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Q60778 (IKBB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NF-kappa-B inhibitor beta

Short name=NF-kappa-BIB
Alternative name(s):
I-kappa-B-beta
Short name=IkB-B
Short name=IkB-beta
Short name=IkappaBbeta
Gene names
Name:Nfkbib
Synonyms:Ikbb
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibits NF-kappa-B by complexing with and trapping it in the cytoplasm. However, the unphosphorylated form resynthesized after cell stimulation is able to bind NF-kappa-B allowing its transport to the nucleus and protecting it to further NFKBIA-dependent inactivation. Association with inhibitor kappa B-interacting NKIRAS1 and NKIRAS2 prevent its phosphorylation rendering it more resistant to degradation, explaining its slower degradation.

Subunit structure

Interacts with COMMD1 and inhibitor kappa B-interacting Ras-like NKIRAS1 and NKIRAS2 By similarity. Interacts with the ligand-binding domain of THRB. Interacts with RELA and REL. Ref.4

Subcellular location

Cytoplasm. Nucleus.

Tissue specificity

Highly expressed in testis followed by spleen.

Post-translational modification

Phosphorylated by RPS6KA1; followed by degradation. Interaction with NKIRAS1 and NKIRAS2 probably prevents phosphorylation.

Sequence similarities

Belongs to the NF-kappa-B inhibitor family.

Contains 6 ANK repeats.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   DomainANK repeat
Repeat
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 12686541PubMed 15102471PubMed 23179078. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359NF-kappa-B inhibitor beta
PRO_0000067005

Regions

Repeat57 – 8630ANK 1
Repeat93 – 12230ANK 2
Repeat126 – 15530ANK 3
Repeat206 – 23530ANK 4
Repeat240 – 26930ANK 5
Repeat273 – 30230ANK 6

Amino acid modifications

Modified residue191Phosphoserine; by RPS6KA1 By similarity
Modified residue231Phosphoserine; by RPS6KA1 By similarity
Modified residue3131Phosphoserine By similarity
Modified residue3181Phosphoserine By similarity

Experimental info

Sequence conflict841T → H in AAC52166. Ref.1

Secondary structure

................................... 359
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q60778 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 0E2B46C89E2404EF

FASTA35937,965
        10         20         30         40         50         60 
MAGVACLGKT ADADEWCDSG LGSLGPDAAA PGGPGLGAEL GPELSWAPLV FGYVTEDGDT 

        70         80         90        100        110        120 
ALHLAVIHQH EPFLDFLLGF SAGTEYLDLQ NDLGQTALHL AAILGEASTV EKLYAAGAGV 

       130        140        150        160        170        180 
LVAERGGHTA LHLACRVRAH TCACVLLQPR PSHPRDASDT YLTQSQDCTP DTSHAPAAVD 

       190        200        210        220        230        240 
SQPNPENEEE PRDEDWRLQL EAENYDGHTP LHVAVIHKDA EMVRLLRDAG ADLNKPEPTC 

       250        260        270        280        290        300 
GRTPLHLAVE AQAASVLELL LKAGADPTAR MYGGRTPLGS ALLRPNPILA RLLRAHGAPE 

       310        320        330        340        350 
PEDEDDKLSP CSSSGSDSDS DNRDEGDEYD DIVVHSGRSQ NRQPPSPASK PLPDDPNPA 

« Hide

References

« Hide 'large scale' references
[1]"IkappaB-beta regulates the persistent response in a biphasic activation of NF-kappaB."
Thompson J.E., Phillips R.J., Erdjument-Bromage H., Tempst P., Ghosh S.
Cell 80:573-582(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: B-cell.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Hypothalamus, Spleen and Tongue.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Role of unphosphorylated, newly synthesized IkappaB beta in persistent activation of NF-kappaB."
Suyang H., Phillips R.J., Douglas I., Ghosh S.
Mol. Cell. Biol. 16:5444-5449(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, INTERACTION WITH RELA AND REL.
[5]"A subclass of Ras proteins that regulate the degradation of IkappaB."
Fenwick C., Na S.-Y., Voll R.E., Zhong H., Im S.-Y., Lee J.W., Ghosh S.
Science 287:869-873(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: KAPPA B RAS-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U19799 mRNA. Translation: AAC52166.1.
AK010218 mRNA. Translation: BAB26774.1.
AK038631 mRNA. Translation: BAC30071.1.
AK156731 mRNA. Translation: BAE33825.1.
CH466593 Genomic DNA. Translation: EDL24117.1.
CH466593 Genomic DNA. Translation: EDL24118.1.
CCDSCCDS21054.1.
RefSeqNP_035038.2. NM_010908.4.
XP_006539676.1. XM_006539613.1.
UniGeneMm.220333.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K3ZX-ray2.50D50-331[»]
1OY3X-ray2.05D50-331[»]
ProteinModelPortalQ60778.
SMRQ60778. Positions 5-346.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201754. 3 interactions.
DIPDIP-37418N.
IntActQ60778. 3 interactions.
MINTMINT-1523907.

PTM databases

PhosphoSiteQ60778.

Proteomic databases

PaxDbQ60778.
PRIDEQ60778.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032815; ENSMUSP00000032815; ENSMUSG00000030595.
ENSMUST00000085851; ENSMUSP00000083012; ENSMUSG00000030595.
GeneID18036.
KEGGmmu:18036.
UCSCuc009fzr.1. mouse.

Organism-specific databases

CTD4793.
MGIMGI:104752. Nfkbib.

Phylogenomic databases

eggNOGCOG0666.
GeneTreeENSGT00550000074527.
HOGENOMHOG000137336.
HOVERGENHBG019039.
InParanoidQ564F1.
KOK02581.
OMADEWCDSG.
OrthoDBEOG7W154S.
TreeFamTF320166.

Gene expression databases

ArrayExpressQ60778.
BgeeQ60778.
GenevestigatorQ60778.

Family and domain databases

Gene3D1.25.40.20. 2 hits.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamPF00023. Ank. 4 hits.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 6 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ60778.
NextBio293133.
PROQ60778.
SOURCESearch...

Entry information

Entry nameIKBB_MOUSE
AccessionPrimary (citable) accession number: Q60778
Secondary accession number(s): Q564F1, Q9D6L5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot