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O00221

- IKBE_HUMAN

UniProt

O00221 - IKBE_HUMAN

Protein

NF-kappa-B inhibitor epsilon

Gene

NFKBIE

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 3 (23 Sep 2008)
      Previous versions | rss
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    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. cytoplasmic sequestering of transcription factor Source: ProtInc
    2. D-serine transport Source: Ensembl

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

    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 epsilonPRO_0000067007Add
    BLAST

    Amino acid modifications

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

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

    Structurei

    3D structure databases

    ProteinModelPortaliO00221.
    SMRiO00221. Positions 257-473.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti63 – 642PA → RP in AAC51216. (PubMed:9135156)Curated
    Sequence conflicti101 – 1011P → R in AAC51216. (PubMed:9135156)Curated
    Sequence conflicti233 – 2331A → P in AAC51216. (PubMed:9135156)Curated
    Sequence conflicti402 – 4021T → S in AAC51216. (PubMed:9135156)Curated

    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 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. 13 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

    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: October 1, 2014
    This is version 135 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