Q60680 (IKKA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Inhibitor of nuclear factor kappa-B kinase subunit alpha
Short name=I-kappa-B kinase alpha
Short name=IKK-A
Short name=IKK-alpha
Short name=IkBKA
Short name=IkappaB kinase
EC=2.7.11.10

Alternative name(s):
Conserved helix-loop-helix ubiquitous kinase
I-kappa-B kinase 1
Short name=IKK1
Nuclear factor NF-kappa-B inhibitor kinase alpha
Short name=NFKBIKA

Gene names

Name:	Chuk
Synonyms:	Ikka

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	745 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. Negatively regulates the pathway by phosphorylating the scaffold protein TAXBP1 and thus promoting the assembly of the A20/TNFAIP3 ubiquitin-editing complex (composed of A20/TNFAIP3, TAX1BP1, and the E3 ligases ITCH and RNF11). Therefore, CHUK plays a key role in the negative feedback of NF-kappa-B canonical signaling to limit inflammatory gene activation. As part of the non-canonical pathway of NF-kappa-B activation, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. In turn, these complexes regulate genes encoding molecules involved in B-cell survival and lymphoid organogenesis. Participates also in the negative feedback of the non-canonical NF-kappa-B signaling pathway by phosphorylating and destabilizing MAP3K14/NIK. Within the nucleus, phosphorylates CREBBP and consequently increases both its transcriptional and histone acetyltransferase activities. Modulates chromatin accessibility at NF-kappa-B-responsive promoters by phosphorylating histones H3 at 'Ser-10' that are subsequently acetylated at 'Lys-14' by CREBBP. Additionally, phosphorylates the CREBBP-interacting protein NCOA3. Ref.11
Catalytic activity	ATP + [I-kappa-B protein] = ADP + [I-kappa-B phosphoprotein].
Enzyme regulation	Activated when phosphorylated and inactivated when dephosphorylated.
Subunit structure	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. Part of a 70-90 kDa complex at least consisting of CHUK/IKKA, IKBKB, NFKBIA, RELA, IKBKAP and MAP3K14. Directly interacts with IKK-gamma/NEMO and TRPC4AP. May interact with TRAF2. Interacts with NALP2. May interact with MAVS/IPS1. Interacts with ARRB1 By similarity. Interacts with NLRC5; prevents CHUK phosphorylation and kinase activity By similarity. Interacts with PIAS1; this interaction induces PIAS1 phosphorylation By similarity. Interacts with ARRB2. Ref.12 Ref.13
Subcellular location	Cytoplasm. Nucleus. Note: Shuttles between the cytoplasm and the nucleus. Ref.11
Tissue specificity	Ubiquitous only for isoform 1, isoforms 2 and 3 are expressed predominantly in brain and T-lymphocytes.
Developmental stage	Maximally expressed at E7 day followed by E11, E15 and E17 days. In the limb development, its expression predominates in the limb buds at E12.5 day.
Domain	The kinase domain is located in the N-terminal region. The leucine zipper is important to allow homo- and hetero-dimerization. At the C-terminal region is located the region responsible for the interaction with NEMO/IKBKG.
Post-translational modification	Phosphorylated by MAP3K14/NIK, AKT and to a lesser extent by MEKK1, and dephosphorylated by PP2A. Autophosphorylated. Ref.7 Ref.9
Disruption phenotype	Mice show abnormal appearance and die within 4 hours after birth. The epidermal cells are highly proliferative with dysregulated epidermal differentiation. Ref.5
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. I-kappa-B kinase subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	I-kappaB phosphorylation Traceable author statement PubMed 9597130. Source: MGI lactation Inferred from mutant phenotype PubMed 11747812. Source: MGI mammary gland alveolus development Inferred from mutant phenotype PubMed 11747812. Source: MGI mammary gland epithelial cell proliferation Inferred from mutant phenotype PubMed 11747812. Source: MGI morphogenesis of an epithelial sheet Inferred from mutant phenotype PubMed 14960276. Source: MGI odontogenesis of dentin-containing tooth Inferred from mutant phenotype PubMed 14960276. Source: MGI osteoclast differentiation Inferred from mutant phenotype PubMed 15485831. Source: MGI positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype PubMed 11747812. Source: MGI
Cellular_component	CD40 receptor complex Inferred from direct assay PubMed 20614026. Source: BHF-UCL cytoplasm Traceable author statement PubMed 9597130. Source: MGI internal side of plasma membrane Inferred from direct assay PubMed 20614026. Source: BHF-UCL nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW IkappaB kinase activity Inferred from electronic annotation. Source: EC receptor signaling protein serine/threonine kinase activity Traceable author statement PubMed 9597130. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Fam92a1	Q8BP22	4	EBI-646260,EBI-646638
Ikbkg	O88522	4	EBI-646245,EBI-998011
Irf7	P70434	3	EBI-646245,EBI-997907
Krt10	P02535	6	EBI-646260,EBI-646288
MAP3K14	Q99558	3	EBI-646264,EBI-358011	From a different organism.
NFKBIA	P25963	2	EBI-646264,EBI-307386	From a different organism.
Pde4dip	B7ZNY0	4	EBI-646260,EBI-659248

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q60680-1)

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: Q60680-2)

Also known as: Delta LH;

The sequence of this isoform differs from the canonical sequence as follows:
     452-471: MLSLLRYNANLTKMKNTLIS → IFRKNVKSMERNGRKGHSLF
     472-745: Missing.

Isoform 3 (identifier: Q60680-3)

Also known as: Delta H;

The sequence of this isoform differs from the canonical sequence as follows:
     577-584: DHLYSDST → GKTLQSQY
     585-745: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 745	745	Inhibitor of nuclear factor kappa-B kinase subunit alpha		PRO_0000086012
Regions
	Domain	15 – 300	286	Protein kinase
	Nucleotide binding	21 – 29	9	ATP By similarity
	Region	455 – 476	22	Leucine-zipper
	Region	738 – 743	6	NEMO-binding
Sites
	Active site	144	1	Proton acceptor By similarity
	Binding site	44	1	ATP By similarity
Amino acid modifications
	Modified residue	23	1	Phosphothreonine; by PKB/AKT1 and SGK1 By similarity
	Modified residue	176	1	Phosphoserine; by MAP3K14 By similarity
	Modified residue	180	1	Phosphoserine; by SGK1 By similarity
Natural variations
	Alternative sequence	452 – 471	20	MLSLL…NTLIS → IFRKNVKSMERNGRKGHSLF in isoform 2.		VSP_004866
	Alternative sequence	472 – 745	274	Missing in isoform 2.		VSP_004867
	Alternative sequence	577 – 584	8	DHLYSDST → GKTLQSQY in isoform 3.		VSP_004868
	Alternative sequence	585 – 745	161	Missing in isoform 3.		VSP_004869
Experimental info
	Sequence conflict	236	1	K → E in BAB31335. Ref.3
	Sequence conflict	400	1	S → Y in BAB31335. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 3FEF5582AFF92233	FASTA	745	84,729
	10 20 30 40 50 60 MERPPGLRPG AGGPWEMRER LGTGGFGNVS LYQHRELDLK IAIKSCRLEL SSKNRERWCH 70 80 90 100 110 120 EIQIMKKLDH ANVVKACDVP EELNFLINDV PLLAMEYCSG GDLRKLLNKP ENCCGLKESQ 130 140 150 160 170 180 ILSLLSDIGS GIRYLHENKI IHRDLKPENI VLQDVGGKTI HKIIDLGYAK DVDQGSLCTS 190 200 210 220 230 240 FVGTLQYLAP ELFENKPYTA TVDYWSFGTM VFECIAGYRP FLHHLQPFTW HEKIKKKDPK 250 260 270 280 290 300 CIFACEEMTG EVRFSSHLPQ PNSLCSLIVE PMESWLQLML NWDPQQRGGP IDLTLKQPRC 310 320 330 340 350 360 FALMDHILNL KIVHILNMTS AKIISFLLPC DESLHSLQSR IERETGINTG SQELLSETGI 370 380 390 400 410 420 SLDPRKPASQ CVLDGVRGCD SYMVYLFDKS KTVYEGPFAS RSLSDCVNYI VQDSKIQLPI 430 440 450 460 470 480 IQLRKVWAEA VHYVSGLKED YSRLFQGQRA AMLSLLRYNA NLTKMKNTLI SASQQLKAKL 490 500 510 520 530 540 EFFRKSIQLD LERYSEQMTY GISSEKMLKA WKEMEEKAIH YSEVGVIGYL EDQIMSLHTE 550 560 570 580 590 600 IMELQKSPYG RRQGDLMESL EQRAIDLYKQ LKHRPPDHLY SDSTEMVKII VHTVQSQDRV 610 620 630 640 650 660 LKELFGHLSK LLGCKQKIID LLPKVEVALS NIKEADNTVM FMQGKRQKEI WHLLKIACTQ 670 680 690 700 710 720 SSARSLVGSS LEGTVTPPVS AWLPPTLADR EHPLTCVVTP QDGETLAQMI EENLNCLGHL 730 740 STIIREANED QSSSLMSLDW SWLAE
	Isoform 2 (Delta LH) [UniParc]. Checksum: 14F1EFF71B4A17EE	FASTA	471	53,544
	10 20 30 40 50 60 MERPPGLRPG AGGPWEMRER LGTGGFGNVS LYQHRELDLK IAIKSCRLEL SSKNRERWCH 70 80 90 100 110 120 EIQIMKKLDH ANVVKACDVP EELNFLINDV PLLAMEYCSG GDLRKLLNKP ENCCGLKESQ 130 140 150 160 170 180 ILSLLSDIGS GIRYLHENKI IHRDLKPENI VLQDVGGKTI HKIIDLGYAK DVDQGSLCTS 190 200 210 220 230 240 FVGTLQYLAP ELFENKPYTA TVDYWSFGTM VFECIAGYRP FLHHLQPFTW HEKIKKKDPK 250 260 270 280 290 300 CIFACEEMTG EVRFSSHLPQ PNSLCSLIVE PMESWLQLML NWDPQQRGGP IDLTLKQPRC 310 320 330 340 350 360 FALMDHILNL KIVHILNMTS AKIISFLLPC DESLHSLQSR IERETGINTG SQELLSETGI 370 380 390 400 410 420 SLDPRKPASQ CVLDGVRGCD SYMVYLFDKS KTVYEGPFAS RSLSDCVNYI VQDSKIQLPI 430 440 450 460 470 IQLRKVWAEA VHYVSGLKED YSRLFQGQRA AIFRKNVKSM ERNGRKGHSL F
	Isoform 3 (Delta H) [UniParc]. Checksum: D99BB8A6DF1CA4EB	FASTA	584	66,805
	10 20 30 40 50 60 MERPPGLRPG AGGPWEMRER LGTGGFGNVS LYQHRELDLK IAIKSCRLEL SSKNRERWCH 70 80 90 100 110 120 EIQIMKKLDH ANVVKACDVP EELNFLINDV PLLAMEYCSG GDLRKLLNKP ENCCGLKESQ 130 140 150 160 170 180 ILSLLSDIGS GIRYLHENKI IHRDLKPENI VLQDVGGKTI HKIIDLGYAK DVDQGSLCTS 190 200 210 220 230 240 FVGTLQYLAP ELFENKPYTA TVDYWSFGTM VFECIAGYRP FLHHLQPFTW HEKIKKKDPK 250 260 270 280 290 300 CIFACEEMTG EVRFSSHLPQ PNSLCSLIVE PMESWLQLML NWDPQQRGGP IDLTLKQPRC 310 320 330 340 350 360 FALMDHILNL KIVHILNMTS AKIISFLLPC DESLHSLQSR IERETGINTG SQELLSETGI 370 380 390 400 410 420 SLDPRKPASQ CVLDGVRGCD SYMVYLFDKS KTVYEGPFAS RSLSDCVNYI VQDSKIQLPI 430 440 450 460 470 480 IQLRKVWAEA VHYVSGLKED YSRLFQGQRA AMLSLLRYNA NLTKMKNTLI SASQQLKAKL 490 500 510 520 530 540 EFFRKSIQLD LERYSEQMTY GISSEKMLKA WKEMEEKAIH YSEVGVIGYL EDQIMSLHTE 550 560 570 580 IMELQKSPYG RRQGDLMESL EQRAIDLYKQ LKHRPPGKTL QSQY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"CHUK, a conserved helix-loop-helix ubiquitous kinase, maps to human chromosome 10 and mouse chromosome 19." Mock B.A., Connelly M.A., McBride O.W., Kozak C.A., Marcu K.B. Genomics 27:348-351(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: BALB/c.
[2]	"CHUK, a new member of the helix-loop-helix and leucine zipper families of interacting proteins, contains a serine-threonine kinase catalytic domain." Connelly M.A., Marcu K.B. Cell. Mol. Biol. Res. 41:537-549(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: BALB/c.
[3]	"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] (ISOFORM 3). Strain: C57BL/6J. Tissue: Colon.
[4]	"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] (ISOFORM 3). Tissue: Eye.
[5]	"Limb and skin abnormalities in mice lacking IKKalpha." Takeda K., Takeuchi O., Tsujimura T., Itami S., Adachi O., Kawai T., Sanjo H., Yoshikawa K., Terada N., Akira S. Science 284:313-316(1999) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[6]	"Functional isoforms of IkappaB kinase alpha (IKKalpha) lacking leucine zipper and helix-loop-helix domains reveal that IKKalpha and IKKbeta have different activation requirements." McKenzie F.R., Connelly M.A., Balzarano D., Mueller J.R., Geleziunas R., Marcu K.B. Mol. Cell. Biol. 20:2635-2649(2000) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING.
[7]	"Differential regulation of IkappaB kinase alpha and beta by two upstream kinases, NF-kappaB-inducing kinase and mitogen-activated protein kinase/ERK kinase kinase-1." Nakano H., Shindo M., Sakon S., Nishinaka S., Mihara M., Yagita H., Okumura K. Proc. Natl. Acad. Sci. U.S.A. 95:3537-3542(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY MAP3K14/NIK.
[8]	"Positive and negative regulation of IkappaB kinase activity through IKKbeta subunit phosphorylation." Delhase M., Hayakawa M., Chen Y., Karin M. Science 284:309-313(1999) [PubMed] [Europe PMC] [Abstract] Cited for: IKKA-IKKB BINDING.
[9]	"Coordinate regulation of IkappaB kinases by mitogen-activated protein kinase kinase kinase 1 and NF-kappaB-inducing kinase." Nemoto S., DiDonato J.A., Lin A. Mol. Cell. Biol. 18:7336-7343(1998) [PubMed] [Europe PMC] [Abstract] Cited for: IKK PHOSPHORYLATION.
[10]	"The I kappa B/NF-kappa B system: a key determinant of mucosal inflammation and protection." Jobin C., Sartor R.B. Am. J. Physiol. 278:C451-C462(2000) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[11]	"Histone H3 phosphorylation by IKK-alpha is critical for cytokine-induced gene expression." Yamamoto Y., Verma U.N., Prajapati S., Kwak Y.T., Gaynor R.B. Nature 423:655-659(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[12]	"Beta2-adrenergic receptor regulates Toll-like receptor-4-induced nuclear factor-kappaB activation through beta-arrestin 2." Kizaki T., Izawa T., Sakurai T., Haga S., Taniguchi N., Tajiri H., Watanabe K., Day N.K., Toba K., Ohno H. Immunology 124:348-356(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ARRB2.
[13]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U12473 mRNA. Translation: AAC52589.1. AK018671 mRNA. Translation: BAB31335.1. BC018243 mRNA. Translation: AAH18243.1.
IPI	IPI00119213. IPI00230069. IPI00400114.
PIR	I49101.
UniGene	Mm.3996.
3D structure databases
ProteinModelPortal	Q60680.
SMR	Q60680. Positions 16-660.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29719N.
IntAct	Q60680. 25 interactions.
MINT	MINT-267529.
PTM databases
PhosphoSite	Q60680.
Proteomic databases
PaxDb	Q60680.
PRIDE	Q60680.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
UCSC	uc008hpi.2. mouse.
Organism-specific databases
MGI	MGI:99484. Chuk.
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000038048.
HOVERGEN	HBG018241.
InParanoid	Q60680.
OrthoDB	EOG4SJ5D7.
Enzyme and pathway databases
BRENDA	2.7.11.10. 3474.
Gene expression databases
CleanEx	MM_CHUK.
Genevestigator	Q60680.
GermOnline	ENSMUSG00000025199. Mus musculus.
Family and domain databases
InterPro	IPR022007. IKKbetaNEMObind. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF12179. IKKbetaNEMObind. 1 hit. 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. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL5380.
SOURCE	Search...

Entry information

Entry name

IKKA_MOUSE

Accession

Primary (citable) accession number: Q60680
Secondary accession number(s): Q80VU2, Q9D2X3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 134 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program