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O88522 (NEMO_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length412 AA.
Sequence statusComplete.
Protein existenceEvidence 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. 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 IKBKE. 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. 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. 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ChukQ606804EBI-998011,EBI-646245
IkbkbO883512EBI-998011,EBI-447960
Rnf31Q924T72EBI-998011,EBI-647680
UBCP0CG483EBI-998011,EBI-3390054From a different organism.
UbcP629912EBI-998011,EBI-413074
VACWR196P247722EBI-998011,EBI-4291651From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 412412NF-kappa-B essential modulator
PRO_0000096783

Regions

Zinc finger389 – 41022C2HC-type
Region44 – 11168Interaction with CHUK/IKBKB By similarity
Region150 – 250101Interaction with TANK
Region242 – 343102Ubiquitin-binding (UBD)
Region246 – 358113Self-association By similarity
Region249 – 412164Required for interaction with TNFAIP3 By similarity
Region250 – 33990Linear polyubiquitin-binding, does not bind to 'Lys-63'-linked polyubiquitin
Region315 – 33622Leucine-zipper Potential
Region375 – 41238Interaction with CYLD By similarity
Coiled coil49 – 345297 Potential

Amino acid modifications

Modified residue311Phosphoserine; by IKKB By similarity
Modified residue431Phosphoserine; by IKKB By similarity
Modified residue681Phosphoserine By similarity
Modified residue851Phosphoserine; by ATM By similarity
Modified residue3691Phosphoserine; by IKKB Ref.10
Modified residue3801Phosphoserine By similarity
Disulfide bond54Interchain By similarity
Disulfide bond340Interchain By similarity
Cross-link111Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link143Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link226Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link246Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link270Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
Cross-link270Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
Cross-link276Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link278Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.13
Cross-link285Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link295Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link302Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
Cross-link302Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
Cross-link314Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.13
Cross-link318Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.13
Cross-link319Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.13
Cross-link392Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.13

Experimental info

Mutagenesis2781K → R: Slight decrease in TRAF6-induced polyubiquitination. Ref.13
Mutagenesis2931V → 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
Mutagenesis3011Y → 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
Mutagenesis3021K → 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
Mutagenesis3051F → A: Abolishes linear polyubiquitin-binding, impairs 'Lys-63'-linked polyubiquitin-binding and impairs of NF-kappa-B activation. Ref.15
Mutagenesis3091R → 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
Mutagenesis3121R → 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
Mutagenesis3131E → 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
Mutagenesis3141K → R: Slight decrease in TRAF6-induced polyubiquitination. Important decrease in TRAF6-induced polyubiquitination; when associated with R-318 and R-319. Ref.13
Mutagenesis3161V → P: Loss of interaction with TRAF6 and TRAF6-induced polyubiquitination. Ref.13
Mutagenesis3171E → A: Abolishes linear polyubiquitin-binding; when associated with A-313 and A-320. Ref.15
Mutagenesis3181K → 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
Mutagenesis3191K → 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
Mutagenesis3201E → A: Abolishes linear polyubiquitin-binding; when associated with A-313 and A-317. Ref.15
Mutagenesis3691S → A: Decreases phosphorylation and increases NF-kappa-B activity. Ref.10
Mutagenesis3751S → A: Decreases phosphorylation and increases NF-kappa-B activity. Ref.10
Mutagenesis3921K → R: 40% decrease in IL1-induced NF-kappa-B activation. Ref.13
Sequence conflict131M → T in AAC40153. Ref.1

Secondary structure

..... 412
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O88522 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 66C693C857A2D5E6

FASTA41247,972
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
RefSeqNP_001154895.1. NM_001161423.1.
NP_034677.2. NM_010547.2.
XP_006527913.1. XM_006527850.1.
XP_006527914.1. XM_006527851.1.
XP_006527915.1. XM_006527852.1.
UniGeneMm.12967.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V4HX-ray2.90A/B251-337[»]
2ZVNX-ray3.00B/D/F/H253-337[»]
2ZVOX-ray2.90B/D250-339[»]
3F89X-ray2.80A/B250-339[»]
3JSVX-ray2.70C/D250-343[»]
4OWFX-ray2.00A/B250-339[»]
ProteinModelPortalO88522.
SMRO88522. Positions 49-109, 193-248, 256-341, 387-412.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200602. 38 interactions.
DIPDIP-29811N.
IntActO88522. 14 interactions.
MINTMINT-143245.
STRING10090.ENSMUSP00000004330.

PTM databases

PhosphoSiteO88522.

Proteomic databases

PaxDbO88522.
PRIDEO88522.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000114127; ENSMUSP00000109762; ENSMUSG00000004221.
ENSMUST00000114128; ENSMUSP00000109763; ENSMUSG00000004221.
ENSMUST00000114133; ENSMUSP00000109768; ENSMUSG00000004221.
ENSMUST00000164101; ENSMUSP00000126770; ENSMUSG00000004221.
GeneID16151.
KEGGmmu:16151.
UCSCuc009toz.2. mouse.

Organism-specific databases

CTD8517.
MGIMGI:1338074. Ikbkg.

Phylogenomic databases

eggNOGNOG138369.
GeneTreeENSGT00530000063808.
HOGENOMHOG000293233.
HOVERGENHBG000417.
InParanoidQ924H4.
KOK07210.
TreeFamTF326608.

Gene expression databases

ArrayExpressO88522.
BgeeO88522.
CleanExMM_IKBKG.
GenevestigatorO88522.

Family and domain databases

InterProIPR021063. NEMO_N.
[Graphical view]
PfamPF11577. NEMO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO88522.
NextBio288945.
PROO88522.
SOURCESearch...

Entry information

Entry nameNEMO_MOUSE
AccessionPrimary (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: April 16, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot