Q9Y6K9 (NEMO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
NF-kappa-B essential modulator
Short name=NEMO

Alternative name(s):
FIP-3
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:	FIP3, NEMO

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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 By similarity. Essential for viral activation of IRF3. Ref.26 Ref.34
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 HTLV-1 Tax oncoprotein; the interaction activates IKBKG. 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 RIPK2. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.21 Ref.23 Ref.24 Ref.27 Ref.28 Ref.30 Ref.31 Ref.32 Ref.41 Ref.51
Subcellular location	Cytoplasm. Nucleus. Note: Sumoylated NEMO accumulates in the nucleus in response to genotoxic stress. Ref.18
Tissue specificity	Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.
Domain	The leucine-zipper domain and the C2HC-type zinc-finger are essential for polyubiquitin binding and for the activation of IRF3. Ref.34 Ref.40
Post-translational modification	Phosphorylation at Ser-68 attenuates aminoterminal homodimerization. Polyubiquitinated on Lys-285 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-399 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-277 and Lys-309; promotes nuclear export. Linear polyubiquitinated on Lys-111, Lys-143, Lys-226, Lys-246, Lys-264, Lys-277, Lys-285, Lys-292, Lys-302, Lys-309 and Lys-326; the head-to-tail polyubiquitination is mediated by the LUBAC complex and plays a key role in NF-kappa-B activation. Sumoylated on Lys-277 and Lys-309 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. Ref.18
Involvement in disease	Defects in IKBKG are the cause of ectodermal dysplasia anhidrotic with immunodeficiency X-linked (EDAID) [MIM:300291]; also known as hypohidrotic ectodermal dysplasia with immunodeficiency (HED-ID). Is a form of ectoderma dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. Characterized by absence of sweat glands, sparse scalp hair, rare conical teeth and immunological abnormalities resulting in severe infectious diseases. Ref.18 Ref.42 Ref.44 Ref.45 Ref.46 Ref.48 Defects in IKBKG are the cause of ectodermal dysplasia anhidrotic with immunodeficiency-osteopetrosis-lymphedema (OLEDAID) [MIM:300301]. Defects in IKBKG are a cause of immunodeficiency NEMO-related without anhidrotic ectodermal dysplasia (NEMOID) [MIM:300584]; also called immunodeficiency without anhidrotic ectodermal dysplasia, isolated immunodeficiency or pure immunodeficiency. Patients manifest immunodeficiency not associated with other abnormalities, and resulting in increased infection susceptibility. Patients suffer from multiple episodes of infectious diseases. Ref.48 Ref.49 Defects in IKBKG are the cause of susceptibility to X-linked familial atypical micobacteriosis type 1 (AMCBX1) [MIM:300636]; also known as X-linked disseminated atypical mycobacterial infection type 1 or X-linked susceptibility to mycobacterial disease type 1. AMCBX1 is the X-linked recessive form of mendelian susceptibility to mycobacterial disease (MSMD). MSMD is a congenital syndrome resulting in predisposition to clinical disease caused by weakly virulent mycobacterial species, such as bacillus Calmette-Guerin vaccines and non-tuberculous, environmental mycobacteria. Patients are also susceptible to the more virulent species Mycobacterium tuberculosis. Ref.50 Defects in IKBKG are the cause of recurrent isolated invasive pneumococcal disease type 2 (IPD2) [MIM:300640]. Recurrent invasive pneumococcal disease (IPD) is defined as two episodes of IPD occurring at least 1 month apart, whether caused by the same or different serotypes or strains. Recurrent IPD occurs in at least 2% of patients in most series, making IPD the most important known risk factor for subsequent IPD. Ref.52 Defects in IKBKG are the cause of incontinentia pigmenti (IP) [MIM:308300]; formerly designed familial incontinentia pigmenti type II (IP2). IP is a genodermatosis usually prenatally lethal in males. In affected females, it causes abnormalities of the skin, hair, eyes, nails, teeth, skeleton, heart, and central nervous system. The prominent skin signs occur in four classic cutaneous stages: perinatal inflammatory vesicles, verrucous patches, a distinctive pattern of hyperpigmentation and dermal scarring. Ref.4 Ref.43 Ref.47 Ref.51 Ref.52
Sequence similarities	Contains 1 C2HC-type zinc finger.

Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Disease	Disease mutation Ectodermal dysplasia Osteopetrosis
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
PTM	Disulfide bond Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	JNK cascade Traceable author statement. Source: Reactome MyD88-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome MyD88-independent toll-like receptor signaling pathway Traceable author statement. Source: Reactome T cell receptor signaling pathway Non-traceable author statement Ref.25. Source: UniProtKB Toll signaling pathway Traceable author statement. Source: Reactome activation of MAPK activity Traceable author statement. Source: Reactome induction of apoptosis Traceable author statement. Source: ProtInc inflammatory response Traceable author statement. Source: UniProtKB innate immune response Traceable author statement. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW nucleotide-binding oligomerization domain containing signaling pathway Traceable author statement. Source: Reactome positive regulation of I-kappaB kinase/NF-kappaB cascade Traceable author statement. Source: Reactome positive regulation of NF-kappaB transcription factor activity Inferred from direct assay Ref.22. Source: UniProtKB response to DNA damage stimulus Inferred from direct assay Ref.18. Source: UniProtKB response to virus Traceable author statement. Source: UniProtKB stress-activated MAPK cascade Traceable author statement. Source: Reactome toll-like receptor 1 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 2 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 3 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 4 signaling pathway Traceable author statement. Source: Reactome transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	IkappaB kinase complex Traceable author statement. Source: UniProtKB nucleus Inferred from direct assay Ref.18. Source: UniProtKB
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein domain specific binding Inferred from physical interaction. Source: UniProtKB signal transducer activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ANXA1	P04083	6	EBI-81279,EBI-354007
CHUK	O15111	9	EBI-81279,EBI-81249
COPS3	Q9UNS2	2	EBI-81279,EBI-350590
GIT2	Q14161	6	EBI-81279,EBI-1046878
IKBKB	O14920	6	EBI-81279,EBI-81266
KRT18	P05783	3	EBI-81279,EBI-297888
KRT8	P05787	2	EBI-81279,EBI-297852
RIPK1	Q13546	6	EBI-81279,EBI-358507
SRC	P12931	3	EBI-81279,EBI-621482
TNFAIP3	P21580	2	EBI-81279,EBI-527670
TNIP2	Q8NFZ5	6	EBI-81279,EBI-359372

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9Y6K9-1)

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.

Isoform 2 (identifier: Q9Y6K9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MALVIQVGKLRPREVRTPQTINPSLFPSLPVKLSSIIEVPSGGERCCSRRTLVYKARAFWKGAPLPCWM

Isoform 3 (identifier: Q9Y6K9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     174-224: Missing.
     257-304: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 419

419

NF-kappa-B essential modulator

PRO_0000096782

Regions

Domain

322 – 343

22

Leucine-zipper Potential

Zinc finger

396 – 417

22

C2HC-type

Region

44 – 111

68

Interaction with CHUK/IKBKB

Region

150 – 257

108

Interaction with TANK

Region

246 – 365

120

Self-association

Region

382 – 419

38

Interaction with CYLD

Coiled coil

49 – 356

308

Potential

Amino acid modifications

Modified residue

31

1

Phosphoserine; by IKKB Ref.19

Modified residue

43

1

Phosphoserine; by IKKB Ref.19

Modified residue

68

1

Phosphoserine Ref.32

Modified residue

85

1

Phosphoserine; by ATM Ref.28

Modified residue

374

1

Phosphotyrosine Ref.35

Modified residue

376

1

Phosphoserine; by IKKB Ref.19

Modified residue

377

1

Phosphoserine Ref.33

Modified residue

387

1

Phosphoserine Ref.33 Ref.35

Disulfide bond

54

Interchain Ref.30

Disulfide bond

347

Interchain Ref.30

Cross-link

111

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.39

Cross-link

139

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.39

Cross-link

143

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.39

Cross-link

226

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.39

Cross-link

246

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.39

Cross-link

264

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.39

Cross-link

277

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.18 Ref.39

Cross-link

277

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

Cross-link

283

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.39

Cross-link

285

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.22 Ref.36 Ref.39

Cross-link

292

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.39

Cross-link

302

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.39

Cross-link

309

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.18 Ref.36 Ref.39

Cross-link

309

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

Cross-link

321

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

Cross-link

325

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

Cross-link

326

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

Cross-link

399

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.26

Natural variations

Alternative sequence

1

1

M → MALVIQVGKLRPREVRTPQT INPSLFPSLPVKLSSIIEVP SGGERCCSRRTLVYKARAFW KGAPLPCWM in isoform 2.

VSP_041000

Alternative sequence

174 – 224

51

Missing in isoform 3.

VSP_041001

Alternative sequence

257 – 304

48

Missing in isoform 3.

VSP_041002

Natural variant

57

1

E → K in IP; shows the same luciferase activity as the control. Ref.43 Ref.47
Corresponds to variant rs148695964 [ dbSNP | Ensembl ].

VAR_026491

Natural variant

90

1

Missing in IP; only 46.3% of the activation obtained with the wild-type protein.

VAR_026492

Natural variant

113

1

D → N. Ref.47
Corresponds to variant rs179363896 [ dbSNP | Ensembl ].

VAR_026493

Natural variant

123

1

R → W in IP; shows the same luciferase activity as the control. Ref.47
Corresponds to variant rs179363895 [ dbSNP | Ensembl ].

VAR_026494

Natural variant

153

1

L → R in EDAID. Ref.46 Ref.48

VAR_026495

Natural variant

173

1

R → G in IPD2. Ref.52
Corresponds to variant rs179363866 [ dbSNP | Ensembl ].

VAR_031958

Natural variant

175

1

R → P in EDAID. Ref.44
Corresponds to variant rs179363868 [ dbSNP | Ensembl ].

VAR_011320

Natural variant

227

1

L → P in EDAID. Ref.44
Corresponds to variant rs179363869 [ dbSNP | Ensembl ].

VAR_011321

Natural variant

288

1

A → G in EDAID. Ref.44

VAR_011322

Natural variant

311

1

D → N in EDAID. Ref.44
Corresponds to variant rs179363867 [ dbSNP | Ensembl ].

VAR_011323

Natural variant

315

1

E → A in AMCBX1. Ref.50

VAR_031959

Natural variant

319

1

R → Q in AMCBX1. Ref.50

VAR_031960

Natural variant

323

1

A → P in IP; diminishes interaction with TRAF6 and polyubiquitination. Ref.51
Corresponds to variant rs179363865 [ dbSNP | Ensembl ].

VAR_042666

Natural variant

406

1

D → V in EDAID. Ref.45

VAR_011324

Natural variant

407

1

M → V in IP. Ref.4 Ref.43

VAR_009182

Natural variant

417

1

C → F in EDAID. Ref.40 Ref.42 Ref.44
Corresponds to variant rs137853326 [ dbSNP | Ensembl ].

VAR_011325

Natural variant

417

1

C → R in EDAID; loss of sumoylation. Ref.18 Ref.42 Ref.44 Ref.45 Ref.46 Ref.48

VAR_011326

Natural variant

417

1

C → Y in NEMOID. Ref.48
Corresponds to variant rs137853326 [ dbSNP | Ensembl ].

VAR_026496

Experimental info

Mutagenesis

68

1

S → A: Increases formation of homodimers. Ref.32

Mutagenesis

68

1

S → E: Abolishes interaction with IKBKB; abolishes TNF-alpha induced NF-kappa-B activity. Ref.32

Mutagenesis

85

1

S → A: Decreases ubiquitination and abolishes nuclear export. Ref.28

Mutagenesis

115

1

K → R: No change in the ubiquitination level; when associated with R-399. Ref.22

Mutagenesis

224

1

K → R: No change in the ubiquitination level; when associated with R-399. Ref.22

Mutagenesis

277

1

K → A: Partial abolition of sumoylation. Abolishes sumoylation and IKK activation; when associated with A-309. Ref.18

Mutagenesis

285

1

K → R: Important decrease in the ubiquitination level; when associated with R-399. Ref.22

Mutagenesis

309

1

K → A: Partial abolition of sumoylation. Abolishes sumoylation and IKK activation; when associated with A-277. Ref.18

Mutagenesis

399

1

K → R: Abolishes BCL10-mediated but not RIPK2-mediated ubiquitination. Important decrease in the ubiquitination level; when associated with R-285. No change in the ubiquitination level; when associated with R-115 or R-224. Ref.22 Ref.26

Sequence conflict

341

1

S → R in AAD12183. Ref.1

Sequence conflict

387

1

S → R in AAD12183. Ref.1

Secondary structure

1

.

.

.

.

.

.

419

Helix Strand Turn

Details...

Helix

50 – 108

59

Turn

194 – 196

3

Helix

197 – 249

53

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 322D1037881447FF	FASTA	419	48,198
	10 20 30 40 50 60 MNRHLWKSQL CEMVQPSGGP AADQDVLGEE SPLGKPAMLH LPSEQGAPET LQRCLEENQE 70 80 90 100 110 120 LRDAIRQSNQ ILRERCEELL HFQASQREEK EFLMCKFQEA RKLVERLGLE KLDLKRQKEQ 130 140 150 160 170 180 ALREVEHLKR CQQQMAEDKA SVKAQVTSLL GELQESQSRL EAATKECQAL EGRARAASEQ 190 200 210 220 230 240 ARQLESEREA LQQQHSVQVD QLRMQGQSVE AALRMERQAA SEEKRKLAQL QVAYHQLFQE 250 260 270 280 290 300 YDNHIKSSVV GSERKRGMQL EDLKQQLQQA EEALVAKQEV IDKLKEEAEQ HKIVMETVPV 310 320 330 340 350 360 LKAQADIYKA DFQAERQARE KLAEKKELLQ EQLEQLQREY SKLKASCQES ARIEDMRKRH 370 380 390 400 410 VEVSQAPLPP APAYLSSPLA LPSQRRSPPE EPPDFCCPKC QYQAPDMDTL QIHVMECIE
	Isoform 2 [UniParc]. Checksum: 7A39E991E0013A73	FASTA	487	55,787
	10 20 30 40 50 60 MALVIQVGKL RPREVRTPQT INPSLFPSLP VKLSSIIEVP SGGERCCSRR TLVYKARAFW 70 80 90 100 110 120 KGAPLPCWMN RHLWKSQLCE MVQPSGGPAA DQDVLGEESP LGKPAMLHLP SEQGAPETLQ 130 140 150 160 170 180 RCLEENQELR DAIRQSNQIL RERCEELLHF QASQREEKEF LMCKFQEARK LVERLGLEKL 190 200 210 220 230 240 DLKRQKEQAL REVEHLKRCQ QQMAEDKASV KAQVTSLLGE LQESQSRLEA ATKECQALEG 250 260 270 280 290 300 RARAASEQAR QLESEREALQ QQHSVQVDQL RMQGQSVEAA LRMERQAASE EKRKLAQLQV 310 320 330 340 350 360 AYHQLFQEYD NHIKSSVVGS ERKRGMQLED LKQQLQQAEE ALVAKQEVID KLKEEAEQHK 370 380 390 400 410 420 IVMETVPVLK AQADIYKADF QAERQAREKL AEKKELLQEQ LEQLQREYSK LKASCQESAR 430 440 450 460 470 480 IEDMRKRHVE VSQAPLPPAP AYLSSPLALP SQRRSPPEEP PDFCCPKCQY QAPDMDTLQI HVMECIE
	Isoform 3 [UniParc]. Checksum: 3BEF2487C4446725	FASTA	320	36,953
	10 20 30 40 50 60 MNRHLWKSQL CEMVQPSGGP AADQDVLGEE SPLGKPAMLH LPSEQGAPET LQRCLEENQE 70 80 90 100 110 120 LRDAIRQSNQ ILRERCEELL HFQASQREEK EFLMCKFQEA RKLVERLGLE KLDLKRQKEQ 130 140 150 160 170 180 ALREVEHLKR CQQQMAEDKA SVKAQVTSLL GELQESQSRL EAATKECQAL EGRRKLAQLQ 190 200 210 220 230 240 VAYHQLFQEY DNHIKSSVVG SERKRADIYK ADFQAERQAR EKLAEKKELL QEQLEQLQRE 250 260 270 280 290 300 YSKLKASCQE SARIEDMRKR HVEVSQAPLP PAPAYLSSPL ALPSQRRSPP EEPPDFCCPK 310 320 CQYQAPDMDT LQIHVMECIE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 9927690] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Isolation of full-length cDNA and chromosomal localization of human NF-kappaB modulator NEMO to Xq28." Jin D.-Y., Jeang K.-T. J. Biomed. Sci. 6:115-120(1999) [PubMed: 10087442] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Mammary cancer.
[3]	"IKK-gamma is an essential regulatory subunit of the IkappaB kinase complex." Rothwarf D.M., Zandi E., Natoli G., Karin M. Nature 395:297-300(1998) [PubMed: 9751060] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE. Tissue: Cervix carcinoma.
[4]	"Genomic rearrangement in NEMO impairs NF-kappaB activation and is a cause of incontinentia pigmenti." Smahi A., Courtois G., Vabres P., Yamaoka S., Heuertz S., Munnich A., Israel A., Heiss N.S., Klauck S.M., Kioschis P., Wiemann S., Poustka A., Esposito T., Bardaro T., Gianfrancesco F., Ciccodicola A., D'Urso M., Woffendin H. , Jakins T., Donnai D., Stewart H., Kenwrick S.J., Aradhya S., Yamagata T., Levy M., Lewis R.A., Nelson D.L. Nature 405:466-472(2000) [PubMed: 10839543] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT IP VAL-407.
[5]	"cDNA cloning by amplification of circularized first strand cDNAs reveals non-IRE-regulated iron-responsive mRNAs." Ye Z., Connor J.R. Biochem. Biophys. Res. Commun. 275:223-227(2000) [PubMed: 10944468] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Astrocytoma.
[6]	"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] (ISOFORM 2).
[7]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[8]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[9]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lung, Placenta and Skin.
[11]	"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: 9891086] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 51-419 (ISOFORM 1), PROTEIN SEQUENCE OF 144-159. Tissue: Cervix carcinoma.
[12]	"Role of adapter function in oncoprotein-mediated activation of NF-kappaB: human T-cell leukemia virus type I Tax interacts directly with IkappaB kinase gamma." Jin D.-Y., Giordano V., Kibler K.V., Nakano H., Jeang K.-T. J. Biol. Chem. 274:17402-17405(1999) [PubMed: 10364167] [Abstract] Cited for: INTERACTION WITH HTLV-1 TAX-1.
[13]	"Activation of IKKalpha and IKKbeta through their fusion with HTLV-I tax protein." Xiao G., Sun S.C. Oncogene 19:5198-5203(2000) [PubMed: 11064457] [Abstract] Cited for: INTERACTION WITH HTLV-1 TAX-1.
[14]	"CSN3 interacts with IKKgamma and inhibits TNF- but not IL-1-induced NF-kappaB activation." Hong X., Xu L.-G., Li X., Zhai Z., Shu H.-B. FEBS Lett. 499:133-136(2001) [PubMed: 11418127] [Abstract] Cited for: INTERACTION WITH COPS3.
[15]	"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: 11080499] [Abstract] Cited for: SUBUNIT OF THE IKK COMPLEX.
[16]	"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: 12133833] [Abstract] Cited for: INTERACTION WITH TANK AND IKBKB.
[17]	"Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator activity by I kappa B kinase." Wu R.-C., Qin J., Hashimoto Y., Wong J., Xu J., Tsai S.Y., Tsai M.-J., O'Malley B.W. Mol. Cell. Biol. 22:3549-3561(2002) [PubMed: 11971985] [Abstract] Cited for: SUBUNIT OF A COMPLEX CONTAINING CREBBP; NCOA2; NCOA3; IKKA AND IKKB.
[18]	"Sequential modification of NEMO/IKKgamma by SUMO-1 and ubiquitin mediates NF-kappaB activation by genotoxic stress." Huang T.T., Wuerzberger-Davis S.M., Wu Z.H., Miyamoto S. Cell 115:565-576(2003) [PubMed: 14651848] [Abstract] Cited for: SUMOYLATION AT LYS-277 AND LYS-309, UBIQUITINATION AT LYS-277 AND LYS-309, MUTAGENESIS OF LYS-277 AND LYS-309, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT EDAID ARG-417.
[19]	"In vivo identification of inducible phosphoacceptors in the IKKgamma/NEMO subunit of human IkappaB kinase." Carter R.S., Pennington K.N., Ungurait B.J., Ballard D.W. J. Biol. Chem. 278:19642-19648(2003) [PubMed: 12657630] [Abstract] Cited for: PHOSPHORYLATION AT SER-31; SER-43 AND SER-376.
[20]	"Tetrameric oligomerization of IkappaB kinase gamma (IKKgamma) is obligatory for IKK complex activity and NF-kappaB activation." Tegethoff S., Behlke J., Scheidereit C. Mol. Cell. Biol. 23:2029-2041(2003) [PubMed: 12612076] [Abstract] Cited for: SELF-ASSOCIATION, COMPOSITION OF THE IKK COMPLEX.
[21]	"The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination." Kovalenko A., Chable-Bessia C., Cantarella G., Israeel A., Wallach D., Courtois G. Nature 424:801-805(2003) [PubMed: 12917691] [Abstract] Cited for: INTERACTION WITH CYLD.
[22]	"The Crohn's disease protein, NOD2, requires RIP2 in order to induce ubiquitinylation of a novel site on NEMO." Abbott D.W., Wilkins A., Asara J.M., Cantley L.C. Curr. Biol. 14:2217-2227(2004) [PubMed: 15620648] [Abstract] Cited for: UBIQUITINATION AT LYS-285, MUTAGENESIS OF LYS-115; LYS-224; LYS-285 AND LYS-399.
[23]	"ZNF216 is an A20-like and IkappaB kinase gamma-interacting inhibitor of NFkappaB activation." Huang J., Teng L., Li L., Liu T., Li L., Chen D., Xu L.-G., Zhai Z., Shu H.-B. J. Biol. Chem. 279:16847-16853(2004) [PubMed: 14754897] [Abstract] Cited for: INTERACTION WITH ZFAND5.
[24]	"PAN1/NALP2/PYPAF2, an inducible inflammatory mediator that regulates NF-kappaB and caspase-1 activation in macrophages." Bruey J.-M., Bruey-Sedano N., Newman R., Chandler S., Stehlik C., Reed J.C. J. Biol. Chem. 279:51897-51907(2004) [PubMed: 15456791] [Abstract] Cited for: INTERACTION WITH NALP2.
[25]	"The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes." Sun L., Deng L., Ea C.-K., Xia Z.-P., Chen Z.J. Mol. Cell 14:289-301(2004) [PubMed: 15125833] [Abstract] Cited for: UBIQUITINATION.
[26]	"Bcl10 activates the NF-kappaB pathway through ubiquitination of NEMO." Zhou H., Wertz I., O'Rourke K., Ultsch M., Seshagiri S., Eby M., Xiao W., Dixit V.M. Nature 427:167-171(2004) [PubMed: 14695475] [Abstract] Cited for: FUNCTION, UBIQUITINATION AT LYS-399, MUTAGENESIS OF LYS-399.
[27]	"PIDD mediates NF-kappaB activation in response to DNA damage." Janssens S., Tinel A., Lippens S., Tschopp J. Cell 123:1079-1092(2005) [PubMed: 16360037] [Abstract] Cited for: INTERACTION WITH LRDD.
[28]	"Molecular linkage between the kinase ATM and NF-kappaB signaling in response to genotoxic stimuli." Wu Z.H., Shi Y., Tibbetts R.S., Miyamoto S. Science 311:1141-1146(2006) [PubMed: 16497931] [Abstract] Cited for: INTERACTION WITH ATM, PHOSPHORYLATION AT SER-85, MUTAGENESIS OF SER-85.
[29]	"Site-specific Lys-63-linked tumor necrosis factor receptor-associated factor 6 auto-ubiquitination is a critical determinant of I kappa B kinase activation." Lamothe B., Besse A., Campos A.D., Webster W.K., Wu H., Darnay B.G. J. Biol. Chem. 282:4102-4112(2007) [PubMed: 17135271] [Abstract] Cited for: UBIQUITINATION.
[30]	"Intermolecular disulfide bond formation in the NEMO dimer requires Cys54 and Cys347." Herscovitch M., Comb W., Ennis T., Coleman K., Yong S., Armstead B., Kalaitzidis D., Chandani S., Gilmore T.D. Biochem. Biophys. Res. Commun. 367:103-108(2008) [PubMed: 18164680] [Abstract] Cited for: SUBUNIT, DISULFIDE BONDS.
[31]	"A critical role of RICK/RIP2 polyubiquitination in Nod-induced NF-kappaB activation." Hasegawa M., Fujimoto Y., Lucas P.C., Nakano H., Fukase K., Nunez G., Inohara N. EMBO J. 27:373-383(2008) [PubMed: 18079694] [Abstract] Cited for: INTERACTION WITH RIPK2.
[32]	"Phosphorylation of serine 68 in the IkappaB kinase (IKK)-binding domain of NEMO interferes with the structure of the IKK complex and tumor necrosis factor-alpha-induced NF-kappaB activity." Palkowitsch L., Leidner J., Ghosh S., Marienfeld R.B. J. Biol. Chem. 283:76-86(2008) [PubMed: 17977820] [Abstract] Cited for: INTERACTION WITH IKBKB, PHOSPHORYLATION AT SER-68, MUTAGENESIS OF SER-68.
[33]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 AND SER-387, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[34]	"Key role of Ubc5 and lysine-63 polyubiquitination in viral activation of IRF3." Zeng W., Xu M., Liu S., Sun L., Chen Z.J. Mol. Cell 36:315-325(2009) [PubMed: 19854139] [Abstract] Cited for: FUNCTION, DOMAIN LEUCINE-ZIPPER AND C2HC-TYPE ZINC-FINGER.
[35]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-374 AND SER-387, MASS SPECTROMETRY.
[36]	"Involvement of linear polyubiquitylation of NEMO in NF-kappaB activation." Tokunaga F., Sakata S., Saeki Y., Satomi Y., Kirisako T., Kamei K., Nakagawa T., Kato M., Murata S., Yamaoka S., Yamamoto M., Akira S., Takao T., Tanaka K., Iwai K. Nat. Cell Biol. 11:123-132(2009) [PubMed: 19136968] [Abstract] Cited for: UBIQUITINATION AT LYS-285 AND LYS-309.
[37]	"Linear ubiquitination prevents inflammation and regulates immune signalling." Gerlach B., Cordier S.M., Schmukle A.C., Emmerich C.H., Rieser E., Haas T.L., Webb A.I., Rickard J.A., Anderton H., Wong W.W., Nachbur U., Gangoda L., Warnken U., Purcell A.W., Silke J., Walczak H. Nature 471:591-596(2011) [PubMed: 21455173] [Abstract] Cited for: UBIQUITINATION BY THE LUBAC COMPLEX.
[38]	"SHARPIN is a component of the NF-kappaB-activating linear ubiquitin chain assembly complex." Tokunaga F., Nakagawa T., Nakahara M., Saeki Y., Taniguchi M., Sakata S., Tanaka K., Nakano H., Iwai K. Nature 471:633-636(2011) [PubMed: 21455180] [Abstract] Cited for: UBIQUITINATION BY THE LUBAC COMPLEX.
[39]	"SHARPIN forms a linear ubiquitin ligase complex regulating NF-kappaB activity and apoptosis." Ikeda F., Deribe Y.L., Skanland S.S., Stieglitz B., Grabbe C., Franz-Wachtel M., van Wijk S.J., Goswami P., Nagy V., Terzic J., Tokunaga F., Androulidaki A., Nakagawa T., Pasparakis M., Iwai K., Sundberg J.P., Schaefer L., Rittinger K., Macek B., Dikic I. Nature 471:637-641(2011) [PubMed: 21455181] [Abstract] Cited for: UBIQUITINATION AT LYS-277; LYS-285; LYS-309; LYS-326; LYS-111; LYS-143; LYS-226; LYS-246; LYS-264; LYS-292 AND LYS-302 BY THE LUBAC COMPLEX, UBIQUITINATION AT LYS-139 AND LYS-283.
[40]	"Solution structure of NEMO zinc finger and impact of an anhidrotic ectodermal dysplasia with immunodeficiency-related point mutation." Cordier F., Vinolo E., Veron M., Delepierre M., Agou F. J. Mol. Biol. 377:1419-1432(2008) [PubMed: 18313693] [Abstract] Cited for: STRUCTURE BY NMR OF 394-419 OF WILD-TYPE AND MUTANT PHE-417, DOMAIN ZINC FINGER.
[41]	"Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site." Rushe M., Silvian L., Bixler S., Chen L.L., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A. Structure 16:798-808(2008) [PubMed: 18462684] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 44-111 IN COMPLEX WITH CHUK AND IKBKB, SUBUNIT.
[42]	"A novel X-linked disorder of immune deficiency and hypohidrotic ectodermal dysplasia is allelic to incontinentia pigmenti and due to mutations in IKK-gamma (NEMO)." Zonana J., Elder M.E., Schneider L.C., Orlow S.J., Moss C., Golabi M., Shapira S.K., Farndon P.A., Wara D.W., Emmal S.A., Ferguson B.M. Am. J. Hum. Genet. 67:1555-1562(2000) [PubMed: 11047757] [Abstract] Cited for: VARIANTS EDAID ARG-417 AND PHE-417.
[43]	"A recurrent deletion in the ubiquitously expressed NEMO (IKK-gamma) gene accounts for the vast majority of incontinentia pigmenti mutations." Aradhya S., Woffendin H., Jakins T., Bardaro T., Esposito T., Smahi A., Shaw C., Levy M., Munnich A., D'Urso M., Lewis R.A., Kenwrick S., Nelson D.L. Hum. Mol. Genet. 10:2171-2179(2001) [PubMed: 11590134] [Abstract] Cited for: VARIANTS IP LYS-57 AND VAL-407.
[44]	"X-linked anhidrotic ectodermal dysplasia with immunodeficiency is caused by impaired NF-kappa B signaling." Doeffinger R., Smahi A., Bessia C., Geissmann F., Feinberg J., Durandy A., Bodemer C., Kenwrick S.J., Dupuis-Girod S., Blanche S., Wood P., Rabia S.H., Headon D.J., Overbeek P.A., Le Deist F., Holland S.M., Belani K., Kumararatne D.S. , Fischer A., Shapiro R., Conley M.E., Reimund E., Kalhoff H., Abinun M., Munnich A., Israael A., Courtois G., Casanova J.-L. Nat. Genet. 27:277-285(2001) [PubMed: 11242109] [Abstract] Cited for: VARIANTS EDAID PRO-175; PRO-227; GLY-288; ASN-311; ARG-417 AND PHE-417.
[45]	"Specific missense mutations in NEMO result in hyper-IgM syndrome with hypohydrotic ectodermal dysplasia." Jain A., Ma C.A., Liu S., Brown M., Cohen J., Strober W. Nat. Immunol. 2:223-228(2001) [PubMed: 11224521] [Abstract] Cited for: VARIANTS EDAID VAL-406 AND ARG-417.
[46]	"Deficient natural killer cell cytotoxicity in patients with IKK-gamma/NEMO mutations." Orange J.S., Brodeur S.R., Jain A., Bonilla F.A., Schneider L.C., Kretschmer R., Nurko S., Rasmussen W.L., Koehler J.R., Gellis S.E., Ferguson B.M., Strominger J.L., Zonana J., Ramesh N., Ballas Z.K., Geha R.S. J. Clin. Invest. 109:1501-1509(2002) [PubMed: 12045264] [Abstract] Cited for: VARIANTS EDAID ARG-153 AND ARG-417.
[47]	"Molecular analysis of the genetic defect in a large cohort of IP patients and identification of novel NEMO mutations interfering with NF-kappaB activation." Fusco F., Bardaro T., Fimiani G., Mercadante V., Miano M.G., Falco G., Israeel A., Courtois G., D'Urso M., Ursini M.V. Hum. Mol. Genet. 13:1763-1773(2004) [PubMed: 15229184] [Abstract] Cited for: VARIANTS IP LYS-57; LYS-90 DEL AND TRP-123, VARIANT ASN-113, CHARACTERIZATION OF VARIANTS IP LYS-57; LYS-90 DEL AND TRP-123, CHARACTERIZATION OF VARIANT ASN-113.
[48]	"The presentation and natural history of immunodeficiency caused by nuclear factor kappaB essential modulator mutation." Orange J.S., Jain A., Ballas Z.K., Schneider L.C., Geha R.S., Bonilla F.A. J. Allergy Clin. Immunol. 113:725-733(2004) [PubMed: 15100680] [Abstract] Cited for: VARIANTS EDAID ARG-153 AND ARG-417, VARIANT NEMOID TYR-417.
[49]	"Human nuclear factor kappa B essential modulator mutation can result in immunodeficiency without ectodermal dysplasia." Orange J.S., Levy O., Brodeur S.R., Krzewski K., Roy R.M., Niemela J.E., Fleisher T.A., Bonilla F.A., Geha R.S. J. Allergy Clin. Immunol. 114:650-656(2004) [PubMed: 15356572] [Abstract] Cited for: INVOLVEMENT IN NEMOID.
[50]	"X-linked susceptibility to mycobacteria is caused by mutations in NEMO impairing CD40-dependent IL-12 production." Filipe-Santos O., Bustamante J., Haverkamp M.H., Vinolo E., Ku C.-L., Puel A., Frucht D.M., Christel K., von Bernuth H., Jouanguy E., Feinberg J., Durandy A., Senechal B., Chapgier A., Vogt G., de Beaucoudrey L., Fieschi C., Picard C. , Garfa M., Chemli J., Bejaoui M., Tsolia M.N., Kutukculer N., Plebani A., Notarangelo L., Bodemer C., Geissmann F., Israeel A., Veron M., Knackstedt M., Barbouche R., Abel L., Magdorf K., Gendrel D., Agou F., Holland S.M., Casanova J.-L. J. Exp. Med. 203:1745-1759(2006) [PubMed: 16818673] [Abstract] Cited for: VARIANTS AMCBX1 ALA-315 AND GLN-319.
[51]	"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: 17728323] [Abstract] Cited for: VARIANT IP PRO-323, CHARACTERIZATION OF VARIANT IP PRO-323, INTERACTION WITH TRAF6.
[52]	"IRAK4 and NEMO mutations in otherwise healthy children with recurrent invasive pneumococcal disease." Ku C.-L., Picard C., Erdos M., Jeurissen A., Bustamante J., Puel A., von Bernuth H., Filipe-Santos O., Chang H.-H., Lawrence T., Raes M., Marodi L., Bossuyt X., Casanova J.-L. J. Med. Genet. 44:16-23(2007) [PubMed: 16950813] [Abstract] Cited for: VARIANT IPD2 GLY-173.
+	Additional computationally mapped references.

Web resources

IKBKGbase

IKBKG mutation db

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF062089 mRNA. Translation: AAD12183.1.
AF091453 mRNA. Translation: AAD38081.1.
AF074382 mRNA. Translation: AAC36330.1.
AJ271718 Genomic DNA. Translation: CAB93146.1.
AF261086 mRNA. Translation: AAF99679.1.
AY114157 mRNA. Translation: AAM44073.1.
AK000593 mRNA. No translation available.
BT019621 mRNA. Translation: AAV38427.1.
AF277315 Genomic DNA. Translation: AAL27012.1.
BC000299 mRNA. Translation: AAH00299.1.
BC012114 mRNA. Translation: AAH12114.1.
BC046922 mRNA. Translation: AAH46922.1.
BC050612 mRNA. Translation: AAH50612.1.

IPI

IPI00002411.
IPI00641117.
IPI00641409.

RefSeq

NP_001093326.2. NM_001099856.2.
NP_001093327.1. NM_001099857.1.
NP_001138727.1. NM_001145255.1.
NP_003630.1. NM_003639.3.

UniGene

Hs.43505.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JVX	NMR	-	A	394-419	[»]
2JVY	NMR	-	A	394-419	[»]
3BRT	X-ray	2.25	B/D	46-111	[»]
3BRV	X-ray	2.20	B/D	44-111	[»]
3CL3	X-ray	3.20	D/E	150-272	[»]
3FX0	X-ray	3.20	A/B	246-337	[»]

ProteinModelPortal

Q9Y6K9.

SMR

Q9Y6K9. Positions 49-109, 193-251, 263-333, 394-419.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-27528N.

IntAct

Q9Y6K9. 47 interactions.

MINT

MINT-1133340.

STRING

Q9Y6K9.

PTM databases

PhosphoSite

Q9Y6K9.

Polymorphism databases

DMDM

6685695.

Proteomic databases

PRIDE

Q9Y6K9.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000369601; ENSP00000358614; ENSG00000073009.
ENST00000369606; ENSP00000358619; ENSG00000073009.
ENST00000369607; ENSP00000358620; ENSG00000073009.
ENST00000369609; ENSP00000358622; ENSG00000073009.

GeneID

8517.

KEGG

hsa:8517.

UCSC

uc004flz.1. human.

Organism-specific databases

CTD

8517.

GeneCards

GC0XP153769.

H-InvDB

HIX0017162.

HGNC

HGNC:5961. IKBKG.

HPA

CAB010373.
HPA000426.

MIM

300248. gene.
300291. phenotype.
300301. phenotype.
300584. phenotype.
300636. phenotype.
300640. phenotype.
308300. phenotype.

neXtProt

NX_Q9Y6K9.

Orphanet

69088. Anhidrotic ectodermal dysplasia - immunodeficiency - osteopetrosis - lymphedema.
98813. Hypohidrotic ectodermal dysplasia with immunodeficiency.
464. Incontinentia pigmenti.
748. Mendelian susceptibility to atypical mycobacteria.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00530000063808.

HOVERGEN

HBG000417.

InParanoid

Q9Y6K9.

OMA

FQEYDNH.

PhylomeDB

Q9Y6K9.

Enzyme and pathway databases

Pathway_Interaction_DB

bcr_5pathway. BCR signaling pathway.
nfkappabcanonicalpathway. Canonical NF-kappaB pathway.
fcer1pathway. Fc-epsilon receptor I signaling in mast cells.
il1pathway. IL1-mediated signaling events.
p75ntrpathway. p75(NTR)-mediated signaling.
tcrpathway. TCR signaling in naive CD4+ T cells.
cd8tcrpathway. TCR signaling in naive CD8+ T cells.
tnfpathway. TNF receptor signaling pathway.
trail_pathway. TRAIL signaling pathway.

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q9Y6K9.

Bgee

Q9Y6K9.

CleanEx

HS_IKBKG.

Genevestigator

Q9Y6K9.

GermOnline

ENSG00000073009. Homo sapiens.

Family and domain databases

InterPro

IPR021063. NEMO_N.
[Graphical view]

KO

K07210.

Pfam

PF11577. NEMO. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

31882.

SOURCE

Search...

Entry information

Entry name

NEMO_HUMAN

Accession

Primary (citable) accession number: Q9Y6K9
Secondary accession number(s): Q7LBY6, Q7Z7F1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 30, 2000
Last modified:	January 25, 2012
This is version 134 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.