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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

  • cellular response to lipopolysaccharide Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-1169091. Activation of NF-kappaB in B cells.
R-MMU-1810476. RIP-mediated NFkB activation via ZBP1.
R-MMU-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-MMU-933542. TRAF6 mediated NF-kB activation.

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
Proteomesi
  • UP000000589 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)DescriptionActionsGraphical viewLength
ChainiPRO_00000670051 – 359NF-kappa-B inhibitor betaAdd BLAST359

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei19Phosphoserine; by RPS6KA1By similarity1
Modified residuei23Phosphoserine; by RPS6KA1By similarity1
Modified residuei313PhosphoserineBy similarity1
Modified residuei318PhosphoserineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ60778.
MaxQBiQ60778.
PaxDbiQ60778.
PeptideAtlasiQ60778.
PRIDEiQ60778.

PTM databases

iPTMnetiQ60778.
PhosphoSitePlusiQ60778.

Expressioni

Tissue specificityi

Highly expressed in testis followed by spleen.

Gene expression databases

BgeeiENSMUSG00000030595.
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 interactors.
DIPiDIP-37418N.
IntActiQ60778. 3 interactors.
MINTiMINT-1523907.
STRINGi10090.ENSMUSP00000032815.

Structurei

Secondary structure

1359
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi61 – 67Combined sources7
Helixi71 – 81Combined sources11
Helixi85 – 88Combined sources4
Helixi97 – 104Combined sources8
Helixi107 – 115Combined sources9
Helixi130 – 134Combined sources5
Turni135 – 138Combined sources4
Helixi140 – 146Combined sources7
Beta strandi147 – 149Combined sources3
Helixi196 – 199Combined sources4
Helixi210 – 216Combined sources7
Helixi220 – 229Combined sources10
Turni238 – 240Combined sources3
Helixi244 – 250Combined sources7
Helixi254 – 262Combined sources9
Helixi277 – 282Combined sources6
Helixi287 – 295Combined sources9
Helixi304 – 307Combined sources4

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ60778.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati57 – 86ANK 1Add BLAST30
Repeati93 – 122ANK 2Add BLAST30
Repeati126 – 155ANK 3Add BLAST30
Repeati206 – 235ANK 4Add BLAST30
Repeati240 – 269ANK 5Add BLAST30
Repeati273 – 302ANK 6Add BLAST30

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

eggNOGiKOG0504. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00550000074527.
HOGENOMiHOG000137336.
HOVERGENiHBG019039.
InParanoidiQ60778.
KOiK02581.
OMAiDEWCDSG.
OrthoDBiEOG091G092R.
TreeFamiTF320166.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF12796. Ank_2. 2 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)DescriptionActionsGraphical viewLength
Sequence conflicti84T → H in AAC52166 (PubMed:7867065).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K3ZX-ray2.50D50-331[»]
1OY3X-ray2.05D50-331[»]
ProteinModelPortaliQ60778.
SMRiQ60778.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ60778.
PhosphoSitePlusiQ60778.

Proteomic databases

EPDiQ60778.
MaxQBiQ60778.
PaxDbiQ60778.
PeptideAtlasiQ60778.
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

eggNOGiKOG0504. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00550000074527.
HOGENOMiHOG000137336.
HOVERGENiHBG019039.
InParanoidiQ60778.
KOiK02581.
OMAiDEWCDSG.
OrthoDBiEOG091G092R.
TreeFamiTF320166.

Enzyme and pathway databases

ReactomeiR-MMU-1169091. Activation of NF-kappaB in B cells.
R-MMU-1810476. RIP-mediated NFkB activation via ZBP1.
R-MMU-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-MMU-933542. TRAF6 mediated NF-kB activation.

Miscellaneous databases

EvolutionaryTraceiQ60778.
PROiQ60778.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000030595.
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]
PfamiPF12796. Ank_2. 2 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...

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: November 2, 2016
This is version 140 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

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 one 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.