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Protein

Inhibitor of nuclear factor kappa-B kinase subunit beta

Gene

IKBKB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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 2 critical 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. In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE. IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs. Phosphorylates FOXO3, mediating the TNF-dependent inactivation of this pro-apoptotic transcription factor. Also phosphorylates other substrates including NCOA3, BCL10 and IRS1. Within the nucleus, acts as an adapter protein for NFKBIA degradation in UV-induced NF-kappa-B activation.8 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei44ATPPROSITE-ProRule annotation1
Active sitei145Proton acceptorPROSITE-ProRule annotation1

Regions

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

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • IkappaB kinase activity Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB
  • scaffold protein binding Source: MGI

GO - Biological processi

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
Biological processHost-virus interaction
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

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-168927 TICAM1, RIP1-mediated IKK complex recruitment
R-HSA-1810476 RIP-mediated NFkB activation via ZBP1
R-HSA-202424 Downstream TCR signaling
R-HSA-209543 p75NTR recruits signalling complexes
R-HSA-209560 NF-kB is activated and signals survival
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-445989 TAK1 activates NFkB by phosphorylation and activation of IKKs complex
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-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5684264 MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-HSA-9020702 Interleukin-1 signaling
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-RKiO14920
SignaLinkiO14920
SIGNORiO14920

Names & Taxonomyi

Protein namesi
Recommended name:
Inhibitor of nuclear factor kappa-B kinase subunit beta (EC:2.7.11.10)
Short name:
I-kappa-B-kinase beta
Short name:
IKK-B
Short name:
IKK-beta
Short name:
IkBKB
Alternative name(s):
I-kappa-B kinase 2
Short name:
IKK2
Nuclear factor NF-kappa-B inhibitor kinase beta
Short name:
NFKBIKB
Gene namesi
Name:IKBKB
Synonyms:IKKB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

EuPathDBiHostDB:ENSG00000104365.13
HGNCiHGNC:5960 IKBKB
MIMi603258 gene
neXtProtiNX_O14920

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Immunodeficiency 15 (IMD15)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive primary immunodeficiency disorder characterized by onset in infancy of life-threatening bacterial, fungal, and viral infections and failure to thrive. Laboratory studies show hypo- or agammaglobulinemia with relatively normal numbers of B and T-cells, and impaired differentiation and activation of immune cells.
See also OMIM:615592

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi44K → A: Loss of kinase activity and no effect on binding to NIK. 2 Publications1
Mutagenesisi163K → R: Monoubiquitinated; when associated with E-177 and E-181. 1 Publication1
Mutagenesisi177 – 181SLCTS → ALCTA: COmplete loss of TBK1-mediated phosphorylation. 1 Publication5
Mutagenesisi177S → A: Decrease of activity. 2 Publications1
Mutagenesisi177S → E: Full activation. Interaction with TRIM21 is enhanced; when associated with E-181. Monoubiquitinated; when associated with R-163 and E-181. Strongly promoted NF-kappa-B gene expression; when associated with E-181. 2 Publications1
Mutagenesisi181S → A: Decrease of activity. 2 Publications1
Mutagenesisi181S → E: Full activation. Interaction with TRIM21 is enhanced; when associated with E-177. Monoubiquitinated; when associated with R-163 and E-177. Strongly promoted NF-kappa-B gene expression; when associated with E-177. 2 Publications1
Mutagenesisi191P → A: Loss of hypoxic inducibility. 1 Publication1

Keywords - Diseasei

SCID

Organism-specific databases

DisGeNETi3551
MalaCardsiIKBKB
MIMi615592 phenotype
OpenTargetsiENSG00000104365
Orphaneti397787 Severe combined immunodeficiency due to IKK2 deficiency
PharmGKBiPA29776

Chemistry databases

ChEMBLiCHEMBL1991
DrugBankiDB06151 Acetylcysteine
DB00945 Acetylsalicylic acid
DB01169 Arsenic trioxide
DB00995 Auranofin
DB00244 Mesalazine
DB05183 MLN0415
DB00795 Sulfasalazine
GuidetoPHARMACOLOGYi2039

Polymorphism and mutation databases

BioMutaiIKBKB

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000860131 – 756Inhibitor of nuclear factor kappa-B kinase subunit betaAdd BLAST756

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki163Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei177Phosphoserine; by TBK1 and PKC/PRKCZ3 Publications1
Modified residuei179S-nitrosocysteine1 Publication1
Modified residuei180O-acetylthreonine; by Yersinia yopJ1 Publication1
Modified residuei181Phosphoserine; by TBK1, PKC/PRKCZ and PDPK14 Publications1
Modified residuei191Hydroxyproline1 Publication1
Modified residuei670Phosphoserine; by autocatalysis1 Publication1
Modified residuei672PhosphoserineCombined sources1 Publication1
Modified residuei675PhosphoserineCombined sources1
Modified residuei675Phosphoserine; by autocatalysisCombined sources1 Publication1
Modified residuei682Phosphoserine; by autocatalysis1 Publication1
Modified residuei689Phosphoserine; by autocatalysis1 Publication1
Modified residuei692Phosphoserine; by autocatalysis1 Publication1
Modified residuei695Phosphoserine; by autocatalysis1 Publication1
Modified residuei697Phosphoserine; by autocatalysis1 Publication1
Modified residuei705Phosphoserine; by autocatalysis1 Publication1
Modified residuei733Phosphoserine; by autocatalysis1 Publication1
Modified residuei740Phosphoserine; by autocatalysis1 Publication1
Modified residuei750Phosphoserine; by autocatalysis1 Publication1

Post-translational modificationi

Upon cytokine stimulation, phosphorylated on Ser-177 and Ser-181 by MEKK1 and/or MAP3K14/NIK as well as TBK1 and PRKCZ; which enhances activity. Once activated, autophosphorylates on the C-terminal serine cluster; which decreases activity and prevents prolonged activation of the inflammatory response. Phosphorylated by the IKK-related kinases TBK1 and IKBKE, which is associated with reduced CHUK/IKKA and IKBKB activity and NF-kappa-B-dependent gene transcription. Dephosphorylated at Ser-177 and Ser-181 by PPM1A and PPM1B.4 Publications
(Microbial infection) Acetylation of Thr-180 by Yersinia yopJ prevents phosphorylation and activation, thus blocking the I-kappa-B pathway.2 Publications
Ubiquitinated. Monoubiquitination involves TRIM21 that leads to inhibition of Tax-induced NF-kappa-B signaling. According to PubMed:19675099, 'Ser-163' does not serve as a monoubiquitination site. According to PubMed:16267042, ubiquitination on 'Ser-163' modulates phosphorylation on C-terminal serine residues.2 Publications
(Microbial infection) Monoubiquitination by TRIM21 is disrupted by Yersinia yopJ.1 Publication
Hydroxylated by PHD1/EGLN2, loss of hydroxylation under hypoxic conditions results in activation of NF-kappa-B.1 Publication

Keywords - PTMi

Acetylation, Hydroxylation, Isopeptide bond, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

EPDiO14920
MaxQBiO14920
PaxDbiO14920
PeptideAtlasiO14920
PRIDEiO14920
ProteomicsDBi48297
48298 [O14920-2]
48299 [O14920-3]
48300 [O14920-4]

PTM databases

iPTMnetiO14920
PhosphoSitePlusiO14920

Expressioni

Tissue specificityi

Highly expressed in heart, placenta, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis and peripheral blood.

Gene expression databases

BgeeiENSG00000104365 Expressed in 227 organ(s), highest expression level in spleen
CleanExiHS_IKBKB
ExpressionAtlasiO14920 baseline and differential
GenevisibleiO14920 HS

Organism-specific databases

HPAiCAB004447
HPA001249

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: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, ELP1 and MAP3K14 (PubMed:9751059). Found in a membrane raft complex, at least composed of BCL10, CARD11, DPP4 and IKBKB (PubMed:17287217). Interacts with SQSTM1 through PRKCZ or PRKCI (PubMed:10356400). Forms an NGF-induced complex with IKBKB, PRKCI and TRAF6 (By similarity). May interact with MAVS/IPS1 (PubMed:16177806). Interacts with NALP2 (PubMed:15456791). Interacts with TICAM1 (PubMed:14739303). Interacts with FAF1; the interaction disrupts the IKK complex formation (PubMed:17684021). Interacts with ATM (PubMed:16497931). Part of a ternary complex consisting of TANK, IKBKB and IKBKG (PubMed:12133833). Interacts with NIBP; the interaction is direct (PubMed:15951441). Interacts with ARRB1 and ARRB2 (PubMed:15173580). Interacts with TRIM21 (PubMed:19675099). Interacts with NLRC5; prevents IKBKB phosphorylation and kinase activity (PubMed:20434986). Interacts with PDPK1 (PubMed:16207722). Interacts with EIF2AK2/PKR (PubMed:10848580). The phosphorylated form interacts with PPM1A and PPM1B (PubMed:18930133). Interacts with ZNF268 isoform 2; the interaction is further increased in a TNF-alpha-dependent manner (PubMed:23091055). Interacts with IKBKE (PubMed:23453969). Interacts with NAA10, leading to NAA10 degradation (PubMed:19716809). Interacts with FOXO3 (PubMed:15084260). Interacts with AKAP13 (PubMed:23090968). Interacts with IFIT5; the interaction synergizes the recruitment of IKK to MAP3K7 and enhances IKK phosphorylation (PubMed:26334375). Interacts with LRRC14; disrupts IKBKB-IKBKG interaction preventing I-kappa-B-kinase (IKK) core complex formation and leading to a decrease of IKBKB phosphorylation and NF-kappaB activation (PubMed:27426725).By similarity24 Publications
(Microbial infection) Interacts with Yersinia yopJ.1 Publication
(Microbial infection) Interacts with vaccinia virus protein B14.1 Publication

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi109767, 146 interactors
ComplexPortaliCPX-3269 IkappaB kinase complex
CORUMiO14920
DIPiDIP-27527N
ELMiO14920
IntActiO14920, 76 interactors
MINTiO14920
STRINGi9606.ENSP00000430684

Chemistry databases

BindingDBiO14920

Structurei

Secondary structure

1756
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliO14920
SMRiO14920
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO14920

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini15 – 300Protein kinasePROSITE-ProRule annotationAdd BLAST286

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni458 – 479Leucine-zipperAdd BLAST22
Regioni737 – 742NEMO-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

Phylogenomic databases

eggNOGiKOG4250 Eukaryota
ENOG410XRMU LUCA
GeneTreeiENSGT00930000150910
HOGENOMiHOG000038048
HOVERGENiHBG018241
InParanoidiO14920
KOiK07209
OMAiWINEINI
OrthoDBiEOG091G02VC
PhylomeDBiO14920
TreeFamiTF324269

Family and domain databases

InterProiView protein in InterPro
IPR022007 IKKbetaNEMObind
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR008271 Ser/Thr_kinase_AS
IPR029071 Ubiquitin-like_domsf
IPR000626 Ubiquitin_dom
PfamiView protein in Pfam
PF12179 IKKbetaNEMObind, 1 hit
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM01239 IKKbetaNEMObind, 1 hit
SM00220 S_TKc, 1 hit
SUPFAMiSSF54236 SSF54236, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

Sequences (4+)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 4 described isoforms and 8 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O14920-1) [UniParc]FASTAAdd to basket

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.

« Hide
        10         20         30         40         50
MSWSPSLTTQ TCGAWEMKER LGTGGFGNVI RWHNQETGEQ IAIKQCRQEL
60 70 80 90 100
SPRNRERWCL EIQIMRRLTH PNVVAARDVP EGMQNLAPND LPLLAMEYCQ
110 120 130 140 150
GGDLRKYLNQ FENCCGLREG AILTLLSDIA SALRYLHENR IIHRDLKPEN
160 170 180 190 200
IVLQQGEQRL IHKIIDLGYA KELDQGSLCT SFVGTLQYLA PELLEQQKYT
210 220 230 240 250
VTVDYWSFGT LAFECITGFR PFLPNWQPVQ WHSKVRQKSE VDIVVSEDLN
260 270 280 290 300
GTVKFSSSLP YPNNLNSVLA ERLEKWLQLM LMWHPRQRGT DPTYGPNGCF
310 320 330 340 350
KALDDILNLK LVHILNMVTG TIHTYPVTED ESLQSLKARI QQDTGIPEED
360 370 380 390 400
QELLQEAGLA LIPDKPATQC ISDGKLNEGH TLDMDLVFLF DNSKITYETQ
410 420 430 440 450
ISPRPQPESV SCILQEPKRN LAFFQLRKVW GQVWHSIQTL KEDCNRLQQG
460 470 480 490 500
QRAAMMNLLR NNSCLSKMKN SMASMSQQLK AKLDFFKTSI QIDLEKYSEQ
510 520 530 540 550
TEFGITSDKL LLAWREMEQA VELCGRENEV KLLVERMMAL QTDIVDLQRS
560 570 580 590 600
PMGRKQGGTL DDLEEQAREL YRRLREKPRD QRTEGDSQEM VRLLLQAIQS
610 620 630 640 650
FEKKVRVIYT QLSKTVVCKQ KALELLPKVE EVVSLMNEDE KTVVRLQEKR
660 670 680 690 700
QKELWNLLKI ACSKVRGPVS GSPDSMNASR LSQPGQLMSQ PSTASNSLPE
710 720 730 740 750
PAKKSEELVA EAHNLCTLLE NAIQDTVREQ DQSFTALDWS WLQTEEEEHS

CLEQAS
Length:756
Mass (Da):86,564
Last modified:January 1, 1998 - v1
Checksum:iF9CADF671AE9E14E
GO
Isoform 2 (identifier: O14920-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MSWSPSLTTQTCGAWEMKERLGTGGFGNVIRWHN → MFSGGCHSPGFGRPSPAFPAPGSPPPAPRPCR

Show »
Length:754
Mass (Da):85,945
Checksum:i9C31F5C1DC92661E
GO
Isoform 3 (identifier: O14920-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     231-256: WHSKVRQKSEVDIVVSEDLNGTVKFS → CVRMWPGTVAHSCNPSTLGGRGRWIS
     257-756: Missing.

Show »
Length:256
Mass (Da):29,236
Checksum:i8B4762DD49F4065A
GO
Isoform 4 (identifier: O14920-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: MSWSPSLTTQTCGAWEMKERLGTGGFGNVIRWHNQETGEQIAIKQCRQELSPRNRERWCLEIQIMR → MSSDGTI

Note: No experimental confirmation available.
Show »
Length:697
Mass (Da):79,509
Checksum:i21B61110941FE1D9
GO

Computationally mapped potential isoform sequencesi

There are 8 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V105G3V105_HUMAN
Inhibitor of kappa light polypeptid...
IKBKB hCG_17395
562Annotation score:
E5RGW5E5RGW5_HUMAN
Inhibitor of nuclear factor kappa-B...
IKBKB
375Annotation score:
J3KNS5J3KNS5_HUMAN
Inhibitor of nuclear factor kappa-B...
IKBKB
164Annotation score:
E5RIW0E5RIW0_HUMAN
Inhibitor of nuclear factor kappa-B...
IKBKB
51Annotation score:
E5RJH2E5RJH2_HUMAN
Inhibitor of nuclear factor kappa-B...
IKBKB
43Annotation score:
E5RFT3E5RFT3_HUMAN
Inhibitor of nuclear factor kappa-B...
IKBKB
76Annotation score:
E5RFG5E5RFG5_HUMAN
Inhibitor of nuclear factor kappa-B...
IKBKB
109Annotation score:
E5RGA0E5RGA0_HUMAN
Inhibitor of nuclear factor kappa-B...
IKBKB
48Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti259L → S in BAG63942 (PubMed:14702039).Curated1
Sequence conflicti259L → S in BAH14789 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_035626360A → S in breast cancer samples; infiltrating ductal carcinoma; somatic mutation. 2 Publications1
Natural variantiVAR_040567369Q → R1 PublicationCorresponds to variant dbSNP:rs56411242Ensembl.1
Natural variantiVAR_040568526R → Q1 PublicationCorresponds to variant dbSNP:rs2272736EnsemblClinVar.1
Natural variantiVAR_021124554R → W1 PublicationCorresponds to variant dbSNP:rs17875749Ensembl.1
Natural variantiVAR_040569710A → T1 PublicationCorresponds to variant dbSNP:rs34309584Ensembl.1
Natural variantiVAR_040570734F → L1 PublicationCorresponds to variant dbSNP:rs56301637Ensembl.1
Natural variantiVAR_051628736A → T. Corresponds to variant dbSNP:rs17611716Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0434081 – 66MSWSP…IQIMR → MSSDGTI in isoform 4. 1 PublicationAdd BLAST66
Alternative sequenceiVSP_0418251 – 34MSWSP…IRWHN → MFSGGCHSPGFGRPSPAFPA PGSPPPAPRPCR in isoform 2. 1 PublicationAdd BLAST34
Alternative sequenceiVSP_041826231 – 256WHSKV…TVKFS → CVRMWPGTVAHSCNPSTLGG RGRWIS in isoform 3. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_041827257 – 756Missing in isoform 3. 1 PublicationAdd BLAST500

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF029684 mRNA Translation: AAC51860.1
AF080158 mRNA Translation: AAD08997.1
AF031416 mRNA Translation: AAC64675.1
AK302723 mRNA Translation: BAG63942.1
AK303528 mRNA Translation: BAG64556.1
AK316418 mRNA Translation: BAH14789.1
AY663108 Genomic DNA Translation: AAT65965.1
AC083973 Genomic DNA No translation available.
BC006231 mRNA Translation: AAH06231.1
CCDSiCCDS55228.1 [O14920-2]
CCDS56535.1 [O14920-4]
CCDS6128.1 [O14920-1]
RefSeqiNP_001177649.1, NM_001190720.2 [O14920-2]
NP_001229707.1, NM_001242778.1 [O14920-4]
NP_001547.1, NM_001556.2 [O14920-1]
UniGeneiHs.597664

Genome annotation databases

EnsembliENST00000416505; ENSP00000404920; ENSG00000104365 [O14920-4]
ENST00000519735; ENSP00000430483; ENSG00000104365 [O14920-3]
ENST00000520810; ENSP00000430684; ENSG00000104365 [O14920-1]
ENST00000520835; ENSP00000430868; ENSG00000104365 [O14920-2]
GeneIDi3551
KEGGihsa:3551
UCSCiuc003xow.3 human [O14920-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF029684 mRNA Translation: AAC51860.1
AF080158 mRNA Translation: AAD08997.1
AF031416 mRNA Translation: AAC64675.1
AK302723 mRNA Translation: BAG63942.1
AK303528 mRNA Translation: BAG64556.1
AK316418 mRNA Translation: BAH14789.1
AY663108 Genomic DNA Translation: AAT65965.1
AC083973 Genomic DNA No translation available.
BC006231 mRNA Translation: AAH06231.1
CCDSiCCDS55228.1 [O14920-2]
CCDS56535.1 [O14920-4]
CCDS6128.1 [O14920-1]
RefSeqiNP_001177649.1, NM_001190720.2 [O14920-2]
NP_001229707.1, NM_001242778.1 [O14920-4]
NP_001547.1, NM_001556.2 [O14920-1]
UniGeneiHs.597664

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BRTX-ray2.25A/C701-730[»]
3BRVX-ray2.20A/C701-745[»]
4E3CX-ray3.98A/B/C/D/E/F11-669[»]
4KIKX-ray2.83A/B2-664[»]
ProteinModelPortaliO14920
SMRiO14920
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109767, 146 interactors
ComplexPortaliCPX-3269 IkappaB kinase complex
CORUMiO14920
DIPiDIP-27527N
ELMiO14920
IntActiO14920, 76 interactors
MINTiO14920
STRINGi9606.ENSP00000430684

Chemistry databases

BindingDBiO14920
ChEMBLiCHEMBL1991
DrugBankiDB06151 Acetylcysteine
DB00945 Acetylsalicylic acid
DB01169 Arsenic trioxide
DB00995 Auranofin
DB00244 Mesalazine
DB05183 MLN0415
DB00795 Sulfasalazine
GuidetoPHARMACOLOGYi2039

PTM databases

iPTMnetiO14920
PhosphoSitePlusiO14920

Polymorphism and mutation databases

BioMutaiIKBKB

Proteomic databases

EPDiO14920
MaxQBiO14920
PaxDbiO14920
PeptideAtlasiO14920
PRIDEiO14920
ProteomicsDBi48297
48298 [O14920-2]
48299 [O14920-3]
48300 [O14920-4]

Protocols and materials databases

DNASUi3551
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000416505; ENSP00000404920; ENSG00000104365 [O14920-4]
ENST00000519735; ENSP00000430483; ENSG00000104365 [O14920-3]
ENST00000520810; ENSP00000430684; ENSG00000104365 [O14920-1]
ENST00000520835; ENSP00000430868; ENSG00000104365 [O14920-2]
GeneIDi3551
KEGGihsa:3551
UCSCiuc003xow.3 human [O14920-1]

Organism-specific databases

CTDi3551
DisGeNETi3551
EuPathDBiHostDB:ENSG00000104365.13
GeneCardsiIKBKB
HGNCiHGNC:5960 IKBKB
HPAiCAB004447
HPA001249
MalaCardsiIKBKB
MIMi603258 gene
615592 phenotype
neXtProtiNX_O14920
OpenTargetsiENSG00000104365
Orphaneti397787 Severe combined immunodeficiency due to IKK2 deficiency
PharmGKBiPA29776
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4250 Eukaryota
ENOG410XRMU LUCA
GeneTreeiENSGT00930000150910
HOGENOMiHOG000038048
HOVERGENiHBG018241
InParanoidiO14920
KOiK07209
OMAiWINEINI
OrthoDBiEOG091G02VC
PhylomeDBiO14920
TreeFamiTF324269

Enzyme and pathway databases

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-168927 TICAM1, RIP1-mediated IKK complex recruitment
R-HSA-1810476 RIP-mediated NFkB activation via ZBP1
R-HSA-202424 Downstream TCR signaling
R-HSA-209543 p75NTR recruits signalling complexes
R-HSA-209560 NF-kB is activated and signals survival
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-445989 TAK1 activates NFkB by phosphorylation and activation of IKKs complex
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-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5684264 MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-HSA-9020702 Interleukin-1 signaling
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-RKiO14920
SignaLinkiO14920
SIGNORiO14920

Miscellaneous databases

ChiTaRSiIKBKB human
EvolutionaryTraceiO14920
GeneWikiiIKK2
GenomeRNAii3551
PROiPR:O14920
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000104365 Expressed in 227 organ(s), highest expression level in spleen
CleanExiHS_IKBKB
ExpressionAtlasiO14920 baseline and differential
GenevisibleiO14920 HS

Family and domain databases

InterProiView protein in InterPro
IPR022007 IKKbetaNEMObind
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR008271 Ser/Thr_kinase_AS
IPR029071 Ubiquitin-like_domsf
IPR000626 Ubiquitin_dom
PfamiView protein in Pfam
PF12179 IKKbetaNEMObind, 1 hit
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM01239 IKKbetaNEMObind, 1 hit
SM00220 S_TKc, 1 hit
SUPFAMiSSF54236 SSF54236, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiIKKB_HUMAN
AccessioniPrimary (citable) accession number: O14920
Secondary accession number(s): B4DZ30, B4E0U4, O75327
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: January 1, 1998
Last modified: November 7, 2018
This is version 209 of the entry and version 1 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  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 chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  7. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
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Main funding by: National Institutes of Health

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