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   24-JAN-2024, entry version 183.
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   SwissPalm; Q60778; -.
DR   EPD; Q60778; -.
DR   jPOST; Q60778; -.
DR   MaxQB; Q60778; -.
DR   PaxDb; 10090-ENSMUSP00000032815; -.
DR   PeptideAtlas; Q60778; -.
DR   ProteomicsDB; 269547; -.
DR   Pumba; Q60778; -.
DR   Antibodypedia; 4179; 891 antibodies from 45 providers.
DR   DNASU; 18036; -.
DR   Ensembl; ENSMUST00000032815.11; ENSMUSP00000032815.5; ENSMUSG00000030595.16.
DR   Ensembl; ENSMUST00000085851.12; ENSMUSP00000083012.6; ENSMUSG00000030595.16.
DR   GeneID; 18036; -.
DR   KEGG; mmu:18036; -.
DR   UCSC; uc009fzr.1; mouse.
DR   AGR; MGI:104752; -.
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; 621606at2759; -.
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 77 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 247 other cell types or tissues.
DR   ExpressionAtlas; Q60778; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
DR   GO; GO:0006954; P:inflammatory response; IGI:MGI.
DR   GO; GO:0043122; P:regulation of canonical NF-kappaB signal transduction; IGI:MGI.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   PANTHER; PTHR47303; -; 1.
DR   PANTHER; PTHR47303:SF1; NF-KAPPA-B INHIBITOR BETA; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 6.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
DR   Genevisible; Q60778; MM.
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
//