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Entry version 167 (02 Jun 2021)
Sequence version 1 (01 May 2000)
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Protein

Inhibitor of nuclear factor kappa-B kinase subunit beta

Gene

Ikbkb

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 (By similarity).

Phosphorylates RIPK1 at 'Ser-25' which represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death (By similarity).

Phosphorylates the C-terminus of IRF5, stimulating IRF5 homodimerization and translocation into the nucleus (By similarity).

By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei44ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei145Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi21 – 29ATPPROSITE-ProRule annotation9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.11.10, 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-1169091, Activation of NF-kappaB in B cells
R-RNO-168638, NOD1/2 Signaling Pathway
R-RNO-1810476, RIP-mediated NFkB activation via ZBP1
R-RNO-202424, Downstream TCR signaling
R-RNO-209543, p75NTR recruits signalling complexes
R-RNO-209560, NF-kB is activated and signals survival
R-RNO-2871837, FCERI mediated NF-kB activation
R-RNO-445989, TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-RNO-5357905, Regulation of TNFR1 signaling
R-RNO-5357956, TNFR1-induced NFkappaB signaling pathway
R-RNO-5607764, CLEC7A (Dectin-1) signaling
R-RNO-5684264, MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-RNO-9020702, Interleukin-1 signaling
R-RNO-933542, TRAF6 mediated NF-kB activation
R-RNO-937039, IRAK1 recruits IKK complex
R-RNO-975144, IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
Serine/threonine protein kinase IKBKB (EC:2.7.11.1By similarity)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Ikbkb
Synonyms:Ikkb
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
621375, Ikbkb

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4524001

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000860151 – 757Inhibitor of nuclear factor kappa-B kinase subunit betaAdd BLAST757

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki163Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei177Phosphoserine; by TBK1 and PKC/PRKCZBy similarity1
Modified residuei179S-nitrosocysteineBy similarity1
Modified residuei181Phosphoserine; by TBK1, PKC/PRKCZ and PDPK1By similarity1
Modified residuei191HydroxyprolineBy similarity1
Modified residuei670Phosphoserine; by autocatalysisBy similarity1
Modified residuei672PhosphoserineCombined sources1
Modified residuei675Phosphoserine; by autocatalysisBy similarity1
Modified residuei682Phosphoserine; by autocatalysisBy similarity1
Modified residuei689Phosphoserine; by autocatalysisBy similarity1
Modified residuei692Phosphoserine; by autocatalysisBy similarity1
Modified residuei697Phosphoserine; by autocatalysisBy similarity1
Modified residuei705Phosphoserine; by autocatalysisBy similarity1
Modified residuei733Phosphoserine; by autocatalysisBy similarity1
Modified residuei740Phosphoserine; by autocatalysisBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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.By similarity
Ubiquitinated. Monoubiquitination involves TRIM21 that leads to inhibition of Tax-induced NF-kappa-B signaling. 'Ser-163' may not serve as a monoubiquitination site. Ubiquitination on 'Ser-163' may modulate phosphorylation on C-terminal serine residues.By similarity
Hydroxylated by PHD1/EGLN2, loss of hydroxylation under hypoxic conditions results in activation of NF-kappa-B.By similarity

Keywords - PTMi

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

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q9QY78

PRoteomics IDEntifications database

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PRIDEi
Q9QY78

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9QY78

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q9QY78

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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. 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, ELP1 and MAP3K14.

Found in a membrane raft complex, at least composed of BCL10, CARD11, DPP4 and IKBKB (By similarity).

Interacts with SQSTM1 through PRKCZ or PRKCI (PubMed:16079148).

Forms an NGF-induced complex with IKBKB, PRKCI and TRAF6 (PubMed:16079148). May interact with MAVS/IPS1.

Interacts with NALP2.

Interacts with TICAM1.

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.

Interacts with NAA10, leading to NAA10 degradation.

Interacts with FOXO3.

Interacts with ZC3H12A (By similarity).

Interacts with AKAP13 (PubMed:23090968).

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 (By similarity).

Interacts with SASH1 (By similarity).

Interacts with ARFIP2 (By similarity).

By similarity2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
249911, 2 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q9QY78

Protein interaction database and analysis system

More...
IntActi
Q9QY78, 4 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000025851

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q9QY78

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini15 – 300Protein kinasePROSITE-ProRule annotationAdd BLAST286

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni458 – 479Leucine-zipperAdd BLAST22
Regioni682 – 703DisorderedSequence analysisAdd BLAST22
Regioni737 – 742NEMO-binding6

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi682 – 698Polar residuesSequence analysisAdd BLAST17

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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 (By similarity).By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG4250, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9QY78

Database of Orthologous Groups

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OrthoDBi
1013139at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9QY78

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR041185, IKBKB_SDD
IPR022007, IKKbetaNEMObind
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR008271, Ser/Thr_kinase_AS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF18397, IKBKB_SDD, 1 hit
PF12179, IKKbetaNEMObind, 1 hit
PF00069, Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01239, IKKbetaNEMObind, 1 hit
SM00220, S_TKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56112, SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50011, PROTEIN_KINASE_DOM, 1 hit
PS00108, PROTEIN_KINASE_ST, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q9QY78-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSWSPSLPTQ TCGAWEMKER LGTGGFGNVI RWHNQVTGEQ IAIKQCRQEL
60 70 80 90 100
SPKNRDRWCL EIQIMRRLNH PNVVAARDVP EGMQNLAPND LPLLAMEYCQ
110 120 130 140 150
GGDLRRYLNQ FENCCGLREG AILTLLSDIA SALRYLHENR IIHRDLKPEN
160 170 180 190 200
IVLQQGEKRL IHKIIDLGYA KELDQGSLCT SFVGTLQYLA PELLEQQKYT
210 220 230 240 250
VTVDYWSFGT LAFECITGFR PFLPNWQPVQ WHSKVRQKSE VDIVVSEDLN
260 270 280 290 300
GTVKFSSSSP FPNNLNSVLA ERLEKWLQLM LTWQPRQRGV DPQYGPNGCF
310 320 330 340 350
RALDDILNLK LVHILNMVTG TIHTYPVMED ESLQSLKTRI REDTGILETD
360 370 380 390 400
QELLQEAGLV LLPDKPATQC ISDSKTNEGL TLDMDLVFLF DNSKMSYETQ
410 420 430 440 450
ITPRPQPESV SCVLQEPKRN LSFFQMRKVW GQVWHSIQTL KEDCNRLQQG
460 470 480 490 500
QRAAMMNLLR NNSCLSKMKN AMASTAQQLK AKLDFFKTSI QIDLEKYREQ
510 520 530 540 550
TEFGITSDKL LLAWREMEQA VEQCGRENDV KVLVERMMAL QTDIVDLQRS
560 570 580 590 600
PMGRKQGGTL DDLEEQAREL YRRLREKPRD QRTEGDSQDM VRLLLQAIQS
610 620 630 640 650
FEKKVRVIYS QLSKTVVCKQ KALELLPKVE EVVRLMNEDE KTVVRLQEKR
660 670 680 690 700
QKELWNLLKI ACSKVRGPVS GSPDSMNVSR LSHPGHLMSQ PSSACDSLPD
710 720 730 740 750
SDKKSEELVA EAHALCSRLE SALQDTVKQQ DRSFTTLDWS WLQMEDEERC

GLEQACD
Length:757
Mass (Da):86,866
Last modified:May 1, 2000 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i3AFFE46A7DF91F9C
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V8H5G3V8H5_RAT
I-kappa-B kinase
Ikbkb rCG_43029
757Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AF115282 mRNA Translation: AAF21978.1

NCBI Reference Sequences

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RefSeqi
NP_445807.2, NM_053355.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
84351

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:84351

UCSC genome browser

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UCSCi
RGD:621375, rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF115282 mRNA Translation: AAF21978.1
RefSeqiNP_445807.2, NM_053355.2

3D structure databases

SMRiQ9QY78
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi249911, 2 interactors
CORUMiQ9QY78
IntActiQ9QY78, 4 interactors
STRINGi10116.ENSRNOP00000025851

Chemistry databases

ChEMBLiCHEMBL4524001

PTM databases

iPTMnetiQ9QY78
PhosphoSitePlusiQ9QY78

Proteomic databases

PaxDbiQ9QY78
PRIDEiQ9QY78

Genome annotation databases

GeneIDi84351
KEGGirno:84351
UCSCiRGD:621375, rat

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
3551
RGDi621375, Ikbkb

Phylogenomic databases

eggNOGiKOG4250, Eukaryota
InParanoidiQ9QY78
OrthoDBi1013139at2759
PhylomeDBiQ9QY78

Enzyme and pathway databases

BRENDAi2.7.11.10, 5301
ReactomeiR-RNO-1169091, Activation of NF-kappaB in B cells
R-RNO-168638, NOD1/2 Signaling Pathway
R-RNO-1810476, RIP-mediated NFkB activation via ZBP1
R-RNO-202424, Downstream TCR signaling
R-RNO-209543, p75NTR recruits signalling complexes
R-RNO-209560, NF-kB is activated and signals survival
R-RNO-2871837, FCERI mediated NF-kB activation
R-RNO-445989, TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-RNO-5357905, Regulation of TNFR1 signaling
R-RNO-5357956, TNFR1-induced NFkappaB signaling pathway
R-RNO-5607764, CLEC7A (Dectin-1) signaling
R-RNO-5684264, MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-RNO-9020702, Interleukin-1 signaling
R-RNO-933542, TRAF6 mediated NF-kB activation
R-RNO-937039, IRAK1 recruits IKK complex
R-RNO-975144, IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation

Miscellaneous databases

Protein Ontology

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PROi
PR:Q9QY78

Family and domain databases

InterProiView protein in InterPro
IPR041185, IKBKB_SDD
IPR022007, IKKbetaNEMObind
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR008271, Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF18397, IKBKB_SDD, 1 hit
PF12179, IKKbetaNEMObind, 1 hit
PF00069, Pkinase, 1 hit
SMARTiView protein in SMART
SM01239, IKKbetaNEMObind, 1 hit
SM00220, S_TKc, 1 hit
SUPFAMiSSF56112, SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50011, PROTEIN_KINASE_DOM, 1 hit
PS00108, PROTEIN_KINASE_ST, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiIKKB_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9QY78
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: May 1, 2000
Last modified: June 2, 2021
This is version 167 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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