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P25963

- IKBA_HUMAN

UniProt

P25963 - IKBA_HUMAN

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Protein

NF-kappa-B inhibitor alpha

Gene

NFKBIA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Inhibits the activity of dimeric NF-kappa-B/REL complexes by trapping REL dimers in the cytoplasm through masking of their nuclear localization signals. On cellular stimulation by immune and proinflammatory responses, becomes phosphorylated promoting ubiquitination and degradation, enabling the dimeric RELA to translocate to the nucleus and activate transcription.1 Publication

GO - Molecular functioni

  1. enzyme binding Source: UniProtKB
  2. identical protein binding Source: IntAct
  3. NF-kappaB binding Source: UniProtKB
  4. nuclear localization sequence binding Source: UniProtKB
  5. transcription factor binding Source: ProtInc
  6. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: ProtInc
  2. cellular response to cold Source: BHF-UCL
  3. cytoplasmic sequestering of NF-kappaB Source: BHF-UCL
  4. cytoplasmic sequestering of transcription factor Source: UniProtKB
  5. Fc-epsilon receptor signaling pathway Source: Reactome
  6. innate immune response Source: Reactome
  7. lipopolysaccharide-mediated signaling pathway Source: Ensembl
  8. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  9. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  10. negative regulation of apoptotic process Source: Reactome
  11. negative regulation of DNA binding Source: UniProtKB
  12. negative regulation of lipid storage Source: BHF-UCL
  13. negative regulation of macrophage derived foam cell differentiation Source: BHF-UCL
  14. negative regulation of myeloid cell differentiation Source: Ensembl
  15. negative regulation of NF-kappaB transcription factor activity Source: MGI
  16. negative regulation of Notch signaling pathway Source: Ensembl
  17. neurotrophin TRK receptor signaling pathway Source: Reactome
  18. nucleotide-binding oligomerization domain containing 1 signaling pathway Source: Ensembl
  19. nucleotide-binding oligomerization domain containing 2 signaling pathway Source: Ensembl
  20. positive regulation of cellular protein metabolic process Source: BHF-UCL
  21. positive regulation of cholesterol efflux Source: BHF-UCL
  22. positive regulation of NF-kappaB transcription factor activity Source: Reactome
  23. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  24. positive regulation of type I interferon production Source: Reactome
  25. protein import into nucleus, translocation Source: Ensembl
  26. regulation of cell proliferation Source: Ensembl
  27. regulation of NF-kappaB import into nucleus Source: UniProtKB
  28. response to exogenous dsRNA Source: Ensembl
  29. response to muramyl dipeptide Source: Ensembl
  30. T cell receptor signaling pathway Source: Reactome
  31. toll-like receptor 10 signaling pathway Source: Reactome
  32. toll-like receptor 2 signaling pathway Source: Reactome
  33. toll-like receptor 3 signaling pathway Source: Reactome
  34. toll-like receptor 4 signaling pathway Source: Reactome
  35. toll-like receptor 5 signaling pathway Source: Reactome
  36. toll-like receptor 9 signaling pathway Source: Reactome
  37. toll-like receptor signaling pathway Source: Reactome
  38. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  39. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  40. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
  41. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_12555. Downstream TCR signaling.
REACT_13696. NF-kB is activated and signals survival.
REACT_163994. FCERI mediated NF-kB activation.
REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_24969. TRAF6 mediated NF-kB activation.
SABIO-RKP25963.
SignaLinkiP25963.

Names & Taxonomyi

Protein namesi
Recommended name:
NF-kappa-B inhibitor alpha
Alternative name(s):
I-kappa-B-alpha
Short name:
IkB-alpha
Short name:
IkappaBalpha
Major histocompatibility complex enhancer-binding protein MAD3
Gene namesi
Name:NFKBIA
Synonyms:IKBA, MAD3, NFKBI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:7797. NFKBIA.

Subcellular locationi

Cytoplasm. Nucleus
Note: Shuttles between the nucleus and the cytoplasm by a nuclear localization signal (NLS) and a CRM1-dependent nuclear export.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. I-kappaB/NF-kappaB complex Source: BHF-UCL
  4. nucleus Source: UniProtKB
  5. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Ectodermal dysplasia, anhidrotic, with T-cell immunodeficiency autosomal dominant (ADEDAID) [MIM:612132]: A form of ectoderma dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. This form of ectodermal dysplasia is associated with decreased production of pro-inflammatory cytokines and certain interferons, rendering patients susceptible to infection.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321S → I in ADEDAID. 1 Publication
Corresponds to variant rs28933100 [ dbSNP | Ensembl ].
VAR_034871

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi21 – 211K → R: Little change in Tax-stimulated transactivation. No sumoylation. Greatly reduced Tax- or cytokine-stimulated transactivation and decrease in ubiquitination and degradation; when associated with R-22. 4 Publications
Mutagenesisi22 – 221K → R: Little change in Tax-stimulated transactivation. No sumoylation. Greatly reduced Tax- or cytokine-stimulated transactivation and decrease in ubiquitination and degradation; when associated with R-21. 4 Publications
Mutagenesisi31 – 311D → A: Loss of phosphorylation; when associated with A-35. 1 Publication
Mutagenesisi32 – 321S → A: Loss of phosphorylation, ubiquitination and degradation; when associated with A-36. 2 Publications
Mutagenesisi32 – 321S → T: Decrease in phosphorylation and degradation; when associated with T-36. 2 Publications
Mutagenesisi35 – 351D → A: Loss in phosphorylation; when associated with A-31. 1 Publication
Mutagenesisi35 – 351D → G: No change neither in phosphorylation, nor on degradation. 1 Publication
Mutagenesisi36 – 361S → A: Loss of phosphorylation, ubiquitination, and degradation; when associated with A-32. 2 Publications
Mutagenesisi36 – 361S → T: Decrease in phosphorylation and degradation; when associated with T-32. 2 Publications
Mutagenesisi38 – 381K → R: No change in Tax-stimulated transactivation. No change in Tax-stimulated transactivation; when associated with R-47. 1 Publication
Mutagenesisi42 – 421Y → F: No phosphorylation. 1 Publication
Mutagenesisi45 – 528MVKELQEI → AAKEAQEA: No nuclear export. 1 Publication
Mutagenesisi47 – 471K → R: Little change in Tax-stimulated transactivation. No change in Tax-stimulated transactivation; when associated with R-38. 1 Publication
Mutagenesisi115 – 1206LHLAVI → AHAAVA: Greatly reduced nuclear localization. Great reduction in its ability to inhibit DNA binding of RELA. 1 Publication
Mutagenesisi210 – 2101N → A: Almost abolished ability to inhibit NF-kappa-B DNA-binding activity; when associated with A-244. 1 Publication
Mutagenesisi234 – 2341S → A: No inducible ubiquitination nor protein degradation. 1 Publication
Mutagenesisi244 – 2441N → A: Almost abolished ability to inhibit NF-kappa-B DNA-binding activity; when associated with A-210. 1 Publication
Mutagenesisi262 – 2621S → A: No inducible ubiquitination nor protein degradation. 1 Publication
Mutagenesisi263 – 2631T → A: No inducible ubiquitination nor protein degradation. 1 Publication

Keywords - Diseasei

Disease mutation, Ectodermal dysplasia

Organism-specific databases

MIMi612132. phenotype.
Orphaneti251579. Giant cell glioblastoma.
251576. Gliosarcoma.
98813. Hypohidrotic ectodermal dysplasia with immunodeficiency.
PharmGKBiPA31601.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 317317NF-kappa-B inhibitor alphaPRO_0000066999Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki21 – 21Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO or ubiquitin)2 Publications
Cross-linki22 – 22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Modified residuei32 – 321Phosphoserine; by IKKA and IKKE2 Publications
Modified residuei36 – 361Phosphoserine; by IKKA, IKKB, IKKE and TBK12 Publications
Modified residuei42 – 421Phosphotyrosine; by Tyr-kinases1 Publication
Modified residuei210 – 2101(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
Modified residuei244 – 2441(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
Modified residuei283 – 2831Phosphoserine; by CK22 Publications
Modified residuei288 – 2881Phosphoserine; by CK21 Publication
Modified residuei291 – 2911Phosphothreonine; by CK22 Publications
Modified residuei293 – 2931Phosphoserine; by CK21 Publication
Modified residuei299 – 2991Phosphothreonine; by CK21 Publication

Post-translational modificationi

Phosphorylated; disables inhibition of NF-kappa-B DNA-binding activity. Phosphorylation at positions 32 and 36 is prerequisite to recognition by UBE2D3 leading to polyubiquitination and subsequent degradation.3 Publications
Sumoylated; sumoylation requires the presence of the nuclear import signal. Sumoylation blocks ubiquitination and proteasome-mediated degradation of the protein thereby increasing the protein stability.3 Publications
Monoubiquitinated at Lys-21 and/or Lys-22 by UBE2D3. Ubiquitin chain elongation is then performed by CDC34 in cooperation with the SCF(FBXW11) E3 ligase complex, building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. The resulting polyubiquitination leads to protein degradation. Also ubiquitinated by SCF(BTRC) following stimulus-dependent phosphorylation at Ser-32 and Ser-36.5 Publications
Deubiquitinated by porcine reproductive and respiratory syndrome virus Nsp2 protein, which thereby interferes with NFKBIA degradation and impairs subsequent NF-kappa-B activation.

Keywords - PTMi

Hydroxylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP25963.
PaxDbiP25963.
PeptideAtlasiP25963.
PRIDEiP25963.

PTM databases

PhosphoSiteiP25963.

Miscellaneous databases

PMAP-CutDBP25963.

Expressioni

Inductioni

Induced in adherent monocytes.

Gene expression databases

BgeeiP25963.
CleanExiHS_NFKBIA.
ExpressionAtlasiP25963. baseline and differential.
GenevestigatoriP25963.

Organism-specific databases

HPAiCAB003815.
HPA029207.

Interactioni

Subunit structurei

Interacts with RELA; the interaction requires the nuclear import signal. Interacts with NKIRAS1 and NKIRAS2. Part of a 70-90 kDa complex at least consisting of CHUK, IKBKB, NFKBIA, RELA, IKBKAP and MAP3K14. Interacts with HBV protein X. Interacts with isoform 1 and isoform 2 of RWDD3; the interaction enhances sumoylation. Interacts (when phosphorylated at the 2 serine residues in the destruction motif D-S-G-X(2,3,4)-S) with BTRC. Associates with the SCF(BTRC) complex, composed of SKP1, CUL1 and BTRC; the association is mediated via interaction with BTRC. Part of a SCF(BTRC)-like complex lacking CUL1, which is associated with RELA; RELA interacts directly with NFKBIA. Interacts with PRMT2. Interacts with PRKACA in platelets; this interaction is disrupted by thrombin and collagen. Interacts with HIF1AN. Interacts with MEFV.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-307386,EBI-307386
CHUKO1511114EBI-307386,EBI-81249
ChukQ60680-22EBI-307386,EBI-646264From a different organism.
COMMD1Q8N6683EBI-307386,EBI-1550112
IKBKBO1492012EBI-307386,EBI-81266
IKBKGQ9Y6K95EBI-307386,EBI-81279
NFKB1P198382EBI-307386,EBI-300010
RELAQ0420614EBI-307386,EBI-73886
RPS3P233966EBI-307386,EBI-351193
UBCP0CG483EBI-307386,EBI-3390054
UL54Q9J0X93EBI-307386,EBI-7967856From a different organism.

Protein-protein interaction databases

BioGridi110859. 133 interactions.
DIPiDIP-139N.
IntActiP25963. 45 interactions.
MINTiMINT-120458.
STRINGi9606.ENSP00000216797.

Structurei

Secondary structure

1
317
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni72 – 743
Helixi79 – 835
Beta strandi87 – 915
Helixi101 – 1044
Helixi114 – 1207
Helixi124 – 1285
Helixi147 – 1548
Helixi157 – 1659
Turni167 – 1704
Beta strandi171 – 1733
Helixi175 – 1773
Helixi186 – 1927
Helixi196 – 20510
Turni214 – 2163
Helixi220 – 2267
Helixi230 – 2378
Turni238 – 2403
Helixi253 – 2564
Helixi263 – 2708
Helixi275 – 2773
Turni285 – 2873

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IKNX-ray2.30D67-302[»]
1NFIX-ray2.70E/F70-282[»]
DisProtiDP00468.
ProteinModelPortaliP25963.
SMRiP25963. Positions 40-281.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25963.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati73 – 10331ANK 1Add
BLAST
Repeati110 – 13930ANK 2Add
BLAST
Repeati143 – 17230ANK 3Add
BLAST
Repeati182 – 21130ANK 4Add
BLAST
Repeati216 – 24530ANK 5Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi30 – 367Destruction motif
Motifi45 – 5410Nuclear export signal
Motifi110 – 12011Nuclear import signalAdd
BLAST

Sequence similaritiesi

Belongs to the NF-kappa-B inhibitor family.Curated
Contains 5 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00550000074527.
HOGENOMiHOG000059576.
HOVERGENiHBG018875.
InParanoidiP25963.
KOiK04734.
OMAiSIHGYLA.
OrthoDBiEOG7W154S.
PhylomeDBiP25963.
TreeFamiTF320166.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF00023. Ank. 4 hits.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 5 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25963 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFQAAERPQE WAMEGPRDGL KKERLLDDRH DSGLDSMKDE EYEQMVKELQ
60 70 80 90 100
EIRLEPQEVP RGSEPWKQQL TEDGDSFLHL AIIHEEKALT MEVIRQVKGD
110 120 130 140 150
LAFLNFQNNL QQTPLHLAVI TNQPEIAEAL LGAGCDPELR DFRGNTPLHL
160 170 180 190 200
ACEQGCLASV GVLTQSCTTP HLHSILKATN YNGHTCLHLA SIHGYLGIVE
210 220 230 240 250
LLVSLGADVN AQEPCNGRTA LHLAVDLQNP DLVSLLLKCG ADVNRVTYQG
260 270 280 290 300
YSPYQLTWGR PSTRIQQQLG QLTLENLQML PESEDEESYD TESEFTEFTE
310
DELPYDDCVF GGQRLTL
Length:317
Mass (Da):35,609
Last modified:May 1, 1992 - v1
Checksum:i088B313226786395
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321S → I in ADEDAID. 1 Publication
Corresponds to variant rs28933100 [ dbSNP | Ensembl ].
VAR_034871

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M69043 mRNA. Translation: AAA16489.1.
AJ249294
, AJ249295, AJ249283, AJ249284, AJ249285, AJ249286 Genomic DNA. Translation: CAB65556.2.
AY033600 mRNA. Translation: AAK51149.1.
BT007091 mRNA. Translation: AAP35754.1.
AY496422 Genomic DNA. Translation: AAR29599.1.
AK313421 mRNA. Translation: BAG36213.1.
AL133163 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65875.1.
BC002601 mRNA. Translation: AAH02601.1.
BC004983 mRNA. Translation: AAH04983.1.
CCDSiCCDS9656.1.
PIRiA39935.
RefSeqiNP_065390.1. NM_020529.2.
UniGeneiHs.81328.

Genome annotation databases

EnsembliENST00000216797; ENSP00000216797; ENSG00000100906.
GeneIDi4792.
KEGGihsa:4792.
UCSCiuc001wtf.4. human.

Polymorphism databases

DMDMi126682.

Cross-referencesi

Web resourcesi

NFKBIAbase

NFKBIA mutation db

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M69043 mRNA. Translation: AAA16489.1 .
AJ249294
, AJ249295 , AJ249283 , AJ249284 , AJ249285 , AJ249286 Genomic DNA. Translation: CAB65556.2 .
AY033600 mRNA. Translation: AAK51149.1 .
BT007091 mRNA. Translation: AAP35754.1 .
AY496422 Genomic DNA. Translation: AAR29599.1 .
AK313421 mRNA. Translation: BAG36213.1 .
AL133163 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW65875.1 .
BC002601 mRNA. Translation: AAH02601.1 .
BC004983 mRNA. Translation: AAH04983.1 .
CCDSi CCDS9656.1.
PIRi A39935.
RefSeqi NP_065390.1. NM_020529.2.
UniGenei Hs.81328.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IKN X-ray 2.30 D 67-302 [» ]
1NFI X-ray 2.70 E/F 70-282 [» ]
DisProti DP00468.
ProteinModelPortali P25963.
SMRi P25963. Positions 40-281.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110859. 133 interactions.
DIPi DIP-139N.
IntActi P25963. 45 interactions.
MINTi MINT-120458.
STRINGi 9606.ENSP00000216797.

Chemistry

BindingDBi P25963.
ChEMBLi CHEMBL2898.
DrugBanki DB00945. Acetylsalicylic acid.

PTM databases

PhosphoSitei P25963.

Polymorphism databases

DMDMi 126682.

Proteomic databases

MaxQBi P25963.
PaxDbi P25963.
PeptideAtlasi P25963.
PRIDEi P25963.

Protocols and materials databases

DNASUi 4792.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216797 ; ENSP00000216797 ; ENSG00000100906 .
GeneIDi 4792.
KEGGi hsa:4792.
UCSCi uc001wtf.4. human.

Organism-specific databases

CTDi 4792.
GeneCardsi GC14M035870.
HGNCi HGNC:7797. NFKBIA.
HPAi CAB003815.
HPA029207.
MIMi 164008. gene.
612132. phenotype.
neXtProti NX_P25963.
Orphaneti 251579. Giant cell glioblastoma.
251576. Gliosarcoma.
98813. Hypohidrotic ectodermal dysplasia with immunodeficiency.
PharmGKBi PA31601.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0666.
GeneTreei ENSGT00550000074527.
HOGENOMi HOG000059576.
HOVERGENi HBG018875.
InParanoidi P25963.
KOi K04734.
OMAi SIHGYLA.
OrthoDBi EOG7W154S.
PhylomeDBi P25963.
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_12555. Downstream TCR signaling.
REACT_13696. NF-kB is activated and signals survival.
REACT_163994. FCERI mediated NF-kB activation.
REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_24969. TRAF6 mediated NF-kB activation.
SABIO-RK P25963.
SignaLinki P25963.

Miscellaneous databases

ChiTaRSi NFKBIA. human.
EvolutionaryTracei P25963.
GeneWikii I%CE%BAB%CE%B1.
GenomeRNAii 4792.
NextBioi 18466.
PMAP-CutDB P25963.
PROi P25963.
SOURCEi Search...

Gene expression databases

Bgeei P25963.
CleanExi HS_NFKBIA.
ExpressionAtlasi P25963. baseline and differential.
Genevestigatori P25963.

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. 4 hits.
[Graphical view ]
PRINTSi PR01415. ANKYRIN.
SMARTi SM00248. ANK. 5 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. "Characterization of an immediate-early gene induced in adherent monocytes that encodes I kappa B-like activity."
    Haskill S., Beg A.A., Tompkins S.M., Morris J.S., Yurochko A.D., Sampson-Johannes A., Mondal K., Ralph P., Baldwin A.S. Jr.
    Cell 65:1281-1289(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Monocyte.
  2. "Clonal deleterious mutations in the IkappaB alpha gene in the malignant cells in Hodgkin's lymphoma."
    Jungnickel B., Staratschek-Jox A., Braeuninger A., Spieker T., Wolf J., Diehl V., Hansmann M.-L., Rajewsky K., Kueppers R.
    J. Exp. Med. 191:395-402(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Lymph node.
  3. "Homo sapiens IkBa mRNA."
    Liu B., Huang A.
    Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. SeattleSNPs variation discovery resource
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "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].
    Tissue: Cerebellum.
  7. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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].
    Tissue: Brain and Kidney.
  10. "I kappa B/MAD-3 masks the nuclear localization signal of NF-kappa B p65 and requires the transactivation domain to inhibit NF-kappa B p65 DNA binding."
    Ganchi P.A., Sun S.C., Greene W.C., Ballard D.W.
    Mol. Biol. Cell 3:1339-1352(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RELA.
  11. "Signal-induced degradation of IkappaB alpha requires site-specific ubiquitination."
    Scherer D.C., Brockman J.A., Chen Z., Maniatis T., Ballard D.W.
    Proc. Natl. Acad. Sci. U.S.A. 92:11259-11263(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-21 AND LYS-22, FUNCTION, MUTAGENESIS OF LYS-21; LYS-22; LYS-38 AND LYS-47.
  12. "Tyrosine phosphorylation of IkappaB-alpha activates NF-kappaB without proteolytic degradation of IkappaB-alpha."
    Imbert V., Rupec R.A., Livolsi A., Pahl H.L., Traenckner E.B.-M., Mueller-Dieckmann C., Farahifar D., Rossi B., Auberger P., Baeuerle P.A., Peyron J.-F.
    Cell 86:787-798(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-42, MUTAGENESIS OF TYR-42.
  13. "Casein kinase II phosphorylates I kappa B alpha at S-283, S-289, S-293, and T-291 and is required for its degradation."
    McElhinny J.A., Trushin S.A., Bren G.D., Chester N., Paya C.V.
    Mol. Cell. Biol. 16:899-906(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-283; SER-288; SER-293 AND THR-291.
  14. "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 LYS-21; LYS-22; ASP-31; SER-32; ASP-35; SER-36; SER-234; SER-262 AND THR-263.
  15. "Phosphorylation of IkappaBalpha in the C-terminal PEST domain by casein kinase II affects intrinsic protein stability."
    Lin R., Beauparlant P., Makris C., Meloche S., Hiscott J.
    Mol. Cell. Biol. 16:1401-1409(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-291; SER-283 AND THR-299.
  16. "Nuclear localization of IkappaB alpha is mediated by the second ankyrin repeat: the IkappaB alpha ankyrin repeats define a novel class of cis-acting nuclear import sequences."
    Sachdev S., Hoffmann A., Hannink M.
    Mol. Cell. Biol. 18:2524-2534(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF 115-LEU--ILE-120.
  17. "A complex containing betaTrCP recruits Cdc34 to catalyse ubiquitination of IkappaBalpha."
    Vuillard L., Nicholson J., Hay R.T.
    FEBS Lett. 455:311-314(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION BY THE SCF(FBXW11) COMPLEX.
  18. "Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IkappaBalpha."
    Gonen H., Bercovich B., Orian A., Carrano A., Takizawa C., Yamanaka K., Pagano M., Iwai K., Ciechanover A.
    J. Biol. Chem. 274:14823-14830(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-32 AND SER-36, MUTAGENESIS OF SER-32 AND SER-36, UBIQUITINATION BY UBE2D2 AND UBE2D3.
  19. "Direct association and nuclear import of the hepatitis B virus X protein with the NF-kappaB inhibitor IkappaBalpha."
    Weil R., Sirma H., Giannini C., Kremsdorf D., Bessia C., Dargemont C., Brechot C., Israel A.
    Mol. Cell. Biol. 19:6345-6354(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HBV PROTEIN X.
  20. "IKK epsilon is part of a novel PMA-inducible IkappaB kinase complex."
    Peters R.T., Liao S.-M., Maniatis T.
    Mol. Cell 5:513-522(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-32 AND SER-36.
  21. Cited for: PHOSPHORYLATION BY TBK1.
  22. "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.
  23. "A nuclear export signal in the N-terminal regulatory domain of IkappaBalpha controls cytoplasmic localization of inactive NF-kappaB/IkappaBalpha complexes."
    Huang T.T., Kudo N., Yoshida M., Miyamoto S.
    Proc. Natl. Acad. Sci. U.S.A. 97:1014-1019(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNAL, MUTAGENESIS OF 45-MET--ILE-52.
  24. "SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting."
    Rodriguez M.S., Dargemont C., Hay R.T.
    J. Biol. Chem. 276:12654-12659(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-21, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-21 AND LYS-22.
  25. "Thrombin and collagen induce a feedback inhibitory signaling pathway in platelets involving dissociation of the catalytic subunit of protein kinase A from an NFkappaB-IkappaB complex."
    Gambaryan S., Kobsar A., Rukoyatkina N., Herterich S., Geiger J., Smolenski A., Lohmann S.M., Walter U.
    J. Biol. Chem. 285:18352-18363(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRKACA.
  26. "Protein methyltransferase 2 inhibits NF-kappaB function and promotes apoptosis."
    Ganesh L., Yoshimoto T., Moorthy N.C., Akahata W., Boehm M., Nabel E.G., Nabel G.J.
    Mol. Cell. Biol. 26:3864-3874(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRMT2, SUBCELLULAR LOCATION.
  27. "Posttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH)."
    Cockman M.E., Lancaster D.E., Stolze I.P., Hewitson K.S., McDonough M.A., Coleman M.L., Coles C.H., Yu X., Hay R.T., Ley S.C., Pugh C.W., Oldham N.J., Masson N., Schofield C.J., Ratcliffe P.J.
    Proc. Natl. Acad. Sci. U.S.A. 103:14767-14772(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIF1AN, HYDROXYLATION AT ASN-210 AND ASN-244, MUTAGENESIS OF ASN-210 AND ASN-244.
  28. "RSUME, a small RWD-containing protein, enhances SUMO conjugation and stabilizes HIF-1alpha during hypoxia."
    Carbia-Nagashima A., Gerez J., Perez-Castro C., Paez-Pereda M., Silberstein S., Stalla G.K., Holsboer F., Arzt E.
    Cell 131:309-323(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RWDD3, SUMOYLATION, MUTAGENESIS OF LYS-21 AND LSY-22.
  29. "The familial Mediterranean fever protein, pyrin, is cleaved by caspase-1 and activates NF-kappaB through its N-terminal fragment."
    Chae J.J., Wood G., Richard K., Jaffe H., Colburn N.T., Masters S.L., Gumucio D.L., Shoham N.G., Kastner D.L.
    Blood 112:1794-1803(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MEFV.
  30. "Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for polyubiquitination on a SCF substrate."
    Wu K., Kovacev J., Pan Z.Q.
    Mol. Cell 37:784-796(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-21 AND LYS-22.
  31. "The cysteine protease domain of porcine reproductive and respiratory syndrome virus nonstructural protein 2 possesses deubiquitinating and interferon antagonism functions."
    Sun Z., Chen Z., Lawson S.R., Fang Y.
    J. Virol. 84:7832-7846(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEUBIQUITINATION BY PORCINE REPRODUCTIVE AND RESPIRATORY SYNDROME VIRUS NSP2 PROTEIN.
  32. "In silico structural and functional characterization of the RSUME splice variants."
    Gerez J., Fuertes M., Tedesco L., Silberstein S., Sevlever G., Paez-Pereda M., Holsboer F., Turjanski A.G., Arzt E.
    PLoS ONE 8:E57795-E57795(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RWDD3.
  33. "Structure of an IkappaBalpha/NF-kappaB complex."
    Jacobs M.D., Harrison S.C.
    Cell 95:749-758(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 70-282.
  34. "The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation."
    Huxford T., Huang D.B., Malek S., Ghosh G.
    Cell 95:759-770(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 73-302.
  35. Cited for: VARIANT ADEDAID ILE-32.
  36. "A novel mutation in NFKBIA/IKBA results in a degradation-resistant N-truncated protein and is associated with ectodermal dysplasia with immunodeficiency."
    Lopez-Granados E., Keenan J.E., Kinney M.C., Leo H., Jain N., Ma C.A., Quinones R., Gelfand E.W., Jain A.
    Hum. Mutat. 29:861-868(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN ADEDAID.

Entry informationi

Entry nameiIKBA_HUMAN
AccessioniPrimary (citable) accession number: P25963
Secondary accession number(s): B2R8L6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: October 29, 2014
This is version 168 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3