Q14164 (IKKE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inhibitor of nuclear factor kappa-B kinase subunit epsilon
Short name=I-kappa-B kinase epsilon
Short name=IKK-E
Short name=IKK-epsilon
Short name=IkBKE
EC=2.7.11.10

Alternative name(s):
Inducible I kappa-B kinase
Short name=IKK-i

Gene names

Name:	IKBKE
Synonyms:	IKKE, IKKI, KIAA0151

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	716 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. May play a special role in the immune response. Protects cells against DNA damage-induced cell death. Ref.14 Ref.15
Catalytic activity	ATP + [I-kappa-B protein] = ADP + [I-kappa-B phosphoprotein].
Subunit structure	May interact with MAVS/IPS1. Interacts with AZI2. 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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14
Subcellular location	Cytoplasm. Nucleus. Nucleus › PML body. Note: Targeting to PML nuclear bodies upon DNA damage is TOPORS-dependent. Ref.14
Tissue specificity	Highly expressed in spleen followed by thymus, peripheral blood leukocytes, pancreas, placenta. Weakly expressed in lung, kidney, prostate, ovary and colon.
Post-translational modification	Autophosphorylated and phosphorylated by IKBKB/IKKB. Ref.15 Sumoylation by TOPORS upon DNA damage is required for protection of cells against DNA damage-induced cell death. Desumoylated by SENP1. Ref.14
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. I-kappa-B kinase subfamily. Contains 1 protein kinase domain.
Sequence caution	The sequence BAA09772.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	DNA damage
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	TRIF-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome innate immune response Traceable author statement. Source: Reactome intrinsic apoptotic signaling pathway in response to DNA damage Inferred from mutant phenotype Ref.14. Source: UniProtKB negative regulation of type I interferon production Traceable author statement. Source: Reactome positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from expression pattern PubMed 12761501. Source: UniProtKB toll-like receptor 3 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 4 signaling pathway Traceable author statement. Source: Reactome
Cellular_component	PML body Inferred from direct assay Ref.14. Source: UniProtKB cytosol Traceable author statement. Source: Reactome endosome membrane Traceable author statement. Source: Reactome
Molecular_function	ATP binding Non-traceable author statement. Source: UniProtKB IkappaB kinase activity Inferred from electronic annotation. Source: EC NF-kappaB-inducing kinase activity Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MAVS	Q7Z434	2	EBI-307369,EBI-995373

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q14164-1)

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: Q14164-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-85: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 716	716	Inhibitor of nuclear factor kappa-B kinase subunit epsilon		PRO_0000086017
Regions
	Domain	9 – 315	307	Protein kinase
	Nucleotide binding	15 – 23	9	ATP By similarity
	Region	436 – 457	22	Leucine-zipper
Sites
	Active site	135	1	Proton acceptor By similarity
	Binding site	38	1	ATP By similarity
Amino acid modifications
	Modified residue	172	1	Phosphoserine; by IKKB
	Modified residue	664	1	Phosphoserine Ref.13
	Cross-link	231		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) Ref.14
Natural variations
	Alternative sequence	1 – 85	85	Missing in isoform 2.		VSP_044305
	Natural variant	128	1	E → K. Ref.4 Corresponds to variant rs41296028 [ dbSNP | Ensembl ].		VAR_038816
	Natural variant	371	1	A → T. Ref.4 Ref.16 Corresponds to variant rs17021877 [ dbSNP | Ensembl ].		VAR_038817
	Natural variant	483	1	T → M. Ref.16 Corresponds to variant rs52817862 [ dbSNP | Ensembl ].		VAR_040571
	Natural variant	515	1	E → D. Ref.4 Corresponds to variant rs41299015 [ dbSNP | Ensembl ].		VAR_038818
	Natural variant	543	1	I → M. Ref.4 Corresponds to variant rs41299037 [ dbSNP | Ensembl ].		VAR_038819
	Natural variant	602	1	A → V. Ref.4 Ref.16 Corresponds to variant rs12059562 [ dbSNP | Ensembl ].		VAR_038820
	Natural variant	660	1	G → E. Ref.16 Corresponds to variant rs55822317 [ dbSNP | Ensembl ].		VAR_040572
	Natural variant	713	1	P → L. Ref.4 Ref.16 Corresponds to variant rs3748022 [ dbSNP | Ensembl ].		VAR_019989
Experimental info
	Mutagenesis	38	1	K → A: Loss of kinase activity and loss of nuclear import. Ref.1
	Mutagenesis	168	1	E → A: Slight decrease of kinase activity. Ref.1
	Mutagenesis	172	1	S → A: Loss of autophosphorylation and of kinase activity. Ref.1
	Mutagenesis	172	1	S → E: Decrease in kinase activity. Ref.1
	Mutagenesis	231	1	K → R: Loss of sumoylation and loss of targeting to nuclear bodies. Ref.14
	Sequence conflict	187	1	R → Q in AAI05925. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 3E5FBE5840734D81	FASTA	716	80,462
	10 20 30 40 50 60 MQSTANYLWH TDDLLGQGAT ASVYKARNKK SGELVAVKVF NTTSYLRPRE VQVREFEVLR 70 80 90 100 110 120 KLNHQNIVKL FAVEETGGSR QKVLVMEYCS SGSLLSVLES PENAFGLPED EFLVVLRCVV 130 140 150 160 170 180 AGMNHLRENG IVHRDIKPGN IMRLVGEEGQ SIYKLTDFGA ARELDDDEKF VSVYGTEEYL 190 200 210 220 230 240 HPDMYERAVL RKPQQKAFGV TVDLWSIGVT LYHAATGSLP FIPFGGPRRN KEIMYRITTE 250 260 270 280 290 300 KPAGAIAGAQ RRENGPLEWS YTLPITCQLS LGLQSQLVPI LANILEVEQA KCWGFDQFFA 310 320 330 340 350 360 ETSDILQRVV VHVFSLSQAV LHHIYIHAHN TIAIFQEAVH KQTSVAPRHQ EYLFEGHLCV 370 380 390 400 410 420 LEPSVSAQHI AHTTASSPLT LFSTAIPKGL AFRDPALDVP KFVPKVDLQA DYNTAKGVLG 430 440 450 460 470 480 AGYQALRLAR ALLDGQELMF RGLHWVMEVL QATCRRTLEV ARTSLLYLSS SLGTERFSSV 490 500 510 520 530 540 AGTPEIQELK AAAELRSRLR TLAEVLSRCS QNITETQESL SSLNRELVKS RDQVHEDRSI 550 560 570 580 590 600 QQIQCCLDKM NFIYKQFKKS RMRPGLGYNE EQIHKLDKVN FSHLAKRLLQ VFQEECVQKY 610 620 630 640 650 660 QASLVTHGKR MRVVHETRNH LRLVGCSVAA CNTEAQGVQE SLSKLLEELS HQLLQDRAKG 670 680 690 700 710 AQASPPPIAP YPSPTRKDLL LHMQELCEGM KLLASDLLDN NRIIERLNRV PAPPDV
	Isoform 2 [UniParc]. Checksum: 1E6CC6C29C88897D	FASTA	631	70,816
	10 20 30 40 50 60 MEYCSSGSLL SVLESPENAF GLPEDEFLVV LRCVVAGMNH LRENGIVHRD IKPGNIMRLV 70 80 90 100 110 120 GEEGQSIYKL TDFGAARELD DDEKFVSVYG TEEYLHPDMY ERAVLRKPQQ KAFGVTVDLW 130 140 150 160 170 180 SIGVTLYHAA TGSLPFIPFG GPRRNKEIMY RITTEKPAGA IAGAQRRENG PLEWSYTLPI 190 200 210 220 230 240 TCQLSLGLQS QLVPILANIL EVEQAKCWGF DQFFAETSDI LQRVVVHVFS LSQAVLHHIY 250 260 270 280 290 300 IHAHNTIAIF QEAVHKQTSV APRHQEYLFE GHLCVLEPSV SAQHIAHTTA SSPLTLFSTA 310 320 330 340 350 360 IPKGLAFRDP ALDVPKFVPK VDLQADYNTA KGVLGAGYQA LRLARALLDG QELMFRGLHW 370 380 390 400 410 420 VMEVLQATCR RTLEVARTSL LYLSSSLGTE RFSSVAGTPE IQELKAAAEL RSRLRTLAEV 430 440 450 460 470 480 LSRCSQNITE TQESLSSLNR ELVKSRDQVH EDRSIQQIQC CLDKMNFIYK QFKKSRMRPG 490 500 510 520 530 540 LGYNEEQIHK LDKVNFSHLA KRLLQVFQEE CVQKYQASLV THGKRMRVVH ETRNHLRLVG 550 560 570 580 590 600 CSVAACNTEA QGVQESLSKL LEELSHQLLQ DRAKGAQASP PPIAPYPSPT RKDLLLHMQE 610 620 630 LCEGMKLLAS DLLDNNRIIE RLNRVPAPPD V

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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] (ISOFORM 1), MUTAGENESIS OF LYS-38; GLU-168 AND SER-172.
[2]	"IKK epsilon is part of a novel PMA-inducible IkappaB kinase complex." Peters R.T., Liao S.-M., Maniatis T. Mol. Cell 5:513-522(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Leukocyte.
[3]	"Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1." Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N. DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Bone marrow.
[4]	SeattleSNPs variation discovery resource Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-128; THR-371; ASP-515; MET-543; VAL-602 AND LEU-713.
[5]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
[8]	"Identification of NAP1, a regulatory subunit of IkappaB kinase-related kinases that potentiates NF-kappaB signaling." Fujita F., Taniguchi Y., Kato T., Narita Y., Furuya A., Ogawa T., Sakurai H., Joh T., Itoh M., Delhase M., Karin M., Nakanishi M. Mol. Cell. Biol. 23:7780-7793(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AZI2.
[9]	"Mechanisms of the TRIF-induced interferon-stimulated response element and NF-kappaB activation and apoptosis pathways." Han K.J., Su X., Xu L.-G., Bin L.H., Zhang J., Shu H.-B. J. Biol. Chem. 279:15652-15661(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TICAM1.
[10]	"SIKE is an IKK epsilon/TBK1-associated suppressor of TLR3- and virus-triggered IRF-3 activation pathways." Huang J., Liu T., Xu L.-G., Chen D., Zhai Z., Shu H.-B. EMBO J. 24:4018-4028(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SIKE1; IRF3; TICAM1 AND DDX58.
[11]	"Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus." Meylan E., Curran J., Hofmann K., Moradpour D., Binder M., Bartenschlager R., Tschopp J. Nature 437:1167-1172(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAVS.
[12]	"The tumour suppressor CYLD is a negative regulator of RIG-I-mediated antiviral response." Friedman C.S., O'Donnell M.A., Legarda-Addison D., Ng A., Cardenas W.B., Yount J.S., Moran T.M., Basler C.F., Komuro A., Horvath C.M., Xavier R., Ting A.T. EMBO Rep. 9:930-936(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CYLD.
[13]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664, MASS SPECTROMETRY.
[14]	"SUMOylation-dependent localization of IKKepsilon in PML nuclear bodies is essential for protection against DNA-damage-triggered cell death." Renner F., Moreno R., Schmitz M.L. Mol. Cell 37:503-515(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH TOPORS, SUMOYLATION AT LYS-231 BY TOPORS, DESUMOYLATION BY SENP1, MUTAGENESIS OF LYS-231, SUBCELLULAR LOCATION.
[15]	"Novel cross-talk within the IKK family controls innate immunity." Clark K., Peggie M., Plater L., Sorcek R.J., Young E.R., Madwed J.B., Hough J., McIver E.G., Cohen P. Biochem. J. 434:93-104(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION BY IKBKB/IKKB.
[16]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-371; MET-483; VAL-602; GLU-660 AND LEU-713.
+	Additional computationally mapped references.

Web resources

SeattleSNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	D63485 mRNA. Translation: BAA09772.2. Different initiation. AB016590 mRNA. Translation: BAA85155.1. AF241789 mRNA. Translation: AAF45307.1. DQ667176 Genomic DNA. Translation: ABG25921.1. AL354681 Genomic DNA. Translation: CAI15250.1. CH471100 Genomic DNA. Translation: EAW93549.1. BC105923 mRNA. Translation: AAI05924.1. BC105924 mRNA. Translation: AAI05925.1. BC107812 mRNA. Translation: AAI07813.1.
IPI	IPI00029045.
RefSeq	NP_001180250.1. NM_001193321.1. NP_001180251.1. NM_001193322.1. NP_054721.1. NM_014002.3.
UniGene	Hs.321045.
3D structure databases
ProteinModelPortal	Q14164.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-27530N.
IntAct	Q14164. 9 interactions.
MINT	MINT-1132084.
STRING	9606.ENSP00000356087.
PTM databases
PhosphoSite	Q14164.
Polymorphism databases
DMDM	14548079.
Proteomic databases
PaxDb	Q14164.
PRIDE	Q14164.
Protocols and materials databases
DNASU	9641.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000367120; ENSP00000356087; ENSG00000143466. ENST00000537984; ENSP00000444529; ENSG00000143466. ENST00000581977; ENSP00000464030; ENSG00000263528. ENST00000584998; ENSP00000462396; ENSG00000263528.
GeneID	9641.
KEGG	hsa:9641.
UCSC	uc001hdz.2. human.
Organism-specific databases
CTD	9641.
GeneCards	GC01P206643.
H-InvDB	HIX0116011.
HGNC	HGNC:14552. IKBKE.
HPA	CAB025983. HPA015788.
MIM	605048. gene.
neXtProt	NX_Q14164.
PharmGKB	PA134962294.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000220867.
HOVERGEN	HBG008494.
InParanoid	Q14164.
KO	K07211.
OMA	HIYIHAH.
OrthoDB	EOG4S4PFW.
PhylomeDB	Q14164.
Enzyme and pathway databases
BRENDA	2.7.11.10. 2681.
Reactome	REACT_6900. Immune System.
SignaLink	Q14164.
Gene expression databases
ArrayExpress	Q14164.
Bgee	Q14164.
CleanEx	HS_IKBKE.
Genevestigator	Q14164.
GermOnline	ENSG00000143466. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. False negative. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q14164.
ChEMBL	CHEMBL3529.
ChiTaRS	IKBKE. human.
GenomeRNAi	9641.
NextBio	36191.
SOURCE	Search...

Entry information

Entry name

IKKE_HUMAN

Accession

Primary (citable) accession number: Q14164
Secondary accession number(s): D3DT78 , Q3B754, Q3KR43, Q5JTS6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	November 1, 1996
Last modified:	May 29, 2013
This is version 138 of the entry and version 1 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.