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Inhibitor of nuclear factor kappa-B kinase subunit alpha (I-kappa-B kinase alpha) (IKK-A) (IKK-alpha) (IkBKA) (EC 2.7.11.10) (I-kappa-B kinase 1) (IKK1) (Nuclear factor NF-kappa-B inhibitor kinase alpha) (NFKBIKA)

 IKKA_BOVIN              Reviewed;         740 AA.
Q95KV1; A7YWD1;
12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
07-NOV-2018, entry version 120.
RecName: Full=Inhibitor of nuclear factor kappa-B kinase subunit alpha;
Short=I-kappa-B kinase alpha;
Short=IKK-A;
Short=IKK-alpha;
Short=IkBKA;
EC=2.7.11.10;
AltName: Full=I-kappa-B kinase 1;
Short=IKK1;
AltName: Full=Nuclear factor NF-kappa-B inhibitor kinase alpha;
Short=NFKBIKA;
Name=CHUK; Synonyms=IKKA;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH IKBKB AND IKBKG.
PubMed=12459277; DOI=10.1016/S0378-1119(02)01011-9;
Rottenberg S., Schmuckli-Maurer J., Grimm S., Heussler V.T.,
Dobbelaere D.A.E.;
"Characterization of the bovine IkappaB kinases (IKK)alpha and
IKKbeta, the regulatory subunit NEMO and their substrate
IkappaBalpha.";
Gene 299:293-300(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Ascending colon;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: 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. Also phosphorylates FOXO3 and
may regulate this pro-apoptotic transcription factor.
{ECO:0000250|UniProtKB:O15111}.
-!- CATALYTIC ACTIVITY: ATP + [I-kappa-B protein] = ADP + [I-kappa-B
phosphoprotein].
-!- ACTIVITY REGULATION: Activated when phosphorylated and inactivated
when dephosphorylated.
-!- SUBUNIT: 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 (PubMed:12459277).
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, ELP1 and MAP3K14. Directly interacts with TRPC4AP.
May interact with TRAF2. Interacts with NALP2. May interact with
MAVS/IPS1. Interacts with ARRB1 and ARRB2. Interacts with NLRC5;
prevents CHUK phosphorylation and kinase activity. Interacts with
PIAS1; this interaction induces PIAS1 phosphorylation. Interacts
with ZNF268 isoform 2; the interaction is further increased in a
TNF-alpha-dependent manner (By similarity). Interacts with IFIT5;
the interaction synergizes the recruitment of IKK to MAP3K7 and
enhances IKK phosphorylation (By similarity). Interacts with
LRRC14 (By similarity). {ECO:0000250|UniProtKB:O15111,
ECO:0000250|UniProtKB:Q60680, ECO:0000269|PubMed:12459277}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between
the cytoplasm and the nucleus. {ECO:0000250}.
-!- DOMAIN: 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 (By similarity).
{ECO:0000250}.
-!- PTM: Phosphorylated by MAP3K14/NIK, AKT and to a lesser extent by
MEKK1, and dephosphorylated by PP2A. Autophosphorylated (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
protein kinase family. I-kappa-B kinase subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AJ414555; CAC93686.1; -; mRNA.
EMBL; BC134510; AAI34511.1; -; mRNA.
RefSeq; NP_776446.1; NM_174021.2.
UniGene; Bt.63925; -.
ProteinModelPortal; Q95KV1; -.
SMR; Q95KV1; -.
BioGrid; 158442; 2.
DIP; DIP-44031N; -.
IntAct; Q95KV1; 2.
STRING; 9913.ENSBTAP00000009985; -.
PaxDb; Q95KV1; -.
PRIDE; Q95KV1; -.
Ensembl; ENSBTAT00000009985; ENSBTAP00000009985; ENSBTAG00000007591.
GeneID; 281073; -.
KEGG; bta:281073; -.
CTD; 1147; -.
VGNC; VGNC:27354; CHUK.
eggNOG; KOG4250; Eukaryota.
eggNOG; ENOG410XRMU; LUCA.
GeneTree; ENSGT00930000150910; -.
HOGENOM; HOG000038048; -.
HOVERGEN; HBG018241; -.
InParanoid; Q95KV1; -.
KO; K04467; -.
OMA; TPQASAW; -.
OrthoDB; EOG091G02VC; -.
TreeFam; TF324269; -.
Reactome; R-BTA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-BTA-168638; NOD1/2 Signaling Pathway.
Reactome; R-BTA-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-BTA-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-BTA-202424; Downstream TCR signaling.
Reactome; R-BTA-2871837; FCERI mediated NF-kB activation.
Reactome; R-BTA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-BTA-5357905; Regulation of TNFR1 signaling.
Reactome; R-BTA-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-BTA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-BTA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-BTA-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-BTA-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
Reactome; R-BTA-9020702; Interleukin-1 signaling.
Reactome; R-BTA-933542; TRAF6 mediated NF-kB activation.
Reactome; R-BTA-937039; IRAK1 recruits IKK complex.
Reactome; R-BTA-937041; IKK complex recruitment mediated by RIP1.
Reactome; R-BTA-975144; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
Proteomes; UP000009136; Chromosome 26.
Bgee; ENSBTAG00000007591; Expressed in 10 organ(s), highest expression level in spleen.
GO; GO:0008385; C:IkappaB kinase complex; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008384; F:IkappaB kinase activity; IEA:UniProtKB-EC.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
GO; GO:0034614; P:cellular response to reactive oxygen species; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
GO; GO:0098586; P:cellular response to virus; IEA:Ensembl.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:0038061; P:NIK/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:1902741; P:positive regulation of interferon-alpha secretion; IEA:Ensembl.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IBA:GO_Central.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IBA:GO_Central.
InterPro; IPR022007; IKKbetaNEMObind.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF12179; IKKbetaNEMObind; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM01239; IKKbetaNEMObind; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 740 Inhibitor of nuclear factor kappa-B
kinase subunit alpha.
/FTId=PRO_0000268159.
DOMAIN 15 302 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 21 29 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 455 476 Leucine-zipper.
REGION 733 738 NEMO-binding. {ECO:0000250}.
ACT_SITE 144 144 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 44 44 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 23 23 Phosphothreonine; by PKB/AKT1.
{ECO:0000250|UniProtKB:O15111}.
MOD_RES 176 176 Phosphoserine; by MAP3K14.
{ECO:0000250|UniProtKB:O15111}.
MOD_RES 180 180 Phosphoserine.
{ECO:0000250|UniProtKB:O15111}.
SEQUENCE 740 AA; 84344 MW; 01903BE11F44D176 CRC64;
MERPPGLRPG AGGPWEMRER LGTGGFGNVC LYQHRELDLK IAIKSCRLEL STKNRERWCH
EIQIMKKLNH ANVVKACDVP EELNFLINDV PLLAMEYCSG GDLRKLLNKP ENCCGLKESQ
ILSLLSDIGS GIRYLHENKI IHRDLKPENI VLQDVGGKIM HKIIDLGYAK DVDQGSLCTS
FVGTLQYLAP ELFENKPYTA TVDYWSFGTM VFECIAGYRP FLHHLQPFTW HEKIKKKDPK
CIFACEEMTG EVRFSSHLPQ PNSLCSLIVE PMENWLQLML NWDPQQRGGP VDLTLKQPRC
FVLMDHILNL KIVHILNMTS AKIISFLLPP DESLHSLQSR IERETGINTG SQELLSEMGI
SLDPRKPASQ CVLDGVRGCD SYMVYLFDKS KTVYEGPFAS RSLSDCVNYI VQDSKIQLPI
IQLRKVWAEA VHYVSGLKED YSRLFQGQRA AMLSLLRYNT NLTKMKNTLI SASQQLKAKL
EFFHKSIQLD LERYSEQMTY GISSEKMLKA WKEMEEKAIH YAEVGVIGYL EDQIMSLHTE
IMELQKSPYG RRQGDLMESL EQRAIDLYKQ LKHRPSDHSY SDSTEMVKII VHTVQSQDRV
LKELFGHLSK LLGCKQKIID LLPKVEMALS NIKEADSTVM FMQGKRQKEI WHLLKIACTQ
SSARSLVGSS LEGVTPQLPP TSAEREHPLS CVVTPQDGET LAQMIEENLN CLGHLSTIIH
EANEKQGNNM MSLDWSWLTE


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