IKBB_MOUSE
ID IKBB_MOUSE Reviewed; 359 AA.
AC Q60778; Q564F1; Q9D6L5;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 175.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=B-cell;
RX PubMed=7867065; DOI=10.1016/0092-8674(95)90511-1;
RA Thompson J.E., Phillips R.J., Erdjument-Bromage H., Tempst P., Ghosh S.;
RT "IkappaB-beta regulates the persistent response in a biphasic activation of
RT NF-kappaB.";
RL Cell 80:573-582(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Hypothalamus, Spleen, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP CHARACTERIZATION, AND INTERACTION WITH RELA AND REL.
RX PubMed=8816457; DOI=10.1128/mcb.16.10.5444;
RA Suyang H., Phillips R.J., Douglas I., Ghosh S.;
RT "Role of unphosphorylated, newly synthesized IkappaB beta in persistent
RT activation of NF-kappaB.";
RL Mol. Cell. Biol. 16:5444-5449(1996).
RN [5]
RP KAPPA B RAS-BINDING.
RX PubMed=10657303; DOI=10.1126/science.287.5454.869;
RA Fenwick C., Na S.-Y., Voll R.E., Zhong H., Im S.-Y., Lee J.W., Ghosh S.;
RT "A subclass of Ras proteins that regulate the degradation of IkappaB.";
RL Science 287:869-873(2000).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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) (By
CC similarity). Interacts with RELA and REL (PubMed:8816457). Interacts
CC with COMMD1 (By similarity). Interacts with inhibitor kappa B-
CC interacting Ras-like NKIRAS1 and NKIRAS2 (PubMed:10657303).
CC {ECO:0000250|UniProtKB:Q15653, ECO:0000269|PubMed:10657303,
CC ECO:0000269|PubMed:8816457}.
CC -!- INTERACTION:
CC Q60778; Q9Z1K6: Arih2; NbExp=2; IntAct=EBI-644469, EBI-6861719;
CC Q60778; P15307: Rel; NbExp=5; IntAct=EBI-644469, EBI-5323778;
CC Q60778; Q04207: Rela; NbExp=12; IntAct=EBI-644469, EBI-644400;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis followed by spleen.
CC -!- PTM: Phosphorylated by RPS6KA1; followed by degradation. Interaction
CC with NKIRAS1 and NKIRAS2 probably prevents phosphorylation.
CC -!- SIMILARITY: Belongs to the NF-kappa-B inhibitor family. {ECO:0000305}.
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DR EMBL; U19799; AAC52166.1; -; mRNA.
DR EMBL; AK010218; BAB26774.1; -; mRNA.
DR EMBL; AK038631; BAC30071.1; -; mRNA.
DR EMBL; AK156731; BAE33825.1; -; mRNA.
DR EMBL; CH466593; EDL24117.1; -; Genomic_DNA.
DR EMBL; CH466593; EDL24118.1; -; Genomic_DNA.
DR CCDS; CCDS21054.1; -.
DR RefSeq; NP_001293151.1; NM_001306222.1.
DR RefSeq; NP_035038.2; NM_010908.5.
DR PDB; 1K3Z; X-ray; 2.50 A; D=50-331.
DR PDB; 1OY3; X-ray; 2.05 A; D=50-331.
DR PDBsum; 1K3Z; -.
DR PDBsum; 1OY3; -.
DR AlphaFoldDB; Q60778; -.
DR SMR; Q60778; -.
DR BioGRID; 201754; 3.
DR DIP; DIP-37418N; -.
DR IntAct; Q60778; 3.
DR MINT; Q60778; -.
DR STRING; 10090.ENSMUSP00000032815; -.
DR iPTMnet; Q60778; -.
DR PhosphoSitePlus; Q60778; -.
DR EPD; Q60778; -.
DR jPOST; Q60778; -.
DR MaxQB; Q60778; -.
DR PaxDb; Q60778; -.
DR PeptideAtlas; Q60778; -.
DR PRIDE; Q60778; -.
DR ProteomicsDB; 269547; -.
DR Antibodypedia; 4179; 808 antibodies from 45 providers.
DR DNASU; 18036; -.
DR Ensembl; ENSMUST00000032815; ENSMUSP00000032815; ENSMUSG00000030595.
DR Ensembl; ENSMUST00000085851; ENSMUSP00000083012; ENSMUSG00000030595.
DR GeneID; 18036; -.
DR KEGG; mmu:18036; -.
DR UCSC; uc009fzr.1; mouse.
DR CTD; 4793; -.
DR MGI; MGI:104752; Nfkbib.
DR VEuPathDB; HostDB:ENSMUSG00000030595; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000161595; -.
DR HOGENOM; CLU_000134_6_0_1; -.
DR InParanoid; Q60778; -.
DR OMA; AEADEWC; -.
DR OrthoDB; 1341288at2759; -.
DR PhylomeDB; Q60778; -.
DR TreeFam; TF320166; -.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-MMU-1810476; RIP-mediated NFkB activation via ZBP1.
DR Reactome; R-MMU-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-MMU-933542; TRAF6 mediated NF-kB activation.
DR BioGRID-ORCS; 18036; 6 hits in 72 CRISPR screens.
DR EvolutionaryTrace; Q60778; -.
DR PRO; PR:Q60778; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q60778; protein.
DR Bgee; ENSMUSG00000030595; Expressed in seminiferous tubule of testis and 243 other tissues.
DR ExpressionAtlas; Q60778; baseline and differential.
DR Genevisible; Q60778; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
DR GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IGI:MGI.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IGI:MGI.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
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 3D-structure; ANK repeat; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..359
FT /note="NF-kappa-B inhibitor beta"
FT /id="PRO_0000067005"
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..194
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 MOD_RES 19
FT /note="Phosphoserine; by RPS6KA1"
FT /evidence="ECO:0000250|UniProtKB:Q15653"
FT MOD_RES 23
FT /note="Phosphoserine; by RPS6KA1"
FT /evidence="ECO:0000250|UniProtKB:Q15653"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15653"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15653"
FT CONFLICT 84
FT /note="T -> H (in Ref. 1; AAC52166)"
FT /evidence="ECO:0000305"
FT HELIX 61..67
FT /evidence="ECO:0007829|PDB:1OY3"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:1OY3"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:1OY3"
FT HELIX 97..104
FT /evidence="ECO:0007829|PDB:1OY3"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:1OY3"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:1OY3"
FT TURN 135..138
FT /evidence="ECO:0007829|PDB:1OY3"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:1OY3"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:1OY3"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:1OY3"
FT HELIX 210..216
FT /evidence="ECO:0007829|PDB:1OY3"
FT HELIX 220..229
FT /evidence="ECO:0007829|PDB:1OY3"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:1OY3"
FT HELIX 244..250
FT /evidence="ECO:0007829|PDB:1OY3"
FT HELIX 254..262
FT /evidence="ECO:0007829|PDB:1OY3"
FT HELIX 277..282
FT /evidence="ECO:0007829|PDB:1OY3"
FT HELIX 287..295
FT /evidence="ECO:0007829|PDB:1OY3"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:1K3Z"
SQ SEQUENCE 359 AA; 37965 MW; 0E2B46C89E2404EF CRC64;
MAGVACLGKT ADADEWCDSG LGSLGPDAAA PGGPGLGAEL GPELSWAPLV FGYVTEDGDT
ALHLAVIHQH EPFLDFLLGF SAGTEYLDLQ NDLGQTALHL AAILGEASTV EKLYAAGAGV
LVAERGGHTA LHLACRVRAH TCACVLLQPR PSHPRDASDT YLTQSQDCTP DTSHAPAAVD
SQPNPENEEE PRDEDWRLQL EAENYDGHTP LHVAVIHKDA EMVRLLRDAG ADLNKPEPTC
GRTPLHLAVE AQAASVLELL LKAGADPTAR MYGGRTPLGS ALLRPNPILA RLLRAHGAPE
PEDEDDKLSP CSSSGSDSDS DNRDEGDEYD DIVVHSGRSQ NRQPPSPASK PLPDDPNPA
