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Q60680

- IKKA_MOUSE

UniProt

Q60680 - IKKA_MOUSE

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Protein
Inhibitor of nuclear factor kappa-B kinase subunit alpha
Gene
Chuk, Ikka
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 441ATP By similarity
Active sitei144 – 1441Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi21 – 299ATP By similarity

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. I-kappaB phosphorylation Source: MGI
  2. cellular response to tumor necrosis factor Source: UniProtKB
  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
Complete GO annotation...

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

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
Complete GO annotation...

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 alpha
PRO_0000086012Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231Phosphothreonine; by PKB/AKT1 and SGK1 By similarity
Modified residuei176 – 1761Phosphoserine; by MAP3K14 By similarity
Modified residuei180 – 1801Phosphoserine; by SGK1 By similarity

Post-translational modificationi

Phosphorylated by MAP3K14/NIK, AKT and to a lesser extent by MEKK1, and dephosphorylated by PP2A. Autophosphorylated.2 Publications

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 ARRB2.2 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 300286Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni455 – 47622Leucine-zipper
Add
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

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei452 – 47120MLSLL…NTLIS → IFRKNVKSMERNGRKGHSLF in isoform 2.
VSP_004866Add
BLAST
Alternative sequencei472 – 745274Missing in isoform 2.
VSP_004867Add
BLAST
Alternative sequencei577 – 5848DHLYSDST → GKTLQSQY in isoform 3.
VSP_004868
Alternative sequencei585 – 745161Missing in isoform 3.
VSP_004869Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti236 – 2361K → E in BAB31335. 1 Publication
Sequence conflicti400 – 4001S → Y in BAB31335. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 146 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

Similar proteinsi