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O14920 (IKKB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 161. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inhibitor of nuclear factor kappa-B kinase subunit beta

Short name=I-kappa-B-kinase beta
Short name=IKK-B
Short name=IKK-beta
Short name=IkBKB
EC=2.7.11.10
Alternative name(s):
I-kappa-B kinase 2
Short name=IKK2
Nuclear factor NF-kappa-B inhibitor kinase beta
Short name=NFKBIKB
Gene names
Name:IKBKB
Synonyms:IKKB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length756 AA.
Sequence statusComplete.
Protein existenceEvidence 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 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. 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. Ref.17 Ref.34 Ref.43 Ref.45 Ref.46 Ref.49

Catalytic activity

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

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. Found in a membrane raft complex, at least composed of BCL10, CARD11, DPP4 and IKBKB. Interacts with SQSTM1 through PRKCZ or PRKCI. Forms an NGF-induced complex with IKBKB, PRKCI and TRAF6. May interact with MAVS/IPS1. Interacts with NALP2. Interacts with TICAM1. Interacts with Yersinia yopJ. Interacts with FAF1; the interaction disrupts the IKK complex formation. Interacts with ATM. Part of a ternary complex consisting of TANK, IKBKB and IKBKG. Interacts with NIBP; the interaction is direct. Interacts with ARRB1 and ARRB2. Interacts with TRIM21. Interacts with NLRC5; prevents IKBKB phosphorylation and kinase activity. Interacts with PDPK1. Interacts with EIF2AK2/PKR. The phosphorylated form interacts with PPM1A and PPM1B. Interacts with ZNF268 isoform 2;the interaction is further increased in a TNF-alpha-dependent manner. Interacts with IKBKE. Ref.11 Ref.12 Ref.15 Ref.18 Ref.19 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26 Ref.28 Ref.30 Ref.31 Ref.32 Ref.33 Ref.40 Ref.43 Ref.44 Ref.50 Ref.51

Subcellular location

Cytoplasm. Nucleus. Membrane raft. Note: Colocalized with DPP4 in membrane rafts. Ref.32 Ref.46

Tissue specificity

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

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. Ref.36

Post-translational modification

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. Ref.10 Ref.13 Ref.14 Ref.16 Ref.26 Ref.40 Ref.49

Acetylation of Thr-180 by Yersinia yopJ prevents phosphorylation and activation, thus blocking the I-kappa-B pathway. Ref.9 Ref.30

Ubiquitinated. Monoubiquitination involves TRIM21 that leads to inhibition of Tax-induced NF-kappa-B signaling. According to Ref.44, 'Ser-163' does not serve as a monoubiquitination site. According to Ref.27, ubiquitination on 'Ser-163' modulates phosphorylation on C-terminal serine residues. Monoubiquitination by TRIM21 is disrupted by Yersinia yopJ. Ref.27 Ref.44

Hydroxylated by PHD1/EGLN2, loss of hydroxylation under hypoxic conditions results in activation of NF-kappaB.

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 componentCytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Hydroxylation
Isopeptide bond
Phosphoprotein
S-nitrosylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processB cell homeostasis

Inferred from electronic annotation. Source: Ensembl

Fc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

I-kappaB kinase/NF-kappaB signaling

Traceable author statement Ref.36. Source: UniProtKB

I-kappaB phosphorylation

Traceable author statement Ref.36. Source: GOC

MyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-independent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

T cell receptor signaling pathway

Traceable author statement. Source: Reactome

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

cellular response to tumor necrosis factor

Inferred from direct assay Ref.50. Source: UniProtKB

inflammatory response

Traceable author statement Ref.36. Source: UniProtKB

innate immune response

Traceable author statement Ref.36. Source: UniProtKB

negative regulation of apoptotic process

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway

Traceable author statement. Source: Reactome

nucleotide-binding oligomerization domain containing signaling pathway

Traceable author statement. Source: Reactome

positive regulation of I-kappaB kinase/NF-kappaB signaling

Traceable author statement. Source: Reactome

positive regulation of NF-kappaB transcription factor activity

Traceable author statement Ref.36. Source: UniProtKB

positive regulation of cation channel activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of sodium ion transport

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.50. Source: UniProtKB

positive regulation of transcription, DNA-templated

Non-traceable author statement Ref.1Ref.2Ref.3. Source: UniProtKB

positive regulation of type I interferon production

Traceable author statement. Source: Reactome

protein phosphorylation

Inferred from direct assay Ref.43. Source: UniProtKB

response to virus

Traceable author statement Ref.36. Source: UniProtKB

serine phosphorylation of STAT protein

Inferred from direct assay PubMed 21399639. Source: UniProtKB

toll-like receptor 10 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 5 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentCD40 receptor complex

Inferred from sequence or structural similarity. Source: BHF-UCL

IkappaB kinase complex

Traceable author statement Ref.36. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytoplasmic side of plasma membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

membrane raft

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

IkappaB kinase activity

Traceable author statement Ref.36. Source: UniProtKB

protein heterodimerization activity

Inferred from direct assay Ref.50. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.50. Source: UniProtKB

protein kinase activity

Inferred from direct assay Ref.43. Source: UniProtKB

protein kinase binding

Inferred from physical interaction PubMed 12492477. Source: UniProtKB

protein serine/threonine kinase activity

Traceable author statement. Source: Reactome

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O14920-1)

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: O14920-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: MSWSPSLTTQTCGAWEMKERLGTGGFGNVIRWHN → MFSGGCHSPGFGRPSPAFPAPGSPPPAPRPCR
Isoform 3 (identifier: O14920-3)

The sequence of this isoform differs from the canonical sequence as follows:
     231-256: WHSKVRQKSEVDIVVSEDLNGTVKFS → CVRMWPGTVAHSCNPSTLGGRGRWIS
     257-756: Missing.
Isoform 4 (identifier: O14920-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: MSWSPSLTTQTCGAWEMKERLGTGGFGNVIRWHNQETGEQIAIKQCRQELSPRNRERWCLEIQIMR → MSSDGTI
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 756756Inhibitor of nuclear factor kappa-B kinase subunit beta
PRO_0000086013

Regions

Domain15 – 300286Protein kinase
Nucleotide binding21 – 299ATP By similarity
Region458 – 47922Leucine-zipper
Region737 – 7426NEMO-binding

Sites

Active site1451Proton acceptor By similarity
Binding site441ATP By similarity

Amino acid modifications

Modified residue1771Phosphoserine; by TBK1 and PKC/PRKCZ Ref.13 Ref.14 Ref.16 Ref.40
Modified residue1791S-nitrosocysteine Ref.24
Modified residue1801O-acetylthreonine; by Yersinia yopJ
Modified residue1811Phosphoserine; by TBK1, PKC/PRKCZ and PDPK1 Ref.13 Ref.14 Ref.16 Ref.26 Ref.40
Modified residue1911Hydroxyproline
Modified residue6701Phosphoserine; by autocatalysis Probable
Modified residue6721Phosphoserine Ref.14 Ref.38 Ref.42
Modified residue6751Phosphoserine; by autocatalysis Probable
Modified residue6821Phosphoserine; by autocatalysis Probable
Modified residue6891Phosphoserine; by autocatalysis Probable
Modified residue6921Phosphoserine; by autocatalysis Probable
Modified residue6951Phosphoserine; by autocatalysis Probable
Modified residue6971Phosphoserine; by autocatalysis Probable
Modified residue7051Phosphoserine; by autocatalysis Probable
Modified residue7331Phosphoserine; by autocatalysis Probable
Modified residue7401Phosphoserine; by autocatalysis Probable
Modified residue7501Phosphoserine; by autocatalysis Probable
Cross-link163Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.27

Natural variations

Alternative sequence1 – 6666MSWSP…IQIMR → MSSDGTI in isoform 4.
VSP_043408
Alternative sequence1 – 3434MSWSP…IRWHN → MFSGGCHSPGFGRPSPAFPA PGSPPPAPRPCR in isoform 2.
VSP_041825
Alternative sequence231 – 25626WHSKV…TVKFS → CVRMWPGTVAHSCNPSTLGG RGRWIS in isoform 3.
VSP_041826
Alternative sequence257 – 756500Missing in isoform 3.
VSP_041827
Natural variant3601A → S in breast cancer samples; infiltrating ductal carcinoma; somatic mutation. Ref.53 Ref.54
VAR_035626
Natural variant3691Q → R. Ref.54
Corresponds to variant rs56411242 [ dbSNP | Ensembl ].
VAR_040567
Natural variant5261R → Q. Ref.54
Corresponds to variant rs2272736 [ dbSNP | Ensembl ].
VAR_040568
Natural variant5541R → W. Ref.6
Corresponds to variant rs17875749 [ dbSNP | Ensembl ].
VAR_021124
Natural variant7101A → T. Ref.54
Corresponds to variant rs34309584 [ dbSNP | Ensembl ].
VAR_040569
Natural variant7341F → L. Ref.54
Corresponds to variant rs56301637 [ dbSNP | Ensembl ].
VAR_040570
Natural variant7361A → T.
Corresponds to variant rs17611716 [ dbSNP | Ensembl ].
VAR_051628

Experimental info

Mutagenesis441K → A: Loss of kinase activity and no effect on binding to NIK. Ref.1 Ref.2
Mutagenesis1631K → R: Monoubiquitinated; when associated with E-177 and E-181. Ref.44
Mutagenesis177 – 1815SLCTS → ALCTA: COmplete loss of TBK1-mediated phosphorylation. Ref.1 Ref.16 Ref.44
Mutagenesis1771S → A: Decrease of activity. Ref.1 Ref.44
Mutagenesis1771S → 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. Ref.1 Ref.44
Mutagenesis1811S → A: Decrease of activity. Ref.1 Ref.44
Mutagenesis1811S → 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. Ref.1 Ref.44
Mutagenesis1911P → A: Loss of hypoxic inducibility. Ref.29
Sequence conflict2591L → S in BAG63942. Ref.5
Sequence conflict2591L → S in BAH14789. Ref.5

Secondary structure

..................................................................................... 756
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: F9CADF671AE9E14E

FASTA75686,564
        10         20         30         40         50         60 
MSWSPSLTTQ TCGAWEMKER LGTGGFGNVI RWHNQETGEQ IAIKQCRQEL SPRNRERWCL 

        70         80         90        100        110        120 
EIQIMRRLTH PNVVAARDVP EGMQNLAPND LPLLAMEYCQ GGDLRKYLNQ FENCCGLREG 

       130        140        150        160        170        180 
AILTLLSDIA SALRYLHENR IIHRDLKPEN IVLQQGEQRL IHKIIDLGYA KELDQGSLCT 

       190        200        210        220        230        240 
SFVGTLQYLA PELLEQQKYT VTVDYWSFGT LAFECITGFR PFLPNWQPVQ WHSKVRQKSE 

       250        260        270        280        290        300 
VDIVVSEDLN GTVKFSSSLP YPNNLNSVLA ERLEKWLQLM LMWHPRQRGT DPTYGPNGCF 

       310        320        330        340        350        360 
KALDDILNLK LVHILNMVTG TIHTYPVTED ESLQSLKARI QQDTGIPEED QELLQEAGLA 

       370        380        390        400        410        420 
LIPDKPATQC ISDGKLNEGH TLDMDLVFLF DNSKITYETQ ISPRPQPESV SCILQEPKRN 

       430        440        450        460        470        480 
LAFFQLRKVW GQVWHSIQTL KEDCNRLQQG QRAAMMNLLR NNSCLSKMKN SMASMSQQLK 

       490        500        510        520        530        540 
AKLDFFKTSI QIDLEKYSEQ TEFGITSDKL LLAWREMEQA VELCGRENEV KLLVERMMAL 

       550        560        570        580        590        600 
QTDIVDLQRS PMGRKQGGTL DDLEEQAREL YRRLREKPRD QRTEGDSQEM VRLLLQAIQS 

       610        620        630        640        650        660 
FEKKVRVIYT QLSKTVVCKQ KALELLPKVE EVVSLMNEDE KTVVRLQEKR QKELWNLLKI 

       670        680        690        700        710        720 
ACSKVRGPVS GSPDSMNASR LSQPGQLMSQ PSTASNSLPE PAKKSEELVA EAHNLCTLLE 

       730        740        750 
NAIQDTVREQ DQSFTALDWS WLQTEEEEHS CLEQAS 

« Hide

Isoform 2 [UniParc].

Checksum: 9C31F5C1DC92661E
Show »

FASTA75485,945
Isoform 3 [UniParc].

Checksum: 8B4762DD49F4065A
Show »

FASTA25629,236
Isoform 4 [UniParc].

Checksum: 21B61110941FE1D9
Show »

FASTA69779,509

References

« Hide 'large scale' references
[1]"IKK-1 and IKK-2: cytokine-activated IkappaB kinases essential for NF-kappaB activation."
Mercurio F., Zhu H., Murray B.W., Shevchenko A., Bennett B.L., Li J.W., Young D.B., Barbosa M., Mann M., Manning A., Rao A.
Science 278:860-866(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF LYS-44; SER-177 AND SER-181.
Tissue: Cervix carcinoma.
[2]"IkappaB kinase-beta: NF-kappaB activation and complex formation with IkappaB kinase-alpha and NIK."
Woronicz J.D., Gao X., Cao Z., Rothe M., Goeddel D.V.
Science 278:866-869(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF LYS-44.
[3]"IkappaB kinase-alpha and -beta genes are coexpressed in adult and embryonic tissues but localized to different human chromosomes."
Hu M.C.-T., Wang Y.-P.
Gene 222:31-40(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Heart.
[4]"Assignment of IkappaB kinase beta (IKBKB) to human chromosome band 8p12-->p11 by in situ hybridization."
Shindo M., Nakano H., Sakon S., Yagita H., Mihara M., Okumura K.
Cytogenet. Cell Genet. 82:32-33(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GENE MAPPING.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
Tissue: Testis and Thymus.
[6]SeattleSNPs variation discovery resource
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TRP-554.
[7]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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: Lung.
[9]"Acetylation of MEK2 and I kappa B kinase (IKK) activation loop residues by YopJ inhibits signaling."
Mittal R., Peak-Chew S.Y., McMahon H.T.
Proc. Natl. Acad. Sci. U.S.A. 103:18574-18579(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 170-182 (ISOFORM 1), INACTIVATION BY YERSINIA YOPJ, ACETYLATION AT THR-180, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"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.
[11]"IKAP is a scaffold protein of the IkappaB kinase complex."
Cohen L., Henzel W.J., Baeuerle P.A.
Nature 395:292-296(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH CHUK; NFKBIA; RELA; IKBKAP AND MAP3K14.
[12]"The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation."
Sanz L., Sanchez P., Lallena M.-J., Diaz-Meco M.T., Moscat J.
EMBO J. 18:3044-3053(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SQSTM1; PRKCZ AND PRKCI.
[13]"Activation of IkappaB kinase beta by protein kinase C isoforms."
Lallena M.J., Diaz-Meco M.T., Bren G., Paya C.V., Moscat J.
Mol. Cell. Biol. 19:2180-2188(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-177 AND SER-181.
[14]"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: PHOSPHORYLATION AT SER-177; SER-181; SER-670; SER-672; SER-675; SER-682; SER-689; SER-692; SER-695; SER-697; SER-705; SER-733; SER-740 AND SER-750.
[15]"PKR stimulates NF-kappaB irrespective of its kinase function by interacting with the IkappaB kinase complex."
Bonnet M.C., Weil R., Dam E., Hovanessian A.G., Meurs E.F.
Mol. Cell. Biol. 20:4532-4542(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF2AK2.
[16]"NAK is an IkappaB kinase-activating kinase."
Tojima Y., Fujimoto A., Delhase M., Chen Y., Hatakeyama S., Nakayama K., Kaneko Y., Nimura Y., Motoyama N., Ikeda K., Karin M., Nakanishi M.
Nature 404:778-782(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-177 AND SER-181 BY TBK1, MUTAGENESIS OF 177-SER--SER-181.
[17]"Direct phosphorylation of NF-kappa B1 p105 by the Ikappa B kinase complex on serine 927 is essential for signal-induced p105 proteolysis."
Salmeron A., Janzen J., Soneji Y., Bump N., Kamens J., Allen H., Ley S.C.
J. Biol. Chem. 276:22215-22222(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF NFKB1.
[18]"Association of the adaptor TANK with the I kappa B kinase (IKK) regulator NEMO connects IKK complexes with IKK epsilon and TBK1 kinases."
Chariot A., Leonardi A., Muller J., Bonif M., Brown K., Siebenlist U.
J. Biol. Chem. 277:37029-37036(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IKBKG AND TANK.
[19]"Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator activity by I kappa B kinase."
Wu R.-C., Qin J., Hashimoto Y., Wong J., Xu J., Tsai S.Y., Tsai M.-J., O'Malley B.W.
Mol. Cell. Biol. 22:3549-3561(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH CREBBP; NCOA2; NCOA3; IKKA AND IKBKG.
[20]"Tetrameric oligomerization of IkappaB kinase gamma (IKKgamma) is obligatory for IKK complex activity and NF-kappaB activation."
Tegethoff S., Behlke J., Scheidereit C.
Mol. Cell. Biol. 23:2029-2041(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPOSITION OF THE IKK COMPLEX.
[21]"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.
[22]"PAN1/NALP2/PYPAF2, an inducible inflammatory mediator that regulates NF-kappaB and caspase-1 activation in macrophages."
Bruey J.-M., Bruey-Sedano N., Newman R., Chandler S., Stehlik C., Reed J.C.
J. Biol. Chem. 279:51897-51907(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NALP2.
[23]"beta-Arrestin inhibits NF-kappaB activity by means of its interaction with the NF-kappaB inhibitor IkappaBalpha."
Witherow D.S., Garrison T.R., Miller W.E., Lefkowitz R.J.
Proc. Natl. Acad. Sci. U.S.A. 101:8603-8607(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARRB1 AND ARRB2.
[24]"Nitric oxide represses inhibitory kappaB kinase through S-nitrosylation."
Reynaert N.L., Ckless K., Korn S.H., Vos N., Guala A.S., Wouters E.F., van der Vliet A., Janssen-Heininger Y.M.
Proc. Natl. Acad. Sci. U.S.A. 101:8945-8950(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: S-NITROSYLATION AT CYS-179.
[25]"NIBP, a novel NIK and IKK(beta)-binding protein that enhances NF-(kappa)B activation."
Hu W.-H., Pendergast J.S., Mo X.-M., Brambilla R., Bracchi-Ricard V., Li F., Walters W.M., Blits B., He L., Schaal S.M., Bethea J.R.
J. Biol. Chem. 280:29233-29241(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NIBP.
[26]"3-Phosphoinositide-dependent protein kinase-1-mediated IkappaB kinase beta (IkkB) phosphorylation activates NF-kappaB signaling."
Tanaka H., Fujita N., Tsuruo T.
J. Biol. Chem. 280:40965-40973(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-181 BY PDPK1, INTERACTION WITH PDPK1.
[27]"Site-specific monoubiquitination of IkappaB kinase IKKbeta regulates its phosphorylation and persistent activation."
Carter R.S., Pennington K.N., Arrate P., Oltz E.M., Ballard D.W.
J. Biol. Chem. 280:43272-43279(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION AT LYS-163.
[28]"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.
[29]"Prolyl hydroxylase-1 negatively regulates IkappaB kinase-beta, giving insight into hypoxia-induced NFkappaB activity."
Cummins E.P., Berra E., Comerford K.M., Ginouves A., Fitzgerald K.T., Seeballuck F., Godson C., Nielsen J.E., Moynagh P., Pouyssegur J., Taylor C.T.
Proc. Natl. Acad. Sci. U.S.A. 103:18154-18159(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: HYDROXYLATION AT PRO-191, MUTAGENESIS OF PRO-191.
[30]"Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation."
Mukherjee S., Keitany G., Li Y., Wang Y., Ball H.L., Goldsmith E.J., Orth K.
Science 312:1211-1214(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH YOPJ, ACETYLATION.
[31]"Molecular linkage between the kinase ATM and NF-kappaB signaling in response to genotoxic stimuli."
Wu Z.H., Shi Y., Tibbetts R.S., Miyamoto S.
Science 311:1141-1146(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATM.
[32]"Caveolin-1 triggers T-cell activation via CD26 in association with CARMA1."
Ohnuma K., Uchiyama M., Yamochi T., Nishibashi K., Hosono O., Takahashi N., Kina S., Tanaka H., Lin X., Dang N.H., Morimoto C.
J. Biol. Chem. 282:10117-10131(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MEMBRANE RAFT COMPLEX, SUBCELLULAR LOCATION.
[33]"FAF1 suppresses IkappaB kinase (IKK) activation by disrupting the IKK complex assembly."
Park M.Y., Moon J.H., Lee K.S., Choi H.I., Chung J., Hong H.J., Kim E.
J. Biol. Chem. 282:27572-27577(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FAF1.
[34]"Negative feedback loop in T cell activation through IkappaB kinase-induced phosphorylation and degradation of Bcl10."
Lobry C., Lopez T., Israel A., Weil R.
Proc. Natl. Acad. Sci. U.S.A. 104:908-913(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF BCL10.
[35]"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.
[36]"The IkappaB kinase complex: master regulator of NF-kappaB signaling."
Solt L.A., May M.J.
Immunol. Res. 42:3-18(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW, DOMAIN.
[37]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[38]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[39]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[40]"PPM1A and PPM1B act as IKKbeta phosphatases to terminate TNFalpha-induced IKKbeta-NF-kappaB activation."
Sun W., Yu Y., Dotti G., Shen T., Tan X., Savoldo B., Pass A.K., Chu M., Zhang D., Lu X., Fu S., Lin X., Yang J.
Cell. Signal. 21:95-102(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: DEPHOSPHORYLATION AT SER-177 AND SER-181, INTERACTION WITH PPM1A AND PPM1B.
[41]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[42]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[43]"NLRC5 negatively regulates the NF-kappaB and type I interferon signaling pathways."
Cui J., Zhu L., Xia X., Wang H.Y., Legras X., Hong J., Ji J., Shen P., Zheng S., Chen Z.J., Wang R.F.
Cell 141:483-496(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NLRC5.
[44]"Ro52-mediated monoubiquitination of IKK{beta} down-regulates NF-{kappa}B signalling."
Wada K., Niida M., Tanaka M., Kamitani T.
J. Biochem. 146:821-832(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIM21, MONOUBIQUITINATION, UBIQUITINATION INACTIVATION BY YERSINIA YOPJ, MUTAGENESIS OF LYS-163; SER-177 AND SER-181.
[45]"Respiratory syncytial virus-mediated NF-kappa B p65 phosphorylation at serine 536 is dependent on RIG-I, TRAF6, and IKK beta."
Yoboua F., Martel A., Duval A., Mukawera E., Grandvaux N.
J. Virol. 84:7267-7277(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF RELA.
[46]"Nuclear IKKbeta is an adaptor protein for IkappaBalpha ubiquitination and degradation in UV-induced NF-kappaB activation."
Tsuchiya Y., Asano T., Nakayama K., Kato T. Jr., Karin M., Kamata H.
Mol. Cell 39:570-582(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION.
[47]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[48]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[49]"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 TBK1 AND IKBKE.
[50]"The zinc finger protein ZNF268 is overexpressed in human cervical cancer and contributes to tumorigenesis via enhancing NF-kappaB signaling."
Wang W., Guo M., Hu L., Cai J., Zeng Y., Luo J., Shu Z., Li W., Huang Z.
J. Biol. Chem. 287:42856-42866(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZNF268, SUBUNIT.
[51]"IKKepsilon-mediated tumorigenesis requires K63-linked polyubiquitination by a cIAP1/cIAP2/TRAF2 E3 ubiquitin ligase complex."
Zhou A.Y., Shen R.R., Kim E., Lock Y.J., Xu M., Chen Z.J., Hahn W.C.
Cell Rep. 3:724-733(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IKBKE.
[52]"Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site."
Rushe M., Silvian L., Bixler S., Chen L.L., Cheung A., Bowes S., Cuervo H., Berkowitz S., Zheng T., Guckian K., Pellegrini M., Lugovskoy A.
Structure 16:798-808(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 701-742.
[53]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-360.
[54]"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. expand/collapse author list , 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] SER-360; ARG-369; GLN-526; THR-710 AND LEU-734.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001177649.1. NM_001190720.2.
NP_001229707.1. NM_001242778.1.
NP_001547.1. NM_001556.2.
UniGeneHs.597664.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalO14920.
SMRO14920. Positions 2-663, 702-743.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109767. 113 interactions.
DIPDIP-27527N.
IntActO14920. 48 interactions.
MINTMINT-107608.
STRING9606.ENSP00000339151.

Chemistry

BindingDBO14920.
ChEMBLCHEMBL1991.
DrugBankDB01169. Arsenic trioxide.
DB00995. Auranofin.
GuidetoPHARMACOLOGY2039.

PTM databases

PhosphoSiteO14920.

Proteomic databases

PaxDbO14920.
PRIDEO14920.

Protocols and materials databases

DNASU3551.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000416505; ENSP00000404920; ENSG00000104365. [O14920-4]
ENST00000519735; ENSP00000430483; ENSG00000104365. [O14920-3]
ENST00000520810; ENSP00000430684; ENSG00000104365. [O14920-1]
ENST00000520835; ENSP00000430868; ENSG00000104365. [O14920-2]
GeneID3551.
KEGGhsa:3551.
UCSCuc003xow.2. human. [O14920-1]
uc011lcq.2. human. [O14920-2]
uc011lcr.2. human. [O14920-4]

Organism-specific databases

CTD3551.
GeneCardsGC08P042146.
HGNCHGNC:5960. IKBKB.
HPACAB004447.
HPA001249.
MIM603258. gene.
neXtProtNX_O14920.
PharmGKBPA29776.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000038048.
HOVERGENHBG018241.
InParanoidO14920.
KOK07209.
OMAGILFYEL.
OrthoDBEOG7FBRH3.
PhylomeDBO14920.
TreeFamTF324269.

Enzyme and pathway databases

BRENDA2.7.11.10. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.
SABIO-RKO14920.
SignaLinkO14920.

Gene expression databases

ArrayExpressO14920.
BgeeO14920.
CleanExHS_IKBKB.
GenevestigatorO14920.

Family and domain databases

InterProIPR022007. IKKbetaNEMObind.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR000626. Ubiquitin-like.
[Graphical view]
PfamPF12179. IKKbetaNEMObind. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO14920.
GeneWikiIKK2.
GenomeRNAi3551.
NextBio13864.
PROO14920.
SOURCESearch...

Entry information

Entry nameIKKB_HUMAN
AccessionPrimary (citable) accession number: O14920
Secondary accession number(s): B4DZ30, B4E0U4, O75327
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 161 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM