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Q60680

- IKKA_MOUSE

UniProt

Q60680 - IKKA_MOUSE

Protein

Inhibitor of nuclear factor kappa-B kinase subunit alpha

Gene

Chuk

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. Negatively regulates the pathway by phosphorylating the scaffold protein TAXBP1 and thus promoting the assembly of the A20/TNFAIP3 ubiquitin-editing complex (composed of A20/TNFAIP3, TAX1BP1, and the E3 ligases ITCH and RNF11). Therefore, CHUK plays a key role in the negative feedback of NF-kappa-B canonical signaling to limit inflammatory gene activation. As part of the non-canonical pathway of NF-kappa-B activation, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. In turn, these complexes regulate genes encoding molecules involved in B-cell survival and lymphoid organogenesis. Participates also in the negative feedback of the non-canonical NF-kappa-B signaling pathway by phosphorylating and destabilizing MAP3K14/NIK. Within the nucleus, phosphorylates CREBBP and consequently increases both its transcriptional and histone acetyltransferase activities. Modulates chromatin accessibility at NF-kappa-B-responsive promoters by phosphorylating histones H3 at 'Ser-10' that are subsequently acetylated at 'Lys-14' by CREBBP. Additionally, phosphorylates the CREBBP-interacting protein NCOA3.1 Publication

    Catalytic activityi

    ATP + [I-kappa-B protein] = ADP + [I-kappa-B phosphoprotein].

    Enzyme regulationi

    Activated when phosphorylated and inactivated when dephosphorylated.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei44 – 441ATPPROSITE-ProRule annotation
    Active sitei144 – 1441Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi21 – 299ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. IkappaB kinase activity Source: UniProtKB-EC
    3. protein binding Source: IntAct
    4. protein heterodimerization activity Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB
    6. protein kinase activity Source: UniProtKB
    7. receptor signaling protein serine/threonine kinase activity Source: MGI
    8. scaffold protein binding Source: MGI

    GO - Biological processi

    1. cellular response to tumor necrosis factor Source: UniProtKB
    2. I-kappaB phosphorylation Source: MGI
    3. lactation Source: MGI
    4. mammary gland alveolus development Source: MGI
    5. mammary gland epithelial cell proliferation Source: MGI
    6. morphogenesis of an epithelial sheet Source: MGI
    7. odontogenesis of dentin-containing tooth Source: MGI
    8. osteoclast differentiation Source: MGI
    9. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
    10. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    11. signal transduction by phosphorylation Source: GOC

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.10. 3474.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inhibitor of nuclear factor kappa-B kinase subunit alpha (EC:2.7.11.10)
    Short name:
    I-kappa-B kinase alpha
    Short name:
    IKK-A
    Short name:
    IKK-alpha
    Short name:
    IkBKA
    Short name:
    IkappaB kinase
    Alternative name(s):
    Conserved helix-loop-helix ubiquitous kinase
    I-kappa-B kinase 1
    Short name:
    IKK1
    Nuclear factor NF-kappa-B inhibitor kinase alpha
    Short name:
    NFKBIKA
    Gene namesi
    Name:Chuk
    Synonyms:Ikka
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:99484. Chuk.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Shuttles between the cytoplasm and the nucleus.

    GO - Cellular componenti

    1. CD40 receptor complex Source: BHF-UCL
    2. cytoplasm Source: MGI
    3. cytoplasmic side of plasma membrane Source: BHF-UCL
    4. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Mice show abnormal appearance and die within 4 hours after birth. The epidermal cells are highly proliferative with dysregulated epidermal differentiation.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 745745Inhibitor of nuclear factor kappa-B kinase subunit alphaPRO_0000086012Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei23 – 231Phosphothreonine; by PKB/AKT1 and SGK1By similarity
    Modified residuei176 – 1761Phosphoserine; by MAP3K14By similarity
    Modified residuei180 – 1801Phosphoserine; by SGK1By similarity

    Post-translational modificationi

    Phosphorylated by MAP3K14/NIK, AKT and to a lesser extent by MEKK1, and dephosphorylated by PP2A. Autophosphorylated.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ60680.
    PaxDbiQ60680.
    PRIDEiQ60680.

    PTM databases

    PhosphoSiteiQ60680.

    Expressioni

    Tissue specificityi

    Ubiquitous only for isoform 1, isoforms 2 and 3 are expressed predominantly in brain and T-lymphocytes.

    Developmental stagei

    Maximally expressed at E7 day followed by E11, E15 and E17 days. In the limb development, its expression predominates in the limb buds at E12.5 day.

    Gene expression databases

    CleanExiMM_CHUK.
    GenevestigatoriQ60680.

    Interactioni

    Subunit structurei

    Component of the I-kappa-B-kinase (IKK) core complex consisting of CHUK, IKBKB and IKBKG; probably four alpha/CHUK-beta/IKBKB dimers are associated with four gamma/IKBKG subunits. The IKK core complex seems to associate with regulatory or adapter proteins to form a IKK-signalosome holo-complex. The IKK complex associates with TERF2IP/RAP1, leading to promote IKK-mediated phosphorylation of RELA/p65. Part of a complex composed of NCOA2, NCOA3, CHUK/IKKA, IKBKB, IKBKG and CREBBP. Part of a 70-90 kDa complex at least consisting of CHUK/IKKA, IKBKB, NFKBIA, RELA, IKBKAP and MAP3K14. Directly interacts with IKK-gamma/NEMO and TRPC4AP. May interact with TRAF2. Interacts with NALP2. May interact with MAVS/IPS1. Interacts with ARRB1 By similarity. Interacts with NLRC5; prevents CHUK phosphorylation and kinase activity By similarity. Interacts with PIAS1; this interaction induces PIAS1 phosphorylation By similarity. Interacts with ZNF268; the interaction is further increased in a TNF-alpha-dependent manner By similarity. Interacts with ARRB2.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Fam92a1Q8BP224EBI-646260,EBI-646638
    IkbkbO883514EBI-646245,EBI-447960
    IkbkgO885224EBI-646245,EBI-998011
    Irf7P704343EBI-646245,EBI-997907
    Krt10P025356EBI-646260,EBI-646288
    MAP3K14Q995583EBI-646264,EBI-358011From a different organism.
    NFKBIAP259632EBI-646264,EBI-307386From a different organism.
    PQ77M193EBI-646245,EBI-6149376From a different organism.
    P/V/CP048622EBI-646245,EBI-8848010From a different organism.
    P/V/CP061642EBI-646245,EBI-8848117From a different organism.
    P/V/CP0C1C72EBI-646245,EBI-6151115From a different organism.
    P/V/CP359772EBI-646245,EBI-8848155From a different organism.
    Pde4dipB7ZNY04EBI-646260,EBI-659248

    Protein-protein interaction databases

    DIPiDIP-29719N.
    IntActiQ60680. 30 interactions.
    MINTiMINT-267529.

    Structurei

    3D structure databases

    ProteinModelPortaliQ60680.
    SMRiQ60680. Positions 5-659.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini15 – 300286Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni455 – 47622Leucine-zipperAdd
    BLAST
    Regioni738 – 7436NEMO-binding

    Domaini

    The kinase domain is located in the N-terminal region. The leucine zipper is important to allow homo- and hetero-dimerization. At the C-terminal region is located the region responsible for the interaction with NEMO/IKBKG.

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. I-kappa-B kinase subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000038048.
    HOVERGENiHBG018241.
    InParanoidiQ60680.
    KOiK04467.
    PhylomeDBiQ60680.

    Family and domain databases

    InterProiIPR022007. IKKbetaNEMObind.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF12179. IKKbetaNEMObind. 1 hit.
    PF00069. Pkinase. 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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q60680-1) [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

    MERPPGLRPG AGGPWEMRER LGTGGFGNVS LYQHRELDLK IAIKSCRLEL    50
    SSKNRERWCH EIQIMKKLDH ANVVKACDVP EELNFLINDV PLLAMEYCSG 100
    GDLRKLLNKP ENCCGLKESQ ILSLLSDIGS GIRYLHENKI IHRDLKPENI 150
    VLQDVGGKTI HKIIDLGYAK DVDQGSLCTS FVGTLQYLAP ELFENKPYTA 200
    TVDYWSFGTM VFECIAGYRP FLHHLQPFTW HEKIKKKDPK CIFACEEMTG 250
    EVRFSSHLPQ PNSLCSLIVE PMESWLQLML NWDPQQRGGP IDLTLKQPRC 300
    FALMDHILNL KIVHILNMTS AKIISFLLPC DESLHSLQSR IERETGINTG 350
    SQELLSETGI SLDPRKPASQ CVLDGVRGCD SYMVYLFDKS KTVYEGPFAS 400
    RSLSDCVNYI VQDSKIQLPI IQLRKVWAEA VHYVSGLKED YSRLFQGQRA 450
    AMLSLLRYNA NLTKMKNTLI SASQQLKAKL EFFRKSIQLD LERYSEQMTY 500
    GISSEKMLKA WKEMEEKAIH YSEVGVIGYL EDQIMSLHTE IMELQKSPYG 550
    RRQGDLMESL EQRAIDLYKQ LKHRPPDHLY SDSTEMVKII VHTVQSQDRV 600
    LKELFGHLSK LLGCKQKIID LLPKVEVALS NIKEADNTVM FMQGKRQKEI 650
    WHLLKIACTQ SSARSLVGSS LEGTVTPPVS AWLPPTLADR EHPLTCVVTP 700
    QDGETLAQMI EENLNCLGHL STIIREANED QSSSLMSLDW SWLAE 745
    Length:745
    Mass (Da):84,729
    Last modified:November 1, 1996 - v1
    Checksum:i3FEF5582AFF92233
    GO
    Isoform 2 (identifier: Q60680-2) [UniParc]FASTAAdd to Basket

    Also known as: Delta LH

    The sequence of this isoform differs from the canonical sequence as follows:
         452-471: MLSLLRYNANLTKMKNTLIS → IFRKNVKSMERNGRKGHSLF
         472-745: Missing.

    Show »
    Length:471
    Mass (Da):53,544
    Checksum:i14F1EFF71B4A17EE
    GO
    Isoform 3 (identifier: Q60680-3) [UniParc]FASTAAdd to Basket

    Also known as: Delta H

    The sequence of this isoform differs from the canonical sequence as follows:
         577-584: DHLYSDST → GKTLQSQY
         585-745: Missing.

    Show »
    Length:584
    Mass (Da):66,805
    Checksum:iD99BB8A6DF1CA4EB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti236 – 2361K → E in BAB31335. (PubMed:16141072)Curated
    Sequence conflicti400 – 4001S → Y in BAB31335. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei452 – 47120MLSLL…NTLIS → IFRKNVKSMERNGRKGHSLF in isoform 2. CuratedVSP_004866Add
    BLAST
    Alternative sequencei472 – 745274Missing in isoform 2. CuratedVSP_004867Add
    BLAST
    Alternative sequencei577 – 5848DHLYSDST → GKTLQSQY in isoform 3. 2 PublicationsVSP_004868
    Alternative sequencei585 – 745161Missing in isoform 3. 2 PublicationsVSP_004869Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U12473 mRNA. Translation: AAC52589.1.
    AK018671 mRNA. Translation: BAB31335.1.
    BC018243 mRNA. Translation: AAH18243.1.
    CCDSiCCDS29843.1. [Q60680-1]
    PIRiI49101.
    RefSeqiXP_006526686.1. XM_006526623.1. [Q60680-2]
    UniGeneiMm.3996.

    Genome annotation databases

    GeneIDi12675.
    KEGGimmu:12675.
    UCSCiuc008hpi.2. mouse. [Q60680-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U12473 mRNA. Translation: AAC52589.1 .
    AK018671 mRNA. Translation: BAB31335.1 .
    BC018243 mRNA. Translation: AAH18243.1 .
    CCDSi CCDS29843.1. [Q60680-1 ]
    PIRi I49101.
    RefSeqi XP_006526686.1. XM_006526623.1. [Q60680-2 ]
    UniGenei Mm.3996.

    3D structure databases

    ProteinModelPortali Q60680.
    SMRi Q60680. Positions 5-659.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-29719N.
    IntActi Q60680. 30 interactions.
    MINTi MINT-267529.

    Chemistry

    ChEMBLi CHEMBL5380.

    PTM databases

    PhosphoSitei Q60680.

    Proteomic databases

    MaxQBi Q60680.
    PaxDbi Q60680.
    PRIDEi Q60680.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 12675.
    KEGGi mmu:12675.
    UCSCi uc008hpi.2. mouse. [Q60680-3 ]

    Organism-specific databases

    CTDi 1147.
    MGIi MGI:99484. Chuk.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000038048.
    HOVERGENi HBG018241.
    InParanoidi Q60680.
    KOi K04467.
    PhylomeDBi Q60680.

    Enzyme and pathway databases

    BRENDAi 2.7.11.10. 3474.

    Miscellaneous databases

    PROi Q60680.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_CHUK.
    Genevestigatori Q60680.

    Family and domain databases

    InterProi IPR022007. IKKbetaNEMObind.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF12179. IKKbetaNEMObind. 1 hit.
    PF00069. Pkinase. 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. "CHUK, a conserved helix-loop-helix ubiquitous kinase, maps to human chromosome 10 and mouse chromosome 19."
      Mock B.A., Connelly M.A., McBride O.W., Kozak C.A., Marcu K.B.
      Genomics 27:348-351(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: BALB/c.
    2. "CHUK, a new member of the helix-loop-helix and leucine zipper families of interacting proteins, contains a serine-threonine kinase catalytic domain."
      Connelly M.A., Marcu K.B.
      Cell. Mol. Biol. Res. 41:537-549(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: BALB/c.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Strain: C57BL/6J.
      Tissue: Colon.
    4. "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 3).
      Tissue: Eye.
    5. Cited for: DISRUPTION PHENOTYPE.
    6. "Functional isoforms of IkappaB kinase alpha (IKKalpha) lacking leucine zipper and helix-loop-helix domains reveal that IKKalpha and IKKbeta have different activation requirements."
      McKenzie F.R., Connelly M.A., Balzarano D., Mueller J.R., Geleziunas R., Marcu K.B.
      Mol. Cell. Biol. 20:2635-2649(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING.
    7. "Differential regulation of IkappaB kinase alpha and beta by two upstream kinases, NF-kappaB-inducing kinase and mitogen-activated protein kinase/ERK kinase kinase-1."
      Nakano H., Shindo M., Sakon S., Nishinaka S., Mihara M., Yagita H., Okumura K.
      Proc. Natl. Acad. Sci. U.S.A. 95:3537-3542(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY MAP3K14/NIK.
    8. "Positive and negative regulation of IkappaB kinase activity through IKKbeta subunit phosphorylation."
      Delhase M., Hayakawa M., Chen Y., Karin M.
      Science 284:309-313(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IKKA-IKKB BINDING.
    9. "Coordinate regulation of IkappaB kinases by mitogen-activated protein kinase kinase kinase 1 and NF-kappaB-inducing kinase."
      Nemoto S., DiDonato J.A., Lin A.
      Mol. Cell. Biol. 18:7336-7343(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IKK PHOSPHORYLATION.
    10. "The I kappa B/NF-kappa B system: a key determinant of mucosal inflammation and protection."
      Jobin C., Sartor R.B.
      Am. J. Physiol. 278:C451-C462(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    11. "Histone H3 phosphorylation by IKK-alpha is critical for cytokine-induced gene expression."
      Yamamoto Y., Verma U.N., Prajapati S., Kwak Y.T., Gaynor R.B.
      Nature 423:655-659(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    12. "Beta2-adrenergic receptor regulates Toll-like receptor-4-induced nuclear factor-kappaB activation through beta-arrestin 2."
      Kizaki T., Izawa T., Sakurai T., Haga S., Taniguchi N., Tajiri H., Watanabe K., Day N.K., Toba K., Ohno H.
      Immunology 124:348-356(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARRB2.
    13. Cited for: INTERACTION WITH TERF2IP.

    Entry informationi

    Entry nameiIKKA_MOUSE
    AccessioniPrimary (citable) accession number: Q60680
    Secondary accession number(s): Q80VU2, Q9D2X3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 147 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3