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Q60778

- IKBB_MOUSE

UniProt

Q60778 - IKBB_MOUSE

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Protein

NF-kappa-B inhibitor beta

Gene

Nfkbib

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.

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-KW
  2. nucleus Source: UniProtKB-KW
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.
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.By similarity1 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

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 12-303.
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_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:
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 .
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:
PDBei
RCSB PDBi
PDBji
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 12-303.
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

MaxQBi Q60778.
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 Q60778.
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

Bgeei Q60778.
ExpressionAtlasi Q60778. baseline and differential.
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: November 26, 2014
This is version 122 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