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Reviewed, UniProtKB/Swiss-Prot O14920 (IKKB_HUMAN)

Last modified February 9, 2010. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Inhibitor of nuclear factor kappa-B kinase subunit beta
      Short name=I-kappa-B-kinase beta
      Short name=IkBKB
      Short name=IKK-beta
      Short name=IKK-B
    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) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length756 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Acts as part of the IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Also phosphorylates NCOA3.

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. 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. Ref.9 Ref.12 Ref.15 Ref.16 Ref.17 Ref.19 Ref.21 Ref.22 Ref.23 Ref.25

Subcellular location

Cytoplasm. Membrane raft. Note: Colocalized with DPP4 in membrane rafts.

Tissue specificity

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

Post-translational modification

Upon cytokine stimulation, phosphorylated on Ser-177 and Ser-181 by MEKK1 and/or MAP3K14/NIK; which enhances activity. Once activated, autophosphorylates on the C-terminal serine cluster; which decreases activity and prevents prolonged activation of the inflammatory response. Ref.7 Ref.10 Ref.26 Ref.27 Ref.29 Ref.31

Yersinia yopJ may acetylate Ser/Thr residues, preventing phosphorylation and activation, which blocks the I-kappa-B signaling pathway.

Ubiquitination on 'Ser-163' modulates phosphorylation on C-terminal serine residues.

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. I-kappa-B kinase subfamily.

Contains 1 protein kinase domain.

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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
Domain458 – 47922Leucine-zipper
Nucleotide binding21 – 299ATP By similarity
Region737 – 7426NEMO-binding

Sites

Active site1451Proton acceptor By similarity
Binding site441ATP By similarity

Amino acid modifications

Modified residue231Phosphothreonine By similarity
Modified residue1771Phosphoserine Ref.10
Modified residue1791S-nitrosocysteine Ref.18
Modified residue1811Phosphoserine Ref.10
Modified residue6701Phosphoserine; by autocatalysis Probable
Modified residue6721Phosphoserine; by autocatalysis Probable
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.20

Natural variations

Natural variant3601A → S in breast cancer samples; infiltrating ductal carcinoma; somatic mutation. Ref.32 Ref.33
VAR_035626
Natural variant3691Q → R: dbSNP rs56411242. Ref.33
VAR_040567
Natural variant5261R → Q: dbSNP rs2272736. Ref.33
VAR_040568
Natural variant5541R → W: dbSNP rs17875749. Ref.5
VAR_021124
Natural variant7101A → T: dbSNP rs34309584. Ref.33
VAR_040569
Natural variant7341F → L: dbSNP rs56301637. Ref.33
VAR_040570
Natural variant7361A → T: dbSNP rs17611716.
VAR_051628

Experimental info

Mutagenesis441K → A: Loss of kinase activity and no effect on binding to NIK. Ref.1 Ref.2
Mutagenesis1771S → A: Decrease of activity. Ref.1
Mutagenesis1771S → E: Full activation. Ref.1
Mutagenesis1811S → A: Decrease of activity. Ref.1
Mutagenesis1811S → E: Full activation. Ref.1
Sequence conflict231 – 25525WHSKV…GTVKF → CVRMWPGTVAHSCNPSTLGG RGRWI Ref.6
Sequence conflict4251Q → H Ref.1

Secondary structure

1 ....... 756
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
O14920-1 [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

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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: 9346484] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 9346485] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 9813230] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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: 9763654] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE MAPPING.
[5]SeattleSNPs variation discovery resource
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TRP-554.
[6]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-256.
Tissue: Lung.
[7]"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: 9819420] [Abstract]
Cited for: IKK PHOSPHORYLATION.
[8]"IKAP is a scaffold protein of the IkappaB kinase complex."
Cohen L., Henzel W.J., Baeuerle P.A.
Nature 395:292-296(1998) [PubMed: 9751059] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH CHUK; NFKBIA; RELA; IKBKAP AND MAP3K14.
[9]"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: 10356400] [Abstract]
Cited for: INTERACTION WITH SQSTM1; PRKCZ AND PRKCI.
[10]"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: 10195894] [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.
[11]"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: 10712233] [Abstract]
Cited for: REVIEW.
[12]"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: 12133833] [Abstract]
Cited for: INTERACTION WITH IKBKG AND TANK.
[13]"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: 11971985] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH CREBBP; NCOA2; NCOA3; IKKA AND IKBKG.
[14]"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: 12612076] [Abstract]
Cited for: COMPOSITION OF THE IKK COMPLEX.
[15]"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: 14739303] [Abstract]
Cited for: INTERACTION WITH TICAM1.
[16]"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: 15456791] [Abstract]
Cited for: INTERACTION WITH NALP2.
[17]"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: 15173580] [Abstract]
Cited for: INTERACTION WITH ARRB1 AND ARRB2.
[18]"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: 15184672] [Abstract]
Cited for: S-NITROSYLATION AT CYS-179.
[19]"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: 15951441] [Abstract]
Cited for: INTERACTION WITH NIBP.
[20]"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: 16267042] [Abstract]
Cited for: UBIQUITINATION AT LYS-163.
[21]"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: 16177806] [Abstract]
Cited for: INTERACTION WITH MAVS.
[22]"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: 16728640] [Abstract]
Cited for: INTERACTION WITH YOPJ, ACETYLATION.
[23]"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: 16497931] [Abstract]
Cited for: INTERACTION WITH ATM.
[24]"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: 17287217] [Abstract]
Cited for: IDENTIFICATION IN A MEMBRANE RAFT COMPLEX, SUBCELLULAR LOCATION.
[25]"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: 17684021] [Abstract]
Cited for: INTERACTION WITH FAF1.
[26]"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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672, MASS SPECTROMETRY.
[27]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672, MASS SPECTROMETRY.
[28]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[29]"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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672, MASS SPECTROMETRY.
[30]"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: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-670 AND SER-672, MASS SPECTROMETRY.
[31]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672, MASS SPECTROMETRY.
Tissue: T-cell.
[32]"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: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-360.
[33]"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: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-360; ARG-369; GLN-526; THR-710 AND LEU-734.
+Additional computationally mapped references.

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Web resources

SeattleSNPs

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF029684 mRNA. Translation: AAC51860.1.
AF080158 mRNA. Translation: AAD08997.1.
AF031416 mRNA. Translation: AAC64675.1.
AY663108 Genomic DNA. Translation: AAT65965.1.
BC006231 mRNA. Translation: AAH06231.1.
IPIIPI00024709.
RefSeqNP_001547.1.
UniGeneHs.597664

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BRTX-ray2.25A/C701-742[»]
3BRVX-ray2.20A/C701-745[»]
SMRO14920. Positions 15-288.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-27527N.
IntActO14920. 46 interactions.
STRINGO14920.

PTM databases

PhosphoSiteO14920.

Proteomic databases

PRIDEO14920.

Genome annotation databases

EnsemblENST00000342222; ENSP00000339151; ENSG00000104365; Homo sapiens. [Genome view]
GeneID3551.
KEGGhsa:3551.
UCSCuc003xow.1. human.

Organism-specific databases

CTD3551.
GeneCardsGC08P042247.
H-InvDBHIX0007480.
HGNCHGNC:5960. IKBKB.
HPACAB004447.
HPA001249.
MIM603258. gene.
PharmGKBPA29776.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG358635.
HOVERGENO14920.
InParanoidO14920.
OMASPDSMNA.
PhylomeDBO14920.

Enzyme and pathway databases

BRENDA2.7.11.10. 247.
Pathway_Interaction_DBnfkappabatypicalpathway. Atypical NF-kappaB pathway.
bcr_5pathway. BCR signaling pathway.
nfkappabcanonicalpathway. Canonical NF-kappaB pathway.
fcer1pathway. Fc-epsilon receptor I signaling in mast cells.
foxopathway. FoxO family signaling.
il1pathway. IL1-mediated signaling events.
p75ntrpathway. p75(NTR)-mediated signaling.
tcrpathway. TCR signaling in naive CD4+ T cells.
cd8tcrpathway. TCR signaling in naive CD8+ T cells.
tnfpathway. TNF receptor signaling pathway.
trail_pathway. TRAIL signaling pathway.
ReactomeREACT_11061. Signalling by NGF.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpressO14920.
BgeeO14920.
CleanExHS_IKBKB.
GenevestigatorO14920.
GermOnlineENSG00000104365. Homo sapiens.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR019955. Ubiquitin_supergroup.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB01169. Arsenic trioxide.
DB00995. Auranofin.
NextBio13864.
SOURCESearch...

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Entry information

Entry nameIKKB_HUMAN
AccessionPrimary (citable) accession number: O14920
Secondary accession number(s): O75327
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: January 1, 1998
Last modified: February 9, 2010
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Index of Protein Data Bank (PDB) cross-references

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Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents