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Reviewed, UniProtKB/Swiss-Prot Q15653 (IKBB_HUMAN)

Last modified January 19, 2010. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    NF-kappa-B inhibitor beta
      Short name=NF-kappa-BIB
Alternative name(s):
    I-kappa-B-beta
      Short name=IkappaBbeta
      Short name=IkB-beta
      Short name=IkB-B
    Thyroid receptor-interacting protein 9
      Short name=TR-interacting protein 9
      Short name=TRIP-9
Gene names
Name: NFKBIB
Synonyms: IKBB, TRIP9
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length356 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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 IKBA-dependent inactivation. Association with inhibitor kappa B-interacting NKIRAS1 and NKIRAS2 prevent its phosphorylation rendering it more resistant to degradation, explaining its slower degradation.

Subunit structure

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. Ref.8 Ref.11 Ref.12 Ref.13

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Tissue specificity

Expressed in all tissues examined.

Post-translational modification

Phosphorylated; followed by degradation. Interaction with NKIRAS1 and NKIRAS2 probably prevents phosphorylation. Ref.10

Sequence similarities

Belongs to the NF-kappa-B inhibitor family.

Contains 6 ANK repeats.

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Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainANK repeat
Repeat
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processtranscription Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentcytosol

Inferred from Experiment. Source: Reactome

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionsignal transducer activity Ref.1

Traceable author statement. Source: ProtInc

transcription coactivator activity Ref.1

Traceable author statement. Source: ProtInc

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

MCCP235081EBI-352889,EBI-307531
RELAQ042063EBI-352889,EBI-73886

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Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15653-1)

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.
Isoform 2 (identifier: Q15653-2)

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

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 356356NF-kappa-B inhibitor beta
PRO_0000067004

Regions

Repeat57 – 8630ANK 1
Repeat93 – 12230ANK 2
Repeat126 – 15530ANK 3
Repeat206 – 23530ANK 4
Repeat240 – 26930ANK 5
Repeat273 – 30230ANK 6
Compositional bias186 – 19510Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue191Phosphoserine By similarity
Modified residue231Phosphoserine By similarity
Modified residue3131Phosphoserine; by CK2 Ref.10
Modified residue3151Phosphoserine; by CK2 Ref.10

Natural variations

Alternative sequence324 – 33815DEYDD…SRSQT → VSQEERQGSPAGGSG in isoform 2.
VSP_012409
Alternative sequence339 – 35618Missing in isoform 2.
VSP_012410
Natural variant3391R → W: dbSNP rs17886215. Ref.3
VAR_020771

Experimental info

Mutagenesis191S → A: No degradation; when associated with A-23. Ref.9
Mutagenesis231S → A: No degradation; when associated with A-19. Ref.9
Sequence conflict191S → T in AAC41742. Ref.1
Sequence conflict3191S → G in AAC41742. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: E84575971B6F81CC

FASTA35637,771
        10         20         30         40         50         60 
MAGVACLGKA ADADEWCDSG LGSLGPDAAA PGGPGLGAEL GPGLSWAPLV FGYVTEDGDT 

        70         80         90        100        110        120 
ALHLAVIHQH EPFLDFLLGF SAGTEYMDLQ NDLGQTALHL AAILGETSTV EKLYAAGAGL 

       130        140        150        160        170        180 
CVAERRGHTA LHLACRVGAH ACARALLQPR PRRPREAPDT YLAQGPDRTP DTNHTPVALY 

       190        200        210        220        230        240 
PDSDLEKEEE ESEEDWKLQL EAENYEGHTP LHVAVIHKDV EMVRLLRDAG ADLDKPEPTC 

       250        260        270        280        290        300 
GRSPLHLAVE AQAADVLELL LRAGANPAAR MYGGRTPLGS AMLRPNPILA RLLRAHGAPE 

       310        320        330        340        350 
PEGEDEKSGP CSSSSDSDSG DEGDEYDDIV VHSSRSQTRL PPTPASKPLP DDPRPV

« Hide

Isoform 2.

Checksum: F024666B851DF976
Show »

FASTA33835,530

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References

« Hide 'large scale' references
[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: 7776974] [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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Lung.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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: 15489334] [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: 8816457] [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: 10657303] [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: 8657102] [Abstract]
Cited for: MUTAGENESIS OF 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: 8887627] [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: 12672800] [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: 15024091] [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: 16573520] [Abstract]
Cited for: INTERACTION WITH COMMD1.
+Additional computationally mapped references.

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Web resources

SeattleSNPs

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00161119.
IPI00514744.
RefSeqNP_001001716.1.
NP_002494.2.
UniGeneHs.9731

3D structure databases

SMRQ15653. Positions 50-302.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-27532N.
IntActQ15653. 71 interactions.
STRINGQ15653.

PTM databases

PhosphoSiteQ15653.

Proteomic databases

PRIDEQ15653.

Genome annotation databases

EnsemblENST00000313582; ENSP00000312988; ENSG00000104825; Homo sapiens. [Genome view]
GeneID4793.
KEGGhsa:4793.
UCSCuc002ojw.1. human.
uc002ojy.1. human.

Organism-specific databases

CTD4793.
GeneCardsGC19P044082.
H-InvDBHIX0015105.
HGNCHGNC:7798. NFKBIB.
HPACAB010447.
MIM604495. gene.
PharmGKBPA31602.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG12368.
HOVERGENQ15653.
OMAYEGHTPL.
PhylomeDBQ15653.

Enzyme and pathway databases

Pathway_Interaction_DBbcr_5pathway. BCR signaling pathway.
ReactomeREACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpressQ15653.
BgeeQ15653.
CleanExHS_NFKBIB.
GenevestigatorQ15653.
GermOnlineENSG00000104825. Homo sapiens.

Family and domain databases

InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR015681. NF_kB_inhbitor.
[Graphical view]
Gene3DG3DSA:1.25.40.20. ANK. 1 hit.
PANTHERPTHR18958:SF236. NF_kB_inhbitor. 1 hit.
PfamPF00023. Ank. 2 hits.
[Graphical view]
SMARTSM00248. ANK. 6 hits.
[Graphical view]
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio18470.
SOURCESearch...

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Entry information

Entry nameIKBB_HUMAN
AccessionPrimary (citable) accession number: Q15653
Secondary accession number(s): A8K3F4, Q96BJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 4, 2005
Last modified: January 19, 2010
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Index of human polymorphisms and disease mutations

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Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents