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Q15653

- IKBB_HUMAN

UniProt

Q15653 - IKBB_HUMAN

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Protein

NF-kappa-B inhibitor beta

Gene

NFKBIB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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. signal transducer activity Source: ProtInc
  2. transcription coactivator activity Source: ProtInc

GO - Biological processi

  1. innate immune response Source: Reactome
  2. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  3. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  4. positive regulation of NF-kappaB transcription factor activity Source: Reactome
  5. positive regulation of type I interferon production Source: Reactome
  6. signal transduction Source: ProtInc
  7. toll-like receptor 10 signaling pathway Source: Reactome
  8. toll-like receptor 2 signaling pathway Source: Reactome
  9. toll-like receptor 3 signaling pathway Source: Reactome
  10. toll-like receptor 4 signaling pathway Source: Reactome
  11. toll-like receptor 5 signaling pathway Source: Reactome
  12. toll-like receptor 9 signaling pathway Source: Reactome
  13. toll-like receptor signaling pathway Source: Reactome
  14. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  15. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  16. transcription, DNA-templated Source: ProtInc
  17. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_24969. TRAF6 mediated NF-kB activation.
SABIO-RKQ15653.
SignaLinkiQ15653.

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
Thyroid receptor-interacting protein 9
Short name:
TR-interacting protein 9
Short name:
TRIP-9
Gene namesi
Name:NFKBIB
Synonyms:IKBB, TRIP9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:7798. NFKBIB.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi19 – 191S → A: No degradation; when associated with A-23. 1 Publication
Mutagenesisi23 – 231S → A: No degradation; when associated with A-19. 1 Publication

Organism-specific databases

PharmGKBiPA31602.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 356356NF-kappa-B inhibitor betaPRO_0000067004Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Phosphoserine; by RPS6KA11 Publication
Modified residuei23 – 231Phosphoserine; by RPS6KA11 Publication
Modified residuei313 – 3131Phosphoserine; by CK21 Publication
Modified residuei315 – 3151Phosphoserine; by CK21 Publication

Post-translational modificationi

Phosphorylated by RPS6KA1; followed by degradation. Interaction with NKIRAS1 and NKIRAS2 probably prevents phosphorylation.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ15653.
PaxDbiQ15653.
PRIDEiQ15653.

PTM databases

PhosphoSiteiQ15653.

Expressioni

Tissue specificityi

Expressed in all tissues examined.

Gene expression databases

BgeeiQ15653.
CleanExiHS_NFKBIB.
ExpressionAtlasiQ15653. baseline and differential.
GenevestigatoriQ15653.

Organism-specific databases

HPAiCAB010447.

Interactioni

Subunit structurei

Interacts with THRB (via ligand-binding domain). Interacts with RELA and REL. Interacts with COMMD1 and inhibitor kappa B-interacting Ras-like NKIRAS1 and NKIRAS2.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FBXW11Q9UKB12EBI-352889,EBI-355189
RELAQ042066EBI-352889,EBI-73886

Protein-protein interaction databases

BioGridi110860. 32 interactions.
DIPiDIP-27532N.
IntActiQ15653. 29 interactions.
MINTiMINT-1131598.
STRINGi9606.ENSP00000312988.

Structurei

3D structure databases

ProteinModelPortaliQ15653.
SMRiQ15653. Positions 5-337.
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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi186 – 19510Asp/Glu-rich (acidic)

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

eggNOGiNOG272177.
GeneTreeiENSGT00550000074527.
HOVERGENiHBG019039.
InParanoidiQ15653.
KOiK02581.
OMAiDEWCDSG.
PhylomeDBiQ15653.
TreeFamiTF320166.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF00023. Ank. 3 hits.
PF12796. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15653-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAGVACLGKA ADADEWCDSG LGSLGPDAAA PGGPGLGAEL GPGLSWAPLV
60 70 80 90 100
FGYVTEDGDT ALHLAVIHQH EPFLDFLLGF SAGTEYMDLQ NDLGQTALHL
110 120 130 140 150
AAILGETSTV EKLYAAGAGL CVAERRGHTA LHLACRVGAH ACARALLQPR
160 170 180 190 200
PRRPREAPDT YLAQGPDRTP DTNHTPVALY PDSDLEKEEE ESEEDWKLQL
210 220 230 240 250
EAENYEGHTP LHVAVIHKDV EMVRLLRDAG ADLDKPEPTC GRSPLHLAVE
260 270 280 290 300
AQAADVLELL LRAGANPAAR MYGGRTPLGS AMLRPNPILA RLLRAHGAPE
310 320 330 340 350
PEGEDEKSGP CSSSSDSDSG DEGDEYDDIV VHSSRSQTRL PPTPASKPLP

DDPRPV
Length:356
Mass (Da):37,771
Last modified:January 4, 2005 - v2
Checksum:iE84575971B6F81CC
GO
Isoform 2 (identifier: Q15653-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     324-338: DEYDDIVVHSSRSQT → VSQEERQGSPAGGSG
     339-356: Missing.

Show »
Length:338
Mass (Da):35,530
Checksum:iF024666B851DF976
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191S → T in AAC41742. (PubMed:7776974)Curated
Sequence conflicti319 – 3191S → G in AAC41742. (PubMed:7776974)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti339 – 3391R → W.1 Publication
Corresponds to variant rs17886215 [ dbSNP | Ensembl ].
VAR_020771

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei324 – 33815DEYDD…SRSQT → VSQEERQGSPAGGSG in isoform 2. 2 PublicationsVSP_012409Add
BLAST
Alternative sequencei339 – 35618Missing in isoform 2. 2 PublicationsVSP_012410Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L40407 Genomic DNA. Translation: AAC41742.1.
BT006743 mRNA. Translation: AAP35389.1.
AY736284 Genomic DNA. Translation: AAU10088.1.
AK290569 mRNA. Translation: BAF83258.1.
CH471126 Genomic DNA. Translation: EAW56843.1.
BC007197 mRNA. Translation: AAH07197.1.
BC015528 mRNA. Translation: AAH15528.1.
CCDSiCCDS12524.1. [Q15653-1]
RefSeqiNP_001230045.1. NM_001243116.1.
NP_002494.2. NM_002503.4. [Q15653-1]
UniGeneiHs.9731.

Genome annotation databases

EnsembliENST00000313582; ENSP00000312988; ENSG00000104825. [Q15653-1]
ENST00000572515; ENSP00000459728; ENSG00000104825. [Q15653-2]
GeneIDi4793.
KEGGihsa:4793.
UCSCiuc002ojw.3. human. [Q15653-1]
uc002ojy.3. human. [Q15653-2]

Polymorphism databases

DMDMi57015399.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L40407 Genomic DNA. Translation: AAC41742.1 .
BT006743 mRNA. Translation: AAP35389.1 .
AY736284 Genomic DNA. Translation: AAU10088.1 .
AK290569 mRNA. Translation: BAF83258.1 .
CH471126 Genomic DNA. Translation: EAW56843.1 .
BC007197 mRNA. Translation: AAH07197.1 .
BC015528 mRNA. Translation: AAH15528.1 .
CCDSi CCDS12524.1. [Q15653-1 ]
RefSeqi NP_001230045.1. NM_001243116.1.
NP_002494.2. NM_002503.4. [Q15653-1 ]
UniGenei Hs.9731.

3D structure databases

ProteinModelPortali Q15653.
SMRi Q15653. Positions 5-337.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110860. 32 interactions.
DIPi DIP-27532N.
IntActi Q15653. 29 interactions.
MINTi MINT-1131598.
STRINGi 9606.ENSP00000312988.

Chemistry

BindingDBi Q15653.

PTM databases

PhosphoSitei Q15653.

Polymorphism databases

DMDMi 57015399.

Proteomic databases

MaxQBi Q15653.
PaxDbi Q15653.
PRIDEi Q15653.

Protocols and materials databases

DNASUi 4793.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000313582 ; ENSP00000312988 ; ENSG00000104825 . [Q15653-1 ]
ENST00000572515 ; ENSP00000459728 ; ENSG00000104825 . [Q15653-2 ]
GeneIDi 4793.
KEGGi hsa:4793.
UCSCi uc002ojw.3. human. [Q15653-1 ]
uc002ojy.3. human. [Q15653-2 ]

Organism-specific databases

CTDi 4793.
GeneCardsi GC19P039390.
HGNCi HGNC:7798. NFKBIB.
HPAi CAB010447.
MIMi 604495. gene.
neXtProti NX_Q15653.
PharmGKBi PA31602.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG272177.
GeneTreei ENSGT00550000074527.
HOVERGENi HBG019039.
InParanoidi Q15653.
KOi K02581.
OMAi DEWCDSG.
PhylomeDBi Q15653.
TreeFami TF320166.

Enzyme and pathway databases

Reactomei REACT_118563. RIP-mediated NFkB activation via ZBP1.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_24969. TRAF6 mediated NF-kB activation.
SABIO-RK Q15653.
SignaLinki Q15653.

Miscellaneous databases

ChiTaRSi NFKBIB. human.
GeneWikii NFKBIB.
GenomeRNAii 4793.
NextBioi 18470.
PROi Q15653.
SOURCEi Search...

Gene expression databases

Bgeei Q15653.
CleanExi HS_NFKBIB.
ExpressionAtlasi Q15653. baseline and differential.
Genevestigatori Q15653.

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. 3 hits.
PF12796. Ank_2. 1 hit.
[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. "Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor."
    Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.
    Mol. Endocrinol. 9:243-254(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2).
    Tissue: Cervix carcinoma.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. SeattleSNPs variation discovery resource
    Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TRP-339.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Lung.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 100-338 (ISOFORM 2).
    Tissue: Pancreas and Uterus.
  7. "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.
  8. "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: INTERACTION WITH NKIRAS1 AND NKIRAS2.
  9. "Mapping of the inducible IkappaB phosphorylation sites that signal its ubiquitination and degradation."
    DiDonato J.A., Mercurio F., Rosette C., Wu-Li J., Suyang H., Ghosh S., Karin M.
    Mol. Cell. Biol. 16:1295-1304(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-19 AND SER-23, PHOSPHORYLATION AT SER-19 AND SER-23.
  10. "Basal phosphorylation of the PEST domain in the I(kappa)B(beta) regulates its functional interaction with the c-rel proto-oncogene product."
    Chu Z.L., McKinsey T.A., Liu L., Qi X., Ballard D.W.
    Mol. Cell. Biol. 16:5974-5984(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-313 AND SER-315.
  11. "KappaB-Ras binds to the unique insert within the ankyrin repeat domain of IkappaBbeta and regulates cytoplasmic retention of IkappaBbeta.NF-kappaB complexes."
    Chen Y., Wu J., Ghosh G.
    J. Biol. Chem. 278:23101-23106(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NKIRAS1.
  12. "Inhibition of NF-kappaB activity by IkappaBbeta in association with kappaB-Ras."
    Chen Y., Vallee S., Wu J., Vu D., Sondek J., Ghosh G.
    Mol. Cell. Biol. 24:3048-3056(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NKIRAS1.
  13. "Characterization of COMMD protein-protein interactions in NF-kappaB signalling."
    de Bie P., van de Sluis B., Burstein E., Duran K.J., Berger R., Duckett C.S., Wijmenga C., Klomp L.W.
    Biochem. J. 398:63-71(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COMMD1.

Entry informationi

Entry nameiIKBB_HUMAN
AccessioniPrimary (citable) accession number: Q15653
Secondary accession number(s): A8K3F4, Q96BJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 4, 2005
Last modified: October 29, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3