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O00221 (IKBE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NF-kappa-B inhibitor epsilon

Short name=NF-kappa-BIE
Alternative name(s):
I-kappa-B-epsilon
Short name=IkB-E
Short name=IkB-epsilon
Short name=IkappaBepsilon
Gene names
Name:NFKBIE
Synonyms:IKBE
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibits NF-kappa-B by complexing with and trapping it in the cytoplasm. Inhibits DNA-binding of NF-kappa-B p50-p65 and p50-c-Rel complexes. Ref.4

Subunit structure

Interacts with RELA, REL, NFKB1 nuclear factor NF-kappa-B p50 subunit and NFKB2 nuclear factor NF-kappa-B p52 subunit. Ref.4

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Highly expressed in spleen, testis and lung, followed by kidney, pancreas, heart, placenta and brain. Also expressed in granulocytes and macrophages.

Post-translational modification

Serine phosphorylated; followed by proteasome-dependent degradation.

Sequence similarities

Belongs to the NF-kappa-B inhibitor family.

Contains 6 ANK repeats.

Sequence caution

The sequence AAC51216.1 differs from that shown. Reason: Frameshift at positions 339 and 351.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 500500NF-kappa-B inhibitor epsilon
PRO_0000067007

Regions

Repeat258 – 29134ANK 1
Repeat293 – 32230ANK 2
Repeat326 – 35530ANK 3
Repeat369 – 39830ANK 4
Repeat403 – 43230ANK 5
Repeat436 – 46530ANK 6

Amino acid modifications

Modified residue1571Phosphoserine Probable
Modified residue1611Phosphoserine Probable

Natural variations

Natural variant951H → Q.
Corresponds to variant rs28362857 [ dbSNP | Ensembl ].
VAR_046631
Natural variant1941V → A.
Corresponds to variant rs2233434 [ dbSNP | Ensembl ].
VAR_046632

Experimental info

Mutagenesis1451K → R: No effect. Ref.1
Mutagenesis1571S → A: No degradation. Ref.1
Mutagenesis1611S → A: No degradation. Ref.1
Sequence conflict63 – 642PA → RP in AAC51216. Ref.1
Sequence conflict1011P → R in AAC51216. Ref.1
Sequence conflict2331A → P in AAC51216. Ref.1
Sequence conflict4021T → S in AAC51216. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O00221 [UniParc].

Last modified September 23, 2008. Version 3.
Checksum: 45E726E7A0E8D478

FASTA50052,864
        10         20         30         40         50         60 
MNQRRSESRP GNHRLQAYAE PGKGDSGGAG PLSGSARRGR GGGGAIRVRR PCWSGGAGRG 

        70         80         90        100        110        120 
GGPAWAVRLP TVTAGWTWPA LRTLSSLRAG PSEPHSPGRR PPRAGRPLCQ ADPQPGKAAR 

       130        140        150        160        170        180 
RSLEPDPAQT GPRPARAAGM SEARKGPDEA EESQYDSGIE SLRSLRSLPE STSAPASGPS 

       190        200        210        220        230        240 
DGSPQPCTHP PGPVKEPQEK EDADGERADS TYGSSSLTYT LSLLGGPEAE DPAPRLPLPH 

       250        260        270        280        290        300 
VGALSPQQLE ALTYISEDGD TLVHLAVIHE APAVLLCCLA LLPQEVLDIQ NNLYQTALHL 

       310        320        330        340        350        360 
AVHLDQPGAV RALVLKGASR ALQDRHGDTA LHVACQRQHL ACARCLLEGR PEPGRGTSHS 

       370        380        390        400        410        420 
LDLQLQNWQG LACLHIATLQ KNQPLMELLL RNGADIDVQE GTSGKTALHL AVETQERGLV 

       430        440        450        460        470        480 
QFLLQAGAQV DARMLNGCTP LHLAAGRGLM GISSTLCKAG ADSLLRNVED ETPQDLTEES 

       490        500 
LVLLPFDDLK ISGKLLLCTD 

« Hide

References

« Hide 'large scale' references
[1]"IkappaB epsilon, a novel member of the IkappaB family, controls RelA and cRel NF-kappaB activity."
Whiteside S.T., Epinat J.-C., Rice N.R., Israel A.
EMBO J. 16:1413-1426(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF LYS-145; SER-157 AND SER-161.
Tissue: Fetal brain.
[2]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]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].
[4]"A new member of the IkappaB protein family, IkappaB epsilon, inhibits RelA (p65)-mediated NF-kappaB transcription."
Li Z., Nabel G.J.
Mol. Cell. Biol. 17:6184-6190(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 140-500, FUNCTION, INTERACTION WITH RELA; REL; NFKB1 AND NFKB2.
Tissue: B-cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U91616 mRNA. Translation: AAC51216.1. Frameshift.
AL139392 Genomic DNA. Translation: CAI20103.1.
CH471081 Genomic DNA. Translation: EAX04262.1.
CCDSCCDS34463.1.
RefSeqNP_004547.2. NM_004556.2.
UniGeneHs.458276.

3D structure databases

ProteinModelPortalO00221.
SMRO00221. Positions 257-473.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110861. 12 interactions.
DIPDIP-27533N.
IntActO00221. 13 interactions.
MINTMINT-1134068.
STRING9606.ENSP00000275015.

Chemistry

BindingDBO00221.

PTM databases

PhosphoSiteO00221.

Proteomic databases

MaxQBO00221.
PaxDbO00221.
PRIDEO00221.

Protocols and materials databases

DNASU4794.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000275015; ENSP00000275015; ENSG00000146232.
GeneID4794.
KEGGhsa:4794.
UCSCuc003oxe.1. human.

Organism-specific databases

CTD4794.
GeneCardsGC06M044226.
H-InvDBHIX0200879.
HGNCHGNC:7799. NFKBIE.
HPACAB010272.
HPA002692.
HPA005941.
MIM604548. gene.
neXtProtNX_O00221.
PharmGKBPA31603.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOGENOMHOG000059576.
HOVERGENHBG108320.
InParanoidO00221.
KOK05872.
OMAKNQPLME.
PhylomeDBO00221.
TreeFamTF320166.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressO00221.
BgeeO00221.
CleanExHS_NFKBIE.
GenevestigatorO00221.

Family and domain databases

Gene3D1.25.40.20. 1 hit.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamPF00023. Ank. 5 hits.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 6 hits.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiNFKBIE.
GenomeRNAi4794.
NextBio18476.
PROO00221.
SOURCESearch...

Entry information

Entry nameIKBE_HUMAN
AccessionPrimary (citable) accession number: O00221
Secondary accession number(s): Q5T9V9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: September 23, 2008
Last modified: July 9, 2014
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM