UniProtKB - P25799 (NFKB1_MOUSE)
Nuclear factor NF-kappa-B p105 subunit
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. Plays a role in the regulation of apoptosis. Isoform 5, isoform 6 and isoform 7 act as inhibitors of transactivation of p50 NF-kappa-B subunit, probably by sequestering it in the cytoplasm. Isoform 3 (p98) (but not p84 or p105) acts as a transactivator of NF-kappa-B-regulated gene expression. In a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is released by proteasome-dependent degradation of NFKB1/p105.
1 PublicationGO - Molecular functioni
- actinin binding Source: MGI
- chromatin binding Source: MGI
- DNA binding Source: MGI
- DNA-binding transcription activator activity, RNA polymerase II-specific Source: MGI
- DNA-binding transcription factor activity Source: UniProtKB
- DNA-binding transcription factor activity, RNA polymerase II-specific Source: MGI
- DNA-binding transcription repressor activity, RNA polymerase II-specific Source: MGI
- double-stranded DNA binding Source: MGI
- enzyme binding Source: MGI
- heat shock protein binding Source: MGI
- identical protein binding Source: MGI
- protein-containing complex binding Source: MGI
- RNA polymerase II cis-regulatory region sequence-specific DNA binding Source: MGI
- RNA polymerase II transcription regulatory region sequence-specific DNA binding Source: MGI
- sequence-specific DNA binding Source: MGI
- transcription cis-regulatory region binding Source: UniProtKB
- transcription coactivator binding Source: MGI
GO - Biological processi
- apoptotic process Source: UniProtKB-KW
- cellular response to angiotensin Source: MGI
- cellular response to brain-derived neurotrophic factor stimulus Source: MGI
- cellular response to carbohydrate stimulus Source: MGI
- cellular response to cytokine stimulus Source: MGI
- cellular response to diterpene Source: MGI
- cellular response to dsRNA Source: MGI
- cellular response to glucoside Source: MGI
- cellular response to interleukin-1 Source: MGI
- cellular response to interleukin-6 Source: MGI
- cellular response to lipopolysaccharide Source: MGI
- cellular response to mechanical stimulus Source: Ensembl
- cellular response to nicotine Source: MGI
- cellular response to organic cyclic compound Source: MGI
- cellular response to peptide Source: MGI
- cellular response to tumor necrosis factor Source: MGI
- cellular response to virus Source: MGI
- JNK cascade Source: MGI
- lymph node development Source: MGI
- MAPK cascade Source: MGI
- negative regulation of apoptotic process Source: MGI
- negative regulation of calcidiol 1-monooxygenase activity Source: MGI
- negative regulation of cytokine production Source: BHF-UCL
- negative regulation of gene expression Source: MGI
- negative regulation of inflammatory response Source: MGI
- negative regulation of interleukin-12 production Source: MGI
- negative regulation of transcription, DNA-templated Source: MGI
- negative regulation of transcription by RNA polymerase II Source: UniProtKB
- positive regulation of canonical Wnt signaling pathway Source: MGI
- positive regulation of gene expression Source: MGI
- positive regulation of gene silencing by miRNA Source: MGI
- positive regulation of hyaluronan biosynthetic process Source: MGI
- positive regulation of miRNA metabolic process Source: MGI
- positive regulation of miRNA transcription Source: MGI
- positive regulation of transcription, DNA-templated Source: UniProtKB
- positive regulation of transcription by RNA polymerase II Source: MGI
- regulation of transcription by RNA polymerase II Source: GO_Central
- response to muscle stretch Source: MGI
- response to organic cyclic compound Source: MGI
- response to oxidative stress Source: MGI
Keywordsi
Molecular function | Activator, DNA-binding |
Biological process | Apoptosis, Transcription, Transcription regulation |
Enzyme and pathway databases
Reactomei | R-MMU-1169091, Activation of NF-kappaB in B cells R-MMU-1810476, RIP-mediated NFkB activation via ZBP1 R-MMU-193692, Regulated proteolysis of p75NTR R-MMU-202424, Downstream TCR signaling R-MMU-209560, NF-kB is activated and signals survival R-MMU-2871837, FCERI mediated NF-kB activation R-MMU-3134963, DEx/H-box helicases activate type I IFN and inflammatory cytokines production R-MMU-3214841, PKMTs methylate histone lysines R-MMU-445989, TAK1 activates NFkB by phosphorylation and activation of IKKs complex R-MMU-448706, Interleukin-1 processing R-MMU-5607764, CLEC7A (Dectin-1) signaling R-MMU-5621575, CD209 (DC-SIGN) signaling R-MMU-5684264, MAP3K8 (TPL2)-dependent MAPK1/3 activation R-MMU-6798695, Neutrophil degranulation R-MMU-9020702, Interleukin-1 signaling R-MMU-933542, TRAF6 mediated NF-kB activation |
Names & Taxonomyi
Protein namesi | Recommended name: Nuclear factor NF-kappa-B p105 subunitAlternative name(s): DNA-binding factor KBF1 EBP-1 NF-kappa-B1 p84/NF-kappa-B1 p98 Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 Cleaved into the following chain: |
Gene namesi | Name:Nfkb1 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:97312, Nfkb1 |
VEuPathDBi | HostDB:ENSMUSG00000028163 |
Subcellular locationi
Cytoplasm and Cytosol
Nucleus
Cytosol
- cytosol Source: MGI
Mitochondrion
- mitochondrion Source: MGI
Nucleus
- NF-kappaB complex Source: MGI
- nucleoplasm Source: MGI
- nucleus Source: MGI
Other locations
- cytoplasm Source: MGI
- neuron projection Source: MGI
- protein-containing complex Source: MGI
Keywords - Cellular componenti
Cytoplasm, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000030312 | 1 – 971 | Nuclear factor NF-kappa-B p105 subunitAdd BLAST | 971 | |
ChainiPRO_0000030313 | 1 – 431 | Nuclear factor NF-kappa-B p50 subunitBy similarityAdd BLAST | 431 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 59 | S-nitrosocysteine; alternateBy similarity | 1 | |
Lipidationi | 59 | S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternateBy similarity | 1 | |
Cross-linki | 323 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 335 | Phosphoserine; by PKASequence analysis | 1 | |
Modified residuei | 438 | N6-acetyllysine; by EP300By similarity | 1 | |
Modified residuei | 447 | PhosphoserineCombined sources | 1 | |
Modified residuei | 674 | (3S)-3-hydroxyasparagine; by HIF1ANBy similarity | 1 | |
Modified residuei | 755 | PhosphoserineBy similarity | 1 | |
Modified residuei | 896 | PhosphoserineBy similarity | 1 | |
Modified residuei | 910 | Phosphoserine; by GSK3-beta; in vitroBy similarity | 1 | |
Modified residuei | 930 | Phosphoserine; by IKKBBy similarity | 1 | |
Modified residuei | 935 | Phosphoserine; by IKKBBy similarity | 1 | |
Modified residuei | 940 | PhosphoserineCombined sources | 1 | |
Modified residuei | 946 | PhosphothreonineCombined sources | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 431 – 432 | Cleavage (when cotranslationally processed)By similarity | 2 |
Keywords - PTMi
Acetylation, Hydroxylation, Isopeptide bond, Lipoprotein, Phosphoprotein, S-nitrosylation, Ubl conjugationProteomic databases
EPDi | P25799 |
jPOSTi | P25799 |
MaxQBi | P25799 |
PaxDbi | P25799 |
PeptideAtlasi | P25799 |
PRIDEi | P25799 |
ProteomicsDBi | 287411 [P25799-1] 287412 [P25799-2] 287413 [P25799-3] 287414 [P25799-4] 287415 [P25799-5] 287416 [P25799-6] 287417 [P25799-7] |
PTM databases
iPTMneti | P25799 |
PhosphoSitePlusi | P25799 |
Expressioni
Inductioni
Gene expression databases
Bgeei | ENSMUSG00000028163, Expressed in spleen and 311 other tissues |
Genevisiblei | P25799, MM |
Interactioni
Subunit structurei
Component of the NF-kappa-B p65-p50 complex (By similarity). Homodimer; component of the NF-kappa-B p50-p50 complex (By similarity).
Component of the NF-kappa-B p105-p50 complex (By similarity).
Component of the NF-kappa-B p50-c-Rel complex (By similarity).
Component of a complex consisting of the NF-kappa-B p50-p50 homodimer and BCL3 (By similarity).
Also interacts with MAP3K8 (By similarity). NF-kappa-B p50 subunit interacts with NCOA3 coactivator, which may coactivate NF-kappa-B dependent expression via its histone acetyltransferase activity (By similarity).
Interacts with DSIPI; this interaction prevents nuclear translocation and DNA-binding (By similarity).
Interacts with SPAG9 and UNC5CL (By similarity). NFKB1/p105 interacts with CFLAR; the interaction inhibits p105 processing into p50 (By similarity). NFKB1/p105 forms a ternary complex with MAP3K8 and TNIP2 (By similarity).
Interacts with GSK3B; the interaction prevents processing of p105 to p50 (By similarity). NFKB1/p50 interacts with NFKBIE (By similarity). NFKB1/p50 interacts with NFKBIZ (PubMed:11356851, PubMed:15241416). Nuclear factor NF-kappa-B p50 subunit interacts with NFKBID (PubMed:11931770). Directly interacts with MEN1 (By similarity).
Interacts with HIF1AN (By similarity).
Interacts with FEM1AA; interaction is direct (PubMed:18270204).
By similarity4 PublicationsBinary interactionsi
P25799
With | #Exp. | IntAct |
---|---|---|
Akap8 [Q9DBR0] | 4 | EBI-643958,EBI-4285802 |
Hdac1 [O09106] | 2 | EBI-643958,EBI-301912 |
Rela [Q04207] | 6 | EBI-643958,EBI-644400 |
NCOA1 [Q15788] from Homo sapiens. | 2 | EBI-643958,EBI-455189 |
Isoform 1 [P25799-1]
With | #Exp. | IntAct |
---|---|---|
Rela [Q04207] | 6 | EBI-643974,EBI-644400 |
Nuclear factor NF-kappa-B p105 subunit (PRO_0000030312)
With | #Exp. | IntAct |
---|---|---|
Rela [Q04207] | 3 | EBI-1209193,EBI-644400 |
Nuclear factor NF-kappa-B p50 subunit (PRO_0000030313)
With | #Exp. | IntAct |
---|---|---|
Ankrd42 [Q3V096] | 3 | EBI-1209141,EBI-15861272 |
Relb [Q04863] | 2 | EBI-1209141,EBI-1209145 |
GO - Molecular functioni
- actinin binding Source: MGI
- enzyme binding Source: MGI
- heat shock protein binding Source: MGI
- identical protein binding Source: MGI
- transcription coactivator binding Source: MGI
Protein-protein interaction databases
BioGRIDi | 201751, 15 interactors |
CORUMi | P25799 |
DIPi | DIP-85N |
IntActi | P25799, 24 interactors |
MINTi | P25799 |
STRINGi | 10090.ENSMUSP00000029812 |
Miscellaneous databases
RNActi | P25799, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P25799 |
SMRi | P25799 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P25799 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 40 – 365 | RHDPROSITE-ProRule annotationAdd BLAST | 326 | |
Repeati | 538 – 567 | ANK 1Add BLAST | 30 | |
Repeati | 577 – 606 | ANK 2Add BLAST | 30 | |
Repeati | 610 – 639 | ANK 3Add BLAST | 30 | |
Repeati | 646 – 675 | ANK 4Add BLAST | 30 | |
Repeati | 680 – 710 | ANK 5Add BLAST | 31 | |
Repeati | 714 – 743 | ANK 6Add BLAST | 30 | |
Repeati | 767 – 797 | ANK 7Add BLAST | 31 | |
Domaini | 801 – 888 | DeathAdd BLAST | 88 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 370 – 392 | GRRAdd BLAST | 23 | |
Regioni | 433 – 971 | Interaction with CFLARBy similarityAdd BLAST | 539 | |
Regioni | 439 – 470 | DisorderedSequence analysisAdd BLAST | 32 | |
Regioni | 646 – 680 | Essential for interaction with HIF1ANBy similarityAdd BLAST | 35 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 358 – 363 | Nuclear localization signalSequence analysis | 6 |
Domaini
Keywords - Domaini
ANK repeat, RepeatPhylogenomic databases
eggNOGi | KOG0504, Eukaryota |
GeneTreei | ENSGT00940000158625 |
HOGENOMi | CLU_004343_1_0_1 |
InParanoidi | P25799 |
OMAi | MTWIPRK |
OrthoDBi | 916931at2759 |
PhylomeDBi | P25799 |
TreeFami | TF325632 |
Family and domain databases
CDDi | cd01177, IPT_NFkappaB, 1 hit |
Gene3Di | 1.10.533.10, 1 hit 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 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 PF00023, Ank, 1 hit PF12796, Ank_2, 2 hits PF00531, Death, 1 hit PF16179, RHD_dimer, 1 hit PF00554, RHD_DNA_bind, 1 hit |
PRINTSi | 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 |
s (7+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 7 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 7 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MADDDPYGTG QMFHLNTALT HSIFNAELYS PEIPLSTDGP YLQILEQPKQ
60 70 80 90 100
RGFRFRYVCE GPSHGGLPGA SSEKNKKSYP QVKICNYVGP AKVIVQLVTN
110 120 130 140 150
GKNIHLHAHS LVGKHCEDGV CTVTAGPKDM VVGFANLGIL HVTKKKVFET
160 170 180 190 200
LEARMTEACI RGYNPGLLVH SDLAYLQAEG GGDRQLTDRE KEIIRQAAVQ
210 220 230 240 250
QTKEMDLSVV RLMFTAFLPD STGSFTRRLE PVVSDAIYDS KAPNASNLKI
260 270 280 290 300
VRMDRTAGCV TGGEEIYLLC DKVQKDDIQI RFYEEEENGG VWEGFGDFSP
310 320 330 340 350
TDVHRQFAIV FKTPKYKDVN ITKPASVFVQ LRRKSDLETS EPKPFLYYPE
360 370 380 390 400
IKDKEEVQRK RQKLMPNFSD SFGGGSGAGA GGGGMFGSGG GGGSTGSPGP
410 420 430 440 450
GYGYSNYGFP PYGGITFHPG VTKSNAGVTH GTINTKFKNG PKDCAKSDDE
460 470 480 490 500
ESLTLPEKET EGEGPSLPMA CTKTEPIALA STMEDKEQDM GFQDNLFLEK
510 520 530 540 550
ALQLARRHAN ALFDYAVTGD VKMLLAVQRH LTAVQDENGD SVLHLAIIHL
560 570 580 590 600
HAQLVRDLLE VTSGLISDDI INMRNDLYQT PLHLAVITKQ EDVVEDLLRV
610 620 630 640 650
GADLSLLDRW GNSVLHLAAK EGHDRILSIL LKSRKAAPLI DHPNGEGLNA
660 670 680 690 700
IHIAVMSNSL PCLLLLVAAG AEVNAQEQKS GRTALHLAVE YDNISLAGCL
710 720 730 740 750
LLEGDAHVDS TTYDGTTPLH IAAGRGSTRL AALLKAAGAD PLVENFEPLY
760 770 780 790 800
DLDDSWEKAG EDEGVVPGTT PLDMAANWQV FDILNGKPYE PVFTSDDILP
810 820 830 840 850
QGDMKQLTED TRLQLCKLLE IPDPDKNWAT LAQKLGLGIL NNAFRLSPAP
860 870 880 890 900
SKTLMDNYEV SGGTIKELME ALQQMGYTEA IEVIQAAFRT PATTASSPVT
910 920 930 940 950
TAQVHCLPLS SSSTRQHIDE LRDSDSVCDS GVETSFRKLS FTESLTGDSP
960 970
LLSLNKMPHG YGQEGPIEGK I
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketF6Z9G5 | F6Z9G5_MOUSE | Nuclear factor NF-kappa-B p105 subu... | Nfkb1 | 534 | Annotation score: | ||
V9GX90 | V9GX90_MOUSE | Nuclear factor NF-kappa-B p105 subu... | Nfkb1 | 270 | Annotation score: | ||
A0A0G2JGK6 | A0A0G2JGK6_MOUSE | Nuclear factor NF-kappa-B p105 subu... | Nfkb1 | 128 | Annotation score: |
Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 111 | L → P in AAR00341 (Ref. 9) Curated | 1 | |
Sequence conflicti | 265 | E → G in BAC35117 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 530 | H → D in BAE34261 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 546 | A → G in BAE34261 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 684 | A → P in AAA40415 (PubMed:2203532).Curated | 1 | |
Sequence conflicti | 684 | A → P in AAB21851 (PubMed:1339305).Curated | 1 | |
Sequence conflicti | 684 | A → P in AAB28573 (PubMed:8398903).Curated | 1 | |
Sequence conflicti | 732 | A → T in BAE34261 (PubMed:16141072).Curated | 1 | |
Sequence conflicti | 950 | P → A in BAE43399 (PubMed:16141072).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_017236 | 1 – 364 | Missing in isoform 5, isoform 6 and isoform 7. 2 PublicationsAdd BLAST | 364 | |
Alternative sequenceiVSP_017237 | 353 – 356 | DKEE → GTWV in isoform 4. 2 Publications | 4 | |
Alternative sequenceiVSP_017238 | 357 – 971 | Missing in isoform 4. 2 PublicationsAdd BLAST | 615 | |
Alternative sequenceiVSP_005583 | 780 – 971 | VFDIL…IEGKI → GT in isoform 2 and isoform 7. 1 PublicationAdd BLAST | 192 | |
Alternative sequenceiVSP_005584 | 860 – 971 | VSGGT…IEGKI → MNSGIVTASVTVVWRHPSAN SALQSLLLETAHCYL in isoform 3 and isoform 6. 1 PublicationAdd BLAST | 112 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M57999 mRNA Translation: AAA40415.1 S89033 mRNA Translation: AAB21851.1 S66656 mRNA Translation: AAB28573.1 AB119195 mRNA Translation: BAC84979.1 AY521462 mRNA Translation: AAS00547.1 AY521463 mRNA Translation: AAS00548.1 CH466532 Genomic DNA Translation: EDL12143.1 BC050841 mRNA Translation: AAH50841.1 BC138535 mRNA Translation: AAI38536.1 BC138536 mRNA Translation: AAI38537.1 AY423849 mRNA Translation: AAR00341.1 AK052726 mRNA Translation: BAC35117.1 Different initiation. AK089660 mRNA Translation: BAE43399.1 AK157915 mRNA Translation: BAE34261.1 |
CCDSi | CCDS17858.1 [P25799-1] |
PIRi | A35697 |
RefSeqi | NP_032715.2, NM_008689.2 [P25799-1] XP_006501169.1, XM_006501106.2 [P25799-3] |
Genome annotation databases
Ensembli | ENSMUST00000029812; ENSMUSP00000029812; ENSMUSG00000028163 [P25799-1] ENSMUST00000164430; ENSMUSP00000128345; ENSMUSG00000028163 [P25799-1] |
GeneIDi | 18033 |
KEGGi | mmu:18033 |
UCSCi | uc008rlw.1, mouse [P25799-1] uc008rly.1, mouse [P25799-4] uc012cyf.1, mouse [P25799-6] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M57999 mRNA Translation: AAA40415.1 S89033 mRNA Translation: AAB21851.1 S66656 mRNA Translation: AAB28573.1 AB119195 mRNA Translation: BAC84979.1 AY521462 mRNA Translation: AAS00547.1 AY521463 mRNA Translation: AAS00548.1 CH466532 Genomic DNA Translation: EDL12143.1 BC050841 mRNA Translation: AAH50841.1 BC138535 mRNA Translation: AAI38536.1 BC138536 mRNA Translation: AAI38537.1 AY423849 mRNA Translation: AAR00341.1 AK052726 mRNA Translation: BAC35117.1 Different initiation. AK089660 mRNA Translation: BAE43399.1 AK157915 mRNA Translation: BAE34261.1 |
CCDSi | CCDS17858.1 [P25799-1] |
PIRi | A35697 |
RefSeqi | NP_032715.2, NM_008689.2 [P25799-1] XP_006501169.1, XM_006501106.2 [P25799-3] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1BFS | X-ray | 2.20 | A | 245-350 | [»] | |
1IKN | X-ray | 2.30 | C | 245-363 | [»] | |
1LE5 | X-ray | 2.75 | B/F | 39-350 | [»] | |
1LE9 | X-ray | 3.00 | B/F | 39-350 | [»] | |
1LEI | X-ray | 2.70 | B | 39-350 | [»] | |
1NFK | X-ray | 2.30 | A/B | 39-363 | [»] | |
1OOA | X-ray | 2.45 | A/B | 39-363 | [»] | |
1U36 | X-ray | 1.89 | A | 245-350 | [»] | |
1U3J | X-ray | 1.90 | A | 245-350 | [»] | |
1U3Y | X-ray | 1.90 | A | 245-350 | [»] | |
1U3Z | X-ray | 1.90 | A | 245-350 | [»] | |
1U41 | X-ray | 2.20 | A/B/C/D | 245-350 | [»] | |
1U42 | X-ray | 2.70 | A | 245-350 | [»] | |
1VKX | X-ray | 2.90 | B | 39-350 | [»] | |
2I9T | X-ray | 2.80 | B | 39-350 | [»] | |
2V2T | X-ray | 3.05 | B | 38-363 | [»] | |
3JV4 | X-ray | 3.15 | B/D/F | 245-359 | [»] | |
AlphaFoldDBi | P25799 | |||||
SMRi | P25799 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 201751, 15 interactors |
CORUMi | P25799 |
DIPi | DIP-85N |
IntActi | P25799, 24 interactors |
MINTi | P25799 |
STRINGi | 10090.ENSMUSP00000029812 |
Chemistry databases
ChEMBLi | CHEMBL1949489 |
PTM databases
iPTMneti | P25799 |
PhosphoSitePlusi | P25799 |
Proteomic databases
EPDi | P25799 |
jPOSTi | P25799 |
MaxQBi | P25799 |
PaxDbi | P25799 |
PeptideAtlasi | P25799 |
PRIDEi | P25799 |
ProteomicsDBi | 287411 [P25799-1] 287412 [P25799-2] 287413 [P25799-3] 287414 [P25799-4] 287415 [P25799-5] 287416 [P25799-6] 287417 [P25799-7] |
Protocols and materials databases
ABCDi | P25799, 1 sequenced antibody |
Antibodypediai | 3415, 2416 antibodies from 51 providers |
DNASUi | 18033 |
Genome annotation databases
Ensembli | ENSMUST00000029812; ENSMUSP00000029812; ENSMUSG00000028163 [P25799-1] ENSMUST00000164430; ENSMUSP00000128345; ENSMUSG00000028163 [P25799-1] |
GeneIDi | 18033 |
KEGGi | mmu:18033 |
UCSCi | uc008rlw.1, mouse [P25799-1] uc008rly.1, mouse [P25799-4] uc012cyf.1, mouse [P25799-6] |
Organism-specific databases
CTDi | 4790 |
MGIi | MGI:97312, Nfkb1 |
VEuPathDBi | HostDB:ENSMUSG00000028163 |
Phylogenomic databases
eggNOGi | KOG0504, Eukaryota |
GeneTreei | ENSGT00940000158625 |
HOGENOMi | CLU_004343_1_0_1 |
InParanoidi | P25799 |
OMAi | MTWIPRK |
OrthoDBi | 916931at2759 |
PhylomeDBi | P25799 |
TreeFami | TF325632 |
Enzyme and pathway databases
Reactomei | R-MMU-1169091, Activation of NF-kappaB in B cells R-MMU-1810476, RIP-mediated NFkB activation via ZBP1 R-MMU-193692, Regulated proteolysis of p75NTR R-MMU-202424, Downstream TCR signaling R-MMU-209560, NF-kB is activated and signals survival R-MMU-2871837, FCERI mediated NF-kB activation R-MMU-3134963, DEx/H-box helicases activate type I IFN and inflammatory cytokines production R-MMU-3214841, PKMTs methylate histone lysines R-MMU-445989, TAK1 activates NFkB by phosphorylation and activation of IKKs complex R-MMU-448706, Interleukin-1 processing R-MMU-5607764, CLEC7A (Dectin-1) signaling R-MMU-5621575, CD209 (DC-SIGN) signaling R-MMU-5684264, MAP3K8 (TPL2)-dependent MAPK1/3 activation R-MMU-6798695, Neutrophil degranulation R-MMU-9020702, Interleukin-1 signaling R-MMU-933542, TRAF6 mediated NF-kB activation |
Miscellaneous databases
BioGRID-ORCSi | 18033, 4 hits in 79 CRISPR screens |
ChiTaRSi | Nfkb1, mouse |
EvolutionaryTracei | P25799 |
PROi | PR:P25799 |
RNActi | P25799, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000028163, Expressed in spleen and 311 other tissues |
Genevisiblei | P25799, MM |
Family and domain databases
CDDi | cd01177, IPT_NFkappaB, 1 hit |
Gene3Di | 1.10.533.10, 1 hit 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 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 PF00023, Ank, 1 hit PF12796, Ank_2, 2 hits PF00531, Death, 1 hit PF16179, RHD_dimer, 1 hit PF00554, RHD_DNA_bind, 1 hit |
PRINTSi | 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 |
MobiDBi | Search... |
Entry informationi
Entry namei | NFKB1_MOUSE | |
Accessioni | P25799Primary (citable) accession number: P25799 Secondary accession number(s): B2RRQ6 Q8C712 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 1, 1992 |
Last sequence update: | July 27, 2011 | |
Last modified: | May 25, 2022 | |
This is version 229 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references