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Q99558

- M3K14_HUMAN

UniProt

Q99558 - M3K14_HUMAN

Protein

Mitogen-activated protein kinase kinase kinase 14

Gene

MAP3K14

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (04 Apr 2006)
      Previous versions | rss
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    Functioni

    Lymphotoxin beta-activated kinase which seems to be exclusively involved in the activation of NF-kappa-B and its transcriptional activity. Promotes proteolytic processing of NFKB2/P100, which leads to activation of NF-kappa-B via the non-canonical pathway. Could act in a receptor-selective manner.1 Publication

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei429 – 4291ATPPROSITE-ProRule annotation
    Active sitei515 – 5151Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi406 – 4149ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. MAP kinase kinase kinase activity Source: UniProtKB-EC
    3. NF-kappaB-inducing kinase activity Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein kinase activity Source: MGI

    GO - Biological processi

    1. cellular response to mechanical stimulus Source: UniProtKB
    2. I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    3. immune response Source: UniProtKB
    4. NIK/NF-kappaB signaling Source: GOC
    5. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    6. T cell costimulation Source: Reactome

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_19358. CD28 dependent PI3K/Akt signaling.
    SignaLinkiQ99558.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitogen-activated protein kinase kinase kinase 14 (EC:2.7.11.25)
    Alternative name(s):
    NF-kappa-beta-inducing kinase
    Short name:
    HsNIK
    Serine/threonine-protein kinase NIK
    Gene namesi
    Name:MAP3K14
    Synonyms:NIK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    Organism-specific databases

    HGNCiHGNC:6853. MAP3K14.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi429 – 4302KK → AA: Loss of autophosphorylation and 'Lys-63'-linked ubiquitination. 1 Publication
    Mutagenesisi559 – 5591T → A: Abolishes 'Lys-63'-linked ubiquitination. 2 Publications

    Organism-specific databases

    PharmGKBiPA30597.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 947947Mitogen-activated protein kinase kinase kinase 14PRO_0000086266Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei559 – 5591Phosphothreonine2 Publications

    Post-translational modificationi

    Autophosphorylated. Phosphorylation at Thr-559 is required to activates its kinase activity and 'Lys-63'-linked polyubiquitination. Phosphorylated by CHUK/IKKA leading to MAP3K14 destabilization.2 Publications
    Ubiquitinated. Undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination. 'Lys-48'-linked polyubiquitination leads to its degradation by the proteasome, while 'Lys-63'-linked polyubiquitination stabilizes and activates it.

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ99558.
    PRIDEiQ99558.

    PTM databases

    PhosphoSiteiQ99558.

    Expressioni

    Tissue specificityi

    Weakly expressed in testis, small intestine, spleen, thymus, peripheral blood leukocytes, prostate, ovary and colon.1 Publication

    Gene expression databases

    CleanExiHS_MAP3K14.
    GenevestigatoriQ99558.

    Interactioni

    Subunit structurei

    Interacts with TRAF2, TRAF5, TRAF6, IKKA and NFKB2/P100 By similarity. Interacts with TRAF3 and PELI3. Interacts with NIBP; the interaction is direct. Interacts with ARRB1 and ARRB2. Interacts with GRB10. Interacts with ZFP91.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ALPLP051864EBI-358011,EBI-1054354
    CDC37Q165432EBI-358011,EBI-295634
    CHUKO151116EBI-358011,EBI-81249
    ChukQ60680-23EBI-358011,EBI-646264From a different organism.
    HSP90AB1P082382EBI-358011,EBI-352572
    IKBKBO149203EBI-358011,EBI-81266
    TRAF6Q9Y4K32EBI-358011,EBI-359276

    Protein-protein interaction databases

    BioGridi114487. 32 interactions.
    DIPiDIP-27522N.
    IntActiQ99558. 28 interactions.
    MINTiMINT-88636.
    STRINGi9606.ENSP00000342059.

    Structurei

    Secondary structure

    1
    947
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi335 – 3417
    Beta strandi345 – 3473
    Helixi350 – 36314
    Beta strandi364 – 3663
    Beta strandi377 – 3815
    Turni395 – 3973
    Beta strandi398 – 40811
    Beta strandi410 – 41910
    Turni420 – 4223
    Beta strandi425 – 4328
    Helixi433 – 4353
    Helixi439 – 4424
    Turni443 – 4464
    Beta strandi455 – 4617
    Beta strandi464 – 4696
    Helixi477 – 4848
    Helixi489 – 50719
    Turni508 – 5103
    Helixi518 – 5203
    Beta strandi521 – 5233
    Beta strandi530 – 5323
    Helixi535 – 5373
    Beta strandi543 – 5475
    Turni550 – 5534
    Helixi560 – 5623
    Helixi565 – 5684
    Helixi576 – 59116
    Turni595 – 5995
    Helixi605 – 6106
    Helixi614 – 6174
    Helixi624 – 63310
    Turni638 – 6403
    Helixi644 – 65815

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4DN5X-ray2.50A/B330-680[»]
    4G3DX-ray2.90A/B/D/E308-673[»]
    4IDTX-ray2.40A/B330-680[»]
    4IDVX-ray2.90A/B/C/D330-680[»]
    ProteinModelPortaliQ99558.
    SMRiQ99558. Positions 333-675.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini400 – 655256Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni401 – 653253Interaction with ZFP91Add
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000113436.
    HOVERGENiHBG052384.
    InParanoidiQ99558.
    KOiK04466.
    PhylomeDBiQ99558.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR017425. MAPKKK14.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038175. MAPKKK14. 1 hit.
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q99558-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAVMEMACPG APGSAVGQQK ELPKAKEKTP PLGKKQSSVY KLEAVEKSPV    50
    FCGKWEILND VITKGTAKEG SEAGPAAISI IAQAECENSQ EFSPTFSERI 100
    FIAGSKQYSQ SESLDQIPNN VAHATEGKMA RVCWKGKRRS KARKKRKKKS 150
    SKSLAHAGVA LAKPLPRTPE QESCTIPVQE DESPLGAPYV RNTPQFTKPL 200
    KEPGLGQLCF KQLGEGLRPA LPRSELHKLI SPLQCLNHVW KLHHPQDGGP 250
    LPLPTHPFPY SRLPHPFPFH PLQPWKPHPL ESFLGKLACV DSQKPLPDPH 300
    LSKLACVDSP KPLPGPHLEP SCLSRGAHEK FSVEEYLVHA LQGSVSSGQA 350
    HSLTSLAKTW AARGSRSREP SPKTEDNEGV LLTEKLKPVD YEYREEVHWA 400
    THQLRLGRGS FGEVHRMEDK QTGFQCAVKK VRLEVFRAEE LMACAGLTSP 450
    RIVPLYGAVR EGPWVNIFME LLEGGSLGQL VKEQGCLPED RALYYLGQAL 500
    EGLEYLHSRR ILHGDVKADN VLLSSDGSHA ALCDFGHAVC LQPDGLGKSL 550
    LTGDYIPGTE THMAPEVVLG RSCDAKVDVW SSCCMMLHML NGCHPWTQFF 600
    RGPLCLKIAS EPPPVREIPP SCAPLTAQAI QEGLRKEPIH RVSAAELGGK 650
    VNRALQQVGG LKSPWRGEYK EPRHPPPNQA NYHQTLHAQP RELSPRAPGP 700
    RPAEETTGRA PKLQPPLPPE PPEPNKSPPL TLSKEESGMW EPLPLSSLEP 750
    APARNPSSPE RKATVPEQEL QQLEIELFLN SLSQPFSLEE QEQILSCLSI 800
    DSLSLSDDSE KNPSKASQSS RDTLSSGVHS WSSQAEARSS SWNMVLARGR 850
    PTDTPSYFNG VKVQIQSLNG EHLHIREFHR VKVGDIATGI SSQIPAAAFS 900
    LVTKDGQPVR YDMEVPDSGI DLQCTLAPDG SFAWSWRVKH GQLENRP 947
    Length:947
    Mass (Da):104,042
    Last modified:April 4, 2006 - v2
    Checksum:iC9D10F67FF7F48AC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251A → P in CAA71306. (PubMed:9020361)Curated
    Sequence conflicti348 – 3481G → S in CAA71306. (PubMed:9020361)Curated
    Sequence conflicti880 – 8801R → G in BAF82892. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti140 – 1401S → N.1 Publication
    Corresponds to variant rs11574819 [ dbSNP | Ensembl ].
    VAR_040711
    Natural varianti255 – 2551T → M.
    Corresponds to variant rs11574820 [ dbSNP | Ensembl ].
    VAR_051641
    Natural varianti514 – 5141G → K in a lung neuroendocrine carcinoma sample; somatic mutation; requires 2 nucleotide substitutions. 1 Publication
    VAR_040712
    Natural varianti674 – 6741H → Y.
    Corresponds to variant rs11867907 [ dbSNP | Ensembl ].
    VAR_051642
    Natural varianti764 – 7641T → A.1 Publication
    Corresponds to variant rs56302559 [ dbSNP | Ensembl ].
    VAR_040713
    Natural varianti852 – 8521T → I in an ovarian mucinous carcinoma sample; somatic mutation. 1 Publication
    VAR_040714
    Natural varianti928 – 9281P → H.1 Publication
    Corresponds to variant rs56036201 [ dbSNP | Ensembl ].
    VAR_040715

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y10256 mRNA. Translation: CAA71306.1.
    AK290203 mRNA. Translation: BAF82892.1.
    DQ314874 Genomic DNA. Translation: ABC40733.1.
    CH471178 Genomic DNA. Translation: EAW51529.1.
    CH471178 Genomic DNA. Translation: EAW51530.1.
    BC035576 mRNA. Translation: AAH35576.1.
    RefSeqiNP_003945.2. NM_003954.4.
    UniGeneiHs.404183.
    Hs.735695.

    Genome annotation databases

    GeneIDi9020.
    KEGGihsa:9020.
    UCSCiuc002iiv.1. human.

    Polymorphism databases

    DMDMi92090612.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y10256 mRNA. Translation: CAA71306.1 .
    AK290203 mRNA. Translation: BAF82892.1 .
    DQ314874 Genomic DNA. Translation: ABC40733.1 .
    CH471178 Genomic DNA. Translation: EAW51529.1 .
    CH471178 Genomic DNA. Translation: EAW51530.1 .
    BC035576 mRNA. Translation: AAH35576.1 .
    RefSeqi NP_003945.2. NM_003954.4.
    UniGenei Hs.404183.
    Hs.735695.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4DN5 X-ray 2.50 A/B 330-680 [» ]
    4G3D X-ray 2.90 A/B/D/E 308-673 [» ]
    4IDT X-ray 2.40 A/B 330-680 [» ]
    4IDV X-ray 2.90 A/B/C/D 330-680 [» ]
    ProteinModelPortali Q99558.
    SMRi Q99558. Positions 333-675.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114487. 32 interactions.
    DIPi DIP-27522N.
    IntActi Q99558. 28 interactions.
    MINTi MINT-88636.
    STRINGi 9606.ENSP00000342059.

    Chemistry

    BindingDBi Q99558.
    ChEMBLi CHEMBL5888.
    GuidetoPHARMACOLOGYi 2074.

    PTM databases

    PhosphoSitei Q99558.

    Polymorphism databases

    DMDMi 92090612.

    Proteomic databases

    PaxDbi Q99558.
    PRIDEi Q99558.

    Protocols and materials databases

    DNASUi 9020.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 9020.
    KEGGi hsa:9020.
    UCSCi uc002iiv.1. human.

    Organism-specific databases

    CTDi 9020.
    GeneCardsi GC17M043466.
    HGNCi HGNC:6853. MAP3K14.
    MIMi 604655. gene.
    neXtProti NX_Q99558.
    PharmGKBi PA30597.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000113436.
    HOVERGENi HBG052384.
    InParanoidi Q99558.
    KOi K04466.
    PhylomeDBi Q99558.

    Enzyme and pathway databases

    Reactomei REACT_19358. CD28 dependent PI3K/Akt signaling.
    SignaLinki Q99558.

    Miscellaneous databases

    ChiTaRSi MAP3K14. human.
    GeneWikii MAP3K14.
    GenomeRNAii 9020.
    NextBioi 33793.
    PROi Q99558.
    SOURCEi Search...

    Gene expression databases

    CleanExi HS_MAP3K14.
    Genevestigatori Q99558.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR017425. MAPKKK14.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038175. MAPKKK14. 1 hit.
    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. "MAP3K-related kinase involved in NF-kappaB induction by TNF, CD95 and IL-1."
      Malinin N.L., Boldin M.P., Kovalenko A.V., Wallach D.
      Nature 385:540-544(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF 429-LYS-LYS-430, TISSUE SPECIFICITY.
    2. "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].
      Tissue: Thalamus.
    3. NHLBI resequencing and genotyping service (RS&G)
      Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
      Tissue: Lymph.
    6. "Pellino3, a novel member of the Pellino protein family, promotes activation of c-Jun and Elk-1 and may act as a scaffolding protein."
      Jensen L.E., Whitehead A.S.
      J. Immunol. 171:1500-1506(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PELI3.
    7. "NIK is a component of the EGF/heregulin receptor signaling complexes."
      Chen D., Xu L.G., Chen L., Li L., Zhai Z., Shu H.B.
      Oncogene 22:4348-4355(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GRB10.
    8. "Regulation of the NF-kappaB-inducing kinase by tumor necrosis factor receptor-associated factor 3-induced degradation."
      Liao G., Zhang M., Harhaj E.W., Sun S.C.
      J. Biol. Chem. 279:26243-26250(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, UBIQUITINATION, INTERACTION WITH TRAF3.
    9. "beta-Arrestin inhibits NF-kappaB activity by means of its interaction with the NF-kappaB inhibitor IkappaBalpha."
      Witherow D.S., Garrison T.R., Miller W.E., Lefkowitz R.J.
      Proc. Natl. Acad. Sci. U.S.A. 101:8603-8607(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARRB1 AND ARRB2.
    10. "NIBP, a novel NIK and IKK(beta)-binding protein that enhances NF-(kappa)B activation."
      Hu W.-H., Pendergast J.S., Mo X.-M., Brambilla R., Bracchi-Ricard V., Li F., Walters W.M., Blits B., He L., Schaal S.M., Bethea J.R.
      J. Biol. Chem. 280:29233-29241(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NIBP.
    11. "Negative feedback in noncanonical NF-kappaB signaling modulates NIK stability through IKKalpha-mediated phosphorylation."
      Razani B., Zarnegar B., Ytterberg A.J., Shiba T., Dempsey P.W., Ware C.F., Loo J.A., Cheng G.
      Sci. Signal. 3:RA41-RA41(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CHUK/IKKA.
    12. "Structure of the nuclear factor kappaB-inducing kinase (NIK) kinase domain reveals a constitutively active conformation."
      Liu J., Sudom A., Min X., Cao Z., Gao X., Ayres M., Lee F., Cao P., Johnstone S., Plotnikova O., Walker N., Chen G., Wang Z.
      J. Biol. Chem. 287:27326-27334(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 330-680.
    13. "The crystal structure of the catalytic domain of the NF-kappaB inducing kinase reveals a narrow but flexible active site."
      de Leon-Boenig G., Bowman K.K., Feng J.A., Crawford T., Everett C., Franke Y., Oh A., Stanley M., Staben S.T., Starovasnik M.A., Wallweber H.J., Wu J., Wu L.C., Johnson A.R., Hymowitz S.G.
      Structure 20:1704-1714(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 308-673.
    14. "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] ASN-140; LYS-514; ALA-764; ILE-852 AND HIS-928.
    15. "An atypical E3 ligase zinc finger protein 91 stabilizes and activates NF-kappaB-inducing kinase via Lys63-linked ubiquitination."
      Jin X., Jin H.R., Jung H.S., Lee S.J., Lee J.H., Lee J.J.
      J. Biol. Chem. 285:30539-30547(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-559, UBIQUITINATION, INTERACTION WITH ZFP91, MUTAGENESIS OF 429-LYS-LYS-430 AND THR-559.

    Entry informationi

    Entry nameiM3K14_HUMAN
    AccessioniPrimary (citable) accession number: Q99558
    Secondary accession number(s): A8K2D8, D3DX67, Q8IYN1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: April 4, 2006
    Last modified: October 1, 2014
    This is version 146 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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