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Q9R0T8

- IKKE_MOUSE

UniProt

Q9R0T8 - IKKE_MOUSE

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Protein

Inhibitor of nuclear factor kappa-B kinase subunit epsilon

Gene

Ikbke

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

Functioni

Serine/threonine kinase that plays an essential role in regulating inflammatory responses to viral infection, through the activation of the type I IFN, NF-kappa-B and STAT signaling. Also involved in TNFA and inflammatory cytokines, like Interleukin-1, signaling. Following activation of viral RNA sensors, such as RIG-I-like receptors, associates with DDX3X and phosphorylates interferon regulatory factors (IRFs), IRF3 and IRF7, as well as DDX3X. This activity allows subsequent homodimerization and nuclear translocation of the IRF3 leading to transcriptional activation of pro-inflammatory and antiviral genes including IFNB. In order to establish such an antiviral state, IKBKE forms several different complexes whose composition depends on the type of cell and cellular stimuli. Thus, several scaffolding molecules including IPS1/MAVS, TANK, AZI2/NAP1 or TBKBP1/SINTBAD can be recruited to the IKBKE-containing-complexes. Activated by polyubiquitination in response to TNFA and interleukin-1, regulates the NF-kappa-B signaling pathway through, at least, the phosphorylation of CYLD. 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. In addition, is also required for the induction of a subset of ISGs which displays antiviral activity, may be through the phosphorylation of STAT1 at 'Ser-708'. Phosphorylation of STAT1 at 'Ser-708' seems also to promote the assembly and DNA binding of ISGF3 (STAT1:STAT2:IRF9) complexes compared to GAF (STAT1:STAT1) complexes, in this way regulating the balance between type I and type II IFN responses. Protects cells against DNA damage-induced cell death. Also plays an important role in energy balance regulation by sustaining a state of chronic, low-grade inflammation in obesity, wich leads to a negative impact on insulin sensitivity. Phosphorylates AKT1.6 Publications

Catalytic activityi

ATP + [I-kappa-B protein] = ADP + [I-kappa-B phosphoprotein].

Enzyme regulationi

Kinase activity is inhibited competitively by amlexanox.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381ATPPROSITE-ProRule annotation
Active sitei135 – 1351Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 239ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. IkappaB kinase activity Source: MGI
  3. NF-kappaB-inducing kinase activity Source: UniProtKB

GO - Biological processi

  1. I-kappaB phosphorylation Source: GOC
  2. intrinsic apoptotic signaling pathway in response to DNA damage Source: UniProtKB
  3. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  4. protein phosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

DNA damage

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.10. 3474.
ReactomeiREACT_198521. TRAF6 mediated IRF7 activation.
REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
REACT_225463. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
REACT_231481. TRAF3-dependent IRF activation pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Inhibitor of nuclear factor kappa-B kinase subunit epsilon (EC:2.7.11.10)
Short name:
I-kappa-B kinase epsilon
Short name:
IKK-E
Short name:
IKK-epsilon
Short name:
IkBKE
Alternative name(s):
Inducible I kappa-B kinase
Short name:
IKK-i
Gene namesi
Name:Ikbke
Synonyms:Ikke, Ikki
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1929612. Ikbke.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity. NucleusPML body By similarity
Note: Targeting to PML nuclear bodies upon DNA damage is TOPORS-dependent.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
  3. PML body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Animals are hypersusceptible to influenza virus infection because of a defect in the activation of a subset of type 1 IFN-stimulated genes, however the amounts of IFNB produced are normals. Lungs of mice infected 7 days with influenza virus exhibit an inflammatory infiltrate consisting of lymphocytes, macrophages and neutrophils. After West Nile virus infection, animals display earlier neurological symptoms, a higher degree of neurovirulence and a failure to recover, compared to wild type. Animals are protected from high-fat diet-induced obesity, liver and adipose inflammation, hepatic steatosis and insulin resistance. They show an increased energy expenditure and thermogenesis and maintain insulin sensitivity in liver and adipose tissue.5 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi38 – 381K → A: Dominant negative. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 717717Inhibitor of nuclear factor kappa-B kinase subunit epsilonPRO_0000086018Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki30 – 30Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei172 – 1721Phosphoserine; by autocatalysis and IKKB
Cross-linki231 – 231Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Cross-linki403 – 403Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei503 – 5031Phosphothreonine1 Publication
Modified residuei665 – 6651PhosphoserineBy similarity

Post-translational modificationi

Sumoylation by TOPORS upon DNA damage is required for protection of cells against DNA damage-induced cell death. Desumoylated by SENP1 (By similarity).By similarity
Autophosphorylated and phosphorylated by IKBKB/IKKB. Phosphorylation at Ser-172 is enhanced by the interaction with DDX3X. Phosphorylated at Thr-503 upon IFN activation.1 Publication
'Lys-63'-linked polyubiquitinated at Lys-30 and Lys-403 by TRAF2:BIRC2 and TRAF2:BIRC3 complexes. Ubiquitination is induced by LPS, TNFA and interleukin-1 and required for full kinase activity and KF-kappa-B pathway activation (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ9R0T8.

PTM databases

PhosphoSiteiQ9R0T8.

Expressioni

Tissue specificityi

Expressed in bone marrow-derived macrophages and at low levels in liver and white adipose tissue (at protein level). Detected in muscle and lung.3 Publications

Inductioni

Induced by lipopolysaccharide (LPS) and TNFA. Under high-fat diet, highly induced (via NF-kappa-B) in adipocytes and M1-polarized adipose tissue macrophages.2 Publications

Gene expression databases

BgeeiQ9R0T8.
CleanExiMM_IKBKE.
ExpressionAtlasiQ9R0T8. baseline and differential.
GenevestigatoriQ9R0T8.

Interactioni

Subunit structurei

Homodimer. Interacts with MAVS/IPS1. Interacts with the adapter proteins AZI2/NAP1, TANK and TBKBP1/SINTBAD. Interacts with SIKE1. Interacts with TICAM1/TRIF, IRF3 and DDX58/RIG-I; interactions are disrupted by the interaction between IKBKE and SIKE1. Interacts with TOPORS; induced by DNA damage. Interacts with CYLD, IKBKB, IKBKG and MYD88. Interacts with DDX3X; the interaction is found to be induced upon virus infection.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Traf3ip2Q8N7N63EBI-6664658,EBI-646165

Protein-protein interaction databases

BioGridi208014. 2 interactions.
IntActiQ9R0T8. 2 interactions.
STRINGi10090.ENSMUSP00000054126.

Structurei

3D structure databases

ProteinModelPortaliQ9R0T8.
SMRiQ9R0T8. Positions 2-648.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 315307Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni385 – 650266Interaction with DDX3XBy similarityAdd
BLAST
Regioni452 – 47322Leucine-zipperAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. I-kappa-B kinase subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00770000120525.
HOGENOMiHOG000220867.
HOVERGENiHBG008494.
InParanoidiQ9R0T8.
KOiK07211.
OMAiHIYIHAH.
OrthoDBiEOG7Z95KH.
TreeFamiTF324269.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9R0T8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQSTTNYLWH TDDLLGQGAT ASVYKARNKK SGEVVAVKVF NSASYRRPPE
60 70 80 90 100
VQVREFEVLR RLNHQNIVKL FAVEETGGSR QKVLIMEYCS SGSLLSVLED
110 120 130 140 150
PENTFGLSEE EFLVVLRCVV AGMNHLRENG IVHRDIKPGN IMRLVGEEGQ
160 170 180 190 200
SIYKLSDFGA ARKLDDDEKF VSVYGTEEYL HPDMYERAVL RKPQQKAFGV
210 220 230 240 250
TVDLWSIGVT LYHAATGSLP FIPFGGPRRN KEIMYRITTE KPAGAISGTQ
260 270 280 290 300
KQENGPLEWS YSLPITCRLS MGLQNQLVPI LANILEVEED KCWGFDQFFA
310 320 330 340 350
ETSDILQRTV IHVFSLPQAV LHHVYIHAHN TIAIFLEAVY EQTNVTPKHQ
360 370 380 390 400
EYLFEGHPCV LEPSLSAQHI AHTAASSPLT LFSMSSDTPK GLAFRDPALD
410 420 430 440 450
VPKFVPKVDL QADYSTAKGV LGAGYQALWL ARVLLDGQAL MLRGLHWVLE
460 470 480 490 500
VLQDTCQQTL EVTRTALLYL SSSLGTERFS SGAGMPDVQE RKEATELRTR
510 520 530 540 550
LQTLSEILSK CSHNVTETQR SLSCLGEELL KNRDQIHEDN KSIQKIQCCL
560 570 580 590 600
DKMHFIYKQF KKSRMRPGLS YNEEQIHKLD KVNFSHLAKR LLQVFQEECV
610 620 630 640 650
QTYQVSLVTH GKRMRQVQRA QNHLHLIGHS VATCNSEARG AQESLNKIFD
660 670 680 690 700
QLLLDRASEQ GAEVSPQPMA PHPGPDPKDL VFHMQELCND MKLLAFDLQD
710
NNRLIERLHR VPSAPDV
Length:717
Mass (Da):80,953
Last modified:July 27, 2011 - v2
Checksum:i0863ECC180AE385A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti471 – 4711S → G in BAA85154. (PubMed:10421793)Curated
Sequence conflicti483 – 4831A → S in BAA85154. (PubMed:10421793)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016589 mRNA. Translation: BAA85154.1.
AK088580 mRNA. Translation: BAC40434.1.
AK149911 mRNA. Translation: BAE29161.1.
CT010206 mRNA. Translation: CAJ18414.1.
CH466520 Genomic DNA. Translation: EDL39710.1.
CCDSiCCDS15269.1.
RefSeqiNP_062751.2. NM_019777.3.
XP_006529824.1. XM_006529761.1.
UniGeneiMm.386783.

Genome annotation databases

EnsembliENSMUST00000062108; ENSMUSP00000054126; ENSMUSG00000042349.
GeneIDi56489.
KEGGimmu:56489.
UCSCiuc007cnf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016589 mRNA. Translation: BAA85154.1 .
AK088580 mRNA. Translation: BAC40434.1 .
AK149911 mRNA. Translation: BAE29161.1 .
CT010206 mRNA. Translation: CAJ18414.1 .
CH466520 Genomic DNA. Translation: EDL39710.1 .
CCDSi CCDS15269.1.
RefSeqi NP_062751.2. NM_019777.3.
XP_006529824.1. XM_006529761.1.
UniGenei Mm.386783.

3D structure databases

ProteinModelPortali Q9R0T8.
SMRi Q9R0T8. Positions 2-648.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 208014. 2 interactions.
IntActi Q9R0T8. 2 interactions.
STRINGi 10090.ENSMUSP00000054126.

PTM databases

PhosphoSitei Q9R0T8.

Proteomic databases

PRIDEi Q9R0T8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000062108 ; ENSMUSP00000054126 ; ENSMUSG00000042349 .
GeneIDi 56489.
KEGGi mmu:56489.
UCSCi uc007cnf.1. mouse.

Organism-specific databases

CTDi 9641.
MGIi MGI:1929612. Ikbke.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00770000120525.
HOGENOMi HOG000220867.
HOVERGENi HBG008494.
InParanoidi Q9R0T8.
KOi K07211.
OMAi HIYIHAH.
OrthoDBi EOG7Z95KH.
TreeFami TF324269.

Enzyme and pathway databases

BRENDAi 2.7.11.10. 3474.
Reactomei REACT_198521. TRAF6 mediated IRF7 activation.
REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
REACT_225463. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
REACT_231481. TRAF3-dependent IRF activation pathway.

Miscellaneous databases

NextBioi 312766.
PROi Q9R0T8.
SOURCEi Search...

Gene expression databases

Bgeei Q9R0T8.
CleanExi MM_IKBKE.
ExpressionAtlasi Q9R0T8. baseline and differential.
Genevestigatori Q9R0T8.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "IKK-i, a novel lipopolysaccharide-inducible kinase that is related to IkappaB kinases."
    Shimada T., Kawai T., Takeda K., Matsumoto M., Inoue J., Tatsumi Y., Kanamaru A., Akira S.
    Int. Immunol. 11:1357-1362(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Macrophage.
  2. "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: C57BL/6J and NOD.
    Tissue: Bone marrow and Thymus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. 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].
  5. "The roles of two IkappaB kinase-related kinases in lipopolysaccharide and double stranded RNA signaling and viral infection."
    Hemmi H., Takeuchi O., Sato S., Yamamoto M., Kaisho T., Sanjo H., Kawai T., Hoshino K., Takeda K., Akira S.
    J. Exp. Med. 199:1641-1650(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  6. "SINTBAD, a novel component of innate antiviral immunity, shares a TBK1-binding domain with NAP1 and TANK."
    Ryzhakov G., Randow F.
    EMBO J. 26:3180-3190(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AZI2; TANK AND TBKBP1.
  7. "Multiple functions of the IKK-related kinase IKKepsilon in interferon-mediated antiviral immunity."
    Tenoever B.R., Ng S.L., Chua M.A., McWhirter S.M., Garcia-Sastre A., Maniatis T.
    Science 315:1274-1278(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN STAT1 ACTIVATION, PHOSPHORYLATION AT THR-503, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-38.
  8. Cited for: FUNCTION IN ENERGY BALANCE, DISRUPTION PHENOTYPE, INDUCTION BY HIGH-FAT DIET, TISSUE SPECIFICITY.
  9. "Inhibitor of kappaB kinase epsilon (IKK(epsilon)), STAT1, and IFIT2 proteins define novel innate immune effector pathway against West Nile virus infection."
    Perwitasari O., Cho H., Diamond M.S., Gale M. Jr.
    J. Biol. Chem. 286:44412-44423(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN STAT1 ACTIVATION, DISRUPTION PHENOTYPE.
  10. "IkappaB kinase epsilon (IKK(epsilon)) regulates the balance between type I and type II interferon responses."
    Ng S.L., Friedman B.A., Schmid S., Gertz J., Myers R.M., Tenoever B.R., Maniatis T.
    Proc. Natl. Acad. Sci. U.S.A. 108:21170-21175(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION REGULATION IN IFN RESPONSE.
  11. "An inhibitor of the protein kinases TBK1 and IKK-[?] improves obesity-related metabolic dysfunctions in mice."
    Reilly S.M., Chiang S.H., Decker S.J., Chang L., Uhm M., Larsen M.J., Rubin J.R., Mowers J., White N.M., Hochberg I., Downes M., Yu R.T., Liddle C., Evans R.M., Oh D., Li P., Olefsky J.M., Saltiel A.R.
    Nat. Med. 19:313-321(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ENERGY BALANCE, DISRUPTION PHENOTYPE, INDUCTION BY HIGH-FAT DIET, TISSUE SPECIFICITY, ENZYME REGULATION.

Entry informationi

Entry nameiIKKE_MOUSE
AccessioniPrimary (citable) accession number: Q9R0T8
Secondary accession number(s): Q8C2I3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 122 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3