NF-kappa-B essential modulator - Rattus norvegicus (Rat)

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Q6TMG5 (NEMO_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 63. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	Ikbkg
Synonyms:	Nemo

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	412 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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.
Subunit structure	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 TANK; the interaction is enhanced by IKBKE and TBK1. Part of a ternary complex consisting of TANK, IKBKB and IKBKG By similarity. 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.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Domain	The leucine-zipper domain and the C2HC-type zinc-finger are essential for polyubiquitin binding and for the activation of IRF3 By similarity.
Post-translational modification	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.
Sequence similarities	Contains 1 C2HC-type zinc finger.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
PTM	Disulfide bond Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell homeostasis Inferred from electronic annotation. Source: Compara NF-kappaB import into nucleus Traceable author statement Ref.1. Source: RGD activation of NF-kappaB-inducing kinase activity Inferred from electronic annotation. Source: Compara positive regulation of NF-kappaB transcription factor activity Traceable author statement Ref.1. Source: RGD response to DNA damage stimulus Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	IkappaB kinase complex Inferred from direct assay PubMed 17419723. Source: RGD nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 412

412

NF-kappa-B essential modulator

PRO_0000269197

Regions

Zinc finger

389 – 410

C2HC-type

Region

44 – 111

Interaction with CHUK/IKBKB By similarity

Region

150 – 250

101

Interaction with TANK By similarity

Region

242 – 343

102

Ubiquitin-binding (UBD)

Region

246 – 358

113

Self-association By similarity

Region

249 – 412

164

Required for interaction with TNFAIP3 By similarity

Region

315 – 336

Leucine-zipper Potential

Region

375 – 412

Interaction with CYLD By similarity

Coiled coil

49 – 343

295

Potential

Amino acid modifications

Modified residue

Phosphoserine; by IKKB By similarity

Modified residue

Phosphoserine; by IKKB By similarity

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine; by ATM By similarity

Modified residue

369

Phosphoserine; by IKKB By similarity

Disulfide bond

Interchain By similarity

Disulfide bond

340

Interchain By similarity

Cross-link

111

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

139

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

143

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

226

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

246

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

270

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity

Cross-link

270

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity

Cross-link

276

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

278

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

285

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

295

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

302

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity

Cross-link

302

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity

Cross-link

314

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

319

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Cross-link

392

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q6TMG5 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 6D5D96B08A4CCEC2
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FASTA

412

48,066

        10         20         30         40         50         60 
MSRHLWKNQL SEMVQPSGGP AEDQDMLGEE SSLGKPAMLH LPSEQGTPET LQRCLEENQE 

        70         80         90        100        110        120 
LRDAIRQSNQ MLRERCEELL HFQVSQREEK EFLMCKFQEA RKLVERLSLE KLDLRRQREQ 

       130        140        150        160        170        180 
ALEDLEHLKK CQQQMAEDKA SVKAQVTSLL GELQESQSRL EAATKERQTL EGRIRAVSEQ 

       190        200        210        220        230        240 
VRQLESEREV LQQQHSVQVD QLRMQNQSVE AALRMERQAA SEEKRKLAQL QAAYHQLFQD 

       250        260        270        280        290        300 
YDSHIKSSKG MQLEDLRQQL QQAEEALVAK QELIDKLKEE AEQHKIVMET VPVLKAQADI 

       310        320        330        340        350        360 
YKADFQAERH AREKLVERKE LLQEQLEQLQ REFNKLKVGC HESARIEDMR KRHVETSQPP 

       370        380        390        400        410 
LLPAPAHHSF HLALSNQRRS PPEEPPDFCC PKCQYQAPDM DTLQIHVMEC IE

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References

[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.

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY392762 mRNA. Translation: AAQ94056.1.
IPI	IPI00400576.
RefSeq	NP_954534.1. NM_199103.1.
UniGene	Rn.214715.
3D structure databases
ProteinModelPortal	Q6TMG5.
SMR	Q6TMG5. Positions 49-109, 193-248, 387-412.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000053114.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000056275; ENSRNOP00000053114; ENSRNOG00000037237.
GeneID	309295.
KEGG	rno:309295.
Organism-specific databases
CTD	8517.
RGD	735223. Ikbkg.
Phylogenomic databases
eggNOG	NOG138369.
GeneTree	ENSGT00530000063808.
HOGENOM	HOG000293233.
HOVERGEN	HBG000417.
InParanoid	Q6TMG5.
KO	K07210.
OrthoDB	EOG42BX8V.
Gene expression databases
ArrayExpress	Q6TMG5.
Genevestigator	Q6TMG5.
Family and domain databases
InterPro	IPR021063. NEMO_N. [Graphical view]
Pfam	PF11577. NEMO. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	660548.

Entry information

Entry name

NEMO_RAT

Accession

Primary (citable) accession number: Q6TMG5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	July 5, 2004
Last modified:	April 3, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents