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Inhibitor of nuclear factor kappa-B kinase subunit beta (I-kappa-B-kinase beta) (IKK-B) (IKK-beta) (IkBKB) (EC 2.7.11.10) (I-kappa-B kinase 2) (IKK2) (Nuclear factor NF-kappa-B inhibitor kinase beta) (NFKBIKB)

 IKKB_BOVIN              Reviewed;         756 AA.
Q95KV0;
05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
28-MAR-2018, entry version 131.
RecName: Full=Inhibitor of nuclear factor kappa-B kinase subunit beta;
Short=I-kappa-B-kinase beta;
Short=IKK-B;
Short=IKK-beta;
Short=IkBKB;
EC=2.7.11.10;
AltName: Full=I-kappa-B kinase 2;
Short=IKK2;
AltName: Full=Nuclear factor NF-kappa-B inhibitor kinase beta;
Short=NFKBIKB;
Name=IKBKB;
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].
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].
PubMed=16305752; DOI=10.1186/1471-2164-6-166;
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
-!- 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 2 critical 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. In addition to
the NF-kappa-B inhibitors, phosphorylates several other components
of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits
RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE.
IKK-related kinase phosphorylations may prevent the overproduction
of inflammatory mediators since they exert a negative regulation
on canonical IKKs. Phosphorylates FOXO3, mediating the TNF-
dependent inactivation of this pro-apoptotic transcription factor.
Also phosphorylates other substrates including NCOA3, BCL10 and
IRS1. Within the nucleus, acts as an adapter protein for NFKBIA
degradation in UV-induced NF-kappa-B activation.
{ECO:0000250|UniProtKB:O14920}.
-!- CATALYTIC ACTIVITY: ATP + [I-kappa-B protein] = ADP + [I-kappa-B
phosphoprotein].
-!- 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. 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. Found in a membrane raft complex, at least
composed of BCL10, CARD11, DPP4 and IKBKB. Interacts with SQSTM1
through PRKCZ or PRKCI. Forms an NGF-induced complex with IKBKB,
PRKCI and TRAF6. May interact with MAVS/IPS1. Interacts with
NALP2. Interacts with TICAM1. Interacts with FAF1; the interaction
disrupts the IKK complex formation. Interacts with ATM. Part of a
ternary complex consisting of TANK, IKBKB and IKBKG. Interacts
with NIBP; the interaction is direct. Interacts with ARRB1 and
ARRB2. Interacts with TRIM21. Interacts with NLRC5; prevents IKBKB
phosphorylation and kinase activity. Interacts with PDPK1.
Interacts with EIF2AK2/PKR. The phosphorylated form interacts with
PPM1A and PPM1B. Interacts with ZNF268; the interaction is further
increased in a TNF-alpha-dependent manner. Interacts with IKBKE.
Interacts with NAA10, leading to NAA10 degradation. Interacts with
FOXO3. Interacts with ZC3H12A. Interacts with AKAP13 (By
similarity). Interacts with IFIT5; the interaction synergizes the
recruitment of IKK to MAP3K7 and enhances IKK phosphorylation (By
similarity). Interacts with LRRC14; disrupts IKBKB-IKBKG
interaction preventing I-kappa-B-kinase (IKK) core complex
formation and leading to a decrease of IKBKB phosphorylation and
NF-kappaB activation (By similarity).
{ECO:0000250|UniProtKB:O14920, ECO:0000250|UniProtKB:O88351,
ECO:0000250|UniProtKB:Q9QY78}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O14920}.
Nucleus {ECO:0000250|UniProtKB:O14920}. Membrane raft
{ECO:0000250|UniProtKB:O14920}. Note=Colocalized with DPP4 in
membrane rafts. {ECO:0000250|UniProtKB:O14920}.
-!- 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: Upon cytokine stimulation, phosphorylated on Ser-177 and Ser-
181 by MEKK1 and/or MAP3K14/NIK as well as TBK1 and PRKCZ; which
enhances activity. Once activated, autophosphorylates on the C-
terminal serine cluster; which decreases activity and prevents
prolonged activation of the inflammatory response. Phosphorylated
by the IKK-related kinases TBK1 and IKBKE, which is associated
with reduced CHUK/IKKA and IKBKB activity and NF-kappa-B-dependent
gene transcription. Dephosphorylated at Ser-177 and Ser-181 by
PPM1A and PPM1B. {ECO:0000250|UniProtKB:O14920}.
-!- PTM: Ubiquitinated. Monoubiquitination involves TRIM21 that leads
to inhibition of Tax-induced NF-kappa-B signaling. 'Ser-163' may
not serve as a monoubiquitination site. Ubiquitination on 'Ser-
163' may modulate phosphorylation on C-terminal serine residues.
{ECO:0000250|UniProtKB:O14920}.
-!- PTM: Hydroxylated by PHD1/EGLN2, loss of hydroxylation under
hypoxic conditions results in activation of NF-kappa-B.
{ECO:0000250|UniProtKB:O14920}.
-!- 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; AJ414556; CAC93687.1; -; mRNA.
EMBL; BT021585; AAX46432.1; -; mRNA.
RefSeq; NP_776778.1; NM_174353.2.
UniGene; Bt.9023; -.
ProteinModelPortal; Q95KV0; -.
SMR; Q95KV0; -.
BioGrid; 159165; 2.
STRING; 9913.ENSBTAP00000009995; -.
PaxDb; Q95KV0; -.
PRIDE; Q95KV0; -.
Ensembl; ENSBTAT00000009995; ENSBTAP00000009995; ENSBTAG00000007599.
GeneID; 281854; -.
KEGG; bta:281854; -.
CTD; 3551; -.
eggNOG; KOG4250; Eukaryota.
eggNOG; ENOG410XRMU; LUCA.
GeneTree; ENSGT00910000144033; -.
HOGENOM; HOG000038048; -.
HOVERGEN; HBG018241; -.
InParanoid; Q95KV0; -.
KO; K07209; -.
OMA; RTLDMDL; -.
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-202424; Downstream TCR signaling.
Reactome; R-BTA-209543; p75NTR recruits signalling complexes.
Reactome; R-BTA-209560; NF-kB is activated and signals survival.
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-5607764; CLEC7A (Dectin-1) 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 27.
Bgee; ENSBTAG00000007599; -.
GO; GO:0008385; C:IkappaB kinase complex; IBA:GO_Central.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IEA:Ensembl.
GO; GO:1903347; P:negative regulation of bicellular tight junction assembly; IEA:Ensembl.
GO; GO:0035509; P:negative regulation of myosin-light-chain-phosphatase activity; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
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:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
GO; GO:1903140; P:regulation of establishment of endothelial barrier; IEA:Ensembl.
GO; GO:0042325; P:regulation of phosphorylation; IEA:Ensembl.
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; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR029071; Ubiquitin-like_domsf.
Pfam; PF12179; IKKbetaNEMObind; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM01239; IKKbetaNEMObind; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF54236; SSF54236; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
2: Evidence at transcript level;
ATP-binding; Complete proteome; Cytoplasm; Hydroxylation;
Isopeptide bond; Kinase; Membrane; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; S-nitrosylation;
Serine/threonine-protein kinase; Transferase; Ubl conjugation.
CHAIN 1 756 Inhibitor of nuclear factor kappa-B
kinase subunit beta.
/FTId=PRO_0000248284.
DOMAIN 15 300 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 21 29 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 458 479 Leucine-zipper.
REGION 737 742 NEMO-binding. {ECO:0000250}.
ACT_SITE 145 145 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 44 44 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 177 177 Phosphoserine; by TBK1 and PKC/PRKCZ.
{ECO:0000250|UniProtKB:O14920}.
MOD_RES 179 179 S-nitrosocysteine.
{ECO:0000250|UniProtKB:O14920}.
MOD_RES 181 181 Phosphoserine; by TBK1, PKC/PRKCZ and
PDPK1. {ECO:0000250|UniProtKB:O14920}.
MOD_RES 191 191 Hydroxyproline. {ECO:0000250}.
MOD_RES 670 670 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:O14920}.
MOD_RES 672 672 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:O14920}.
MOD_RES 675 675 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:O14920}.
MOD_RES 682 682 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:O14920}.
MOD_RES 689 689 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:O14920}.
MOD_RES 697 697 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:O14920}.
MOD_RES 705 705 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:O14920}.
MOD_RES 733 733 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:O14920}.
MOD_RES 740 740 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:O14920}.
CROSSLNK 163 163 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:O14920}.
SEQUENCE 756 AA; 86647 MW; A072D15614A176E5 CRC64;
MSWSPSLPTQ TCGAWEMKER LGTGGFGNVI RWHNQETGEQ IAIKQCRQEL SPRNRERWCL
EIQIMRRLNH PNVVAARDVP EGMQSLAPND LPLLAMEYCQ GGDLRKYLNQ FENCCGLREG
AILTLLSDIA SALRYLHENR IIHRDLKPEN IVLQQGEQRL IHKIIDLGYA KELDQGSLCT
SFVGTLQYLA PELLEQQKYT VTVDYWSFGT LAFECITGFR PFLPNWQPVQ WHSKVRQKSE
MDIVVSEDLN GAVKFSSSLP HPNNLNSVLA QRLEKWLQLM LMWHPRQRGT DPVYGPNGCF
KALDDILNLK LLHVLNMVTG TLHTYPVTED ESLQSLKARI RQDTGILEED QELLQEAGLA
LIPDKPAAQC LSDGKLNEGR TLDMDLVFLF DNSRVTYESQ VSPQPQPESV SCILQEPKRN
LPFFQLRKVW GQVWHSIQAL KEDCSRLQQG QRAAMMNLLR NNSCLSKMKN SMASMSQQLK
AKLDFFKTSI QIDLEKYREQ TEFGITSDKL LLAWREMEQA VELCGRENEV KHLVERMMAL
QTDIVDLQRS PMGRKQGGTL DDLEEQAREL YRRLREKPRD QRTDGDSQEM VRLLLQAIQG
FEKKVRVIYT QLSKTVVCKQ KALELLPKVE EVVSLMSEDE KMVVRLQEKR QKELWNLLKI
ACSKVRGPVS GSPDSMNASR LSHPCQLMSQ PCTAPDSLPE AAEKSEDLVA EAHTLCTQLE
NALQDTMKEQ DQSLRSLDWS WLQSEEEEQQ SLERAS


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