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O00221

- IKBE_HUMAN

UniProt

O00221 - IKBE_HUMAN

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Protein
NF-kappa-B inhibitor epsilon
Gene
NFKBIE, IKBE
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. Inhibits DNA-binding of NF-kappa-B p50-p65 and p50-c-Rel complexes.1 Publication

GO - Molecular functioni

  1. protein binding Source: IntAct

GO - Biological processi

  1. D-serine transport Source: Ensembl
  2. cytoplasmic sequestering of transcription factor Source: ProtInc
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_118656. Activation of NF-kappaB in B cells.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:NFKBIE
Synonyms:IKBE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:7799. NFKBIE.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. Golgi apparatus Source: Ensembl
  2. cytoplasm Source: ProtInc
  3. cytosol Source: Reactome
  4. perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi145 – 1451K → R: No effect. 1 Publication
Mutagenesisi157 – 1571S → A: No degradation. 1 Publication
Mutagenesisi161 – 1611S → A: No degradation. 1 Publication

Organism-specific databases

PharmGKBiPA31603.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 500500NF-kappa-B inhibitor epsilon
PRO_0000067007Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei157 – 1571Phosphoserine Inferred
Modified residuei161 – 1611Phosphoserine Inferred

Post-translational modificationi

Serine phosphorylated; followed by proteasome-dependent degradation.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO00221.
PaxDbiO00221.
PRIDEiO00221.

PTM databases

PhosphoSiteiO00221.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiO00221.
BgeeiO00221.
CleanExiHS_NFKBIE.
GenevestigatoriO00221.

Organism-specific databases

HPAiCAB010272.
HPA002692.
HPA005941.

Interactioni

Subunit structurei

Interacts with RELA, REL, NFKB1 nuclear factor NF-kappa-B p50 subunit and NFKB2 nuclear factor NF-kappa-B p52 subunit.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ANKHD1Q8IWZ32EBI-355098,EBI-359558
PPP6R1Q9UPN72EBI-355098,EBI-359745
PPP6R2O751702EBI-355098,EBI-359739

Protein-protein interaction databases

BioGridi110861. 12 interactions.
DIPiDIP-27533N.
IntActiO00221. 13 interactions.
MINTiMINT-1134068.
STRINGi9606.ENSP00000275015.

Structurei

3D structure databases

ProteinModelPortaliO00221.
SMRiO00221. Positions 257-473.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati258 – 29134ANK 1
Add
BLAST
Repeati293 – 32230ANK 2
Add
BLAST
Repeati326 – 35530ANK 3
Add
BLAST
Repeati369 – 39830ANK 4
Add
BLAST
Repeati403 – 43230ANK 5
Add
BLAST
Repeati436 – 46530ANK 6
Add
BLAST

Sequence similaritiesi

Contains 6 ANK repeats.

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiCOG0666.
HOGENOMiHOG000059576.
HOVERGENiHBG108320.
InParanoidiO00221.
KOiK05872.
OMAiKNQPLME.
PhylomeDBiO00221.
TreeFamiTF320166.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF00023. Ank. 5 hits.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 6 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O00221-1 [UniParc]FASTAAdd to Basket

« Hide

MNQRRSESRP GNHRLQAYAE PGKGDSGGAG PLSGSARRGR GGGGAIRVRR    50
PCWSGGAGRG GGPAWAVRLP TVTAGWTWPA LRTLSSLRAG PSEPHSPGRR 100
PPRAGRPLCQ ADPQPGKAAR RSLEPDPAQT GPRPARAAGM SEARKGPDEA 150
EESQYDSGIE SLRSLRSLPE STSAPASGPS DGSPQPCTHP PGPVKEPQEK 200
EDADGERADS TYGSSSLTYT LSLLGGPEAE DPAPRLPLPH VGALSPQQLE 250
ALTYISEDGD TLVHLAVIHE APAVLLCCLA LLPQEVLDIQ NNLYQTALHL 300
AVHLDQPGAV RALVLKGASR ALQDRHGDTA LHVACQRQHL ACARCLLEGR 350
PEPGRGTSHS LDLQLQNWQG LACLHIATLQ KNQPLMELLL RNGADIDVQE 400
GTSGKTALHL AVETQERGLV QFLLQAGAQV DARMLNGCTP LHLAAGRGLM 450
GISSTLCKAG ADSLLRNVED ETPQDLTEES LVLLPFDDLK ISGKLLLCTD 500
Length:500
Mass (Da):52,864
Last modified:September 23, 2008 - v3
Checksum:i45E726E7A0E8D478
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti95 – 951H → Q.
Corresponds to variant rs28362857 [ dbSNP | Ensembl ].
VAR_046631
Natural varianti194 – 1941V → A.
Corresponds to variant rs2233434 [ dbSNP | Ensembl ].
VAR_046632

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 642PA → RP in AAC51216. 1 Publication
Sequence conflicti101 – 1011P → R in AAC51216. 1 Publication
Sequence conflicti233 – 2331A → P in AAC51216. 1 Publication
Sequence conflicti402 – 4021T → S in AAC51216. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U91616 mRNA. Translation: AAC51216.1. Frameshift.
AL139392 Genomic DNA. Translation: CAI20103.1.
CH471081 Genomic DNA. Translation: EAX04262.1.
CCDSiCCDS34463.1.
RefSeqiNP_004547.2. NM_004556.2.
UniGeneiHs.458276.

Genome annotation databases

EnsembliENST00000275015; ENSP00000275015; ENSG00000146232.
GeneIDi4794.
KEGGihsa:4794.
UCSCiuc003oxe.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U91616 mRNA. Translation: AAC51216.1 . Frameshift.
AL139392 Genomic DNA. Translation: CAI20103.1 .
CH471081 Genomic DNA. Translation: EAX04262.1 .
CCDSi CCDS34463.1.
RefSeqi NP_004547.2. NM_004556.2.
UniGenei Hs.458276.

3D structure databases

ProteinModelPortali O00221.
SMRi O00221. Positions 257-473.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110861. 12 interactions.
DIPi DIP-27533N.
IntActi O00221. 13 interactions.
MINTi MINT-1134068.
STRINGi 9606.ENSP00000275015.

Chemistry

BindingDBi O00221.

PTM databases

PhosphoSitei O00221.

Proteomic databases

MaxQBi O00221.
PaxDbi O00221.
PRIDEi O00221.

Protocols and materials databases

DNASUi 4794.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000275015 ; ENSP00000275015 ; ENSG00000146232 .
GeneIDi 4794.
KEGGi hsa:4794.
UCSCi uc003oxe.1. human.

Organism-specific databases

CTDi 4794.
GeneCardsi GC06M044226.
H-InvDB HIX0200879.
HGNCi HGNC:7799. NFKBIE.
HPAi CAB010272.
HPA002692.
HPA005941.
MIMi 604548. gene.
neXtProti NX_O00221.
PharmGKBi PA31603.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0666.
HOGENOMi HOG000059576.
HOVERGENi HBG108320.
InParanoidi O00221.
KOi K05872.
OMAi KNQPLME.
PhylomeDBi O00221.
TreeFami TF320166.

Enzyme and pathway databases

Reactomei REACT_118656. Activation of NF-kappaB in B cells.

Miscellaneous databases

GeneWikii NFKBIE.
GenomeRNAii 4794.
NextBioi 18476.
PROi O00221.
SOURCEi Search...

Gene expression databases

ArrayExpressi O00221.
Bgeei O00221.
CleanExi HS_NFKBIE.
Genevestigatori O00221.

Family and domain databases

Gene3Di 1.25.40.20. 1 hit.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view ]
Pfami PF00023. Ank. 5 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. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiIKBE_HUMAN
AccessioniPrimary (citable) accession number: O00221
Secondary accession number(s): Q5T9V9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: September 23, 2008
Last modified: September 3, 2014
This is version 134 of the entry and version 3 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 6
    Human chromosome 6: 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

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