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Q60778

- IKBB_MOUSE

UniProt

Q60778 - IKBB_MOUSE

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Protein
NF-kappa-B inhibitor beta
Gene
Nfkbib, Ikbb
Organism
Mus musculus (Mouse)
Status
Reviewed - 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 - Molecular functioni

  1. protein binding Source: IntAct
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_199121. Activation of NF-kappaB in B cells.
REACT_202898. TRAF6 mediated NF-kB activation.
REACT_219800. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_222971. RIP-mediated NFkB activation via ZBP1.

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: Chromosome 7

Organism-specific databases

MGIiMGI:104752. Nfkbib.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359NF-kappa-B inhibitor beta
PRO_0000067005Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Phosphoserine; by RPS6KA1 By similarity
Modified residuei23 – 231Phosphoserine; by RPS6KA1 By similarity
Modified residuei313 – 3131Phosphoserine By similarity
Modified residuei318 – 3181Phosphoserine By similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ60778.
PRIDEiQ60778.

PTM databases

PhosphoSiteiQ60778.

Expressioni

Tissue specificityi

Highly expressed in testis followed by spleen.

Gene expression databases

ArrayExpressiQ60778.
BgeeiQ60778.
GenevestigatoriQ60778.

Interactioni

Subunit structurei

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.1 Publication

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.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K3ZX-ray2.50D50-331[»]
1OY3X-ray2.05D50-331[»]
ProteinModelPortaliQ60778.
SMRiQ60778. Positions 5-346.

Miscellaneous databases

EvolutionaryTraceiQ60778.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 6 ANK repeats.

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00550000074527.
HOGENOMiHOG000137336.
HOVERGENiHBG019039.
InParanoidiQ564F1.
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

MAGVACLGKT ADADEWCDSG LGSLGPDAAA PGGPGLGAEL GPELSWAPLV    50
FGYVTEDGDT ALHLAVIHQH EPFLDFLLGF SAGTEYLDLQ NDLGQTALHL 100
AAILGEASTV EKLYAAGAGV LVAERGGHTA LHLACRVRAH TCACVLLQPR 150
PSHPRDASDT YLTQSQDCTP DTSHAPAAVD SQPNPENEEE PRDEDWRLQL 200
EAENYDGHTP LHVAVIHKDA EMVRLLRDAG ADLNKPEPTC GRTPLHLAVE 250
AQAASVLELL LKAGADPTAR MYGGRTPLGS ALLRPNPILA RLLRAHGAPE 300
PEDEDDKLSP CSSSGSDSDS DNRDEGDEYD DIVVHSGRSQ NRQPPSPASK 350
PLPDDPNPA 359
Length:359
Mass (Da):37,965
Last modified:July 27, 2011 - v2
Checksum:i0E2B46C89E2404EF
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841T → H in AAC52166. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_035038.2. NM_010908.4.
XP_006539676.1. XM_006539613.1.
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS21054.1.
RefSeqi NP_035038.2. NM_010908.4.
XP_006539676.1. XM_006539613.1.
UniGenei Mm.220333.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1K3Z X-ray 2.50 D 50-331 [» ]
1OY3 X-ray 2.05 D 50-331 [» ]
ProteinModelPortali Q60778.
SMRi Q60778. Positions 5-346.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201754. 3 interactions.
DIPi DIP-37418N.
IntActi Q60778. 3 interactions.
MINTi MINT-1523907.

PTM databases

PhosphoSitei Q60778.

Proteomic databases

PaxDbi Q60778.
PRIDEi Q60778.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000032815 ; ENSMUSP00000032815 ; ENSMUSG00000030595 .
ENSMUST00000085851 ; ENSMUSP00000083012 ; ENSMUSG00000030595 .
GeneIDi 18036.
KEGGi mmu:18036.
UCSCi uc009fzr.1. mouse.

Organism-specific databases

CTDi 4793.
MGIi MGI:104752. Nfkbib.

Phylogenomic databases

eggNOGi COG0666.
GeneTreei ENSGT00550000074527.
HOGENOMi HOG000137336.
HOVERGENi HBG019039.
InParanoidi Q564F1.
KOi K02581.
OMAi DEWCDSG.
OrthoDBi EOG7W154S.
TreeFami TF320166.

Enzyme and pathway databases

Reactomei REACT_199121. Activation of NF-kappaB in B cells.
REACT_202898. TRAF6 mediated NF-kB activation.
REACT_219800. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_222971. RIP-mediated NFkB activation via ZBP1.

Miscellaneous databases

EvolutionaryTracei Q60778.
NextBioi 293133.
PROi Q60778.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q60778.
Bgeei Q60778.
Genevestigatori Q60778.

Family and domain databases

Gene3Di 1.25.40.20. 2 hits.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view ]
Pfami PF00023. Ank. 4 hits.
[Graphical view ]
PRINTSi PR01415. ANKYRIN.
SMARTi SM00248. ANK. 6 hits.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 119 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

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