NFKB1

Functionⁱ

NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally. p50 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. In a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is released by proteasome-dependent degradation of NFKB1/p105.1 Publication

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Activator, DNA-binding
Biological process	Apoptosis, Transcription, Transcription regulation

Enzyme and pathway databases

PathwayCommonsⁱ	P19838
Reactomeⁱ	R-HSA-1169091, Activation of NF-kappaB in B cells R-HSA-1810476, RIP-mediated NFkB activation via ZBP1 R-HSA-193692, Regulated proteolysis of p75NTR R-HSA-202424, Downstream TCR signaling R-HSA-209560, NF-kB is activated and signals survival R-HSA-2559582, Senescence-Associated Secretory Phenotype (SASP) R-HSA-2871837, FCERI mediated NF-kB activation R-HSA-3134963, DEx/H-box helicases activate type I IFN and inflammatory cytokines production R-HSA-3214841, PKMTs methylate histone lysines R-HSA-381340, Transcriptional regulation of white adipocyte differentiation R-HSA-445989, TAK1 activates NFkB by phosphorylation and activation of IKKs complex R-HSA-448706, Interleukin-1 processing R-HSA-5603029, IkBA variant leads to EDA-ID R-HSA-5607764, CLEC7A (Dectin-1) signaling R-HSA-5621575, CD209 (DC-SIGN) signaling R-HSA-5660668, CLEC7A/inflammasome pathway R-HSA-5684264, MAP3K8 (TPL2)-dependent MAPK1/3 activation R-HSA-6798695, Neutrophil degranulation R-HSA-844456, The NLRP3 inflammasome R-HSA-8853884, Transcriptional Regulation by VENTX R-HSA-9020702, Interleukin-1 signaling R-HSA-933542, TRAF6 mediated NF-kB activation R-HSA-9609690, HCMV Early Events R-HSA-9660826, Purinergic signaling in leishmaniasis infection
SignaLinkⁱ	P19838
SIGNORⁱ	P19838

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Nuclear factor NF-kappa-B p105 subunit Alternative name(s): DNA-binding factor KBF1 EBP-1 Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 Cleaved into the following chain: Nuclear factor NF-kappa-B p50 subunit
Gene namesⁱ	Name:NFKB1
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 4

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000109320.11
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:7794, NFKB1
MIMⁱ	164011, gene
neXtProtⁱ	NX_P19838

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Immunodeficiency, common variable, 12 (CVID12)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA primary immunodeficiency characterized by antibody deficiency, hypogammaglobulinemia, recurrent bacterial infections and an inability to mount an antibody response to antigen.

Related information in OMIM

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	61	C → S: Suppresses S-nitrosylation-induced inhibition of DNA-binding activity. Loss of S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine-induced inhibition of DNA-binding activity. 2 Publications	1
Mutagenesisⁱ	678	N → A: Fails to promote HIF1AN-dependent 2-oxoglutarate decarboxylation. 1 Publication	1
Mutagenesisⁱ	903	S → A: Prevents p105 proteolysis in response to TNF-alpha. 1 Publication	1
Mutagenesisⁱ	907	S → A: Prevents p105 proteolysis in response to TNF-alpha. 1 Publication	1
Mutagenesisⁱ	921	S → A: Decrease in stimuli-induced phosphorylation. Loss of phosphorylation; when associated with A-923 and A-932. 1 Publication	1
Mutagenesisⁱ	923	S → A: Decrease in stimuli-induced phosphorylation. Loss of phosphorylation; when associated with A-921 and A-932. 1 Publication	1
Mutagenesisⁱ	932	S → A: Decrease in stimuli-induced phosphorylation. Loss of phosphorylation; when associated with A-921 and A-923. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	4790
MalaCards human disease database More...MalaCardsⁱ	NFKB1
MIMⁱ	616576, phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000109320
Orphanetⁱ	1572, Common variable immunodeficiency
PharmGKBⁱ	PA248

Miscellaneous databases

Pharosⁱ	P19838, Tchem

Pharosⁱ

P19838, Tchem

Chemistry databases

ChEMBLⁱ	CHEMBL3251
Drug and drug target database More...DrugBankⁱ	DB05767, Andrographolide DB05487, Custirsen DB00843, Donepezil DB13961, Fish oil DB13751, Glycyrrhizic acid DB05212, HE3286 DB05559, NF-kappaB Decoy DB05464, NOX-700 DB05451, P54 DB01411, Pranlukast DB00852, Pseudoephedrine DB14059, SC-236 DB05471, SGN-30 DB01041, Thalidomide DB08814, Triflusal
DrugCentral More...DrugCentralⁱ	P19838

Polymorphism and mutation databases

BioMutaⁱ	NFKB1
DMDMⁱ	21542418

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000030310	1 – 968	Nuclear factor NF-kappa-B p105 subunitAdd BLAST		968
ChainⁱPRO_0000030311	1 – 433	Nuclear factor NF-kappa-B p50 subunitAdd BLAST		433

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	61	S-nitrosocysteine; alternate1 Publication	1
Lipidationⁱ	61	S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternate1 Publication	1
Cross-linkⁱ	325	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residueⁱ	337	Phosphoserine; by PKASequence analysis	1
Modified residueⁱ	431	N6-acetyllysine; by EP3001 Publication	1
Modified residueⁱ	440	N6-acetyllysine; by EP3001 Publication	1
Modified residueⁱ	441	N6-acetyllysine; by EP3001 Publication	1
Modified residueⁱ	449	PhosphoserineBy similarity	1
Modified residueⁱ	678	(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication	1
Modified residueⁱ	759	PhosphoserineBy similarity	1
Modified residueⁱ	892	PhosphoserineCombined sources	1
Modified residueⁱ	903	Phosphoserine; by GSK3-beta; in vitroCombined sources1 Publication	1
Modified residueⁱ	907	Phosphoserine; by GSK3-beta; in vitroCombined sources1 Publication	1
Modified residueⁱ	927	Phosphoserine; by IKKB2 Publications	1
Modified residueⁱ	932	Phosphoserine; by IKKB1 Publication	1
Modified residueⁱ	937	PhosphoserineCombined sources	1
Modified residueⁱ	943	PhosphothreonineBy similarity	1

Post-translational modificationⁱ

While translation occurs, the particular unfolded structure after the GRR repeat promotes the generation of p50 making it an acceptable substrate for the proteasome. This process is known as cotranslational processing. The processed form is active and the unprocessed form acts as an inhibitor (I kappa B-like), being able to form cytosolic complexes with NF-kappa B, trapping it in the cytoplasm. Complete folding of the region downstream of the GRR repeat precludes processing.1 Publication

Phosphorylation at 'Ser-903' and 'Ser-907' primes p105 for proteolytic processing in response to TNF-alpha stimulation. Phosphorylation at 'Ser-927' and 'Ser-932' are required for BTRC/BTRCP-mediated proteolysis.4 Publications

Polyubiquitination seems to allow p105 processing.2 Publications

S-nitrosylation of Cys-61 affects DNA binding.2 Publications

The covalent modification of cysteine by 15-deoxy-Delta12,14-prostaglandin-J2 is autocatalytic and reversible. It may occur as an alternative to other cysteine modifications, such as S-nitrosylation and S-palmitoylation.

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	433 – 434	Cleavage (when cotranslationally processed)		2

Keywords - PTMⁱ

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

Proteomic databases

The CPTAC Assay portal More...CPTACⁱ	CPTAC-1260 CPTAC-1330
EPDⁱ	P19838
jPOSTⁱ	P19838
MassIVEⁱ	P19838
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P19838
PaxDbⁱ	P19838
PeptideAtlas More...PeptideAtlasⁱ	P19838
PRIDEⁱ	P19838
ProteomicsDBⁱ	53694 [P19838-1] 53695 [P19838-2] 53696 [P19838-3]

PTM databases

iPTMnetⁱ	P19838
MetOSiteⁱ	P19838
PhosphoSitePlusⁱ	P19838

Expressionⁱ

Inductionⁱ

By phorbol ester and TNF.

Gene expression databases

Bgeeⁱ	ENSG00000109320, Expressed in bone marrow and 212 other tissues
ExpressionAtlasⁱ	P19838, baseline and differential
Genevisibleⁱ	P19838, HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000109320, Low tissue specificity

HPAⁱ

ENSG00000109320, Low tissue specificity

Interactionⁱ

Subunit structureⁱ

Component of the NF-kappa-B p65-p50 complex.

Component of the NF-kappa-B p65-p50 complex. Homodimer; component of the NF-kappa-B p50-p50 complex.

Component of the NF-kappa-B p105-p50 complex.

Component of the NF-kappa-B p50-c-Rel complex.

Component of a complex consisting of the NF-kappa-B p50-p50 homodimer and BCL3.

Also interacts with MAP3K8. NF-kappa-B p50 subunit interacts with NCOA3 coactivator, which may coactivate NF-kappa-B dependent expression via its histone acetyltransferase activity.

Interacts with DSIPI; this interaction prevents nuclear translocation and DNA-binding.

Interacts with SPAG9 and UNC5CL. NFKB1/p105 interacts with CFLAR; the interaction inhibits p105 processing into p50. NFKB1/p105 forms a ternary complex with MAP3K8 and TNIP2.

Interacts with GSK3B; the interaction prevents processing of p105 to p50. NFKB1/p50 interacts with NFKBIE. NFKB1/p50 interacts with NFKBIZ. Nuclear factor NF-kappa-B p50 subunit interacts with NFKBID (By similarity). Directly interacts with MEN1.

Interacts with HIF1AN.

By similarity17 Publications

Binary interactionsⁱ

Hide details

P19838

With	#Exp.	IntAct
ABCC2 [Q92887]	3	EBI-300010,EBI-3916193
CHUK [O15111]	3	EBI-300010,EBI-81249
COPB2 [P35606]	3	EBI-300010,EBI-1056534
CTNNB1 [P35222]	3	EBI-300010,EBI-491549
HDAC1 [Q13547]	5	EBI-300010,EBI-301834
HIF1AN [Q9NWT6]	7	EBI-300010,EBI-745632
HSP90AB1 [P08238]	3	EBI-300010,EBI-352572
HSPA1L [P34931]	3	EBI-300010,EBI-354912
IKBKB [O14920]	3	EBI-300010,EBI-81266
MAP3K8 [P41279]	13	EBI-300010,EBI-354900
itself	7	EBI-300010,EBI-300010
NFKB2 [Q00653]	6	EBI-300010,EBI-307326
NFKBIA [P25963]	6	EBI-300010,EBI-307386
NOTCH1 [P46531]	2	EBI-300010,EBI-636374
PDCD11 [Q14690]	2	EBI-300010,EBI-300028
PELP1 [Q8IZL8]	2	EBI-300010,EBI-716449
PLD3 [Q8IV08]	2	EBI-300010,EBI-2689908
RELA [Q04206]	12	EBI-300010,EBI-73886
RELB [Q01201]	3	EBI-300010,EBI-357837
RPS3 [P23396]	4	EBI-300010,EBI-351193
TNIP1 [Q15025]	4	EBI-300010,EBI-357849
TNIP2 [Q8NFZ5]	5	EBI-300010,EBI-359372
UL42 [P10226] from Human herpesvirus 1 (strain 17).	4	EBI-300010,EBI-1029310

Isoform 1 [P19838-1]

With	#Exp.	IntAct
TNIP2 [Q8NFZ5]	8	EBI-1452239,EBI-359372

Nuclear factor NF-kappa-B p50 subunit (PRO_0000030311)

With	#Exp.	IntAct
ESR1 [P03372]	3	EBI-697771,EBI-78473
MEN1 [O00255]	2	EBI-697771,EBI-592789
MEN1 - isoform 2 [O00255-2]	4	EBI-697771,EBI-9869387
RELA [Q04206]	7	EBI-697771,EBI-73886
UL42 [P10226] from Human herpesvirus 1 (strain 17).	2	EBI-697771,EBI-1029310

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGRIDⁱ	110857, 201 interactors
ComplexPortalⁱ	CPX-5828, NF-kappaB DNA-binding transcription factor complex, p50/p65 CPX-5832, NF-kappaB DNA-binding transcription factor complex, p50/c-Rel CPX-5833, NF-kappaB DNA-binding transcription factor complex, p50/RelB CPX-5837, NF-kappaB transcription regulation complex complex, p50/p52 CPX-5838, NF-kappaB transcription regulation complex, p50/p50
CORUMⁱ	P19838
Database of interacting proteins More...DIPⁱ	DIP-106N
ELMⁱ	P19838
IntActⁱ	P19838, 489 interactors
Molecular INTeraction database More...MINTⁱ	P19838
STRINGⁱ	9606.ENSP00000226574

Chemistry databases

BindingDBⁱ

P19838

Miscellaneous databases

RNActⁱ	P19838, protein

RNActⁱ

P19838, protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	43 – 48	Combined sources	6
Beta strandⁱ	52 – 54	Combined sources	3
Helixⁱ	60 – 62	Combined sources	3
Beta strandⁱ	83 – 88	Combined sources	6
Beta strandⁱ	94 – 100	Combined sources	7
Beta strandⁱ	103 – 105	Combined sources	3
Beta strandⁱ	110 – 115	Combined sources	6
Beta strandⁱ	122 – 126	Combined sources	5
Beta strandⁱ	133 – 135	Combined sources	3
Beta strandⁱ	138 – 143	Combined sources	6
Helixⁱ	146 – 148	Combined sources	3
Helixⁱ	149 – 163	Combined sources	15
Helixⁱ	167 – 170	Combined sources	4
Helixⁱ	173 – 178	Combined sources	6
Beta strandⁱ	180 – 182	Combined sources	3
Turnⁱ	184 – 187	Combined sources	4
Helixⁱ	190 – 204	Combined sources	15
Beta strandⁱ	211 – 221	Combined sources	11
Beta strandⁱ	223 – 225	Combined sources	3
Beta strandⁱ	227 – 230	Combined sources	4
Beta strandⁱ	234 – 240	Combined sources	7
Helixⁱ	245 – 247	Combined sources	3
Beta strandⁱ	252 – 256	Combined sources	5
Beta strandⁱ	258 – 261	Combined sources	4
Beta strandⁱ	267 – 274	Combined sources	8
Helixⁱ	277 – 279	Combined sources	3
Beta strandⁱ	281 – 288	Combined sources	8
Turnⁱ	289 – 291	Combined sources	3
Beta strandⁱ	292 – 297	Combined sources	6
Helixⁱ	302 – 304	Combined sources	3
Turnⁱ	307 – 309	Combined sources	3
Beta strandⁱ	310 – 314	Combined sources	5
Beta strandⁱ	319 – 322	Combined sources	4
Beta strandⁱ	327 – 334	Combined sources	8
Turnⁱ	336 – 338	Combined sources	3
Beta strandⁱ	345 – 350	Combined sources	6
Helixⁱ	813 – 823	Combined sources	11
Helixⁱ	832 – 839	Combined sources	8
Helixⁱ	842 – 844	Combined sources	3
Helixⁱ	845 – 850	Combined sources	6
Helixⁱ	854 – 864	Combined sources	11
Helixⁱ	869 – 879	Combined sources	11
Helixⁱ	883 – 892	Combined sources	10

Show more details

3D structure databases

SMRⁱ	P19838
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P19838

EvolutionaryTraceⁱ

P19838

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	42 – 367	RHDPROSITE-ProRule annotationAdd BLAST	326
Repeatⁱ	542 – 571	ANK 1Add BLAST	30
Repeatⁱ	581 – 610	ANK 2Add BLAST	30
Repeatⁱ	614 – 643	ANK 3Add BLAST	30
Repeatⁱ	650 – 679	ANK 4Add BLAST	30
Repeatⁱ	684 – 714	ANK 5Add BLAST	31
Repeatⁱ	718 – 747	ANK 6Add BLAST	30
Repeatⁱ	771 – 801	ANK 7Add BLAST	31
Domainⁱ	805 – 892	DeathAdd BLAST	88

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	372 – 394	GRRAdd BLAST	23
Regionⁱ	435 – 968	Interaction with CFLAR1 PublicationAdd BLAST	534
Regionⁱ	650 – 684	Essential for interaction with HIF1AN1 PublicationAdd BLAST	35

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	360 – 365	Nuclear localization signalSequence analysis		6

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	375 – 433	Gly-richAdd BLAST		59

Domainⁱ

The C-terminus of p105 might be involved in cytoplasmic retention, inhibition of DNA-binding, and transcription activation.

Glycine-rich region (GRR) appears to be a critical element in the generation of p50.

Keywords - Domainⁱ

ANK repeat, Repeat

Phylogenomic databases

eggNOGⁱ	KOG0504, Eukaryota
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000158625
HOGENOMⁱ	CLU_004343_1_0_1
InParanoidⁱ	P19838
OMAⁱ	CAIHLAV
Database of Orthologous Groups More...OrthoDBⁱ	916931at2759
PhylomeDBⁱ	P19838
TreeFamⁱ	TF325632

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd01177, IPT_NFkappaB, 1 hit
Gene3Dⁱ	1.25.40.20, 1 hit 2.60.40.10, 1 hit 2.60.40.340, 1 hit
InterProⁱ	View protein in InterPro IPR002110, Ankyrin_rpt IPR020683, Ankyrin_rpt-contain_dom IPR036770, Ankyrin_rpt-contain_sf IPR011029, DEATH-like_dom_sf IPR000488, Death_domain IPR013783, Ig-like_fold IPR014756, Ig_E-set IPR002909, IPT_dom IPR033926, IPT_NFkappaB IPR030503, NF-kB_p105 IPR000451, NFkB/Dor IPR008967, p53-like_TF_DNA-bd IPR030492, RHD_CS IPR032397, RHD_dimer IPR011539, RHD_DNA_bind_dom IPR037059, RHD_DNA_bind_dom_sf
PANTHERⁱ	PTHR24169, PTHR24169, 1 hit PTHR24169:SF9, PTHR24169:SF9, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF12796, Ank_2, 2 hits PF00531, Death, 1 hit PF16179, RHD_dimer, 1 hit PF00554, RHD_DNA_bind, 1 hit
PRINTSⁱ	PR01415, ANKYRIN PR00057, NFKBTNSCPFCT
SMARTⁱ	View protein in SMART SM00248, ANK, 6 hits SM00005, DEATH, 1 hit SM00429, IPT, 1 hit
SUPFAMⁱ	SSF47986, SSF47986, 1 hit SSF48403, SSF48403, 1 hit SSF49417, SSF49417, 1 hit SSF81296, SSF81296, 1 hit
PROSITEⁱ	View protein in PROSITE PS50297, ANK_REP_REGION, 1 hit PS50088, ANK_REPEAT, 5 hits PS01204, REL_1, 1 hit PS50254, REL_2, 1 hit

Sequences (3+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 3 described isoforms and 6 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: P19838-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the canonicalⁱ sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAEDDPYLGR PEQMFHLDPS LTHTIFNPEV FQPQMALPTD GPYLQILEQP 
        60         70         80         90        100
KQRGFRFRYV CEGPSHGGLP GASSEKNKKS YPQVKICNYV GPAKVIVQLV 
       110        120        130        140        150
TNGKNIHLHA HSLVGKHCED GICTVTAGPK DMVVGFANLG ILHVTKKKVF 
       160        170        180        190        200
ETLEARMTEA CIRGYNPGLL VHPDLAYLQA EGGGDRQLGD REKELIRQAA 
       210        220        230        240        250
LQQTKEMDLS VVRLMFTAFL PDSTGSFTRR LEPVVSDAIY DSKAPNASNL 
       260        270        280        290        300
KIVRMDRTAG CVTGGEEIYL LCDKVQKDDI QIRFYEEEEN GGVWEGFGDF 
       310        320        330        340        350
SPTDVHRQFA IVFKTPKYKD INITKPASVF VQLRRKSDLE TSEPKPFLYY 
       360        370        380        390        400
PEIKDKEEVQ RKRQKLMPNF SDSFGGGSGA GAGGGGMFGS GGGGGGTGST 
       410        420        430        440        450
GPGYSFPHYG FPTYGGITFH PGTTKSNAGM KHGTMDTESK KDPEGCDKSD 
       460        470        480        490        500
DKNTVNLFGK VIETTEQDQE PSEATVGNGE VTLTYATGTK EESAGVQDNL 
       510        520        530        540        550
FLEKAMQLAK RHANALFDYA VTGDVKMLLA VQRHLTAVQD ENGDSVLHLA 
       560        570        580        590        600
IIHLHSQLVR DLLEVTSGLI SDDIINMRND LYQTPLHLAV ITKQEDVVED 
       610        620        630        640        650
LLRAGADLSL LDRLGNSVLH LAAKEGHDKV LSILLKHKKA ALLLDHPNGD 
       660        670        680        690        700
GLNAIHLAMM SNSLPCLLLL VAAGADVNAQ EQKSGRTALH LAVEHDNISL 
       710        720        730        740        750
AGCLLLEGDA HVDSTTYDGT TPLHIAAGRG STRLAALLKA AGADPLVENF 
       760        770        780        790        800
EPLYDLDDSW ENAGEDEGVV PGTTPLDMAT SWQVFDILNG KPYEPEFTSD 
       810        820        830        840        850
DLLAQGDMKQ LAEDVKLQLY KLLEIPDPDK NWATLAQKLG LGILNNAFRL 
       860        870        880        890        900
SPAPSKTLMD NYEVSGGTVR ELVEALRQMG YTEAIEVIQA ASSPVKTTSQ 
       910        920        930        940        950
AHSLPLSPAS TRQQIDELRD SDSVCDSGVE TSFRKLSFTE SLTSGASLLT 
       960 
LNKMPHDYGQ EGPLEGKI

Length:968

Mass (Da):105,356

Last modified:June 20, 2002 - v2

Checksum:ⁱ2A7C8FF86A10D1A8

GO

Isoform 2 (identifier: P19838-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
39-39: T → TA

« Hide

        10         20         30         40         50
MAEDDPYLGR PEQMFHLDPS LTHTIFNPEV FQPQMALPTA DGPYLQILEQ 
        60         70         80         90        100
PKQRGFRFRY VCEGPSHGGL PGASSEKNKK SYPQVKICNY VGPAKVIVQL 
       110        120        130        140        150
VTNGKNIHLH AHSLVGKHCE DGICTVTAGP KDMVVGFANL GILHVTKKKV 
       160        170        180        190        200
FETLEARMTE ACIRGYNPGL LVHPDLAYLQ AEGGGDRQLG DREKELIRQA 
       210        220        230        240        250
ALQQTKEMDL SVVRLMFTAF LPDSTGSFTR RLEPVVSDAI YDSKAPNASN 
       260        270        280        290        300
LKIVRMDRTA GCVTGGEEIY LLCDKVQKDD IQIRFYEEEE NGGVWEGFGD 
       310        320        330        340        350
FSPTDVHRQF AIVFKTPKYK DINITKPASV FVQLRRKSDL ETSEPKPFLY 
       360        370        380        390        400
YPEIKDKEEV QRKRQKLMPN FSDSFGGGSG AGAGGGGMFG SGGGGGGTGS 
       410        420        430        440        450
TGPGYSFPHY GFPTYGGITF HPGTTKSNAG MKHGTMDTES KKDPEGCDKS 
       460        470        480        490        500
DDKNTVNLFG KVIETTEQDQ EPSEATVGNG EVTLTYATGT KEESAGVQDN 
       510        520        530        540        550
LFLEKAMQLA KRHANALFDY AVTGDVKMLL AVQRHLTAVQ DENGDSVLHL 
       560        570        580        590        600
AIIHLHSQLV RDLLEVTSGL ISDDIINMRN DLYQTPLHLA VITKQEDVVE 
       610        620        630        640        650
DLLRAGADLS LLDRLGNSVL HLAAKEGHDK VLSILLKHKK AALLLDHPNG 
       660        670        680        690        700
DGLNAIHLAM MSNSLPCLLL LVAAGADVNA QEQKSGRTAL HLAVEHDNIS 
       710        720        730        740        750
LAGCLLLEGD AHVDSTTYDG TTPLHIAAGR GSTRLAALLK AAGADPLVEN 
       760        770        780        790        800
FEPLYDLDDS WENAGEDEGV VPGTTPLDMA TSWQVFDILN GKPYEPEFTS 
       810        820        830        840        850
DDLLAQGDMK QLAEDVKLQL YKLLEIPDPD KNWATLAQKL GLGILNNAFR 
       860        870        880        890        900
LSPAPSKTLM DNYEVSGGTV RELVEALRQM GYTEAIEVIQ AASSPVKTTS 
       910        920        930        940        950
QAHSLPLSPA STRQQIDELR DSDSVCDSGV ETSFRKLSFT ESLTSGASLL 
       960 
TLNKMPHDYG QEGPLEGKI

Show »

Length:969

Mass (Da):105,427

Checksum:ⁱB4D57AC8A410941D

GO

Isoform 3 (identifier: P19838-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-180: Missing.
181-189: EGGGDRQLG → MNGLCCMAL

« Hide

        10         20         30         40         50
MNGLCCMALD REKELIRQAA LQQTKEMDLS VVRLMFTAFL PDSTGSFTRR 
        60         70         80         90        100
LEPVVSDAIY DSKAPNASNL KIVRMDRTAG CVTGGEEIYL LCDKVQKDDI 
       110        120        130        140        150
QIRFYEEEEN GGVWEGFGDF SPTDVHRQFA IVFKTPKYKD INITKPASVF 
       160        170        180        190        200
VQLRRKSDLE TSEPKPFLYY PEIKDKEEVQ RKRQKLMPNF SDSFGGGSGA 
       210        220        230        240        250
GAGGGGMFGS GGGGGGTGST GPGYSFPHYG FPTYGGITFH PGTTKSNAGM 
       260        270        280        290        300
KHGTMDTESK KDPEGCDKSD DKNTVNLFGK VIETTEQDQE PSEATVGNGE 
       310        320        330        340        350
VTLTYATGTK EESAGVQDNL FLEKAMQLAK RHANALFDYA VTGDVKMLLA 
       360        370        380        390        400
VQRHLTAVQD ENGDSVLHLA IIHLHSQLVR DLLEVTSGLI SDDIINMRND 
       410        420        430        440        450
LYQTPLHLAV ITKQEDVVED LLRAGADLSL LDRLGNSVLH LAAKEGHDKV 
       460        470        480        490        500
LSILLKHKKA ALLLDHPNGD GLNAIHLAMM SNSLPCLLLL VAAGADVNAQ 
       510        520        530        540        550
EQKSGRTALH LAVEHDNISL AGCLLLEGDA HVDSTTYDGT TPLHIAAGRG 
       560        570        580        590        600
STRLAALLKA AGADPLVENF EPLYDLDDSW ENAGEDEGVV PGTTPLDMAT 
       610        620        630        640        650
SWQVFDILNG KPYEPEFTSD DLLAQGDMKQ LAEDVKLQLY KLLEIPDPDK 
       660        670        680        690        700
NWATLAQKLG LGILNNAFRL SPAPSKTLMD NYEVSGGTVR ELVEALRQMG 
       710        720        730        740        750
YTEAIEVIQA ASSPVKTTSQ AHSLPLSPAS TRQQIDELRD SDSVCDSGVE 
       760        770        780 
TSFRKLSFTE SLTSGASLLT LNKMPHDYGQ EGPLEGKI

Show »

Length:788

Mass (Da):85,520

Checksum:ⁱ7B9913B97F25DD3F

GO

Computationally mapped potential isoform sequencesⁱ

There are 6 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

A0A494C1E9	A0A494C1E9_HUMAN	Nuclear factor NF-kappa-B p105 subu... Nuclear factor NF-kappa-B p105 subunit	NFKB1	511	Annotation score:
D6RF93	D6RF93_HUMAN	Nuclear factor NF-kappa-B p105 subu... Nuclear factor NF-kappa-B p105 subunit	NFKB1	196	Annotation score:
D6RH30	D6RH30_HUMAN	Nuclear factor NF-kappa-B p105 subu... Nuclear factor NF-kappa-B p105 subunit	NFKB1	198	Annotation score:
D6RC45	D6RC45_HUMAN	Nuclear factor NF-kappa-B p105 subu... Nuclear factor NF-kappa-B p105 subunit	NFKB1	144	Annotation score:
D6RDI9	D6RDI9_HUMAN	Nuclear factor NF-kappa-B p105 subu... Nuclear factor NF-kappa-B p105 subunit	NFKB1	74	Annotation score:
A0A494C157	A0A494C157_HUMAN	Nuclear factor NF-kappa-B p105 subu... Nuclear factor NF-kappa-B p105 subunit	NFKB1	253	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	243	K → SE in CAB94757 (PubMed:8825636).Curated	1
Sequence conflictⁱ	361	R → G in CAH18336 (PubMed:17974005).Curated	1
Sequence conflictⁱ	551 – 552	II → SS in CAB94757 (PubMed:8825636).Curated	2
Sequence conflictⁱ	573	D → G in BAF84139 (PubMed:14702039).Curated	1
Sequence conflictⁱ	726	A → V in CAB94757 (PubMed:8825636).Curated	1
Sequence conflictⁱ	825	I → T in CAH18336 (PubMed:17974005).Curated	1
Sequence conflictⁱ	869	V → I in CAB94757 (PubMed:8825636).Curated	1
Sequence conflictⁱ	927	S → T in AAA36361 (PubMed:2203531).Curated	1
Sequence conflictⁱ	927	S → T in AAA36360 (PubMed:1992489).Curated	1
Sequence conflictⁱ	927	S → T in CAB94757 (PubMed:8825636).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_016268	489	T → I1 PublicationCorresponds to variant dbSNP:rs4648065Ensembl.	1
Natural variantⁱVAR_016269	506	M → V1 PublicationCorresponds to variant dbSNP:rs4648072Ensembl.	1
Natural variantⁱVAR_016270	566	T → I1 PublicationCorresponds to variant dbSNP:rs4648085Ensembl.	1
Natural variantⁱVAR_016271	578	R → K1 PublicationCorresponds to variant dbSNP:rs4648086Ensembl.	1
Natural variantⁱVAR_016272	711	H → Q1 PublicationCorresponds to variant dbSNP:rs4648099Ensembl.	1
Natural variantⁱVAR_016273	901	A → T1 PublicationCorresponds to variant dbSNP:rs4648118Ensembl.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_042869	1 – 180	Missing in isoform 3. 1 PublicationAdd BLAST	180
Alternative sequenceⁱVSP_021025	39	T → TA in isoform 2. 3 Publications	1
Alternative sequenceⁱVSP_042870	181 – 189	EGGGDRQLG → MNGLCCMAL in isoform 3. 1 Publication	9

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M55643 mRNA Translation: AAA36361.1 M58603 mRNA Translation: AAA36360.1 Z47748 Z47744 Genomic DNA Translation: CAB94757.1 AF213884 Genomic DNA Translation: AAF35232.1 AK122850 mRNA Translation: BAG53760.1 AK291450 mRNA Translation: BAF84139.1 CR749522 mRNA Translation: CAH18336.1 AY223820 Genomic DNA Translation: AAO30127.1 BC033210 mRNA Translation: AAH33210.1 BC051765 mRNA Translation: AAH51765.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS3657.1 [P19838-2] CCDS54783.1 [P19838-1]
PIRⁱ	A37867
NCBI Reference Sequences More...RefSeqⁱ	NP_001158884.1, NM_001165412.1 [P19838-1] NP_001306155.1, NM_001319226.1 [P19838-1] NP_003989.2, NM_003998.3 [P19838-2]

Genome annotation databases

Ensemblⁱ	ENST00000226574; ENSP00000226574; ENSG00000109320 [P19838-2] ENST00000394820; ENSP00000378297; ENSG00000109320 [P19838-1] ENST00000505458; ENSP00000424790; ENSG00000109320 [P19838-1] ENST00000600343; ENSP00000469340; ENSG00000109320 [P19838-3]
GeneIDⁱ	4790
KEGGⁱ	hsa:4790
UCSC genome browser More...UCSCⁱ	uc011cep.2, human [P19838-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P19838	Nuclear factor NF-kappa-B p105 subunit		PANTR		968	UniRef100_P19838
Nuclear factor NF-kappa-B p105 subunit (Fragment)		HUMAN		74
NFKB1 isoform 12 (Fragment)		PONAB		74
NFKB1 isoform 3 (Fragment)		PANTR		74
+2
P19838-2	Nuclear factor NF-kappa-B p105 subunit		PANTR		969	UniRef100_H2QPY8
Nuclear factor NF-kappa-B p105 subunit		GORGO		969
Nuclear factor NF-kappa-B p105 subunit		PANTR		969
NFKB1 isoform 4 (Fragment)		PANTR		506
NFKB1 isoform 6 (Fragment)		PANTR		498
+2
P19838-3	Nuclear factor NF-kappa-B p105 subunit		PANTR		788	UniRef100_A0A2J8MAY9

Protein	Similar proteins		Species	Score	Length	Source
P19838	Nuclear factor NF-kappa-B p105 subunit		PANTR		968	UniRef90_P19838
Nuclear factor NF-kappa-B p105 subunit (Fragment)		HUMAN		74
NFKB1 isoform 12 (Fragment)		PONAB		74
Nuclear factor NF-kappa-B p105 subunit		MACMU		977
Nuclear factor NF-kappa-B p105 subunit		PAPAN		977
+93
P19838-3	Nuclear factor NF-kappa-B p105 subunit		PANTR		788	UniRef90_A0A2J8MAY9
Nuclear factor NF-kappa-B p105 subunit		PONAB		788

Protein	Similar proteins		Species	Score	Length	Source
P19838	Nuclear factor NF-kappa-B p105 subunit		CANLF		972	UniRef50_P19838
Nuclear factor NF-kappa-B p105 subunit		CHICK		983
Nuclear factor NF-kappa-B p105 subunit	)	MOUSE		971
Nuclear factor NF-kappa-B p105 subunit		PANTR		968
Nuclear factor NF-kappa-B p105 subunit (Fragment)		HUMAN		74
+549
P19838-3	Isoform 2 of Nuclear factor NF-kappa-B p105 subunit		MOUSE		781	UniRef50_P25799-2
Uncharacterized protein (Fragment)		BAMTH		689
Nuclear factor kappa B subunit 1		URSAM		707
Nuclear factor NF-kappa-B p105 subunit		PANTR		788
Nuclear factor NF-kappa-B p105 subunit		PONAB		788
+10

Cross-referencesⁱ

Web resourcesⁱ

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M55643 mRNA Translation: AAA36361.1 M58603 mRNA Translation: AAA36360.1 Z47748 Z47744 Genomic DNA Translation: CAB94757.1 AF213884 Genomic DNA Translation: AAF35232.1 AK122850 mRNA Translation: BAG53760.1 AK291450 mRNA Translation: BAF84139.1 CR749522 mRNA Translation: CAH18336.1 AY223820 Genomic DNA Translation: AAO30127.1 BC033210 mRNA Translation: AAH33210.1 BC051765 mRNA Translation: AAH51765.1
CCDSⁱ	CCDS3657.1 [P19838-2] CCDS54783.1 [P19838-1]
PIRⁱ	A37867
RefSeqⁱ	NP_001158884.1, NM_001165412.1 [P19838-1] NP_001306155.1, NM_001319226.1 [P19838-1] NP_003989.2, NM_003998.3 [P19838-2]

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1MDI	NMR	-	B	55-67	[»]
	1MDJ	NMR	-	B	55-67	[»]
	1MDK	NMR	-	B	55-67	[»]
	1NFI	X-ray	2.70	B/D	248-354	[»]
	1SVC	X-ray	2.60	P	2-365	[»]
	2DBF	NMR	-	A	806-893	[»]
	2O61	X-ray	2.80	B	40-352	[»]
	3GUT	X-ray	3.59	B/D/F/H	41-352	[»]
SMRⁱ	P19838
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGRIDⁱ	110857, 201 interactors
ComplexPortalⁱ	CPX-5828, NF-kappaB DNA-binding transcription factor complex, p50/p65 CPX-5832, NF-kappaB DNA-binding transcription factor complex, p50/c-Rel CPX-5833, NF-kappaB DNA-binding transcription factor complex, p50/RelB CPX-5837, NF-kappaB transcription regulation complex complex, p50/p52 CPX-5838, NF-kappaB transcription regulation complex, p50/p50
CORUMⁱ	P19838
DIPⁱ	DIP-106N
ELMⁱ	P19838
IntActⁱ	P19838, 489 interactors
MINTⁱ	P19838
STRINGⁱ	9606.ENSP00000226574

Chemistry databases

BindingDBⁱ	P19838
ChEMBLⁱ	CHEMBL3251
DrugBankⁱ	DB05767, Andrographolide DB05487, Custirsen DB00843, Donepezil DB13961, Fish oil DB13751, Glycyrrhizic acid DB05212, HE3286 DB05559, NF-kappaB Decoy DB05464, NOX-700 DB05451, P54 DB01411, Pranlukast DB00852, Pseudoephedrine DB14059, SC-236 DB05471, SGN-30 DB01041, Thalidomide DB08814, Triflusal
DrugCentralⁱ	P19838

PTM databases

iPTMnetⁱ	P19838
MetOSiteⁱ	P19838
PhosphoSitePlusⁱ	P19838

Polymorphism and mutation databases

BioMutaⁱ	NFKB1
DMDMⁱ	21542418

Proteomic databases

CPTACⁱ	CPTAC-1260 CPTAC-1330
EPDⁱ	P19838
jPOSTⁱ	P19838
MassIVEⁱ	P19838
MaxQBⁱ	P19838
PaxDbⁱ	P19838
PeptideAtlasⁱ	P19838
PRIDEⁱ	P19838
ProteomicsDBⁱ	53694 [P19838-1] 53695 [P19838-2] 53696 [P19838-3]

Protocols and materials databases

Antibodypediaⁱ	3415, 2305 antibodies
The DNASU plasmid repository More...DNASUⁱ	4790

Genome annotation databases

Ensemblⁱ	ENST00000226574; ENSP00000226574; ENSG00000109320 [P19838-2] ENST00000394820; ENSP00000378297; ENSG00000109320 [P19838-1] ENST00000505458; ENSP00000424790; ENSG00000109320 [P19838-1] ENST00000600343; ENSP00000469340; ENSG00000109320 [P19838-3]
GeneIDⁱ	4790
KEGGⁱ	hsa:4790
UCSCⁱ	uc011cep.2, human [P19838-1]

Organism-specific databases

CTDⁱ	4790
DisGeNETⁱ	4790
EuPathDBⁱ	HostDB:ENSG00000109320.11
GeneCardsⁱ	NFKB1
HGNCⁱ	HGNC:7794, NFKB1
HPAⁱ	ENSG00000109320, Low tissue specificity
MalaCardsⁱ	NFKB1
MIMⁱ	164011, gene 616576, phenotype
neXtProtⁱ	NX_P19838
OpenTargetsⁱ	ENSG00000109320
Orphanetⁱ	1572, Common variable immunodeficiency
PharmGKBⁱ	PA248
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0504, Eukaryota
GeneTreeⁱ	ENSGT00940000158625
HOGENOMⁱ	CLU_004343_1_0_1
InParanoidⁱ	P19838
OMAⁱ	CAIHLAV
OrthoDBⁱ	916931at2759
PhylomeDBⁱ	P19838
TreeFamⁱ	TF325632

Enzyme and pathway databases

PathwayCommonsⁱ	P19838
Reactomeⁱ	R-HSA-1169091, Activation of NF-kappaB in B cells R-HSA-1810476, RIP-mediated NFkB activation via ZBP1 R-HSA-193692, Regulated proteolysis of p75NTR R-HSA-202424, Downstream TCR signaling R-HSA-209560, NF-kB is activated and signals survival R-HSA-2559582, Senescence-Associated Secretory Phenotype (SASP) R-HSA-2871837, FCERI mediated NF-kB activation R-HSA-3134963, DEx/H-box helicases activate type I IFN and inflammatory cytokines production R-HSA-3214841, PKMTs methylate histone lysines R-HSA-381340, Transcriptional regulation of white adipocyte differentiation R-HSA-445989, TAK1 activates NFkB by phosphorylation and activation of IKKs complex R-HSA-448706, Interleukin-1 processing R-HSA-5603029, IkBA variant leads to EDA-ID R-HSA-5607764, CLEC7A (Dectin-1) signaling R-HSA-5621575, CD209 (DC-SIGN) signaling R-HSA-5660668, CLEC7A/inflammasome pathway R-HSA-5684264, MAP3K8 (TPL2)-dependent MAPK1/3 activation R-HSA-6798695, Neutrophil degranulation R-HSA-844456, The NLRP3 inflammasome R-HSA-8853884, Transcriptional Regulation by VENTX R-HSA-9020702, Interleukin-1 signaling R-HSA-933542, TRAF6 mediated NF-kB activation R-HSA-9609690, HCMV Early Events R-HSA-9660826, Purinergic signaling in leishmaniasis infection
SignaLinkⁱ	P19838
SIGNORⁱ	P19838

Miscellaneous databases

BioGRID-ORCSⁱ	4790, 13 hits in 872 CRISPR screens
ChiTaRSⁱ	NFKB1, human
EvolutionaryTraceⁱ	P19838
GeneWikiⁱ	NFKB1
GenomeRNAiⁱ	4790
Pharosⁱ	P19838, Tchem
Protein Ontology More...PROⁱ	PR:P19838
RNActⁱ	P19838, protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000109320, Expressed in bone marrow and 212 other tissues
ExpressionAtlasⁱ	P19838, baseline and differential
Genevisibleⁱ	P19838, HS

Family and domain databases

CDDⁱ	cd01177, IPT_NFkappaB, 1 hit
Gene3Dⁱ	1.25.40.20, 1 hit 2.60.40.10, 1 hit 2.60.40.340, 1 hit
InterProⁱ	View protein in InterPro IPR002110, Ankyrin_rpt IPR020683, Ankyrin_rpt-contain_dom IPR036770, Ankyrin_rpt-contain_sf IPR011029, DEATH-like_dom_sf IPR000488, Death_domain IPR013783, Ig-like_fold IPR014756, Ig_E-set IPR002909, IPT_dom IPR033926, IPT_NFkappaB IPR030503, NF-kB_p105 IPR000451, NFkB/Dor IPR008967, p53-like_TF_DNA-bd IPR030492, RHD_CS IPR032397, RHD_dimer IPR011539, RHD_DNA_bind_dom IPR037059, RHD_DNA_bind_dom_sf
PANTHERⁱ	PTHR24169, PTHR24169, 1 hit PTHR24169:SF9, PTHR24169:SF9, 1 hit
Pfamⁱ	View protein in Pfam PF12796, Ank_2, 2 hits PF00531, Death, 1 hit PF16179, RHD_dimer, 1 hit PF00554, RHD_DNA_bind, 1 hit
PRINTSⁱ	PR01415, ANKYRIN PR00057, NFKBTNSCPFCT
SMARTⁱ	View protein in SMART SM00248, ANK, 6 hits SM00005, DEATH, 1 hit SM00429, IPT, 1 hit
SUPFAMⁱ	SSF47986, SSF47986, 1 hit SSF48403, SSF48403, 1 hit SSF49417, SSF49417, 1 hit SSF81296, SSF81296, 1 hit
PROSITEⁱ	View protein in PROSITE PS50297, ANK_REP_REGION, 1 hit PS50088, ANK_REPEAT, 5 hits PS01204, REL_1, 1 hit PS50254, REL_2, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	NFKB1_HUMAN
Accessionⁱ	P19838Primary (citable) accession number: P19838 Secondary accession number(s): A8K5Y5 , B3KVE8, Q68D84, Q86V43, Q8N4X7, Q9NZC0
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
	Last sequence update:	June 20, 2002
	Last modified:	December 2, 2020
	This is version 253 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Direct protein sequencing, Reference proteome

Documents

Human chromosome 4
Human chromosome 4: entries, gene names and cross-references to MIM
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations

Annotation systems

Supporting data

UniProtKB - P19838 (NFKB1_HUMAN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the 'basket' to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Nuclear factor NF-kappa-B p105 subunit

Select a section on the left to see content.

<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

<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

Enzyme and pathway databases

<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

Organism-specific databases

<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

Nucleus

Other locations

Cytosol

Extracellular region or secreted

Mitochondrion

Nucleus

Other locations

Keywords - Cellular componenti

<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

Mutagenesis

Organism-specific databases

Miscellaneous databases

Chemistry databases

Polymorphism and mutation databases

<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

Amino acid modifications

Sites

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<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

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

Miscellaneous databases

<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

Secondary structure

3D structure databases

Miscellaneous databases

<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

Region

Motif

Compositional bias

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ