Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9Y6R4

- M3K4_HUMAN

UniProt

Q9Y6R4 - M3K4_HUMAN

Protein

Mitogen-activated protein kinase kinase kinase 4

Gene

MAP3K4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Component of a protein kinase signal transduction cascade. Activates the CSBP2, P38 and JNK MAPK pathways, but not the ERK pathway. Specifically phosphorylates and activates MAP2K4 and MAP2K6.2 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Enzyme regulationi

    N-terminal autoinhibitory domain interacts with the C-terminal kinase domain, inhibiting kinase activity, and preventing interaction with its substrate, MAP2K6. The GADD45 proteins activate the kinase by binding to the N-terminal domain. Activated by phosphorylation on Thr-1505.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1372 – 13721ATPPROSITE-ProRule annotation
    Active sitei1463 – 14631Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1349 – 13579ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. MAP kinase kinase kinase activity Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. activation of MAPKK activity Source: UniProtKB
    2. chorionic trophoblast cell differentiation Source: Ensembl
    3. intracellular signal transduction Source: UniProtKB
    4. male germ-line sex determination Source: Ensembl
    5. MAPK cascade Source: GOC
    6. placenta development Source: Ensembl
    7. positive regulation of JUN kinase activity Source: UniProtKB
    8. positive regulation of p38MAPK cascade Source: UniProtKB
    9. regulation of gene expression Source: Ensembl
    10. response to UV-C Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BRENDAi2.7.12.2. 2681.
    SignaLinkiQ9Y6R4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase kinase kinase 4 (EC:2.7.11.25)
    Alternative name(s):
    MAP three kinase 1
    MAPK/ERK kinase kinase 4
    Short name:
    MEK kinase 4
    Short name:
    MEKK 4
    Gene namesi
    Name:MAP3K4
    Synonyms:KIAA0213, MAPKKK4, MEKK4, MTK1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:6856. MAP3K4.

    Subcellular locationi

    Cytoplasmperinuclear region By similarity
    Note: Localized in perinuclear vesicular-like structures, probably Golgi-associated vesicles.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1372 – 13721K → R: Loss of activity. 2 Publications

    Organism-specific databases

    PharmGKBiPA30600.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 16081608Mitogen-activated protein kinase kinase kinase 4PRO_0000086247Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei456 – 4561Phosphoserine1 Publication
    Modified residuei457 – 4571Phosphoserine1 Publication
    Modified residuei458 – 4581Phosphothreonine1 Publication
    Modified residuei461 – 4611Phosphoserine1 Publication
    Modified residuei499 – 4991Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y6R4.
    PaxDbiQ9Y6R4.
    PRIDEiQ9Y6R4.

    PTM databases

    PhosphoSiteiQ9Y6R4.

    Expressioni

    Tissue specificityi

    Expressed at high levels in heart, placenta, skeletal muscle and pancreas, and at lower levels in other tissues.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y6R4.
    BgeeiQ9Y6R4.
    CleanExiHS_MAP3K4.
    GenevestigatoriQ9Y6R4.

    Organism-specific databases

    HPAiHPA007625.

    Interactioni

    Subunit structurei

    Monomer and homodimer. Homodimerization enhances kinase activity. Interacts with TRAF4; this promotes homodimerization By similarity. Binds both upstream activators and downstream substrates in multimolecular complexes. Interacts with AXIN1 and DIXDC1; interaction with DIXDC1 prevents interaction with AXIN1.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FLNBO753692EBI-448104,EBI-352089
    GADD45BO752932EBI-448104,EBI-448187
    MAP2K6P525642EBI-448104,EBI-448135
    SH3KBP1Q96B975EBI-448104,EBI-346595
    UBCP0CG482EBI-448104,EBI-3390054

    Protein-protein interaction databases

    BioGridi110380. 22 interactions.
    IntActiQ9Y6R4. 13 interactions.
    MINTiMINT-1213156.
    STRINGi9606.ENSP00000375986.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y6R4.
    SMRiQ9Y6R4. Positions 1301-1603.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1343 – 1601259Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi4 – 74Poly-Ala
    Compositional biasi25 – 3814Poly-ProAdd
    BLAST
    Compositional biasi1190 – 120213Poly-AlaAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG006304.
    InParanoidiQ9Y6R4.
    KOiK04428.
    OMAiFVKVCTD.
    OrthoDBiEOG7P5T02.
    PhylomeDBiQ9Y6R4.
    TreeFamiTF105114.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y6R4-1) [UniParc]FASTAAdd to Basket

    Also known as: A

    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

    MREAAAALVP PPAFAVTPAA AMEEPPPPPP PPPPPPEPET ESEPECCLAA     50
    RQEGTLGDSA CKSPESDLED FSDETNTENL YGTSPPSTPR QMKRMSTKHQ 100
    RNNVGRPASR SNLKEKMNAP NQPPHKDTGK TVENVEEYSY KQEKKIRAAL 150
    RTTERDRKKN VQCSFMLDSV GGSLPKKSIP DVDLNKPYLS LGCSNAKLPV 200
    SVPMPIARPA RQTSRTDCPA DRLKFFETLR LLLKLTSVSK KKDREQRGQE 250
    NTSGFWLNRS NELIWLELQA WHAGRTINDQ DFFLYTARQA IPDIINEILT 300
    FKVDYGSFAF VRDRAGFNGT SVEGQCKATP GTKIVGYSTH HEHLQRQRVS 350
    FEQVKRIMEL LEYIEALYPS LQALQKDYEK YAAKDFQDRV QALCLWLNIT 400
    KDLNQKLRIM GTVLGIKNLS DIGWPVFEIP SPRPSKGNEP EYEGDDTEGE 450
    LKELESSTDE SEEEQISDPR VPEIRQPIDN SFDIQSRDCI SKKLERLESE 500
    DDSLGWGAPD WSTEAGFSRH CLTSIYRPFV DKALKQMGLR KLILRLHKLM 550
    DGSLQRARIA LVKNDRPVEF SEFPDPMWGS DYVQLSRTPP SSEEKCSAVS 600
    WEELKAMDLP SFEPAFLVLC RVLLNVIHEC LKLRLEQRPA GEPSLLSIKQ 650
    LVRECKEVLK GGLLMKQYYQ FMLQEVLEDL EKPDCNIDAF EEDLHKMLMV 700
    YFDYMRSWIQ MLQQLPQASH SLKNLLEEEW NFTKEITHYI RGGEAQAGKL 750
    FCDIAGMLLK STGSFLEFGL QESCAEFWTS ADDSSASDEI RRSVIEISRA 800
    LKELFHEARE RASKALGFAK MLRKDLEIAA EFRLSAPVRD LLDVLKSKQY 850
    VKVQIPGLEN LQMFVPDTLA EEKSIILQLL NAAAGKDCSK DSDDVLIDAY 900
    LLLTKHGDRA RDSEDSWGTW EAQPVKVVPQ VETVDTLRSM QVDNLLLVVM 950
    QSAHLTIQRK AFQQSIEGLM TLCQEQTSSQ PVIAKALQQL KNDALELCNR 1000
    ISNAIDRVDH MFTSEFDAEV DESESVTLQQ YYREAMIQGY NFGFEYHKEV 1050
    VRLMSGEFRQ KIGDKYISFA RKWMNYVLTK CESGRGTRPR WATQGFDFLQ 1100
    AIEPAFISAL PEDDFLSLQA LMNECIGHVI GKPHSPVTGL YLAIHRNSPR 1150
    PMKVPRCHSD PPNPHLIIPT PEGFSTRSMP SDARSHGSPA AAAAAAAAAV 1200
    AASRPSPSGG DSVLPKSISS AHDTRGSSVP ENDRLASIAA ELQFRSLSRH 1250
    SSPTEERDEP AYPRGDSSGS TRRSWELRTL ISQSKDTASK LGPIEAIQKS 1300
    VRLFEEKRYR EMRRKNIIGQ VCDTPKSYDN VMHVGLRKVT FKWQRGNKIG 1350
    EGQYGKVYTC ISVDTGELMA MKEIRFQPND HKTIKETADE LKIFEGIKHP 1400
    NLVRYFGVEL HREEMYIFME YCDEGTLEEV SRLGLQEHVI RLYSKQITIA 1450
    INVLHEHGIV HRDIKGANIF LTSSGLIKLG DFGCSVKLKN NAQTMPGEVN 1500
    STLGTAAYMA PEVITRAKGE GHGRAADIWS LGCVVIEMVT GKRPWHEYEH 1550
    NFQIMYKVGM GHKPPIPERL SPEGKDFLSH CLESDPKMRW TASQLLDHSF 1600
    VKVCTDEE 1608
    Length:1,608
    Mass (Da):181,685
    Last modified:May 18, 2010 - v2
    Checksum:iC22294914945EA91
    GO
    Isoform 2 (identifier: Q9Y6R4-2) [UniParc]FASTAAdd to Basket

    Also known as: B

    The sequence of this isoform differs from the canonical sequence as follows:
         1175-1224: Missing.

    Show »
    Length:1,558
    Mass (Da):177,014
    Checksum:i4F94E9CF82E88354
    GO

    Sequence cautioni

    The sequence BAA13204.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAC12766.2 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAH70639.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAH70640.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI20815.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI20816.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI21477.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI41309.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI41310.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti35 – 351P → PP in AAI36277. (PubMed:15489334)Curated
    Sequence conflicti500 – 5001E → D in AAI46771. (PubMed:15489334)Curated
    Sequence conflicti791 – 7911R → I in AAB68804. (PubMed:9305639)Curated
    Sequence conflicti1190 – 11901Missing in EAW47587. 1 PublicationCurated
    Sequence conflicti1190 – 11901Missing in AAI43736. (PubMed:15489334)Curated
    Sequence conflicti1190 – 11901Missing in AAI36277. (PubMed:15489334)Curated
    Sequence conflicti1199 – 11991Missing in AAB68804. (PubMed:9305639)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti157 – 1571R → H.1 Publication
    Corresponds to variant rs4559074 [ dbSNP | Ensembl ].
    VAR_059767
    Natural varianti294 – 2941I → T.1 Publication
    Corresponds to variant rs35842248 [ dbSNP | Ensembl ].
    VAR_040686
    Natural varianti335 – 3351V → I.1 Publication
    Corresponds to variant rs35730939 [ dbSNP | Ensembl ].
    VAR_040687
    Natural varianti566 – 5661R → H.1 Publication
    Corresponds to variant rs55765351 [ dbSNP | Ensembl ].
    VAR_040688
    Natural varianti584 – 5841Q → H.1 Publication
    Corresponds to variant rs34018542 [ dbSNP | Ensembl ].
    VAR_040689
    Natural varianti906 – 9061H → P.1 Publication
    Corresponds to variant rs35533223 [ dbSNP | Ensembl ].
    VAR_040690
    Natural varianti1413 – 14131E → Q in an ovarian serous carcinoma sample; somatic mutation. 1 Publication
    VAR_040691
    Natural varianti1492 – 14921A → V.1 Publication
    Corresponds to variant rs41267837 [ dbSNP | Ensembl ].
    VAR_040692

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1175 – 122450Missing in isoform 2. 2 PublicationsVSP_004884Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF002715 mRNA. Translation: AAB68804.1.
    D86968 mRNA. Translation: BAA13204.2. Different initiation.
    AL109942
    , AL139393, AL591045, AL596452 Genomic DNA. Translation: CAC12766.2. Sequence problems.
    AL109942
    , AL139393, AL591045, AL596452 Genomic DNA. Translation: CAI21477.1. Sequence problems.
    AL139393
    , AL109942, AL591045, AL596452 Genomic DNA. Translation: CAI20815.1. Sequence problems.
    AL139393
    , AL109942, AL591045, AL596452 Genomic DNA. Translation: CAI20816.1. Sequence problems.
    AL591045
    , AL109942, AL139393, AL596452 Genomic DNA. Translation: CAH70639.1. Sequence problems.
    AL591045
    , AL109942, AL139393, AL596452 Genomic DNA. Translation: CAH70640.1. Sequence problems.
    AL596452
    , AL109942, AL139393, AL591045 Genomic DNA. Translation: CAI41309.1. Sequence problems.
    AL596452
    , AL109942, AL139393, AL591045 Genomic DNA. Translation: CAI41310.1. Sequence problems.
    CH471051 Genomic DNA. Translation: EAW47587.1.
    BC136276 mRNA. Translation: AAI36277.1.
    BC143735 mRNA. Translation: AAI43736.1.
    BC146770 mRNA. Translation: AAI46771.1.
    CCDSiCCDS34565.1. [Q9Y6R4-1]
    CCDS34566.1. [Q9Y6R4-2]
    PIRiT03022.
    RefSeqiNP_005913.2. NM_005922.2.
    NP_006715.2. NM_006724.2.
    UniGeneiHs.390428.

    Genome annotation databases

    EnsembliENST00000366919; ENSP00000355886; ENSG00000085511. [Q9Y6R4-2]
    ENST00000392142; ENSP00000375986; ENSG00000085511. [Q9Y6R4-1]
    GeneIDi4216.
    KEGGihsa:4216.
    UCSCiuc003qtn.3. human. [Q9Y6R4-1]
    uc003qto.3. human. [Q9Y6R4-2]

    Polymorphism databases

    DMDMi296434576.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF002715 mRNA. Translation: AAB68804.1 .
    D86968 mRNA. Translation: BAA13204.2 . Different initiation.
    AL109942
    , AL139393 , AL591045 , AL596452 Genomic DNA. Translation: CAC12766.2 . Sequence problems.
    AL109942
    , AL139393 , AL591045 , AL596452 Genomic DNA. Translation: CAI21477.1 . Sequence problems.
    AL139393
    , AL109942 , AL591045 , AL596452 Genomic DNA. Translation: CAI20815.1 . Sequence problems.
    AL139393
    , AL109942 , AL591045 , AL596452 Genomic DNA. Translation: CAI20816.1 . Sequence problems.
    AL591045
    , AL109942 , AL139393 , AL596452 Genomic DNA. Translation: CAH70639.1 . Sequence problems.
    AL591045
    , AL109942 , AL139393 , AL596452 Genomic DNA. Translation: CAH70640.1 . Sequence problems.
    AL596452
    , AL109942 , AL139393 , AL591045 Genomic DNA. Translation: CAI41309.1 . Sequence problems.
    AL596452
    , AL109942 , AL139393 , AL591045 Genomic DNA. Translation: CAI41310.1 . Sequence problems.
    CH471051 Genomic DNA. Translation: EAW47587.1 .
    BC136276 mRNA. Translation: AAI36277.1 .
    BC143735 mRNA. Translation: AAI43736.1 .
    BC146770 mRNA. Translation: AAI46771.1 .
    CCDSi CCDS34565.1. [Q9Y6R4-1 ]
    CCDS34566.1. [Q9Y6R4-2 ]
    PIRi T03022.
    RefSeqi NP_005913.2. NM_005922.2.
    NP_006715.2. NM_006724.2.
    UniGenei Hs.390428.

    3D structure databases

    ProteinModelPortali Q9Y6R4.
    SMRi Q9Y6R4. Positions 1301-1603.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110380. 22 interactions.
    IntActi Q9Y6R4. 13 interactions.
    MINTi MINT-1213156.
    STRINGi 9606.ENSP00000375986.

    Chemistry

    ChEMBLi CHEMBL4853.
    GuidetoPHARMACOLOGYi 2079.

    PTM databases

    PhosphoSitei Q9Y6R4.

    Polymorphism databases

    DMDMi 296434576.

    Proteomic databases

    MaxQBi Q9Y6R4.
    PaxDbi Q9Y6R4.
    PRIDEi Q9Y6R4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000366919 ; ENSP00000355886 ; ENSG00000085511 . [Q9Y6R4-2 ]
    ENST00000392142 ; ENSP00000375986 ; ENSG00000085511 . [Q9Y6R4-1 ]
    GeneIDi 4216.
    KEGGi hsa:4216.
    UCSCi uc003qtn.3. human. [Q9Y6R4-1 ]
    uc003qto.3. human. [Q9Y6R4-2 ]

    Organism-specific databases

    CTDi 4216.
    GeneCardsi GC06P161412.
    H-InvDB HIX0151295.
    HGNCi HGNC:6856. MAP3K4.
    HPAi HPA007625.
    MIMi 602425. gene.
    neXtProti NX_Q9Y6R4.
    PharmGKBi PA30600.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG006304.
    InParanoidi Q9Y6R4.
    KOi K04428.
    OMAi FVKVCTD.
    OrthoDBi EOG7P5T02.
    PhylomeDBi Q9Y6R4.
    TreeFami TF105114.

    Enzyme and pathway databases

    BRENDAi 2.7.12.2. 2681.
    SignaLinki Q9Y6R4.

    Miscellaneous databases

    ChiTaRSi MAP3K4. human.
    GeneWikii MAP3K4.
    GenomeRNAii 4216.
    NextBioi 16627.
    PROi Q9Y6R4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y6R4.
    Bgeei Q9Y6R4.
    CleanExi HS_MAP3K4.
    Genevestigatori Q9Y6R4.

    Family and domain databases

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

    Publicationsi

    1. "A human homolog of the yeast Ssk2/Ssk22 MAP kinase kinase kinases, MTK1, mediates stress-induced activation of the p38 and JNK pathways."
      Takekawa M., Posas F., Saito H.
      EMBO J. 16:4973-4982(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING, MUTAGENESIS OF LYS-1372.
      Tissue: Fetal liver and Skeletal muscle.
    2. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
      Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
      DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Bone marrow.
    3. Ohara O., Nagase T., Kikuno R., Nomura N.
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [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] (ISOFORMS 1 AND 2), VARIANT HIS-157.
      Tissue: Cerebellum.
    7. "Regulation of MTK1/MEKK4 kinase activity by its N-terminal autoinhibitory domain and GADD45 binding."
      Mita H., Tsutsui J., Takekawa M., Witten E.A., Saito H.
      Mol. Cell. Biol. 22:4544-4555(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH GADD45 AND MAP2K6, MUTAGENESIS OF LYS-1372.
    8. "The DIX domain protein coiled-coil-DIX1 inhibits c-Jun N-terminal kinase activation by Axin and dishevelled through distinct mechanisms."
      Wong C.K., Luo W., Deng Y., Zou H., Ye Z., Lin S.-C.
      J. Biol. Chem. 279:39366-39373(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AXIN1 AND DIXDC1.
    9. "MEKK4 is an effector of the embryonic TRAF4 for JNK activation."
      Abell A.N., Johnson G.L.
      J. Biol. Chem. 280:35793-35796(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRAF4.
    10. "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].
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456; SER-457; THR-458 AND SER-461, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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] THR-294; ILE-335; HIS-566; HIS-584; PRO-906; GLN-1413 AND VAL-1492.

    Entry informationi

    Entry nameiM3K4_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y6R4
    Secondary accession number(s): A6H8W0
    , B7ZLD3, B9EG75, Q5VTT8, Q5VTT9, Q92612, Q9H408
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 141 of the entry and version 2 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 6
      Human chromosome 6: 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