Q6TMG5 (NEMO_RAT) Reviewed, UniProtKB/Swiss-Prot

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)

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. 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 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 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. 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 by 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.
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	NF-kappaB import into nucleus Traceable author statement Ref.1. Source: RGD positive regulation of NF-kappaB transcription factor activity Traceable author statement Ref.1. Source: RGD transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	IkappaB kinase complex Inferred from direct assay. 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
	Domain	315 – 336	22	Leucine-zipper Potential
	Zinc finger	389 – 410	22	C2HC-type
	Region	44 – 111	68	Interaction with CHUK/IKBKB By similarity
	Region	150 – 250	101	Interaction with TANK By similarity
	Region	246 – 358	113	Self-association By similarity
	Region	375 – 412	38	Interaction with CYLD By similarity
	Coiled coil	49 – 343	295	Potential
Amino acid modifications
	Modified residue	31	1	Phosphoserine; by IKKB By similarity
	Modified residue	43	1	Phosphoserine; by IKKB By similarity
	Modified residue	68	1	Phosphoserine By similarity
	Modified residue	85	1	Phosphoserine; by ATM By similarity
	Modified residue	369	1	Phosphoserine; by IKKB By similarity
	Modified residue	380	1	Phosphoserine By similarity
	Disulfide bond	54		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)
	Q6TMG5 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 6D5D96B08A4CCEC2	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

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: 12968033] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Fischer 344.

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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	Q6TMG5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	309295.
KEGG	rno:309295.
Organism-specific databases
CTD	8517.
RGD	735223. Ikbkg.
Phylogenomic databases
eggNOG	roNOG09128.
GeneTree	ENSGT00530000063808.
HOVERGEN	HBG000417.
InParanoid	Q6TMG5.
OrthoDB	EOG42BX8V.
Gene expression databases
Genevestigator	Q6TMG5.
Family and domain databases
InterPro	IPR021063. NEMO_N. [Graphical view]
KO	K07210.
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:	November 16, 2011
This is version 54 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program