O88522 (NEMO_MOUSE) 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
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 names

Name:	Ikbkg
Synonyms:	Nemo

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	412 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. 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 By similarity. Ref.8
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 TBK1 and IKBKE. Part of a ternary complex consisting of TANK, IKBKB and IKBKG. Interacts with ZFAND5. Interacts with RIPK2 By similarity. 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. Ref.11 Ref.12 Ref.14
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	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	B cell homeostasis Inferred from mutant phenotype PubMed 12235208. Source: MGI activation of NF-kappaB-inducing kinase activity Inferred from direct assay PubMed 14654787. Source: MGI regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay PubMed 14654787. Source: MGI nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Chuk	Q60680	4	EBI-998011,EBI-646245
Ikbkb	O88351	2	EBI-998011,EBI-447960
VACWR196	P24772	2	EBI-998011,EBI-4291651	From a different organism.

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_0000096783

Regions

Zinc finger

389 – 410

22

C2HC-type

Region

44 – 111

68

Interaction with CHUK/IKBKB By similarity

Region

150 – 250

101

Interaction with TANK

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

250 – 339

90

Linear polyubiquitin-binding, does not bind to 'Lys-63'-linked polyubiquitin

Region

315 – 336

22

Leucine-zipper Potential

Region

375 – 412

38

Interaction with CYLD By similarity

Coiled coil

49 – 345

297

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 Ref.10

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) Ref.13

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) 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) Ref.13

Cross-link

318

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.13

Cross-link

319

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.13

Cross-link

392

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.13

Experimental info

Mutagenesis

278

1

K → R: Slight decrease in TRAF6-induced polyubiquitination. Ref.13

Mutagenesis

293

1

V → 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. Ref.15

Mutagenesis

301

1

Y → 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. Ref.15

Mutagenesis

302

1

K → 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. Ref.15

Mutagenesis

305

1

F → A: Abolishes linear polyubiquitin-binding, impairs 'Lys-63'-linked polyubiquitin-binding and impairs of NF-kappa-B activation. Ref.15

Mutagenesis

309

1

R → 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. Ref.15

Mutagenesis

312

1

R → 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. Ref.15

Mutagenesis

313

1

E → 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. Ref.15

Mutagenesis

314

1

K → R: Slight decrease in TRAF6-induced polyubiquitination. Important decrease in TRAF6-induced polyubiquitination; when associated with R-318 and R-319. Ref.13

Mutagenesis

316

1

V → P: Loss of interaction with TRAF6 and TRAF6-induced polyubiquitination. Ref.13

Mutagenesis

317

1

E → A: Abolishes linear polyubiquitin-binding; when associated with A-313 and A-320. Ref.15

Mutagenesis

318

1

K → 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. Ref.13

Mutagenesis

319

1

K → 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. Ref.13

Mutagenesis

320

1

E → A: Abolishes linear polyubiquitin-binding; when associated with A-313 and A-317. Ref.15

Mutagenesis

369

1

S → A: Decreases phosphorylation and increases NF-kappa-B activity. Ref.10

Mutagenesis

375

1

S → A: Decreases phosphorylation and increases NF-kappa-B activity. Ref.10

Mutagenesis

392

1

K → R: 40% decrease in IL1-induced NF-kappa-B activation. Ref.13

Sequence conflict

13

1

M → T in AAC40153. Ref.1

Secondary structure

1

.

.

.

.

.

412

Helix Strand Turn

Details...

Helix

253 – 317

65

Helix

321 – 331

11

Sequences

	Sequence		Length	Mass (Da)
	O88522 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 66C693C857A2D5E6	FASTA	412	47,972
	10 20 30 40 50 60 MNKHPWKNQL SEMVQPSGGP AEDQDMLGEE SSLGKPAMLH LPSEQGTPET LQRCLEENQE 70 80 90 100 110 120 LRDAIRQSNQ MLRERCEELL HFQVSQREEK EFLMCKFQEA RKLVERLSLE KLDLRSQREQ 130 140 150 160 170 180 ALKELEQLKK CQQQMAEDKA SVKAQVTSLL GELQESQSRL EAATKDRQAL 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 AREKLVEKKE YLQEQLEQLQ REFNKLKVGC HESARIEDMR KRHVETPQPP 370 380 390 400 410 LLPAPAHHSF HLALSNQRRS PPEEPPDFCC PKCQYQAPDM DTLQIHVMEC IE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] 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]	"Telomere-independent Rap1 is an IKK adaptor and regulates NF-kappaB-dependent gene expression." Teo H., Ghosh S., Luesch H., Ghosh A., Wong E.T., Malik N., Orth A., de Jesus P., Perry A.S., Oliver J.D., Tran N.L., Speiser L.J., Wong M., Saez E., Schultz P., Chanda S.K., Verma I.M., Tergaonkar V. Nat. Cell Biol. 12:758-767(2010) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00914699.

RefSeq

NP_001154895.1. NM_001161423.1.
NP_034677.2. NM_010547.2.

UniGene

Mm.12967.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

O88522.

SMR

O88522. Positions 49-109, 193-248, 256-341, 387-412.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29811N.

IntAct

O88522. 4 interactions.

MINT

MINT-143245.

STRING

10090.ENSMUSP00000004330.

PTM databases

PhosphoSite

O88522.

Proteomic databases

PaxDb

O88522.

PRIDE

O88522.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000114127; ENSMUSP00000109762; ENSMUSG00000004221.
ENSMUST00000114128; ENSMUSP00000109763; ENSMUSG00000004221.
ENSMUST00000114133; ENSMUSP00000109768; ENSMUSG00000004221.
ENSMUST00000164101; ENSMUSP00000126770; ENSMUSG00000004221.

GeneID

16151.

KEGG

mmu:16151.

Organism-specific databases

CTD

8517.

MGI

MGI:1338074. Ikbkg.

Phylogenomic databases

eggNOG

NOG138369.

GeneTree

ENSGT00530000063808.

HOGENOM

HOG000293233.

HOVERGEN

HBG000417.

InParanoid

Q924H4.

KO

K07210.

OrthoDB

EOG42BX8V.

Gene expression databases

ArrayExpress

O88522.

Bgee

O88522.

CleanEx

MM_IKBKG.

Genevestigator

O88522.

GermOnline

ENSMUSG00000004221. Mus musculus.

Family and domain databases

InterPro

IPR021063. NEMO_N.
[Graphical view]

Pfam

PF11577. NEMO. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O88522.

NextBio

288945.

SOURCE

Search...

Entry information

Entry name

NEMO_MOUSE

Accession

Primary (citable) accession number: O88522
Secondary accession number(s): Q924H4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program