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Protein

Inhibitor of nuclear factor kappa-B kinase subunit alpha

Gene

CHUK

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Also phosphorylates FOXO3 and may regulate this pro-apoptotic transcription factor (PubMed:15084260).6 Publications

Catalytic activityi

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

Enzyme regulationi

Activated when phosphorylated and inactivated when dephosphorylated.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei44ATPPROSITE-ProRule annotation1
Active sitei144Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi21 – 29ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • IkappaB kinase activity Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase activity Source: UniProtKB
  • scaffold protein binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000107566-MONOMER.
BRENDAi2.7.11.10. 2681.
ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1236974. ER-Phagosome pathway.
R-HSA-168638. NOD1/2 Signaling Pathway.
R-HSA-1810476. RIP-mediated NFkB activation via ZBP1.
R-HSA-198323. AKT phosphorylates targets in the cytosol.
R-HSA-202424. Downstream TCR signaling.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-HSA-446652. Interleukin-1 signaling.
R-HSA-5357905. Regulation of TNFR1 signaling.
R-HSA-5357956. TNFR1-induced NFkappaB signaling pathway.
R-HSA-5602636. IKBKB deficiency causes SCID.
R-HSA-5603027. IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (EDA-ID) (via TLR).
R-HSA-5603029. IkBA variant leads to EDA-ID.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5674400. Constitutive Signaling by AKT1 E17K in Cancer.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-5684264. MAP3K8 (TPL2)-dependent MAPK1/3 activation.
R-HSA-933542. TRAF6 mediated NF-kB activation.
R-HSA-933543. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
R-HSA-937039. IRAK1 recruits IKK complex.
R-HSA-937041. IKK complex recruitment mediated by RIP1.
R-HSA-975144. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
SABIO-RKO15111.
SignaLinkiO15111.
SIGNORiO15111.

Names & Taxonomyi

Protein namesi
Recommended name:
Inhibitor of nuclear factor kappa-B kinase subunit alpha (EC:2.7.11.10)
Short name:
I-kappa-B kinase alpha
Short name:
IKK-A
Short name:
IKK-alpha
Short name:
IkBKA
Short name:
IkappaB kinase
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
Transcription factor 16
Short name:
TCF-16
Gene namesi
Name:CHUK
Synonyms:IKKA, TCF16
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:1974. CHUK.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Cocoon syndrome (COCOS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA lethal syndrome characterized by multiple fetal malformations including defective face and seemingly absent limbs, which are bound to the trunk and encased under the skin.
See also OMIM:613630

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi23T → A: Loss of phosphorylation and decrease of kinase activity. 1 Publication1
Mutagenesisi44K → A: Loss of kinase activity. 2 Publications1
Mutagenesisi44K → M: Loss of autophosphorylation. 2 Publications1
Mutagenesisi176S → A: Loss of phosphorylation and of activity. 2 Publications1
Mutagenesisi176S → E: Full activation. 2 Publications1
Mutagenesisi179T → A: No change in phosphorylation. 1 Publication1
Mutagenesisi180S → A: No change in phosphorylation. 1 Publication1

Organism-specific databases

DisGeNETi1147.
MalaCardsiCHUK.
MIMi613630. phenotype.
OpenTargetsiENSG00000213341.
PharmGKBiPA26510.

Chemistry databases

ChEMBLiCHEMBL3476.
DrugBankiDB06151. Acetylcysteine.
DB00233. Aminosalicylic Acid.
DB00244. Mesalazine.
DB00795. Sulfasalazine.
GuidetoPHARMACOLOGYi1989.

Polymorphism and mutation databases

BioMutaiCHUK.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000860111 – 745Inhibitor of nuclear factor kappa-B kinase subunit alphaAdd BLAST745

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei23Phosphothreonine; by PKB/AKT1 and SGK12 Publications1
Modified residuei176Phosphoserine; by MAP3K141 Publication1
Modified residuei179O-acetylthreonine; by Yersinia yopJ1 Publication1
Modified residuei180Phosphoserine; by SGK11 Publication1

Post-translational modificationi

Phosphorylated by MAP3K14/NIK, AKT and to a lesser extent by MEKK1, and dephosphorylated by PP2A. Autophosphorylated.
(Microbial infection) Acetylation of Thr-179 by Yersinia yopJ prevents phosphorylation and activation, thus blocking the I-kappa-B signaling pathway.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO15111.
MaxQBiO15111.
PaxDbiO15111.
PeptideAtlasiO15111.
PRIDEiO15111.

PTM databases

iPTMnetiO15111.
PhosphoSitePlusiO15111.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiENSG00000213341.
CleanExiHS_CHUK.
GenevisibleiO15111. HS.

Organism-specific databases

HPAiCAB004240.
CAB018564.
HPA001402.

Interactioni

Subunit structurei

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 (PubMed:10195894, PubMed:12612076). The IKK complex associates with TERF2IP/RAP1, leading to promote IKK-mediated phosphorylation of RELA/p65 (By similarity). Part of a complex composed of NCOA2, NCOA3, CHUK/IKKA, IKBKB, IKBKG and CREBBP (PubMed:11971985). Part of a 70-90 kDa complex at least consisting of CHUK/IKKA, IKBKB, NFKBIA, RELA, IKBKAP and MAP3K14 (PubMed:9751059). Directly interacts with TRPC4AP (By similarity). May interact with TRAF2 (PubMed:19150425). Interacts with NALP2 (PubMed:15456791). May interact with MAVS/IPS1 (PubMed:16177806). Interacts with ARRB1 and ARRB2 (PubMed:15173580). Interacts with NLRC5; prevents CHUK phosphorylation and kinase activity (PubMed:20434986). Interacts with PIAS1; this interaction induces PIAS1 phosphorylation (PubMed:17540171). Interacts with ZNF268 isoform 2; the interaction is further increased in a TNF-alpha-dependent manner (PubMed:23091055). Interacts with FOXO3 (PubMed:15084260).By similarity12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARRB2P321213EBI-81249,EBI-714559
CDC37Q165434EBI-81249,EBI-295634
CDKN1BP465274EBI-81249,EBI-519280
E7P031292EBI-81249,EBI-866453From a different organism.
E7Q078572EBI-81249,EBI-9690349From a different organism.
E7Q6TY282EBI-81249,EBI-9690312From a different organism.
E7Q6TY352EBI-81249,EBI-9690239From a different organism.
E7Q809012EBI-81249,EBI-9690278From a different organism.
E7Q8B5B52EBI-81249,EBI-9690330From a different organism.
FKBP5Q134512EBI-81249,EBI-306914
HSP90AA1P079003EBI-81249,EBI-296047
IKBKBO1492015EBI-81249,EBI-81266
IKBKGQ9Y6K921EBI-81249,EBI-81279
IRF7Q929854EBI-81249,EBI-968267
MAP3K14Q995586EBI-81249,EBI-358011
MLK4Q5TCX82EBI-81249,EBI-1057380
MYCP011063EBI-81249,EBI-447544
NFKB1P198383EBI-81249,EBI-300010
NFKBIAP2596314EBI-81249,EBI-307386
PQ77M192EBI-81249,EBI-6149376From a different organism.
RELAQ042062EBI-81249,EBI-73886
TAX1BP1Q86VP12EBI-81249,EBI-529518
VACWR196P247723EBI-81249,EBI-4291651From a different organism.

GO - Molecular functioni

  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • scaffold protein binding Source: MGI

Protein-protein interaction databases

BioGridi107569. 130 interactors.
DIPiDIP-27526N.
IntActiO15111. 59 interactors.
MINTiMINT-88648.
STRINGi9606.ENSP00000359424.

Chemistry databases

BindingDBiO15111.

Structurei

Secondary structure

1745
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi735 – 737Combined sources3
Helixi741 – 743Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BRTX-ray2.25A/C732-745[»]
ProteinModelPortaliO15111.
SMRiO15111.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15111.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini15 – 302Protein kinasePROSITE-ProRule annotationAdd BLAST288

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni455 – 476Leucine-zipperAdd BLAST22
Regioni738 – 743NEMO-binding6

Domaini

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.1 Publication

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

eggNOGiKOG4250. Eukaryota.
ENOG410XRMU. LUCA.
GeneTreeiENSGT00820000127009.
HOGENOMiHOG000038048.
HOVERGENiHBG018241.
InParanoidiO15111.
KOiK04467.
OMAiFVLMDHI.
OrthoDBiEOG091G02VC.
PhylomeDBiO15111.
TreeFamiTF324269.

Family and domain databases

InterProiIPR022007. IKKbetaNEMObind.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF12179. IKKbetaNEMObind. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM01239. IKKbetaNEMObind. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O15111-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERPPGLRPG AGGPWEMRER LGTGGFGNVC LYQHRELDLK IAIKSCRLEL
60 70 80 90 100
STKNRERWCH EIQIMKKLNH ANVVKACDVP EELNILIHDV PLLAMEYCSG
110 120 130 140 150
GDLRKLLNKP ENCCGLKESQ ILSLLSDIGS GIRYLHENKI IHRDLKPENI
160 170 180 190 200
VLQDVGGKII HKIIDLGYAK DVDQGSLCTS FVGTLQYLAP ELFENKPYTA
210 220 230 240 250
TVDYWSFGTM VFECIAGYRP FLHHLQPFTW HEKIKKKDPK CIFACEEMSG
260 270 280 290 300
EVRFSSHLPQ PNSLCSLVVE PMENWLQLML NWDPQQRGGP VDLTLKQPRC
310 320 330 340 350
FVLMDHILNL KIVHILNMTS AKIISFLLPP DESLHSLQSR IERETGINTG
360 370 380 390 400
SQELLSETGI SLDPRKPASQ CVLDGVRGCD SYMVYLFDKS KTVYEGPFAS
410 420 430 440 450
RSLSDCVNYI VQDSKIQLPI IQLRKVWAEA VHYVSGLKED YSRLFQGQRA
460 470 480 490 500
AMLSLLRYNA NLTKMKNTLI SASQQLKAKL EFFHKSIQLD LERYSEQMTY
510 520 530 540 550
GISSEKMLKA WKEMEEKAIH YAEVGVIGYL EDQIMSLHAE IMELQKSPYG
560 570 580 590 600
RRQGDLMESL EQRAIDLYKQ LKHRPSDHSY SDSTEMVKII VHTVQSQDRV
610 620 630 640 650
LKELFGHLSK LLGCKQKIID LLPKVEVALS NIKEADNTVM FMQGKRQKEI
660 670 680 690 700
WHLLKIACTQ SSARSLVGSS LEGAVTPQTS AWLPPTSAEH DHSLSCVVTP
710 720 730 740
QDGETSAQMI EENLNCLGHL STIIHEANEE QGNSMMNLDW SWLTE
Length:745
Mass (Da):84,640
Last modified:January 11, 2011 - v2
Checksum:i4EA55C6FFC66FA16
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti543E → G in AAC51671 (PubMed:9252186).Curated1
Sequence conflicti604L → R in AAC50713 (PubMed:8777433).Curated1
Sequence conflicti679 – 680TS → AY in AAC50713 (PubMed:8777433).Curated2
Sequence conflicti684P → A no nucleotide entry (PubMed:9346484).Curated1
Sequence conflicti684P → A in AAC50713 (PubMed:8777433).Curated1
Sequence conflicti686 – 687TS → DL in AAC50713 (PubMed:8777433).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_040565126S → C.1 PublicationCorresponds to variant rs34427437dbSNPEnsembl.1
Natural variantiVAR_040566155V → A.1 PublicationCorresponds to variant rs2230803dbSNPEnsembl.1
Natural variantiVAR_021359268V → I.6 PublicationsCorresponds to variant rs2230804dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF012890 mRNA. Translation: AAC51662.1.
AF009225 mRNA. Translation: AAC51671.1.
AF080157 mRNA. Translation: AAD08996.1.
AY652653 Genomic DNA. Translation: AAT49098.1.
AL138921 Genomic DNA. Translation: CAH72401.1.
U22512 mRNA. Translation: AAC50713.1.
CCDSiCCDS7488.1.
RefSeqiNP_001269.3. NM_001278.4.
UniGeneiHs.198998.

Genome annotation databases

EnsembliENST00000370397; ENSP00000359424; ENSG00000213341.
GeneIDi1147.
KEGGihsa:1147.
UCSCiuc001kqp.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF012890 mRNA. Translation: AAC51662.1.
AF009225 mRNA. Translation: AAC51671.1.
AF080157 mRNA. Translation: AAD08996.1.
AY652653 Genomic DNA. Translation: AAT49098.1.
AL138921 Genomic DNA. Translation: CAH72401.1.
U22512 mRNA. Translation: AAC50713.1.
CCDSiCCDS7488.1.
RefSeqiNP_001269.3. NM_001278.4.
UniGeneiHs.198998.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BRTX-ray2.25A/C732-745[»]
ProteinModelPortaliO15111.
SMRiO15111.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107569. 130 interactors.
DIPiDIP-27526N.
IntActiO15111. 59 interactors.
MINTiMINT-88648.
STRINGi9606.ENSP00000359424.

Chemistry databases

BindingDBiO15111.
ChEMBLiCHEMBL3476.
DrugBankiDB06151. Acetylcysteine.
DB00233. Aminosalicylic Acid.
DB00244. Mesalazine.
DB00795. Sulfasalazine.
GuidetoPHARMACOLOGYi1989.

PTM databases

iPTMnetiO15111.
PhosphoSitePlusiO15111.

Polymorphism and mutation databases

BioMutaiCHUK.

Proteomic databases

EPDiO15111.
MaxQBiO15111.
PaxDbiO15111.
PeptideAtlasiO15111.
PRIDEiO15111.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370397; ENSP00000359424; ENSG00000213341.
GeneIDi1147.
KEGGihsa:1147.
UCSCiuc001kqp.4. human.

Organism-specific databases

CTDi1147.
DisGeNETi1147.
GeneCardsiCHUK.
H-InvDBHIX0201495.
HGNCiHGNC:1974. CHUK.
HPAiCAB004240.
CAB018564.
HPA001402.
MalaCardsiCHUK.
MIMi600664. gene.
613630. phenotype.
neXtProtiNX_O15111.
OpenTargetsiENSG00000213341.
PharmGKBiPA26510.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4250. Eukaryota.
ENOG410XRMU. LUCA.
GeneTreeiENSGT00820000127009.
HOGENOMiHOG000038048.
HOVERGENiHBG018241.
InParanoidiO15111.
KOiK04467.
OMAiFVLMDHI.
OrthoDBiEOG091G02VC.
PhylomeDBiO15111.
TreeFamiTF324269.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000107566-MONOMER.
BRENDAi2.7.11.10. 2681.
ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1236974. ER-Phagosome pathway.
R-HSA-168638. NOD1/2 Signaling Pathway.
R-HSA-1810476. RIP-mediated NFkB activation via ZBP1.
R-HSA-198323. AKT phosphorylates targets in the cytosol.
R-HSA-202424. Downstream TCR signaling.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-HSA-446652. Interleukin-1 signaling.
R-HSA-5357905. Regulation of TNFR1 signaling.
R-HSA-5357956. TNFR1-induced NFkappaB signaling pathway.
R-HSA-5602636. IKBKB deficiency causes SCID.
R-HSA-5603027. IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (EDA-ID) (via TLR).
R-HSA-5603029. IkBA variant leads to EDA-ID.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5674400. Constitutive Signaling by AKT1 E17K in Cancer.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-5684264. MAP3K8 (TPL2)-dependent MAPK1/3 activation.
R-HSA-933542. TRAF6 mediated NF-kB activation.
R-HSA-933543. NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10.
R-HSA-937039. IRAK1 recruits IKK complex.
R-HSA-937041. IKK complex recruitment mediated by RIP1.
R-HSA-975144. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
SABIO-RKO15111.
SignaLinkiO15111.
SIGNORiO15111.

Miscellaneous databases

ChiTaRSiCHUK. human.
EvolutionaryTraceiO15111.
GeneWikiiCHUK.
GenomeRNAii1147.
PROiO15111.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000213341.
CleanExiHS_CHUK.
GenevisibleiO15111. HS.

Family and domain databases

InterProiIPR022007. IKKbetaNEMObind.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF12179. IKKbetaNEMObind. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM01239. IKKbetaNEMObind. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIKKA_HUMAN
AccessioniPrimary (citable) accession number: O15111
Secondary accession number(s): O14666
, Q13132, Q5W0I4, Q92467
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: January 11, 2011
Last modified: November 30, 2016
This is version 186 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. 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.