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Q14164

- IKKE_HUMAN

UniProt

Q14164 - IKKE_HUMAN

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Protein

Inhibitor of nuclear factor kappa-B kinase subunit epsilon

Gene
IKBKE, IKKE, IKKI, KIAA0151
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Serine/threonine kinase that plays an essential role in regulating inflammatory responses to viral infection, through the activation of the type I IFN, NF-kappa-B and STAT signaling. Also involved in TNFA and inflammatory cytokines, like Interleukin-1, signaling. Following activation of viral RNA sensors, such as RIG-I-like receptors, associates with DDX3X and phosphorylates interferon regulatory factors (IRFs), IRF3 and IRF7, as well as DDX3X. This activity allows subsequent homodimerization and nuclear translocation of the IRF3 leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNB. In order to establish such an antiviral state, IKBKE forms several different complexes whose composition depends on the type of cell and cellular stimuli. Thus, several scaffolding molecules including IPS1/MAVS, TANK, AZI2/NAP1 or TBKBP1/SINTBAD can be recruited to the IKBKE-containing-complexes. Activated by polyubiquitination in response to TNFA and interleukin-1, regulates the NF-kappa-B signaling pathway through, at least, the phosphorylation of CYLD. Phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. In addition, is also required for the induction of a subset of ISGs which displays antiviral activity, may be through the phosphorylation of STAT1 at 'Ser-708'. Phosphorylation of STAT1 at 'Ser-708' seems also to promote the assembly and DNA binding of ISGF3 (STAT1:STAT2:IRF9) complexes compared to GAF (STAT1:STAT1) complexes, in this way regulating the balance between type I and type II IFN responses. Protects cells against DNA damage-induced cell death. Also plays an important role in energy balance regulation by sustaining a state of chronic, low-grade inflammation in obesity, wich leads to a negative impact on insulin sensitivity. Phosphorylates AKT1.9 Publications

Catalytic activityi

ATP + [I-kappa-B protein] = ADP + [I-kappa-B phosphoprotein].

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381ATP Inferred
Active sitei135 – 1351Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 239ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. IkappaB kinase activity Source: UniProtKB-EC
  3. NF-kappaB-inducing kinase activity Source: UniProtKB
  4. protein binding Source: UniProtKB

GO - Biological processi

  1. immune response Source: UniProtKB
  2. innate immune response Source: Reactome
  3. intrinsic apoptotic signaling pathway in response to DNA damage Source: UniProtKB
  4. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  5. negative regulation of type I interferon production Source: Reactome
  6. NIK/NF-kappaB signaling Source: GOC
  7. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  8. protein phosphorylation Source: UniProtKB
  9. toll-like receptor 3 signaling pathway Source: Reactome
  10. toll-like receptor 4 signaling pathway Source: Reactome
  11. toll-like receptor signaling pathway Source: Reactome
  12. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

DNA damage

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.10. 2681.
ReactomeiREACT_24938. TRAF6 mediated IRF7 activation.
REACT_25026. TRAF3-dependent IRF activation pathway.
REACT_25148. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
SABIO-RKQ14164.
SignaLinkiQ14164.

Names & Taxonomyi

Protein namesi
Recommended name:
Inhibitor of nuclear factor kappa-B kinase subunit epsilon (EC:2.7.11.10)
Short name:
I-kappa-B kinase epsilon
Short name:
IKK-E
Short name:
IKK-epsilon
Short name:
IkBKE
Alternative name(s):
Inducible I kappa-B kinase
Short name:
IKK-i
Gene namesi
Name:IKBKE
Synonyms:IKKE, IKKI, KIAA0151
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:14552. IKBKE.

Subcellular locationi

Cytoplasm. Nucleus. NucleusPML body
Note: Targeting to PML nuclear bodies upon DNA damage is TOPORS-dependent.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. endosome membrane Source: Reactome
  4. nucleus Source: UniProtKB
  5. PML body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi30 – 301K → A: Loss of ubiquitination and decreased kinase activity. No effect on homodimerization. 1 Publication
Mutagenesisi30 – 301K → R: Loss of ubiquitination and decreased kinase activity. Decreases interaction with IKBKB, IKBKG and MYD88. No effect on homodimerization. 1 Publication
Mutagenesisi38 – 381K → A: Loss of kinase activity and loss of nuclear import. 1 Publication
Mutagenesisi168 – 1681E → A: Slight decrease of kinase activity. 1 Publication
Mutagenesisi172 – 1721S → A: Loss of autophosphorylation and of kinase activity. 1 Publication
Mutagenesisi172 – 1721S → E: Decrease in kinase activity. 1 Publication
Mutagenesisi231 – 2311K → R: Loss of sumoylation and loss of targeting to nuclear bodies. 1 Publication
Mutagenesisi401 – 4011K → A: Loss of ubiquitination and decreased kinase activity. No effect on homodimerization. 1 Publication
Mutagenesisi401 – 4011K → R: Loss of ubiquitination and decreased kinase activity. Decreases interaction with IKBKB, IKBKG and MYD88. No effect on homodimerization. 1 Publication
Mutagenesisi416 – 4161K → A: No effect on ubiquitination. 1 Publication
Mutagenesisi416 – 4161K → R: No effect on ubiquitination. 1 Publication

Organism-specific databases

PharmGKBiPA134962294.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 716716Inhibitor of nuclear factor kappa-B kinase subunit epsilonPRO_0000086017Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki30 – 30Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei172 – 1721Phosphoserine; by autocatalysis and IKKB1 Publication
Cross-linki231 – 231Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)1 Publication
Cross-linki401 – 401Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei501 – 5011Phosphothreonine By similarity
Modified residuei664 – 6641Phosphoserine1 Publication

Post-translational modificationi

Autophosphorylated and phosphorylated by IKBKB/IKKB. Phosphorylation at Ser-172 is enhanced by the interaction with DDX3X. Phosphorylated at Thr-501 upon IFN activation.3 Publications
Sumoylation by TOPORS upon DNA damage is required for protection of cells against DNA damage-induced cell death. Desumoylated by SENP1.1 Publication
'Lys-63'-linked polyubiquitinated at Lys-30 and Lys-401 by TRAF2:BIRC2 and TRAF2:BIRC3 complexes. Ubiquitination is induced by LPS, TNFA and interleukin-1 and required for full kinase activity and KF-kappa-B pathway activation.

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ14164.
PaxDbiQ14164.
PRIDEiQ14164.

PTM databases

PhosphoSiteiQ14164.

Expressioni

Tissue specificityi

Highly expressed in spleen followed by thymus, peripheral blood leukocytes, pancreas, placenta. Weakly expressed in lung, kidney, prostate, ovary and colon.

Inductioni

Induced by lipopolysaccharide (LPS) and TNFA.1 Publication

Gene expression databases

BgeeiQ14164.
CleanExiHS_IKBKE.
GenevestigatoriQ14164.

Organism-specific databases

HPAiCAB025983.
HPA015788.

Interactioni

Subunit structurei

Homodimer. Interacts with MAVS/IPS1. Interacts with the adapter proteins AZI2/NAP1, TANK and TBKBP1/SINTBAD. Interacts with SIKE1. Interacts with TICAM1/TRIF, IRF3 and DDX58/RIG-I; interactions are disrupted by the interaction between IKBKE and SIKE1. Interacts with TOPORS; induced by DNA damage. Interacts with CYLD. Interacts (when poylubiquitinated) with IKBKB, IKBKG and MYD88. Interacts with DDX3X; the interaction is found to be induced upon virus infection. Interacts (via Protein kinase domain) with arenavirus protein N; the interaction inhibits IKBKE kinase function. Interacts with Ebola virus protein VP35; the interaction leads to inhibition of cellular antiviral response by blocking necessary interactions between the IKBKE and MAVS/IPS as well as its substrates IRF3 and IRF7.13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
K7Y1A22EBI-307369,EBI-8788634From a different organism.
P279582EBI-307369,EBI-6919131From a different organism.
CDC37Q165432EBI-307369,EBI-295634
DDX3XO005714EBI-307369,EBI-353779
HSP90AB1P082382EBI-307369,EBI-352572
MAVSQ7Z4342EBI-307369,EBI-995373
TANKQ928442EBI-307369,EBI-356349
TBK1Q9UHD22EBI-307369,EBI-356402
TBKBP1A7MCY63EBI-307369,EBI-359969

Protein-protein interaction databases

BioGridi115000. 62 interactions.
DIPiDIP-27530N.
IntActiQ14164. 19 interactions.
MINTiMINT-1132084.
STRINGi9606.ENSP00000356087.

Structurei

3D structure databases

ProteinModelPortaliQ14164.
SMRiQ14164. Positions 2-621.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 315307Protein kinaseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni383 – 647265Interaction with DDX3XAdd
BLAST
Regioni436 – 45722Leucine-zipperAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000220867.
HOVERGENiHBG008494.
InParanoidiQ14164.
KOiK07211.
OMAiHIYIHAH.
OrthoDBiEOG7Z95KH.
PhylomeDBiQ14164.
TreeFamiTF324269.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q14164-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MQSTANYLWH TDDLLGQGAT ASVYKARNKK SGELVAVKVF NTTSYLRPRE    50
VQVREFEVLR KLNHQNIVKL FAVEETGGSR QKVLVMEYCS SGSLLSVLES 100
PENAFGLPED EFLVVLRCVV AGMNHLRENG IVHRDIKPGN IMRLVGEEGQ 150
SIYKLTDFGA ARELDDDEKF VSVYGTEEYL HPDMYERAVL RKPQQKAFGV 200
TVDLWSIGVT LYHAATGSLP FIPFGGPRRN KEIMYRITTE KPAGAIAGAQ 250
RRENGPLEWS YTLPITCQLS LGLQSQLVPI LANILEVEQA KCWGFDQFFA 300
ETSDILQRVV VHVFSLSQAV LHHIYIHAHN TIAIFQEAVH KQTSVAPRHQ 350
EYLFEGHLCV LEPSVSAQHI AHTTASSPLT LFSTAIPKGL AFRDPALDVP 400
KFVPKVDLQA DYNTAKGVLG AGYQALRLAR ALLDGQELMF RGLHWVMEVL 450
QATCRRTLEV ARTSLLYLSS SLGTERFSSV AGTPEIQELK AAAELRSRLR 500
TLAEVLSRCS QNITETQESL SSLNRELVKS RDQVHEDRSI QQIQCCLDKM 550
NFIYKQFKKS RMRPGLGYNE EQIHKLDKVN FSHLAKRLLQ VFQEECVQKY 600
QASLVTHGKR MRVVHETRNH LRLVGCSVAA CNTEAQGVQE SLSKLLEELS 650
HQLLQDRAKG AQASPPPIAP YPSPTRKDLL LHMQELCEGM KLLASDLLDN 700
NRIIERLNRV PAPPDV 716
Length:716
Mass (Da):80,462
Last modified:November 1, 1996 - v1
Checksum:i3E5FBE5840734D81
GO
Isoform 2 (identifier: Q14164-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-85: Missing.

Show »
Length:631
Mass (Da):70,816
Checksum:i1E6CC6C29C88897D
GO

Sequence cautioni

The sequence BAA09772.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti128 – 1281E → K.1 Publication
Corresponds to variant rs41296028 [ dbSNP | Ensembl ].
VAR_038816
Natural varianti371 – 3711A → T.2 Publications
Corresponds to variant rs17021877 [ dbSNP | Ensembl ].
VAR_038817
Natural varianti483 – 4831T → M.1 Publication
Corresponds to variant rs52817862 [ dbSNP | Ensembl ].
VAR_040571
Natural varianti515 – 5151E → D.1 Publication
Corresponds to variant rs41299015 [ dbSNP | Ensembl ].
VAR_038818
Natural varianti543 – 5431I → M.1 Publication
Corresponds to variant rs41299037 [ dbSNP | Ensembl ].
VAR_038819
Natural varianti602 – 6021A → V.2 Publications
Corresponds to variant rs12059562 [ dbSNP | Ensembl ].
VAR_038820
Natural varianti660 – 6601G → E.1 Publication
Corresponds to variant rs55822317 [ dbSNP | Ensembl ].
VAR_040572
Natural varianti713 – 7131P → L.2 Publications
Corresponds to variant rs3748022 [ dbSNP | Ensembl ].
VAR_019989

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8585Missing in isoform 2. VSP_044305Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti187 – 1871R → Q in AAI05925. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D63485 mRNA. Translation: BAA09772.2. Different initiation.
AB016590 mRNA. Translation: BAA85155.1.
AF241789 mRNA. Translation: AAF45307.1.
DQ667176 Genomic DNA. Translation: ABG25921.1.
AL354681 Genomic DNA. Translation: CAI15250.1.
CH471100 Genomic DNA. Translation: EAW93549.1.
BC105923 mRNA. Translation: AAI05924.1.
BC105924 mRNA. Translation: AAI05925.1.
BC107812 mRNA. Translation: AAI07813.1.
CCDSiCCDS30996.1. [Q14164-1]
CCDS53464.1. [Q14164-2]
RefSeqiNP_001180250.1. NM_001193321.1. [Q14164-2]
NP_001180251.1. NM_001193322.1.
NP_054721.1. NM_014002.3. [Q14164-1]
XP_005273413.1. XM_005273356.2. [Q14164-1]
UniGeneiHs.321045.

Genome annotation databases

EnsembliENST00000367120; ENSP00000356087; ENSG00000143466. [Q14164-1]
ENST00000537984; ENSP00000444529; ENSG00000143466. [Q14164-2]
ENST00000581977; ENSP00000464030; ENSG00000263528. [Q14164-1]
ENST00000584998; ENSP00000462396; ENSG00000263528. [Q14164-2]
GeneIDi9641.
KEGGihsa:9641.
UCSCiuc001hdz.2. human. [Q14164-1]

Polymorphism databases

DMDMi14548079.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D63485 mRNA. Translation: BAA09772.2 . Different initiation.
AB016590 mRNA. Translation: BAA85155.1 .
AF241789 mRNA. Translation: AAF45307.1 .
DQ667176 Genomic DNA. Translation: ABG25921.1 .
AL354681 Genomic DNA. Translation: CAI15250.1 .
CH471100 Genomic DNA. Translation: EAW93549.1 .
BC105923 mRNA. Translation: AAI05924.1 .
BC105924 mRNA. Translation: AAI05925.1 .
BC107812 mRNA. Translation: AAI07813.1 .
CCDSi CCDS30996.1. [Q14164-1 ]
CCDS53464.1. [Q14164-2 ]
RefSeqi NP_001180250.1. NM_001193321.1. [Q14164-2 ]
NP_001180251.1. NM_001193322.1.
NP_054721.1. NM_014002.3. [Q14164-1 ]
XP_005273413.1. XM_005273356.2. [Q14164-1 ]
UniGenei Hs.321045.

3D structure databases

ProteinModelPortali Q14164.
SMRi Q14164. Positions 2-621.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115000. 62 interactions.
DIPi DIP-27530N.
IntActi Q14164. 19 interactions.
MINTi MINT-1132084.
STRINGi 9606.ENSP00000356087.

Chemistry

BindingDBi Q14164.
ChEMBLi CHEMBL3038486.
GuidetoPHARMACOLOGYi 2040.

PTM databases

PhosphoSitei Q14164.

Polymorphism databases

DMDMi 14548079.

Proteomic databases

MaxQBi Q14164.
PaxDbi Q14164.
PRIDEi Q14164.

Protocols and materials databases

DNASUi 9641.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000367120 ; ENSP00000356087 ; ENSG00000143466 . [Q14164-1 ]
ENST00000537984 ; ENSP00000444529 ; ENSG00000143466 . [Q14164-2 ]
ENST00000581977 ; ENSP00000464030 ; ENSG00000263528 . [Q14164-1 ]
ENST00000584998 ; ENSP00000462396 ; ENSG00000263528 . [Q14164-2 ]
GeneIDi 9641.
KEGGi hsa:9641.
UCSCi uc001hdz.2. human. [Q14164-1 ]

Organism-specific databases

CTDi 9641.
GeneCardsi GC01P206643.
H-InvDB HIX0116011.
HGNCi HGNC:14552. IKBKE.
HPAi CAB025983.
HPA015788.
MIMi 605048. gene.
neXtProti NX_Q14164.
PharmGKBi PA134962294.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000220867.
HOVERGENi HBG008494.
InParanoidi Q14164.
KOi K07211.
OMAi HIYIHAH.
OrthoDBi EOG7Z95KH.
PhylomeDBi Q14164.
TreeFami TF324269.

Enzyme and pathway databases

BRENDAi 2.7.11.10. 2681.
Reactomei REACT_24938. TRAF6 mediated IRF7 activation.
REACT_25026. TRAF3-dependent IRF activation pathway.
REACT_25148. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
SABIO-RK Q14164.
SignaLinki Q14164.

Miscellaneous databases

ChiTaRSi IKBKE. human.
GeneWikii IKBKE.
GenomeRNAii 9641.
NextBioi 36191.
PROi Q14164.
SOURCEi Search...

Gene expression databases

Bgeei Q14164.
CleanExi HS_IKBKE.
Genevestigatori Q14164.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "IKK-i, a novel lipopolysaccharide-inducible kinase that is related to IkappaB kinases."
    Shimada T., Kawai T., Takeda K., Matsumoto M., Inoue J., Tatsumi Y., Kanamaru A., Akira S.
    Int. Immunol. 11:1357-1362(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF LYS-38; GLU-168 AND SER-172.
  2. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Leukocyte.
  3. "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
    DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Bone marrow.
  4. SeattleSNPs variation discovery resource
    Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-128; THR-371; ASP-515; MET-543; VAL-602 AND LEU-713.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORMS 1 AND 2).
  8. "Identification of NAP1, a regulatory subunit of IkappaB kinase-related kinases that potentiates NF-kappaB signaling."
    Fujita F., Taniguchi Y., Kato T., Narita Y., Furuya A., Ogawa T., Sakurai H., Joh T., Itoh M., Delhase M., Karin M., Nakanishi M.
    Mol. Cell. Biol. 23:7780-7793(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AZI2.
  9. "Mechanisms of the TRIF-induced interferon-stimulated response element and NF-kappaB activation and apoptosis pathways."
    Han K.J., Su X., Xu L.-G., Bin L.H., Zhang J., Shu H.-B.
    J. Biol. Chem. 279:15652-15661(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TICAM1.
  10. "SIKE is an IKK epsilon/TBK1-associated suppressor of TLR3- and virus-triggered IRF-3 activation pathways."
    Huang J., Liu T., Xu L.-G., Chen D., Zhai Z., Shu H.-B.
    EMBO J. 24:4018-4028(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIKE1; IRF3; TICAM1 AND DDX58.
  11. "Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus."
    Meylan E., Curran J., Hofmann K., Moradpour D., Binder M., Bartenschlager R., Tschopp J.
    Nature 437:1167-1172(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAVS.
  12. "SINTBAD, a novel component of innate antiviral immunity, shares a TBK1-binding domain with NAP1 and TANK."
    Ryzhakov G., Randow F.
    EMBO J. 26:3180-3190(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AZI2; TANK AND TBKBP1.
  13. "The DEAD-box helicase DDX3X is a critical component of the TANK-binding kinase 1-dependent innate immune response."
    Soulat D., Burckstummer T., Westermayer S., Goncalves A., Bauch A., Stefanovic A., Hantschel O., Bennett K.L., Decker T., Superti-Furga G.
    EMBO J. 27:2135-2146(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF DDX3X.
  14. "Viral targeting of DEAD box protein 3 reveals its role in TBK1/IKKepsilon-mediated IRF activation."
    Schroder M., Baran M., Bowie A.G.
    EMBO J. 27:2147-2157(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDX3X.
  15. Cited for: INTERACTION WITH CYLD.
  16. "Ebola virus protein VP35 impairs the function of interferon regulatory factor-activating kinases IKKepsilon and TBK-1."
    Prins K.C., Cardenas W.B., Basler C.F.
    J. Virol. 83:3069-3077(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN IRF3 PHOSPHORYLATION, INTERACTION WITH EBOLAVIRUS PROTEIN VP35, AUTOPHOSPHORYLATION.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "SUMOylation-dependent localization of IKKepsilon in PML nuclear bodies is essential for protection against DNA-damage-triggered cell death."
    Renner F., Moreno R., Schmitz M.L.
    Mol. Cell 37:503-515(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TOPORS, SUMOYLATION AT LYS-231 BY TOPORS, DESUMOYLATION BY SENP1, MUTAGENESIS OF LYS-231, SUBCELLULAR LOCATION.
  19. "Hepatitis B virus polymerase blocks pattern recognition receptor signaling via interaction with DDX3: implications for immune evasion."
    Wang H., Ryu W.S.
    PLoS Pathog. 6:E1000986-E1000986(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDX3X.
  20. Cited for: FUNCTION, PHOSPHORYLATION BY IKBKB/IKKB.
  21. "IkappaB kinase epsilon and TANK-binding kinase 1 activate AKT by direct phosphorylation."
    Xie X., Zhang D., Zhao B., Lu M.K., You M., Condorelli G., Wang C.Y., Guan K.L.
    Proc. Natl. Acad. Sci. U.S.A. 108:6474-6479(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN AKT PHOSPHORYLATION, SUBCELLULAR LOCATION.
  22. "Arenavirus nucleoprotein targets interferon regulatory factor-activating kinase IKKepsilon."
    Pythoud C., Rodrigo W.W., Pasqual G., Rothenberger S., Martinez-Sobrido L., de la Torre J.C., Kunz S.
    J. Virol. 86:7728-7738(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ARENAVIRUS PROTEIN N.
  23. "IKKepsilon-mediated tumorigenesis requires K63-linked polyubiquitination by a cIAP1/cIAP2/TRAF2 E3 ubiquitin ligase complex."
    Zhou A.Y., Shen R.R., Kim E., Lock Y.J., Xu M., Chen Z.J., Hahn W.C.
    Cell Rep. 3:724-733(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HOMODIMER, INTERACTION WITH IKBKB; IKBKG AND MYD88, INDUCTION BY LPS, UBIQUITINATION AT LYS-30 AND LYS-401, MUTAGENESIS OF LYS-30; LYS-401 AND LYS-416.
  24. "Human DEAD box helicase 3 couples IkappaB kinase epsilon to interferon regulatory factor 3 activation."
    Gu L., Fullam A., Brennan R., Schroder M.
    Mol. Cell. Biol. 33:2004-2015(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DDX3X AND IRF3 PHOSPHORYLATION, INTERACTION WITH DDX3X AND IRF3, PHOSPHORYLATION AT SER-172.
  25. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-371; MET-483; VAL-602; GLU-660 AND LEU-713.

Entry informationi

Entry nameiIKKE_HUMAN
AccessioniPrimary (citable) accession number: Q14164
Secondary accession number(s): D3DT78
, Q3B754, Q3KR43, Q5JTS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: November 1, 1996
Last modified: September 3, 2014
This is version 151 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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