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Q9NYL2

- MLTK_HUMAN

UniProt

Q9NYL2 - MLTK_HUMAN

Protein

Mitogen-activated protein kinase kinase kinase MLT

Gene

ZAK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 3 (30 Nov 2010)
      Previous versions | rss
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    Functioni

    Stress-activated component of a protein kinase signal transduction cascade. Regulates the JNK and p38 pathways. Pro-apoptotic. Role in regulation of S and G2 cell cycle checkpoint by direct phosphorylation of CHEK2. Isoform 1, but not isoform 2, causes cell shrinkage and disruption of actin stress fibers. Isoform 1 may have role in neoplastic cell transformation and cancer development. Isoform 1, but not isoform 2, phosphorylates histone H3 at 'Ser-28'.6 Publications

    Catalytic activityi

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

    Cofactori

    Magnesium.1 Publication

    Enzyme regulationi

    Activated by phosphorylation by PKN1 and autophosphorylation on Thr-161 and Ser-165.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei45 – 451ATP1 PublicationPROSITE-ProRule annotation
    Active sitei133 – 1331Proton acceptorBy similarityPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi22 – 309ATPBy similarityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. magnesium ion binding Source: UniProtKB
    3. MAP kinase kinase kinase activity Source: UniProtKB
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: IntAct
    6. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. activation of JUN kinase activity Source: UniProtKB
    2. activation of MAPKK activity Source: UniProtKB
    3. cell cycle arrest Source: UniProtKB
    4. cell cycle checkpoint Source: UniProtKB
    5. cell death Source: UniProtKB
    6. cell differentiation Source: UniProtKB
    7. cell proliferation Source: UniProtKB
    8. cytoskeleton organization Source: Ensembl
    9. DNA damage checkpoint Source: UniProtKB
    10. intracellular signal transduction Source: UniProtKB
    11. positive regulation of apoptotic process Source: UniProtKB
    12. protein phosphorylation Source: UniProtKB
    13. response to radiation Source: UniProtKB
    14. response to stress Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle

    Keywords - Ligandi

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

    Enzyme and pathway databases

    SignaLinkiQ9NYL2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase kinase kinase MLT (EC:2.7.11.25)
    Alternative name(s):
    Human cervical cancer suppressor gene 4 protein
    Short name:
    HCCS-4
    Leucine zipper- and sterile alpha motif-containing kinase
    MLK-like mitogen-activated protein triple kinase
    Mixed lineage kinase-related kinase
    Short name:
    MLK-related kinase
    Short name:
    MRK
    Sterile alpha motif- and leucine zipper-containing kinase AZK
    Gene namesi
    Name:ZAK
    Synonyms:MLTK
    ORF Names:HCCS4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Translocates to the nucleus upon ultraviolet B irradiation.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi45 – 451K → M: Loss of kinase activity. 1 Publication
    Mutagenesisi161 – 1611T → A: Loss of autophosphorylation activity. 1 Publication
    Mutagenesisi162 – 1621T → A: Slight loss of autophosphorylation activity. 1 Publication
    Mutagenesisi165 – 1651S → A: Loss of autophosphorylation activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 800800Mitogen-activated protein kinase kinase kinase MLTPRO_0000086338Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21Phosphoserine
    Modified residuei3 – 31Phosphoserine
    Modified residuei155 – 1551Phosphoserine
    Modified residuei161 – 1611Phosphothreonine; by autocatalysis1 Publication
    Modified residuei165 – 1651Phosphoserine; by autocatalysis1 Publication
    Modified residuei264 – 2641Phosphoserine
    Modified residuei268 – 2681Phosphoserine
    Modified residuei275 – 2751Phosphoserine
    Modified residuei302 – 3021Phosphoserine
    Modified residuei326 – 3261Phosphoserine
    Modified residuei328 – 3281Phosphothreonine
    Modified residuei557 – 5571Phosphoserine
    Modified residuei565 – 5651Phosphoserine
    Modified residuei568 – 5681Phosphoserine
    Modified residuei584 – 5841Phosphoserine
    Modified residuei586 – 5861Phosphothreonine
    Modified residuei591 – 5911Phosphoserine
    Modified residuei593 – 5931Phosphoserine
    Modified residuei599 – 5991Phosphoserine1 Publication
    Modified residuei628 – 6281Phosphothreonine3 Publications
    Modified residuei633 – 6331Phosphoserine3 Publications
    Modified residuei635 – 6351Phosphoserine
    Modified residuei636 – 6361Phosphoserine
    Modified residuei637 – 6371Phosphoserine
    Modified residuei639 – 6391Phosphothreonine
    Modified residuei648 – 6481Phosphoserine
    Modified residuei660 – 6601Phosphoserine
    Modified residuei666 – 6661Phosphothreonine
    Modified residuei667 – 6671Phosphoserine
    Modified residuei668 – 6681Phosphoserine
    Modified residuei687 – 6871Phosphoserine
    Modified residuei690 – 6901Phosphoserine
    Modified residuei691 – 6911Phosphoserine
    Modified residuei718 – 7181Phosphoserine
    Modified residuei727 – 7271Phosphoserine4 Publications
    Modified residuei733 – 7331Phosphoserine2 Publications
    Modified residuei754 – 7541Phosphoserine
    Modified residuei781 – 7811Phosphoserine

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NYL2.
    PaxDbiQ9NYL2.
    PRIDEiQ9NYL2.

    PTM databases

    PhosphoSiteiQ9NYL2.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Isoform 2 is the predominant form in all tissues examined, except for liver, in which isoform 1 is more highly expressed.2 Publications

    Gene expression databases

    ArrayExpressiQ9NYL2.
    BgeeiQ9NYL2.
    GenevestigatoriQ9NYL2.

    Organism-specific databases

    HPAiHPA017205.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with PKN1 and ZNF33A.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PKN1Q165122EBI-687346,EBI-602382
    RPS6KA5O755824EBI-602273,EBI-73869
    YWHAZP631044EBI-602273,EBI-347088

    Protein-protein interaction databases

    BioGridi119725. 29 interactions.
    IntActiQ9NYL2. 23 interactions.
    MINTiMINT-1465549.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NYL2.
    SMRiQ9NYL2. Positions 9-325.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 277262Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini339 – 41072SAMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni287 – 30822Leucine-zipperAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG080445.
    KOiK04424.
    OMAiLHSGMQI.
    PhylomeDBiQ9NYL2.

    Family and domain databases

    Gene3Di1.10.150.50. 1 hit.
    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR021129. SAM_type1.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF07714. Pkinase_Tyr. 1 hit.
    PF00536. SAM_1. 1 hit.
    [Graphical view]
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00454. SAM. 1 hit.
    [Graphical view]
    SUPFAMiSSF47769. SSF47769. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50105. SAM_DOMAIN. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q9NYL2-1) [UniParc]FASTAAdd to Basket

    Also known as: Alpha

    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

    MSSLGASFVQ IKFDDLQFFE NCGGGSFGSV YRAKWISQDK EVAVKKLLKI    50
    EKEAEILSVL SHRNIIQFYG VILEPPNYGI VTEYASLGSL YDYINSNRSE 100
    EMDMDHIMTW ATDVAKGMHY LHMEAPVKVI HRDLKSRNVV IAADGVLKIC 150
    DFGASRFHNH TTHMSLVGTF PWMAPEVIQS LPVSETCDTY SYGVVLWEML 200
    TREVPFKGLE GLQVAWLVVE KNERLTIPSS CPRSFAELLH QCWEADAKKR 250
    PSFKQIISIL ESMSNDTSLP DKCNSFLHNK AEWRCEIEAT LERLKKLERD 300
    LSFKEQELKE RERRLKMWEQ KLTEQSNTPL LPSFEIGAWT EDDVYCWVQQ 350
    LVRKGDSSAE MSVYASLFKE NNITGKRLLL LEEEDLKDMG IVSKGHIIHF 400
    KSAIEKLTHD YINLFHFPPL IKDSGGEPEE NEEKIVNLEL VFGFHLKPGT 450
    GPQDCKWKMY MEMDGDEIAI TYIKDVTFNT NLPDAEILKM TKPPFVMEKW 500
    IVGIAKSQTV ECTVTYESDV RTPKSTKHVH SIQWSRTKPQ DEVKAVQLAI 550
    QTLFTNSDGN PGSRSDSSAD CQWLDTLRMR QIASNTSLQR SQSNPILGSP 600
    FFSHFDGQDS YAAAVRRPQV PIKYQQITPV NQSRSSSPTQ YGLTKNFSSL 650
    HLNSRDSGFS SGNTDTSSER GRYSDRSRNK YGRGSISLNS SPRGRYSGKS 700
    QHSTPSRGRY PGKFYRVSQS ALNPHQSPDF KRSPRDLHQP NTIPGMPLHP 750
    ETDSRASEED SKVSEGGWTK VEYRKKPHRP SPAKTNKERA RGDHRGWRNF 800
    Length:800
    Mass (Da):91,155
    Last modified:November 30, 2010 - v3
    Checksum:iB2814509EC54B07A
    GO
    Isoform 21 Publication (identifier: Q9NYL2-2) [UniParc]FASTAAdd to Basket

    Also known as: Beta

    The sequence of this isoform differs from the canonical sequence as follows:
         332-455: PSFEIGAWTE...LKPGTGPQDC → LPLAARMSEE...EEDNDMDNSE
         456-800: Missing.

    Note: Contains a phosphoserine at position 339. Contains a phosphoserine at position 429. Contains a phosphoserine at position 434. Contains a phosphoserine at position 454.

    Show »
    Length:455
    Mass (Da):51,582
    Checksum:iE87DB84A4D58B752
    GO
    Isoform 3 (identifier: Q9NYL2-3) [UniParc]FASTAAdd to Basket

    Also known as: HCCS-4

    The sequence of this isoform differs from the canonical sequence as follows:
         285-312: CEIEATLERLKKLERDLSFKEQELKERE → WVAPTAGHSVWLSKTITRLNEEVNQRSE
         313-800: Missing.

    Show »
    Length:312
    Mass (Da):35,468
    Checksum:iB655E873246339FB
    GO

    Sequence cautioni

    The sequence BAD92211.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti346 – 3461C → W in AAF63490. (PubMed:10924358)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti267 – 2671T → M.1 Publication
    Corresponds to variant rs6758025 [ dbSNP | Ensembl ].
    VAR_040806
    Natural varianti281 – 2811A → T in an ovarian endometrioid sample; somatic mutation. 1 Publication
    VAR_040807
    Natural varianti281 – 2811A → V.1 Publication
    Corresponds to variant rs34683477 [ dbSNP | Ensembl ].
    VAR_040808
    Natural varianti531 – 5311S → L.5 Publications
    Corresponds to variant rs3769148 [ dbSNP | Ensembl ].
    VAR_022827
    Natural varianti580 – 5801R → W.1 Publication
    Corresponds to variant rs7593622 [ dbSNP | Ensembl ].
    VAR_040809
    Natural varianti740 – 7401P → T.1 Publication
    Corresponds to variant rs56202258 [ dbSNP | Ensembl ].
    VAR_040810
    Natural varianti773 – 7731Y → H.1 Publication
    Corresponds to variant rs35608243 [ dbSNP | Ensembl ].
    VAR_040811
    Natural varianti784 – 7841K → T.2 Publications
    Corresponds to variant rs55830025 [ dbSNP | Ensembl ].
    VAR_040812

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei285 – 31228CEIEA…LKERE → WVAPTAGHSVWLSKTITRLN EEVNQRSE in isoform 3. 1 PublicationVSP_051741Add
    BLAST
    Alternative sequencei313 – 800488Missing in isoform 3. 1 PublicationVSP_051742Add
    BLAST
    Alternative sequencei332 – 455124PSFEI…GPQDC → LPLAARMSEESYFESKTEES NSAEMSCQITATSNGEGHGM NPSLQAMMLMGFGDIFSMNK AGAVMHSGMQINMQAKQNSS KTTSKRRGKKVNMALGFSDF DLSEGDDDDDDDGEEEDNDM DNSE in isoform 2. 5 PublicationsVSP_051743Add
    BLAST
    Alternative sequencei456 – 800345Missing in isoform 2. 5 PublicationsVSP_051744Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF238255 mRNA. Translation: AAF63490.1.
    AB049733 mRNA. Translation: BAB16444.1.
    AB049734 mRNA. Translation: BAB16445.1.
    AF325454 mRNA. Translation: AAK11615.1.
    AF480461 mRNA. Translation: AAL85891.1.
    AF480462 mRNA. Translation: AAL85892.1.
    AB030034 mRNA. Translation: BAB12040.1.
    AF251441 mRNA. Translation: AAF65822.1.
    AF465843 mRNA. Translation: AAO33376.1.
    AK056310 mRNA. Translation: BAG51674.1.
    AB208974 mRNA. Translation: BAD92211.1. Different initiation.
    AC092573 Genomic DNA. Translation: AAX82002.1.
    AC013461 Genomic DNA. Translation: AAX93067.1.
    AC019046 Genomic DNA. No translation available.
    CH471058 Genomic DNA. Translation: EAX11164.1.
    BC001401 mRNA. Translation: AAH01401.1.
    CCDSiCCDS2251.1. [Q9NYL2-2]
    CCDS42777.1. [Q9NYL2-1]
    RefSeqiNP_057737.2. NM_016653.2. [Q9NYL2-1]
    NP_598407.1. NM_133646.2. [Q9NYL2-2]
    XP_005246697.1. XM_005246640.1. [Q9NYL2-1]
    UniGeneiHs.444451.

    Genome annotation databases

    GeneIDi51776.
    KEGGihsa:51776.
    UCSCiuc002uhx.3. human. [Q9NYL2-3]
    uc002uhz.3. human. [Q9NYL2-1]

    Polymorphism databases

    DMDMi313104215.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF238255 mRNA. Translation: AAF63490.1 .
    AB049733 mRNA. Translation: BAB16444.1 .
    AB049734 mRNA. Translation: BAB16445.1 .
    AF325454 mRNA. Translation: AAK11615.1 .
    AF480461 mRNA. Translation: AAL85891.1 .
    AF480462 mRNA. Translation: AAL85892.1 .
    AB030034 mRNA. Translation: BAB12040.1 .
    AF251441 mRNA. Translation: AAF65822.1 .
    AF465843 mRNA. Translation: AAO33376.1 .
    AK056310 mRNA. Translation: BAG51674.1 .
    AB208974 mRNA. Translation: BAD92211.1 . Different initiation.
    AC092573 Genomic DNA. Translation: AAX82002.1 .
    AC013461 Genomic DNA. Translation: AAX93067.1 .
    AC019046 Genomic DNA. No translation available.
    CH471058 Genomic DNA. Translation: EAX11164.1 .
    BC001401 mRNA. Translation: AAH01401.1 .
    CCDSi CCDS2251.1. [Q9NYL2-2 ]
    CCDS42777.1. [Q9NYL2-1 ]
    RefSeqi NP_057737.2. NM_016653.2. [Q9NYL2-1 ]
    NP_598407.1. NM_133646.2. [Q9NYL2-2 ]
    XP_005246697.1. XM_005246640.1. [Q9NYL2-1 ]
    UniGenei Hs.444451.

    3D structure databases

    ProteinModelPortali Q9NYL2.
    SMRi Q9NYL2. Positions 9-325.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119725. 29 interactions.
    IntActi Q9NYL2. 23 interactions.
    MINTi MINT-1465549.

    Chemistry

    BindingDBi Q9NYL2.
    ChEMBLi CHEMBL3886.
    GuidetoPHARMACOLOGYi 2289.

    PTM databases

    PhosphoSitei Q9NYL2.

    Polymorphism databases

    DMDMi 313104215.

    Proteomic databases

    MaxQBi Q9NYL2.
    PaxDbi Q9NYL2.
    PRIDEi Q9NYL2.

    Protocols and materials databases

    DNASUi 51776.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 51776.
    KEGGi hsa:51776.
    UCSCi uc002uhx.3. human. [Q9NYL2-3 ]
    uc002uhz.3. human. [Q9NYL2-1 ]

    Organism-specific databases

    CTDi 51776.
    GeneCardsi GC02P173940.
    H-InvDB HIX0030332.
    HPAi HPA017205.
    MIMi 609479. gene.
    neXtProti NX_Q9NYL2.

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG080445.
    KOi K04424.
    OMAi LHSGMQI.
    PhylomeDBi Q9NYL2.

    Enzyme and pathway databases

    SignaLinki Q9NYL2.

    Miscellaneous databases

    ChiTaRSi ZAK. human.
    GeneWikii ZAK.
    GenomeRNAii 51776.
    NextBioi 55903.
    PROi Q9NYL2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NYL2.
    Bgeei Q9NYL2.
    Genevestigatori Q9NYL2.

    Family and domain databases

    Gene3Di 1.10.150.50. 1 hit.
    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR021129. SAM_type1.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF07714. Pkinase_Tyr. 1 hit.
    PF00536. SAM_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00454. SAM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47769. SSF47769. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50105. SAM_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of ZAK, a mixed lineage kinase-like protein containing a leucine-zipper and a sterile-alpha motif."
      Liu T.-C., Huang C.-J., Chu Y.-C., Wei C.-C., Chou C.-C., Chou M.-Y., Chou C.-K., Yang J.-J.
      Biochem. Biophys. Res. Commun. 274:811-816(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, HOMODIMERIZATION, VARIANT LEU-531.
      Tissue: Placenta1 Publication.
    2. "Identification and characterization of a novel MAP kinase kinase kinase, MLTK."
      Gotoh I., Adachi M., Nishida E.
      J. Biol. Chem. 276:4276-4286(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, PHOSPHORYLATION, VARIANT LEU-531.
      Tissue: Fetal brain1 Publication.
    3. "Tissue distribution and functional expression of a cDNA encoding a novel mixed lineage kinase."
      Bloem L.J., Pickard T.R., Acton S., Donoghue M., Beavis R.C., Knierman M.D., Wang X.
      J. Mol. Cell. Cardiol. 33:1739-1750(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Heart1 Publication.
    4. "MRK, a mixed lineage kinase-related molecule that plays a role in gamma-radiation-induced cell cycle arrest."
      Gross E.A., Callow M.G., Waldbaum L., Thomas S., Ruggieri R.
      J. Biol. Chem. 277:13873-13882(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-45, VARIANT LEU-531.
      Tissue: T-cell1 Publication.
    5. "Placible mixed-lineage kinase derived from LAK cell."
      Abe Y., Ueda N.
      Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Lymphoid tissue.
    6. "Cloning and characterisation of AZK, a mixed lineage kinase containing a sterile-alpha motif."
      McNee J.J., Frima N., Diamond T.E., Dower S.K., Guesdon F.
      Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LEU-531.
    7. "Identification of a new tumor suppressor in human cancers."
      Kim J.W.
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    8. "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).
    9. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-784.
      Tissue: BrainImported.
    10. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. "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: ColonImported.
    13. "A novel zinc finger protein, ZZaPK, interacts with ZAK and stimulates the ZAK-expressing cells re-entering the cell cycle."
      Yang J.-J.
      Biochem. Biophys. Res. Commun. 301:71-77(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZNF33A.
    14. "Regulation of a mitogen-activated protein kinase kinase kinase, MLTK by PKN."
      Takahashi M., Gotoh Y., Isagawa T., Nishimura T., Goyama E., Kim H.-S., Mukai H., Ono Y.
      J. Biochem. 133:181-187(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH PKN1.
    15. "A novel role for mixed-lineage kinase-like mitogen-activated protein triple kinase alpha in neoplastic cell transformation and tumor development."
      Cho Y.-Y., Bode A.M., Mizuno H., Choi B.Y., Choi H.S., Dong Z.
      Cancer Res. 64:3855-3864(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "The stress kinase MRK contributes to regulation of DNA damage checkpoints through a p38gamma-independent pathway."
      Tosti E., Waldbaum L., Warshaw G., Gross E.A., Ruggieri R.
      J. Biol. Chem. 279:47652-47660(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DNA DAMAGE CHECKPOINTS, FUNCTION IN PHOSPHORYLATION OF CHEK2, ENZYME REGULATION, PHOSPHORYLATION AT THR-161 AND SER-165, MUTAGENESIS OF THR-161; THR-162 AND SER-165.
    17. "Phosphorylation of Ser28 in histone H3 mediated by mixed lineage kinase-like mitogen-activated protein triple kinase alpha."
      Choi H.S., Choi B.Y., Cho Y.-Y., Zhu F., Bode A.M., Dong Z.
      J. Biol. Chem. 280:13545-13553(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3, SUBCELLULAR LOCATION.
    18. "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 THR-628; SER-727 AND SER-733, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599; THR-628; SER-633; SER-727 AND SER-733, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-628; SER-633 AND SER-727, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "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-633, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    23. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "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] MET-267; THR-281; VAL-281; LEU-531; TRP-580; THR-740; HIS-773 AND THR-784.

    Entry informationi

    Entry nameiMLTK_HUMAN
    AccessioniPrimary (citable) accession number: Q9NYL2
    Secondary accession number(s): B3KPG2
    , Q53SX1, Q580W8, Q59GY5, Q86YW8, Q9HCC4, Q9HCC5, Q9HDD2, Q9NYE9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 129 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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