SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O88522

- NEMO_MOUSE

UniProt

O88522 - NEMO_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

NF-kappa-B essential modulator

Gene
Ikbkg, Nemo
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Regulatory subunit of the IKK core complex which 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. Its binding to scaffolding polyubiquitin seems to play a role in IKK activation by multiple signaling receptor pathways. Also considered to be a mediator for TAX activation of NF-kappa-B. Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri389 – 41022C2HC-typeAdd
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. protein binding Source: UniProtKB
  3. protein heterodimerization activity Source: UniProtKB
  4. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. activation of NF-kappaB-inducing kinase activity Source: MGI
  2. B cell homeostasis Source: MGI
  3. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_198543. IRAK1 recruits IKK complex.
REACT_198546. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_202898. TRAF6 mediated NF-kB activation.
REACT_204812. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
REACT_205561. FCERI mediated NF-kB activation.
REACT_205717. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
REACT_211125. NOD1/2 Signaling Pathway.
REACT_219800. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_222971. RIP-mediated NFkB activation via ZBP1.
REACT_224208. Interleukin-1 signaling.
REACT_225145. Downstream TCR signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
NF-kappa-B essential modulator
Short name:
NEMO
Alternative name(s):
IkB kinase-associated protein 1
Short name:
IKKAP1
Short name:
mFIP-3
Inhibitor of nuclear factor kappa-B kinase subunit gamma
Short name:
I-kappa-B kinase subunit gamma
Short name:
IKK-gamma
Short name:
IKKG
Short name:
IkB kinase subunit gamma
NF-kappa-B essential modifier
Gene namesi
Name:Ikbkg
Synonyms:Nemo
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:1338074. Ikbkg.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. IkappaB kinase complex Source: MGI
  3. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi278 – 2781K → R: Slight decrease in TRAF6-induced polyubiquitination. 1 Publication
Mutagenesisi293 – 2931V → A: Abolishes linear polyubiquitin-binding, impairs 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-301 and A-302. 1 Publication
Mutagenesisi301 – 3011Y → A: Abolishes linear polyubiquitin-binding, impairs 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-293 and A-302. 1 Publication
Mutagenesisi302 – 3021K → A: Abolishes linear polyubiquitin-binding, impairs 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-293 and A-301. 1 Publication
Mutagenesisi305 – 3051F → A: Abolishes linear polyubiquitin-binding, impairs 'Lys-63'-linked polyubiquitin-binding and impairs of NF-kappa-B activation. 1 Publication
Mutagenesisi309 – 3091R → A: Abolishes linear polyubiquitin-binding, no effect on 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-312 and A-313. 1 Publication
Mutagenesisi312 – 3121R → A: Abolishes linear polyubiquitin-binding, no effect on 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-309 and A-313. 1 Publication
Mutagenesisi313 – 3131E → A: Impairs linear polyubiquitin-binding. Abolishes linear polyubiquitin-binding, no effect on 'Lys-63'-linked polyubiquitin-binding and impairs NF-kappa-B activation; when associated with A-309 and A-312. Abolishes linear polyubiquitin-binding; when associated with A-317 and A-320. 1 Publication
Mutagenesisi314 – 3141K → R: Slight decrease in TRAF6-induced polyubiquitination. Important decrease in TRAF6-induced polyubiquitination; when associated with R-318 and R-319. 1 Publication
Mutagenesisi316 – 3161V → P: Loss of interaction with TRAF6 and TRAF6-induced polyubiquitination. 1 Publication
Mutagenesisi317 – 3171E → A: Abolishes linear polyubiquitin-binding; when associated with A-313 and A-320. 1 Publication
Mutagenesisi318 – 3181K → R: Slight decrease in TRAF6-induced polyubiquitination. Decrease in TRAF6-induced polyubiquitination; when associated with R-319. Important decrease in TRAF6-induced polyubiquitination; when associated with R-314 and R-319. 1 Publication
Mutagenesisi319 – 3191K → R: Slight decrease in TRAF6-induced polyubiquitination. Decrease in TRAF6-induced polyubiquitination; when associated with R-318. Important decrease in TRAF6-induced polyubiquitination; when associated with R-314 and R-318. 1 Publication
Mutagenesisi320 – 3201E → A: Abolishes linear polyubiquitin-binding; when associated with A-313 and A-317. 1 Publication
Mutagenesisi369 – 3691S → A: Decreases phosphorylation and increases NF-kappa-B activity. 1 Publication
Mutagenesisi375 – 3751S → A: Decreases phosphorylation and increases NF-kappa-B activity. 1 Publication
Mutagenesisi392 – 3921K → R: 40% decrease in IL1-induced NF-kappa-B activation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 412412NF-kappa-B essential modulatorPRO_0000096783Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311Phosphoserine; by IKKB By similarity
Modified residuei43 – 431Phosphoserine; by IKKB By similarity
Disulfide bondi54 – 54Interchain By similarity
Modified residuei68 – 681Phosphoserine By similarity
Modified residuei85 – 851Phosphoserine; by ATM By similarity
Cross-linki111 – 111Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-linki139 – 139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-linki143 – 143Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-linki226 – 226Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-linki246 – 246Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-linki270 – 270Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
Cross-linki270 – 270Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
Cross-linki276 – 276Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-linki278 – 278Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki285 – 285Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-linki295 – 295Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-linki302 – 302Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
Cross-linki302 – 302Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
Cross-linki314 – 314Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki318 – 318Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki319 – 319Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Disulfide bondi340 – 340Interchain By similarity
Modified residuei369 – 3691Phosphoserine; by IKKB1 Publication
Modified residuei380 – 3801Phosphoserine By similarity
Cross-linki392 – 392Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Phosphorylation at Ser-68 attenuates aminoterminal homodimerization By similarity.
Polyubiquitinated on Lys-278 through 'Lys-63'; the ubiquitination is mediated by NOD2 and RIPK2 and probably plays a role in signaling by facilitating interactions with ubiquitin domain-containing proteins and activates the NF-kappa-B pathway. Polyubiquitinated on Lys-392 through 'Lys-63'; the ubiquitination is mediated by BCL10, MALT1 and TRAF6 and probably plays a role in signaling by facilitating interactions with ubiquitin domain-containing proteins and activates the NF-kappa-B pathway. Monoubiquitinated on Lys-270 and Lys-302; promotes nuclear export. Polyubiquitinated through 'Lys-27' by TRIM23; involved in antiviral innate and inflammatory responses. Linear polyubiquitinated on Lys-111, Lys-143, Lys-226, Lys-246, Lys-270, Lys-278, Lys-285, Lys-295, Lys-302 and Lys-319; the head-to-tail polyubiquitination is mediated by the LUBAC complex and plays a key role in NF-kappa-B activation By similarity.
Sumoylated on Lys-270 and Lys-302 with SUMO1; the modification results in phosphorylation of Ser-85 by ATM leading to a replacement of the sumoylation by mono-ubiquitination on these residues By similarity.
Neddylated by TRIM40, resulting in stabilization of NFKBIA and down-regulation of NF-kappa-B activity By similarity.

Keywords - PTMi

Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO88522.
PaxDbiO88522.
PRIDEiO88522.

PTM databases

PhosphoSiteiO88522.

Expressioni

Gene expression databases

ArrayExpressiO88522.
BgeeiO88522.
CleanExiMM_IKBKG.
GenevestigatoriO88522.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Component of the I-kappa-B-kinase (IKK) core complex consisting of CHUK, IKBKB and IKBKG; probably four alpha/CHUK-beta/IKBKB dimers are associated with four gamma/IKBKG subunits. The IKK core complex seems to associate with regulatory or adapter proteins to form a IKK-signalosome holo-complex. The IKK complex associates with TERF2IP/RAP1, leading to promote IKK-mediated phosphorylation of RELA/p65. Part of a complex composed of NCOA2, NCOA3, CHUK/IKKA, IKBKB, IKBKG and CREBBP. Interacts with COPS3, CYLD, NALP2, TRPC4AP and LRDD. Interacts with ATM; the complex is exported from the nucleus. Interacts with TRAF6. Interacts with IKBKE. Interacts with TANK; the interaction is enhanced by TBK1 and IKBKE. Part of a ternary complex consisting of TANK, IKBKB and IKBKG. Interacts with ZFAND5. Interacts with RIPK2. Interacts with TNIP1 and TNFAIP3; TNIP1 facilitates the TNFAIP3-mediated de-ubiquitination of IKBKG. Interacts with TNFAIP3; the interaction is induced by TNF stimulation and by polyubiquitin. Interacts with NLRP10.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ChukQ606804EBI-998011,EBI-646245
IkbkbO883513EBI-998011,EBI-447960
Rnf31Q924T72EBI-998011,EBI-647680
UBCP0CG483EBI-998011,EBI-3390054From a different organism.
UbcP629912EBI-998011,EBI-413074
VACWR196P247722EBI-998011,EBI-4291651From a different organism.

Protein-protein interaction databases

BioGridi200602. 40 interactions.
DIPiDIP-29811N.
IntActiO88522. 14 interactions.
MINTiMINT-143245.
STRINGi10090.ENSMUSP00000004330.

Structurei

Secondary structure

1
412
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi253 – 28937
Helixi291 – 33343

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2V4HX-ray2.90A/B251-337[»]
2ZVNX-ray3.00B/D/F/H253-337[»]
2ZVOX-ray2.90B/D250-339[»]
3F89X-ray2.80A/B250-339[»]
3JSVX-ray2.70C/D250-343[»]
4OWFX-ray2.00A/B250-339[»]
ProteinModelPortaliO88522.
SMRiO88522. Positions 49-109, 193-248, 256-341, 387-412.

Miscellaneous databases

EvolutionaryTraceiO88522.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni44 – 11168Interaction with CHUK/IKBKB By similarityAdd
BLAST
Regioni150 – 250101Interaction with TANKAdd
BLAST
Regioni242 – 343102Ubiquitin-binding (UBD)Add
BLAST
Regioni246 – 358113Self-association By similarityAdd
BLAST
Regioni249 – 412164Required for interaction with TNFAIP3 By similarityAdd
BLAST
Regioni250 – 33990Linear polyubiquitin-binding, does not bind to 'Lys-63'-linked polyubiquitinAdd
BLAST
Regioni315 – 33622Leucine-zipper Reviewed predictionAdd
BLAST
Regioni375 – 41238Interaction with CYLD By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili49 – 345297 Reviewed predictionAdd
BLAST

Domaini

The leucine-zipper domain and the C2HC-type zinc-finger are essential for polyubiquitin binding and for the activation of IRF3 By similarity.

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri389 – 41022C2HC-typeAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG138369.
GeneTreeiENSGT00530000063808.
HOGENOMiHOG000293233.
HOVERGENiHBG000417.
InParanoidiQ924H4.
KOiK07210.
TreeFamiTF326608.

Family and domain databases

InterProiIPR021063. NEMO_N.
[Graphical view]
PfamiPF11577. NEMO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O88522-1 [UniParc]FASTAAdd to Basket

« Hide

MNKHPWKNQL SEMVQPSGGP AEDQDMLGEE SSLGKPAMLH LPSEQGTPET    50
LQRCLEENQE LRDAIRQSNQ MLRERCEELL HFQVSQREEK EFLMCKFQEA 100
RKLVERLSLE KLDLRSQREQ ALKELEQLKK CQQQMAEDKA SVKAQVTSLL 150
GELQESQSRL EAATKDRQAL EGRIRAVSEQ VRQLESEREV LQQQHSVQVD 200
QLRMQNQSVE AALRMERQAA SEEKRKLAQL QAAYHQLFQD YDSHIKSSKG 250
MQLEDLRQQL QQAEEALVAK QELIDKLKEE AEQHKIVMET VPVLKAQADI 300
YKADFQAERH AREKLVEKKE YLQEQLEQLQ REFNKLKVGC HESARIEDMR 350
KRHVETPQPP LLPAPAHHSF HLALSNQRRS PPEEPPDFCC PKCQYQAPDM 400
DTLQIHVMEC IE 412
Length:412
Mass (Da):47,972
Last modified:July 27, 2011 - v2
Checksum:i66C693C857A2D5E6
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti13 – 131M → T in AAC40153. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF069542 mRNA. Translation: AAC40153.1.
AF326207 Genomic DNA. Translation: AAK69186.1.
AF513109 mRNA. Translation: AAP47160.1.
AK154095 mRNA. Translation: BAE32372.1.
AL669976 Genomic DNA. Translation: CAM45971.1.
CH466650 Genomic DNA. Translation: EDL29810.1.
CCDSiCCDS41023.1.
RefSeqiNP_001154895.1. NM_001161423.1.
NP_034677.2. NM_010547.2.
XP_006527913.1. XM_006527850.1.
XP_006527914.1. XM_006527851.1.
XP_006527915.1. XM_006527852.1.
UniGeneiMm.12967.

Genome annotation databases

EnsembliENSMUST00000114127; ENSMUSP00000109762; ENSMUSG00000004221.
ENSMUST00000114128; ENSMUSP00000109763; ENSMUSG00000004221.
ENSMUST00000114133; ENSMUSP00000109768; ENSMUSG00000004221.
ENSMUST00000164101; ENSMUSP00000126770; ENSMUSG00000004221.
GeneIDi16151.
KEGGimmu:16151.
UCSCiuc009toz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF069542 mRNA. Translation: AAC40153.1 .
AF326207 Genomic DNA. Translation: AAK69186.1 .
AF513109 mRNA. Translation: AAP47160.1 .
AK154095 mRNA. Translation: BAE32372.1 .
AL669976 Genomic DNA. Translation: CAM45971.1 .
CH466650 Genomic DNA. Translation: EDL29810.1 .
CCDSi CCDS41023.1.
RefSeqi NP_001154895.1. NM_001161423.1.
NP_034677.2. NM_010547.2.
XP_006527913.1. XM_006527850.1.
XP_006527914.1. XM_006527851.1.
XP_006527915.1. XM_006527852.1.
UniGenei Mm.12967.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2V4H X-ray 2.90 A/B 251-337 [» ]
2ZVN X-ray 3.00 B/D/F/H 253-337 [» ]
2ZVO X-ray 2.90 B/D 250-339 [» ]
3F89 X-ray 2.80 A/B 250-339 [» ]
3JSV X-ray 2.70 C/D 250-343 [» ]
4OWF X-ray 2.00 A/B 250-339 [» ]
ProteinModelPortali O88522.
SMRi O88522. Positions 49-109, 193-248, 256-341, 387-412.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200602. 40 interactions.
DIPi DIP-29811N.
IntActi O88522. 14 interactions.
MINTi MINT-143245.
STRINGi 10090.ENSMUSP00000004330.

PTM databases

PhosphoSitei O88522.

Proteomic databases

MaxQBi O88522.
PaxDbi O88522.
PRIDEi O88522.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000114127 ; ENSMUSP00000109762 ; ENSMUSG00000004221 .
ENSMUST00000114128 ; ENSMUSP00000109763 ; ENSMUSG00000004221 .
ENSMUST00000114133 ; ENSMUSP00000109768 ; ENSMUSG00000004221 .
ENSMUST00000164101 ; ENSMUSP00000126770 ; ENSMUSG00000004221 .
GeneIDi 16151.
KEGGi mmu:16151.
UCSCi uc009toz.2. mouse.

Organism-specific databases

CTDi 8517.
MGIi MGI:1338074. Ikbkg.

Phylogenomic databases

eggNOGi NOG138369.
GeneTreei ENSGT00530000063808.
HOGENOMi HOG000293233.
HOVERGENi HBG000417.
InParanoidi Q924H4.
KOi K07210.
TreeFami TF326608.

Enzyme and pathway databases

Reactomei REACT_198543. IRAK1 recruits IKK complex.
REACT_198546. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_202898. TRAF6 mediated NF-kB activation.
REACT_204812. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
REACT_205561. FCERI mediated NF-kB activation.
REACT_205717. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
REACT_211125. NOD1/2 Signaling Pathway.
REACT_219800. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_222971. RIP-mediated NFkB activation via ZBP1.
REACT_224208. Interleukin-1 signaling.
REACT_225145. Downstream TCR signaling.

Miscellaneous databases

EvolutionaryTracei O88522.
NextBioi 288945.
PROi O88522.
SOURCEi Search...

Gene expression databases

ArrayExpressi O88522.
Bgeei O88522.
CleanExi MM_IKBKG.
Genevestigatori O88522.

Family and domain databases

InterProi IPR021063. NEMO_N.
[Graphical view ]
Pfami PF11577. NEMO. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Complementation cloning of NEMO, a component of the I-kappaB kinase complex essential for NF-kappaB activation."
    Yamaoka S., Courtois G., Bessia C., Whiteside S.T., Weil R., Agou F., Kirk H.E., Kay R.J., Israel A.
    Cell 93:1231-1240(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: T-cell.
  2. "Human-mouse comparative sequence analysis of the NEMO gene reveals an alternative promoter within the neighboring G6PD gene."
    Galgoczy P., Rosenthal A., Platzer M.
    Gene 271:93-98(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Ikbkg gene modulates the herpes virus susceptibility in mice."
    Perelygin A.A., Perelygina L.M.
    Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Liver.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "IkappaB kinase (IKK)-associated protein 1, a common component of the heterogeneous IKK complex."
    Mercurio F., Murray B.W., Shevchenko A., Bennett B.L., Young D.B., Li J.W., Pascual G., Motiwala A., Zhu H., Mann M., Manning A.M.
    Mol. Cell. Biol. 19:1526-1538(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 85-412, PROTEIN SEQUENCE OF 144-159.
    Tissue: Cervix carcinoma.
  8. "Identification of a cell protein (FIP-3) as a modulator of NF-kappaB activity and as a target of an adenovirus inhibitor of tumor necrosis factor alpha-induced apoptosis."
    Li Y., Kang J., Friedman J., Tarassishin L., Ye J., Kovalenko A., Wallach D., Horwitz M.S.
    Proc. Natl. Acad. Sci. U.S.A. 96:1042-1047(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Role of ikkgamma/nemo in assembly of the IkappaB kinase complex."
    Li X.-H., Fang X., Gaynor R.B.
    J. Biol. Chem. 276:4494-4500(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IKK COMPLEX.
  10. "Regulation of Ikappa B kinase (IKK)gamma /NEMO function by IKKbeta -mediated phosphorylation."
    Prajapati S., Gaynor R.B.
    J. Biol. Chem. 277:24331-24339(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-369, MUTAGENESIS OF SER-369 AND SER-375.
  11. "Association of the adaptor TANK with the I kappa B kinase (IKK) regulator NEMO connects IKK complexes with IKK epsilon and TBK1 kinases."
    Chariot A., Leonardi A., Muller J., Bonif M., Brown K., Siebenlist U.
    J. Biol. Chem. 277:37029-37036(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TANK AND IKBKB.
  12. "ABIN-1 binds to NEMO/IKKgamma and co-operates with A20 in inhibiting NF-kappaB."
    Mauro C., Pacifico F., Lavorgna A., Mellone S., Iannetti A., Acquaviva R., Formisano S., Vito P., Leonardi A.
    J. Biol. Chem. 281:18482-18488(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TNIP1 AND TNFAIP3.
  13. "Identification of TRAF6-dependent NEMO polyubiquitination sites through analysis of a new NEMO mutation causing incontinentia pigmenti."
    Sebban-Benin H., Pescatore A., Fusco F., Pascuale V., Gautheron J., Yamaoka S., Moncla A., Ursini M.V., Courtois G.
    Hum. Mol. Genet. 16:2805-2815(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-278; LYS-314; LYS-318; LYS-319 AND LYS-392, MUTAGENESIS OF LYS-278; LYS-314; VAL-316; LYS-318; LYS-319 AND LYS-392.
  14. Cited for: INTERACTION WITH TERF2IP.
  15. "Specific recognition of linear ubiquitin chains by NEMO is important for NF-kappaB activation."
    Rahighi S., Ikeda F., Kawasaki M., Akutsu M., Suzuki N., Kato R., Kensche T., Uejima T., Bloor S., Komander D., Randow F., Wakatsuki S., Dikic I.
    Cell 136:1098-1109(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 250-343 IN COMPLEX WITH UBIQUITIN, UBIQUITIN-BINDING, MUTAGENESIS OF VAL-293; TYR-301; LYS-302; PHE-305; ARG-309; ARG-312; GLU-313; GLU-313; GLU-317 AND GLU-320.
  16. "DARPin-assisted crystallography of the CC2-LZ domain of NEMO reveals a coupling between dimerization and ubiquitin binding."
    Grubisha O., Kaminska M., Duquerroy S., Fontan E., Cordier F., Haouz A., Raynal B., Chiaravalli J., Delepierre M., Israel A., Veron M., Agou F.
    J. Mol. Biol. 395:89-104(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 251-337, UBIQUITIN-BINDING, OLIGOMETRIZATION.

Entry informationi

Entry nameiNEMO_MOUSE
AccessioniPrimary (citable) accession number: O88522
Secondary accession number(s): Q924H4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi