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Q6TMG5

- NEMO_RAT

UniProt

Q6TMG5 - NEMO_RAT

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Protein
NF-kappa-B essential modulator
Gene
Ikbkg, Nemo
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript 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. Essential for viral activation of IRF3. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination By similarity.

Regions

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

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. peroxisome proliferator activated receptor binding Source: RGD
  3. protein heterodimerization activity Source: RGD
  4. protein homodimerization activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. B cell homeostasis Source: Ensembl
  2. NF-kappaB import into nucleus Source: RGD
  3. activation of NF-kappaB-inducing kinase activity Source: Ensembl
  4. cellular response to DNA damage stimulus Source: Ensembl
  5. positive regulation of NF-kappaB transcription factor activity Source: RGD
  6. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  7. 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_194364. RIP-mediated NFkB activation via ZBP1.
REACT_197513. FCERI mediated NF-kB activation.
REACT_198989. IRAK1 recruits IKK complex.
REACT_199026. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
REACT_199247. Activation of NF-kappaB in B cells.

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
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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 1

Organism-specific databases

RGDi735223. Ikbkg.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 412412NF-kappa-B essential modulator
PRO_0000269197Add
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) By similarity
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) By similarity
Cross-linki319 – 319Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Disulfide bondi340 – 340Interchain By similarity
Modified residuei369 – 3691Phosphoserine; by IKKB By similarity
Modified residuei380 – 3801Phosphoserine By similarity
Cross-linki392 – 392Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

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

Expressioni

Gene expression databases

GenevestigatoriQ6TMG5.

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 IKBKE and TBK1. Part of a ternary complex consisting of TANK, IKBKB and IKBKG. Interacts with ZFAND5. 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 By similarity.

Protein-protein interaction databases

BioGridi259339. 1 interaction.
STRINGi10116.ENSRNOP00000053114.

Structurei

3D structure databases

ProteinModelPortaliQ6TMG5.
SMRiQ6TMG5. Positions 49-109, 193-248, 387-412.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni44 – 11168Interaction with CHUK/IKBKB By similarity
Add
BLAST
Regioni150 – 250101Interaction with TANK By similarity
Add
BLAST
Regioni242 – 343102Ubiquitin-binding (UBD)
Add
BLAST
Regioni246 – 358113Self-association By similarity
Add
BLAST
Regioni249 – 412164Required for interaction with TNFAIP3 By similarity
Add
BLAST
Regioni315 – 33622Leucine-zipper Reviewed prediction
Add
BLAST
Regioni375 – 41238Interaction with CYLD By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili49 – 343295 Reviewed prediction
Add
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

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG138369.
GeneTreeiENSGT00530000063808.
HOGENOMiHOG000293233.
HOVERGENiHBG000417.
InParanoidiQ6TMG5.
KOiK07210.
OMAiPETFQRC.
OrthoDBiEOG7D2FD7.
PhylomeDBiQ6TMG5.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q6TMG5-1 [UniParc]FASTAAdd to Basket

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MSRHLWKNQL SEMVQPSGGP AEDQDMLGEE SSLGKPAMLH LPSEQGTPET    50
LQRCLEENQE LRDAIRQSNQ MLRERCEELL HFQVSQREEK EFLMCKFQEA 100
RKLVERLSLE KLDLRRQREQ ALEDLEHLKK CQQQMAEDKA SVKAQVTSLL 150
GELQESQSRL EAATKERQTL EGRIRAVSEQ VRQLESEREV LQQQHSVQVD 200
QLRMQNQSVE AALRMERQAA SEEKRKLAQL QAAYHQLFQD YDSHIKSSKG 250
MQLEDLRQQL QQAEEALVAK QELIDKLKEE AEQHKIVMET VPVLKAQADI 300
YKADFQAERH AREKLVERKE LLQEQLEQLQ REFNKLKVGC HESARIEDMR 350
KRHVETSQPP LLPAPAHHSF HLALSNQRRS PPEEPPDFCC PKCQYQAPDM 400
DTLQIHVMEC IE 412
Length:412
Mass (Da):48,066
Last modified:July 5, 2004 - v1
Checksum:i6D5D96B08A4CCEC2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY392762 mRNA. Translation: AAQ94056.1.
RefSeqiNP_954534.1. NM_199103.1.
XP_006229646.1. XM_006229584.1.
XP_006229647.1. XM_006229585.1.
XP_006229648.1. XM_006229586.1.
UniGeneiRn.214715.

Genome annotation databases

EnsembliENSRNOT00000056275; ENSRNOP00000053114; ENSRNOG00000037237.
GeneIDi309295.
KEGGirno:309295.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY392762 mRNA. Translation: AAQ94056.1 .
RefSeqi NP_954534.1. NM_199103.1.
XP_006229646.1. XM_006229584.1.
XP_006229647.1. XM_006229585.1.
XP_006229648.1. XM_006229586.1.
UniGenei Rn.214715.

3D structure databases

ProteinModelPortali Q6TMG5.
SMRi Q6TMG5. Positions 49-109, 193-248, 387-412.
ModBasei Search...

Protein-protein interaction databases

BioGridi 259339. 1 interaction.
STRINGi 10116.ENSRNOP00000053114.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000056275 ; ENSRNOP00000053114 ; ENSRNOG00000037237 .
GeneIDi 309295.
KEGGi rno:309295.

Organism-specific databases

CTDi 8517.
RGDi 735223. Ikbkg.

Phylogenomic databases

eggNOGi NOG138369.
GeneTreei ENSGT00530000063808.
HOGENOMi HOG000293233.
HOVERGENi HBG000417.
InParanoidi Q6TMG5.
KOi K07210.
OMAi PETFQRC.
OrthoDBi EOG7D2FD7.
PhylomeDBi Q6TMG5.

Enzyme and pathway databases

Reactomei REACT_194364. RIP-mediated NFkB activation via ZBP1.
REACT_197513. FCERI mediated NF-kB activation.
REACT_198989. IRAK1 recruits IKK complex.
REACT_199026. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
REACT_199247. Activation of NF-kappaB in B cells.

Miscellaneous databases

NextBioi 660548.

Gene expression databases

Genevestigatori Q6TMG5.

Family and domain databases

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

Publicationsi

  1. "Two carboxyl-terminal activation regions of Epstein-Barr virus latent membrane protein 1 activate NF-kappaB through distinct signaling pathways in fibroblast cell lines."
    Saito N., Courtois G., Chiba A., Yamamoto N., Nitta T., Hironaka N., Rowe M., Yamamoto N., Yamaoka S.
    J. Biol. Chem. 278:46565-46575(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Fischer 344.

Entry informationi

Entry nameiNEMO_RAT
AccessioniPrimary (citable) accession number: Q6TMG5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: July 5, 2004
Last modified: September 3, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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