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Protein

NF-kappa-B inhibitor beta

Gene

Nfkbib

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_275137. TRAF6 mediated NF-kB activation.
REACT_275686. Activation of NF-kappaB in B cells.
REACT_283225. RIP-mediated NFkB activation via ZBP1.
REACT_305279. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Nfkbib
Synonyms:Ikbb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:104752. Nfkbib.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359NF-kappa-B inhibitor betaPRO_0000067005Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Phosphoserine; by RPS6KA1By similarity
Modified residuei23 – 231Phosphoserine; by RPS6KA1By similarity
Modified residuei313 – 3131PhosphoserineBy similarity
Modified residuei318 – 3181PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ60778.
PaxDbiQ60778.
PRIDEiQ60778.

PTM databases

PhosphoSiteiQ60778.

Expressioni

Tissue specificityi

Highly expressed in testis followed by spleen.

Gene expression databases

BgeeiQ60778.
ExpressionAtlasiQ60778. baseline and differential.
GenevisibleiQ60778. MM.

Interactioni

Subunit structurei

Interacts with THRB (via ligand-binding domain) (By similarity). Interacts with RELA and REL (PubMed:8816457). Interacts with COMMD1 (By similarity). Interacts with inhibitor kappa B-interacting Ras-like NKIRAS1 and NKIRAS2 (PubMed:10657303). Interacts with DDRGK1; positively regulates NFKBIB phosphorylation and degradation (By similarity).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Arih2Q9Z1K62EBI-644469,EBI-6861719
RelaQ042078EBI-644469,EBI-644400

Protein-protein interaction databases

BioGridi201754. 3 interactions.
DIPiDIP-37418N.
IntActiQ60778. 3 interactions.
MINTiMINT-1523907.
STRINGi10090.ENSMUSP00000032815.

Structurei

Secondary structure

1
359
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi61 – 677Combined sources
Helixi71 – 8111Combined sources
Helixi85 – 884Combined sources
Helixi97 – 1048Combined sources
Helixi107 – 1159Combined sources
Helixi130 – 1345Combined sources
Turni135 – 1384Combined sources
Helixi140 – 1467Combined sources
Beta strandi147 – 1493Combined sources
Helixi196 – 1994Combined sources
Helixi210 – 2167Combined sources
Helixi220 – 22910Combined sources
Turni238 – 2403Combined sources
Helixi244 – 2507Combined sources
Helixi254 – 2629Combined sources
Helixi277 – 2826Combined sources
Helixi287 – 2959Combined sources
Helixi304 – 3074Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K3ZX-ray2.50D50-331[»]
1OY3X-ray2.05D50-331[»]
ProteinModelPortaliQ60778.
SMRiQ60778. Positions 5-315.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ60778.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati57 – 8630ANK 1Add
BLAST
Repeati93 – 12230ANK 2Add
BLAST
Repeati126 – 15530ANK 3Add
BLAST
Repeati206 – 23530ANK 4Add
BLAST
Repeati240 – 26930ANK 5Add
BLAST
Repeati273 – 30230ANK 6Add
BLAST

Sequence similaritiesi

Belongs to the NF-kappa-B inhibitor family.Curated
Contains 6 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00550000074527.
HOGENOMiHOG000137336.
HOVERGENiHBG019039.
InParanoidiQ60778.
KOiK02581.
OMAiDEWCDSG.
OrthoDBiEOG7W154S.
TreeFamiTF320166.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF00023. Ank. 4 hits.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 6 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q60778-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGVACLGKT ADADEWCDSG LGSLGPDAAA PGGPGLGAEL GPELSWAPLV
60 70 80 90 100
FGYVTEDGDT ALHLAVIHQH EPFLDFLLGF SAGTEYLDLQ NDLGQTALHL
110 120 130 140 150
AAILGEASTV EKLYAAGAGV LVAERGGHTA LHLACRVRAH TCACVLLQPR
160 170 180 190 200
PSHPRDASDT YLTQSQDCTP DTSHAPAAVD SQPNPENEEE PRDEDWRLQL
210 220 230 240 250
EAENYDGHTP LHVAVIHKDA EMVRLLRDAG ADLNKPEPTC GRTPLHLAVE
260 270 280 290 300
AQAASVLELL LKAGADPTAR MYGGRTPLGS ALLRPNPILA RLLRAHGAPE
310 320 330 340 350
PEDEDDKLSP CSSSGSDSDS DNRDEGDEYD DIVVHSGRSQ NRQPPSPASK

PLPDDPNPA
Length:359
Mass (Da):37,965
Last modified:July 27, 2011 - v2
Checksum:i0E2B46C89E2404EF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841T → H in AAC52166 (PubMed:7867065).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS21054.1.
RefSeqiNP_001293151.1. NM_001306222.1.
NP_035038.2. NM_010908.5.
UniGeneiMm.220333.

Genome annotation databases

EnsembliENSMUST00000032815; ENSMUSP00000032815; ENSMUSG00000030595.
ENSMUST00000085851; ENSMUSP00000083012; ENSMUSG00000030595.
GeneIDi18036.
KEGGimmu:18036.
UCSCiuc009fzr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS21054.1.
RefSeqiNP_001293151.1. NM_001306222.1.
NP_035038.2. NM_010908.5.
UniGeneiMm.220333.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K3ZX-ray2.50D50-331[»]
1OY3X-ray2.05D50-331[»]
ProteinModelPortaliQ60778.
SMRiQ60778. Positions 5-315.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201754. 3 interactions.
DIPiDIP-37418N.
IntActiQ60778. 3 interactions.
MINTiMINT-1523907.
STRINGi10090.ENSMUSP00000032815.

PTM databases

PhosphoSiteiQ60778.

Proteomic databases

MaxQBiQ60778.
PaxDbiQ60778.
PRIDEiQ60778.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032815; ENSMUSP00000032815; ENSMUSG00000030595.
ENSMUST00000085851; ENSMUSP00000083012; ENSMUSG00000030595.
GeneIDi18036.
KEGGimmu:18036.
UCSCiuc009fzr.1. mouse.

Organism-specific databases

CTDi4793.
MGIiMGI:104752. Nfkbib.

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00550000074527.
HOGENOMiHOG000137336.
HOVERGENiHBG019039.
InParanoidiQ60778.
KOiK02581.
OMAiDEWCDSG.
OrthoDBiEOG7W154S.
TreeFamiTF320166.

Enzyme and pathway databases

ReactomeiREACT_275137. TRAF6 mediated NF-kB activation.
REACT_275686. Activation of NF-kappaB in B cells.
REACT_283225. RIP-mediated NFkB activation via ZBP1.
REACT_305279. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.

Miscellaneous databases

EvolutionaryTraceiQ60778.
NextBioi293133.
PROiQ60778.
SOURCEiSearch...

Gene expression databases

BgeeiQ60778.
ExpressionAtlasiQ60778. baseline and differential.
GenevisibleiQ60778. MM.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF00023. Ank. 4 hits.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 6 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiIKBB_MOUSE
AccessioniPrimary (citable) accession number: Q60778
Secondary accession number(s): Q564F1, Q9D6L5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: July 27, 2011
Last modified: July 22, 2015
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.