Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

NF-kappa-B essential modulator

Gene

Ikbkg

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri382 – 412CCHC NOA-typePROSITE-ProRule annotationAdd BLAST31

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA damage, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-1169091. Activation of NF-kappaB in B cells.
R-MMU-168638. NOD1/2 Signaling Pathway.
R-MMU-1810476. RIP-mediated NFkB activation via ZBP1.
R-MMU-202424. Downstream TCR signaling.
R-MMU-2871837. FCERI mediated NF-kB activation.
R-MMU-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-MMU-446652. Interleukin-1 signaling.
R-MMU-450302. activated TAK1 mediates p38 MAPK activation.
R-MMU-450321. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
R-MMU-5357905. Regulation of TNFR1 signaling.
R-MMU-5357956. TNFR1-induced NFkappaB signaling pathway.
R-MMU-5607764. CLEC7A (Dectin-1) signaling.
R-MMU-5684264. MAP3K8 (TPL2)-dependent MAPK1/3 activation.
R-MMU-5689880. Ub-specific processing proteases.
R-MMU-5689896. Ovarian tumor domain proteases.
R-MMU-933542. TRAF6 mediated NF-kB activation.
R-MMU-937039. IRAK1 recruits IKK complex.
R-MMU-975144. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Ikbkg
Synonyms:Nemo
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1338074. Ikbkg.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi278K → R: Slight decrease in TRAF6-induced polyubiquitination. 1 Publication1
Mutagenesisi293V → 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. 1 Publication1
Mutagenesisi301Y → 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. 1 Publication1
Mutagenesisi302K → 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. 1 Publication1
Mutagenesisi305F → A: Abolishes linear polyubiquitin-binding, impairs 'Lys-63'-linked polyubiquitin-binding and impairs of NF-kappa-B activation. 1 Publication1
Mutagenesisi309R → 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. 1 Publication1
Mutagenesisi312R → 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. 1 Publication1
Mutagenesisi313E → 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. 1 Publication1
Mutagenesisi314K → R: Slight decrease in TRAF6-induced polyubiquitination. Important decrease in TRAF6-induced polyubiquitination; when associated with R-318 and R-319. 1 Publication1
Mutagenesisi316V → P: Loss of interaction with TRAF6 and TRAF6-induced polyubiquitination. 1 Publication1
Mutagenesisi317E → A: Abolishes linear polyubiquitin-binding; when associated with A-313 and A-320. 1 Publication1
Mutagenesisi318K → 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. 1 Publication1
Mutagenesisi319K → 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. 1 Publication1
Mutagenesisi320E → A: Abolishes linear polyubiquitin-binding; when associated with A-313 and A-317. 1 Publication1
Mutagenesisi369S → A: Decreases phosphorylation and increases NF-kappa-B activity. 1 Publication1
Mutagenesisi375S → A: Decreases phosphorylation and increases NF-kappa-B activity. 1 Publication1
Mutagenesisi392K → R: 40% decrease in IL1-induced NF-kappa-B activation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000967831 – 412NF-kappa-B essential modulatorAdd BLAST412

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei31Phosphoserine; by IKKBBy similarity1
Modified residuei43Phosphoserine; by IKKBBy similarity1
Disulfide bondi54InterchainBy similarity
Modified residuei68PhosphoserineBy similarity1
Modified residuei85Phosphoserine; by ATMBy similarity1
Cross-linki111Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki143Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki226Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki246Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki270Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki270Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki276Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki278Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki285Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki295Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki302Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki302Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki314Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki318Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki319Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Disulfide bondi340InterchainBy similarity
Modified residuei369Phosphoserine; by IKKB1 Publication1
Modified residuei380PhosphoserineCombined sources1
Cross-linki392Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

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. Deubiquitinated by USP10 in a TANK-dependent and -independent manner, leading to the negative regulation of NF-kappaB signaling upon DNA damage (By similarity).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

Keywords - PTMi

Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO88522.
MaxQBiO88522.
PaxDbiO88522.
PRIDEiO88522.

PTM databases

iPTMnetiO88522.
PhosphoSitePlusiO88522.

Expressioni

Gene expression databases

BgeeiENSMUSG00000004221.
CleanExiMM_IKBKG.
ExpressionAtlasiO88522. baseline and differential.
GenevisibleiO88522. MM.

Interactioni

Subunit structurei

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. Interacts with TANK; this interaction increases in response to DNA damage (By similarity). Interacts with USP10; this interaction increases in response to DNA damage (By similarity). Interacts with ZC3H12A; this interaction increases in response to DNA damage (By similarity).By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ChukQ606804EBI-998011,EBI-646245
IkbkbO883513EBI-998011,EBI-447960
Rnf31Q924T77EBI-998011,EBI-647680
UBCP0CG483EBI-998011,EBI-3390054From a different organism.
UbcP629912EBI-998011,EBI-413074
VACWR196P247722EBI-998011,EBI-4291651From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi200602. 40 interactors.
DIPiDIP-29811N.
IntActiO88522. 16 interactors.
MINTiMINT-143245.
STRINGi10090.ENSMUSP00000004330.

Structurei

Secondary structure

1412
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi253 – 289Combined sources37
Helixi291 – 333Combined sources43
Helixi337 – 340Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliO88522.
SMRiO88522.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO88522.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni44 – 111Interaction with CHUK/IKBKBBy similarityAdd BLAST68
Regioni150 – 250Interaction with TANK1 PublicationAdd BLAST101
Regioni242 – 343Ubiquitin-binding (UBD)Add BLAST102
Regioni246 – 358Self-associationBy similarityAdd BLAST113
Regioni249 – 412Required for interaction with TNFAIP3By similarityAdd BLAST164
Regioni250 – 339Linear polyubiquitin-binding, does not bind to 'Lys-63'-linked polyubiquitinAdd BLAST90
Regioni315 – 336Leucine-zipperSequence analysisAdd BLAST22
Regioni375 – 412Interaction with CYLDBy similarityAdd BLAST38

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili49 – 345Sequence analysisAdd BLAST297

Domaini

The leucine-zipper domain and the CCHC NOA-type zinc-finger are essential for polyubiquitin binding and for the activation of IRF3.By similarity

Sequence similaritiesi

Contains 1 CCHC NOA-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri382 – 412CCHC NOA-typePROSITE-ProRule annotationAdd BLAST31

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IJBJ. Eukaryota.
ENOG410Y1FG. LUCA.
GeneTreeiENSGT00530000063808.
HOGENOMiHOG000293233.
HOVERGENiHBG000417.
InParanoidiO88522.
KOiK07210.
TreeFamiTF326608.

Family and domain databases

InterProiIPR032419. CC2-LZ_dom.
IPR021063. NEMO_N.
[Graphical view]
PfamiPF16516. CC2-LZ. 1 hit.
PF11577. NEMO. 1 hit.
[Graphical view]
PROSITEiPS51801. ZF_CCHC_NOA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O88522-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKHPWKNQL SEMVQPSGGP AEDQDMLGEE SSLGKPAMLH LPSEQGTPET
60 70 80 90 100
LQRCLEENQE LRDAIRQSNQ MLRERCEELL HFQVSQREEK EFLMCKFQEA
110 120 130 140 150
RKLVERLSLE KLDLRSQREQ ALKELEQLKK CQQQMAEDKA SVKAQVTSLL
160 170 180 190 200
GELQESQSRL EAATKDRQAL EGRIRAVSEQ VRQLESEREV LQQQHSVQVD
210 220 230 240 250
QLRMQNQSVE AALRMERQAA SEEKRKLAQL QAAYHQLFQD YDSHIKSSKG
260 270 280 290 300
MQLEDLRQQL QQAEEALVAK QELIDKLKEE AEQHKIVMET VPVLKAQADI
310 320 330 340 350
YKADFQAERH AREKLVEKKE YLQEQLEQLQ REFNKLKVGC HESARIEDMR
360 370 380 390 400
KRHVETPQPP LLPAPAHHSF HLALSNQRRS PPEEPPDFCC PKCQYQAPDM
410
DTLQIHVMEC IE
Length:412
Mass (Da):47,972
Last modified:July 27, 2011 - v2
Checksum:i66C693C857A2D5E6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti13M → T in AAC40153 (PubMed:9657155).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41023.1.
RefSeqiNP_001154895.1. NM_001161423.1.
NP_034677.2. NM_010547.2.
XP_006527913.1. XM_006527850.2.
XP_006527914.1. XM_006527851.2.
XP_006527915.1. XM_006527852.2.
XP_011245829.1. XM_011247527.2.
UniGeneiMm.12967.

Genome annotation databases

EnsembliENSMUST00000114127; ENSMUSP00000109762; ENSMUSG00000004221.
ENSMUST00000114128; ENSMUSP00000109763; ENSMUSG00000004221.
ENSMUST00000114133; ENSMUSP00000109768; ENSMUSG00000004221.
ENSMUST00000164101; ENSMUSP00000126770; ENSMUSG00000004221.
GeneIDi16151.
KEGGimmu:16151.
UCSCiuc009toz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41023.1.
RefSeqiNP_001154895.1. NM_001161423.1.
NP_034677.2. NM_010547.2.
XP_006527913.1. XM_006527850.2.
XP_006527914.1. XM_006527851.2.
XP_006527915.1. XM_006527852.2.
XP_011245829.1. XM_011247527.2.
UniGeneiMm.12967.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliO88522.
SMRiO88522.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200602. 40 interactors.
DIPiDIP-29811N.
IntActiO88522. 16 interactors.
MINTiMINT-143245.
STRINGi10090.ENSMUSP00000004330.

PTM databases

iPTMnetiO88522.
PhosphoSitePlusiO88522.

Proteomic databases

EPDiO88522.
MaxQBiO88522.
PaxDbiO88522.
PRIDEiO88522.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000114127; ENSMUSP00000109762; ENSMUSG00000004221.
ENSMUST00000114128; ENSMUSP00000109763; ENSMUSG00000004221.
ENSMUST00000114133; ENSMUSP00000109768; ENSMUSG00000004221.
ENSMUST00000164101; ENSMUSP00000126770; ENSMUSG00000004221.
GeneIDi16151.
KEGGimmu:16151.
UCSCiuc009toz.2. mouse.

Organism-specific databases

CTDi8517.
MGIiMGI:1338074. Ikbkg.

Phylogenomic databases

eggNOGiENOG410IJBJ. Eukaryota.
ENOG410Y1FG. LUCA.
GeneTreeiENSGT00530000063808.
HOGENOMiHOG000293233.
HOVERGENiHBG000417.
InParanoidiO88522.
KOiK07210.
TreeFamiTF326608.

Enzyme and pathway databases

ReactomeiR-MMU-1169091. Activation of NF-kappaB in B cells.
R-MMU-168638. NOD1/2 Signaling Pathway.
R-MMU-1810476. RIP-mediated NFkB activation via ZBP1.
R-MMU-202424. Downstream TCR signaling.
R-MMU-2871837. FCERI mediated NF-kB activation.
R-MMU-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-MMU-446652. Interleukin-1 signaling.
R-MMU-450302. activated TAK1 mediates p38 MAPK activation.
R-MMU-450321. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
R-MMU-5357905. Regulation of TNFR1 signaling.
R-MMU-5357956. TNFR1-induced NFkappaB signaling pathway.
R-MMU-5607764. CLEC7A (Dectin-1) signaling.
R-MMU-5684264. MAP3K8 (TPL2)-dependent MAPK1/3 activation.
R-MMU-5689880. Ub-specific processing proteases.
R-MMU-5689896. Ovarian tumor domain proteases.
R-MMU-933542. TRAF6 mediated NF-kB activation.
R-MMU-937039. IRAK1 recruits IKK complex.
R-MMU-975144. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.

Miscellaneous databases

EvolutionaryTraceiO88522.
PROiO88522.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000004221.
CleanExiMM_IKBKG.
ExpressionAtlasiO88522. baseline and differential.
GenevisibleiO88522. MM.

Family and domain databases

InterProiIPR032419. CC2-LZ_dom.
IPR021063. NEMO_N.
[Graphical view]
PfamiPF16516. CC2-LZ. 1 hit.
PF11577. NEMO. 1 hit.
[Graphical view]
PROSITEiPS51801. ZF_CCHC_NOA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNEMO_MOUSE
AccessioniPrimary (citable) accession number: O88522
Secondary accession number(s): Q924H4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 27, 2011
Last modified: November 2, 2016
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.