IKBB_RAT
ID IKBB_RAT Reviewed; 359 AA.
AC Q9JIA3;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=NF-kappa-B inhibitor beta;
DE Short=NF-kappa-BIB;
DE AltName: Full=I-kappa-B-beta;
DE Short=IkB-B;
DE Short=IkB-beta;
DE Short=IkappaBbeta;
GN Name=Nfkbib; Synonyms=Ikbb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX PubMed=10827092; DOI=10.1074/jbc.m910284199;
RA Stasiolek M., Gavrilyuk V., Sharp A., Horvath P., Selmaj K.,
RA Feinstein D.L.;
RT "Inhibitory and stimulatory effects of lactacystin on expression of nitric
RT oxide synthase type 2 in brain glial cells: the role of I kappa B-beta.";
RL J. Biol. Chem. 275:24847-24856(2000).
RN [2]
RP PHOSPHORYLATION AT SER-19 AND SER-23.
RX PubMed=16822942; DOI=10.1152/ajpcell.00552.2005;
RA Xu S., Bayat H., Hou X., Jiang B.;
RT "Ribosomal S6 kinase-1 modulates interleukin-1beta-induced persistent
RT activation of NF-kappaB through phosphorylation of IkappaBbeta.";
RL Am. J. Physiol. 291:C1336-C1345(2006).
CC -!- FUNCTION: Inhibits NF-kappa-B by complexing with and trapping it in the
CC cytoplasm. However, the unphosphorylated form resynthesized after cell
CC stimulation is able to bind NF-kappa-B allowing its transport to the
CC nucleus and protecting it to further NFKBIA-dependent inactivation.
CC Association with inhibitor kappa B-interacting NKIRAS1 and NKIRAS2
CC prevent its phosphorylation rendering it more resistant to degradation,
CC explaining its slower degradation.
CC -!- SUBUNIT: Interacts with THRB (via ligand-binding domain). Interacts
CC with RELA and REL. Interacts with COMMD1. Interacts with inhibitor
CC kappa B-interacting Ras-like NKIRAS1 and NKIRAS2.
CC {ECO:0000250|UniProtKB:Q15653}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- PTM: Phosphorylated by RPS6KA1; followed by degradation. Interaction
CC with NKIRAS1 and NKIRAS2 probably prevents phosphorylation (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NF-kappa-B inhibitor family. {ECO:0000305}.
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DR EMBL; AF246634; AAF64191.1; -; mRNA.
DR AlphaFoldDB; Q9JIA3; -.
DR SMR; Q9JIA3; -.
DR STRING; 10116.ENSRNOP00000027212; -.
DR iPTMnet; Q9JIA3; -.
DR PhosphoSitePlus; Q9JIA3; -.
DR PaxDb; Q9JIA3; -.
DR UCSC; RGD:621887; rat.
DR RGD; 621887; Nfkbib.
DR eggNOG; KOG0504; Eukaryota.
DR InParanoid; Q9JIA3; -.
DR PhylomeDB; Q9JIA3; -.
DR Reactome; R-RNO-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-RNO-1810476; RIP-mediated NFkB activation via ZBP1.
DR Reactome; R-RNO-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-RNO-933542; TRAF6 mediated NF-kB activation.
DR PRO; PR:Q9JIA3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0033256; C:I-kappaB/NF-kappaB complex; IC:RGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051059; F:NF-kappaB binding; IC:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; IMP:RGD.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IDA:RGD.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 1: Evidence at protein level;
KW ANK repeat; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..359
FT /note="NF-kappa-B inhibitor beta"
FT /id="PRO_0000067006"
FT REPEAT 57..86
FT /note="ANK 1"
FT REPEAT 93..122
FT /note="ANK 2"
FT REPEAT 126..155
FT /note="ANK 3"
FT REPEAT 206..235
FT /note="ANK 4"
FT REPEAT 240..269
FT /note="ANK 5"
FT REPEAT 273..302
FT /note="ANK 6"
FT REGION 153..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..359
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 19
FT /note="Phosphoserine; by RPS6KA1"
FT /evidence="ECO:0000269|PubMed:16822942"
FT MOD_RES 23
FT /note="Phosphoserine; by RPS6KA1"
FT /evidence="ECO:0000269|PubMed:16822942"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15653"
SQ SEQUENCE 359 AA; 38081 MW; B8602C815C72B1AB CRC64;
MAGVACLGKT ADADEWCDSG LGSLGPDAAA PGGPGLVAEL SPELSWAPLV FGYVTEDGDT
ALHLAVIHQH EPFLDFLLGF SAGTEYLDLQ NDLGQTALHL AAILGEASTV EKLYAAGAGV
LVTERGGHTA LHLACRVRAH TCAYVLLQPR PSHPRDASDT YLTQSQDHTP DTSHAPVATD
PQPNPGNEEE LRDEDWRLQL EAENYDGHTP LHVAVIHKDA EMVQLLRDAG ADLNKPEPTC
GRTPLHLAVE GQAAGVLALL LKAGADPTAR MYGGRTPLGS ALLRPNPVLA RLLRAHGAPE
PEDKDDKLSP CSNSSSDSDS DNRDEGDEYD DIVVHSRRSQ NQPPPSPAAK PLPDDPNPA
