PROiP80192.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP80192.
    CleanExiHS_MAP3K9.
    ExpressionAtlasiP80192. baseline and differential.
    GenevisibleiP80192. HS.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR016231. MLK1/MLK2/MLK4.
    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]
    PfamiPF00069. Pkinase. 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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Phosphoregulation of mixed-lineage kinase 1 activity by multiple phosphorylation in the activation loop."
      Durkin J.T., Holskin B.P., Kopec K.K., Reed M.S., Spais C.M., Steffy B.M., Gessner G., Angeles T.S., Pohl J., Ator M.A., Meyer S.L.
      Biochemistry 43:16348-16355(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-304; THR-305; SER-308 AND THR-312, MUTAGENESIS OF LYS-171; THR-304; THR-305; SER-308 AND THR-312.
    2. "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).
    3. "cDNA sequence and gene organisation of mixed lineage kinase 1."
      McNee J.J., Dower S.K., Guesdon F.
      Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 53-1104 (ISOFORM 2).
    4. "Identification of a new family of human epithelial protein kinases containing two leucine/isoleucine-zipper domains."
      Dorow D.S., Devereux L., Dietzsch E., de Kretser T.
      Eur. J. Biochem. 213:701-710(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 142-535, TISSUE SPECIFICITY.
      Tissue: Colon epithelium.
    5. Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHORYLATION OF MAP2K4/MKK4.
    6. "The MLK family mediates c-Jun N-terminal kinase activation in neuronal apoptosis."
      Xu Z., Maroney A.C., Dobrzanski P., Kukekov N.V., Greene L.A.
      Mol. Cell. Biol. 21:4713-4724(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN THE APOPTOSIS PATHWAY.
    7. Cited for: ENZYME REGULATION.
    8. "Genomic profiling of 766 cancer-related genes in archived esophageal normal and carcinoma tissues."
      Chen J., Guo L., Peiffer D.A., Zhou L., Chan O.T., Bibikova M., Wickham-Garcia E., Lu S.H., Zhan Q., Wang-Rodriguez J., Jiang W., Fan J.B.
      Int. J. Cancer 122:2249-2254(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: POSSIBLE ROLE IN ESOPHAGEAL CANCER.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Mixed-lineage kinase 1 and mixed-lineage kinase 3 subtype-selective dihydronaphthyl[3,4-a]pyrrolo[3,4-c]carbazole-5-ones: optimization, mixed-lineage kinase 1 crystallography, and oral in vivo activity in 1-methyl-4-phenyltetrahydropyridine models."
      Hudkins R.L., Diebold J.L., Tao M., Josef K.A., Park C.H., Angeles T.S., Aimone L.D., Husten J., Ator M.A., Meyer S.L., Holskin B.P., Durkin J.T., Fedorov A.A., Fedorov E.V., Almo S.C., Mathiasen J.R., Bozyczko-Coyne D., Saporito M.S., Scott R.W., Mallamo J.P.
      J. Med. Chem. 51:5680-5689(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 136-406.
    11. "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-246; CYS-467; GLN-497 AND CYS-646.

    Entry informationi

    Entry nameiM3K9_HUMAN
    AccessioniPrimary (citable) accession number: P80192
    Secondary accession number(s): A3KN85
    , Q0D2G7, Q6EH31, Q9H2N5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: October 17, 2006
    Last modified: July 22, 2015
    This is version 153 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 14
      Human chromosome 14: 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.