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Protein

NF-kappa-B inhibitor beta

Gene

Nfkbib

Organism
Rattus norvegicus (Rat)
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 - Molecular functioni

  • NF-kappaB binding Source: RGD

GO - Biological processi

  • cytoplasmic sequestering of NF-kappaB Source: RGD
  • signal transduction Source: RGD
Complete GO annotation...

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621887. Nfkbib.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • cytosol Source: RGD
  • I-kappaB/NF-kappaB complex Source: RGD
  • 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 betaPRO_0000067006Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Phosphoserine; by RPS6KA11 Publication
Modified residuei23 – 231Phosphoserine; by RPS6KA11 Publication
Modified residuei318 – 3181PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by RPS6KA1; followed by degradation. Interaction with NKIRAS1 and NKIRAS2 probably prevents phosphorylation (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9JIA3.
PRIDEiQ9JIA3.

PTM databases

iPTMnetiQ9JIA3.
PhosphoSiteiQ9JIA3.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • NF-kappaB binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027212.

Structurei

3D structure databases

ProteinModelPortaliQ9JIA3.
SMRiQ9JIA3. Positions 50-303.
ModBaseiSearch...
MobiDBiSearch...

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

eggNOGiKOG0504. Eukaryota.
COG0666. LUCA.
HOGENOMiHOG000137336.
HOVERGENiHBG019039.
InParanoidiQ9JIA3.
PhylomeDBiQ9JIA3.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF12796. Ank_2. 1 hit.
[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.

Q9JIA3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGVACLGKT ADADEWCDSG LGSLGPDAAA PGGPGLVAEL SPELSWAPLV
60 70 80 90 100
FGYVTEDGDT ALHLAVIHQH EPFLDFLLGF SAGTEYLDLQ NDLGQTALHL
110 120 130 140 150
AAILGEASTV EKLYAAGAGV LVTERGGHTA LHLACRVRAH TCAYVLLQPR
160 170 180 190 200
PSHPRDASDT YLTQSQDHTP DTSHAPVATD PQPNPGNEEE LRDEDWRLQL
210 220 230 240 250
EAENYDGHTP LHVAVIHKDA EMVQLLRDAG ADLNKPEPTC GRTPLHLAVE
260 270 280 290 300
GQAAGVLALL LKAGADPTAR MYGGRTPLGS ALLRPNPVLA RLLRAHGAPE
310 320 330 340 350
PEDKDDKLSP CSNSSSDSDS DNRDEGDEYD DIVVHSRRSQ NQPPPSPAAK

PLPDDPNPA
Length:359
Mass (Da):38,081
Last modified:October 1, 2000 - v1
Checksum:iB8602C815C72B1AB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF246634 mRNA. Translation: AAF64191.1.
UniGeneiRn.8395.

Genome annotation databases

UCSCiRGD:621887. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF246634 mRNA. Translation: AAF64191.1.
UniGeneiRn.8395.

3D structure databases

ProteinModelPortaliQ9JIA3.
SMRiQ9JIA3. Positions 50-303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027212.

PTM databases

iPTMnetiQ9JIA3.
PhosphoSiteiQ9JIA3.

Proteomic databases

PaxDbiQ9JIA3.
PRIDEiQ9JIA3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:621887. rat.

Organism-specific databases

RGDi621887. Nfkbib.

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
COG0666. LUCA.
HOGENOMiHOG000137336.
HOVERGENiHBG019039.
InParanoidiQ9JIA3.
PhylomeDBiQ9JIA3.

Miscellaneous databases

PROiQ9JIA3.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF12796. Ank_2. 1 hit.
[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

  1. "Inhibitory and stimulatory effects of lactacystin on expression of nitric oxide synthase type 2 in brain glial cells: the role of I kappa B-beta."
    Stasiolek M., Gavrilyuk V., Sharp A., Horvath P., Selmaj K., Feinstein D.L.
    J. Biol. Chem. 275:24847-24856(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
  2. "Ribosomal S6 kinase-1 modulates interleukin-1beta-induced persistent activation of NF-kappaB through phosphorylation of IkappaBbeta."
    Xu S., Bayat H., Hou X., Jiang B.
    Am. J. Physiol. 291:C1336-C1345(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-19 AND SER-23.

Entry informationi

Entry nameiIKBB_RAT
AccessioniPrimary (citable) accession number: Q9JIA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: October 1, 2000
Last modified: May 11, 2016
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.