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Protein

Nuclear factor NF-kappa-B p105 subunit

Gene

Nfkb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-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-2559582. Senescence-Associated Secretory Phenotype (SASP).
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-933542. TRAF6 mediated NF-kB activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear factor NF-kappa-B p105 subunit
Alternative 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:97312. Nfkb1.

Subcellular locationi

  • Nucleus
  • Cytoplasm

  • Note: Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B).

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • I-kappaB/NF-kappaB complex Source: GO_Central
  • mitochondrion Source: MGI
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1949489.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000303121 – 971Nuclear factor NF-kappa-B p105 subunitAdd BLAST971
ChainiPRO_00000303131 – 431Nuclear factor NF-kappa-B p50 subunitBy similarityAdd BLAST431

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei59S-nitrosocysteineBy similarity1
Lipidationi59S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternateBy similarity1
Modified residuei335Phosphoserine; by PKASequence analysis1
Modified residuei438N6-acetyllysine; by EP300By similarity1
Modified residuei447PhosphoserineCombined sources1
Modified residuei674(3S)-3-hydroxyasparagine; by HIF1ANBy similarity1
Modified residuei755PhosphoserineBy similarity1
Modified residuei896PhosphoserineBy similarity1
Modified residuei910Phosphoserine; by GSK3-beta; in vitroBy similarity1
Modified residuei930Phosphoserine; by IKKBBy similarity1
Modified residuei935Phosphoserine; by IKKBBy similarity1
Modified residuei940PhosphoserineCombined sources1
Modified residuei946PhosphothreonineCombined sources1

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.
Phosphorylation at 'Ser-930' and 'Ser-935' are required for BTRC/BTRCP-mediated proteolysis.By similarity
Polyubiquitination seems to allow p105 processing.
S-nitrosylation of Cys-59 affects DNA binding.By similarity
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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei431 – 432Cleavage (when cotranslationally processed)By similarity2

Keywords - PTMi

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

Proteomic databases

EPDiP25799.
MaxQBiP25799.
PaxDbiP25799.
PeptideAtlasiP25799.
PRIDEiP25799.

PTM databases

iPTMnetiP25799.
PhosphoSitePlusiP25799.

Expressioni

Inductioni

By phorbol ester and TNF-alpha.

Gene expression databases

BgeeiENSMUSG00000028163.
ExpressionAtlasiP25799. baseline and differential.
GenevisibleiP25799. MM.

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 (By similarity). NFKB1/p50 interacts with NFKBIZ. Nuclear factor NF-kappa-B p50 subunit interacts with NFKBID. Directly interacts with MEN1 (By similarity). Interacts with HIF1AN (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Akap8Q9DBR04EBI-643958,EBI-4285802
Hdac1O091062EBI-643958,EBI-301912
NCOA1Q157882EBI-643958,EBI-455189From a different organism.
RelaQ042075EBI-643958,EBI-644400
RelbQ048632EBI-1209141,EBI-1209145

GO - Molecular functioni

Protein-protein interaction databases

BioGridi201751. 13 interactors.
DIPiDIP-85N.
IntActiP25799. 15 interactors.
MINTiMINT-236136.
STRINGi10090.ENSMUSP00000029812.

Structurei

Secondary structure

1971
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi41 – 46Combined sources6
Beta strandi50 – 52Combined sources3
Helixi58 – 60Combined sources3
Beta strandi62 – 64Combined sources3
Beta strandi74 – 76Combined sources3
Beta strandi81 – 85Combined sources5
Beta strandi92 – 98Combined sources7
Beta strandi100 – 103Combined sources4
Beta strandi108 – 113Combined sources6
Beta strandi117 – 119Combined sources3
Beta strandi120 – 124Combined sources5
Beta strandi131 – 133Combined sources3
Beta strandi138 – 140Combined sources3
Helixi144 – 146Combined sources3
Helixi147 – 160Combined sources14
Beta strandi162 – 164Combined sources3
Helixi165 – 169Combined sources5
Helixi171 – 173Combined sources3
Beta strandi179 – 182Combined sources4
Helixi188 – 203Combined sources16
Beta strandi209 – 219Combined sources11
Beta strandi221 – 223Combined sources3
Beta strandi225 – 228Combined sources4
Beta strandi232 – 239Combined sources8
Beta strandi240 – 242Combined sources3
Turni243 – 246Combined sources4
Beta strandi250 – 254Combined sources5
Beta strandi256 – 259Combined sources4
Beta strandi265 – 271Combined sources7
Turni275 – 277Combined sources3
Beta strandi279 – 284Combined sources6
Helixi287 – 289Combined sources3
Beta strandi292 – 295Combined sources4
Helixi300 – 302Combined sources3
Turni305 – 307Combined sources3
Beta strandi308 – 312Combined sources5
Beta strandi325 – 332Combined sources8
Turni334 – 336Combined sources3
Beta strandi343 – 348Combined sources6
Beta strandi351 – 354Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BFSX-ray2.20A245-350[»]
1IKNX-ray2.30C245-363[»]
1LE5X-ray2.75B/F39-350[»]
1LE9X-ray3.00B/F39-350[»]
1LEIX-ray2.70B39-350[»]
1NFKX-ray2.30A/B39-363[»]
1OOAX-ray2.45A/B39-363[»]
1U36X-ray1.89A245-350[»]
1U3JX-ray1.90A245-350[»]
1U3YX-ray1.90A245-350[»]
1U3ZX-ray1.90A245-350[»]
1U41X-ray2.20A/B/C/D245-350[»]
1U42X-ray2.70A245-350[»]
1VKXX-ray2.90B39-350[»]
2I9TX-ray2.80B39-350[»]
2V2TX-ray3.05B38-363[»]
3JV4X-ray3.15B/D/F245-359[»]
ProteinModelPortaliP25799.
SMRiP25799.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25799.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini40 – 365RHDPROSITE-ProRule annotationAdd BLAST326
Repeati538 – 567ANK 1Add BLAST30
Repeati577 – 606ANK 2Add BLAST30
Repeati610 – 639ANK 3Add BLAST30
Repeati646 – 675ANK 4Add BLAST30
Repeati680 – 710ANK 5Add BLAST31
Repeati714 – 743ANK 6Add BLAST30
Repeati767 – 797ANK 7Add BLAST31
Domaini801 – 888DeathAdd BLAST88

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni370 – 392GRRAdd BLAST23
Regioni433 – 971Interaction with CFLARBy similarityAdd BLAST539
Regioni646 – 680Essential for interaction with HIF1ANBy similarityAdd BLAST35

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi358 – 363Nuclear localization signalSequence analysis6

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi373 – 431Gly-richAdd BLAST59

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.

Sequence similaritiesi

Contains 7 ANK repeats.PROSITE-ProRule annotation
Contains 1 death domain.Curated
Contains 1 RHD (Rel-like) domain.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00500000044765.
HOVERGENiHBG052613.
InParanoidiP25799.
KOiK02580.
OMAiHEQMFHL.
OrthoDBiEOG091G03PF.
TreeFamiTF325632.

Family and domain databases

CDDicd01177. IPT_NFkappaB. 1 hit.
Gene3Di1.10.533.10. 1 hit.
1.25.40.20. 1 hit.
2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
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.
[Graphical view]
PANTHERiPTHR24169. PTHR24169. 2 hits.
PTHR24169:SF9. PTHR24169:SF9. 2 hits.
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 1 hit.
PF00531. Death. 1 hit.
PF16179. RHD_dimer. 1 hit.
PF00554. RHD_DNA_bind. 1 hit.
[Graphical view]
PRINTSiPR00057. NFKBTNSCPFCT.
SMARTiSM00248. ANK. 6 hits.
SM00005. DEATH. 1 hit.
SM00429. IPT. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view]

Sequences (7)i

Sequence statusi: Complete.

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

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P25799-1) [UniParc]FASTAAdd to basket
Also known as: p105

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

« Hide

        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
Length:971
Mass (Da):105,615
Last modified:July 27, 2011 - v2
Checksum:i91EA9C595E375C30
GO
Isoform 2 (identifier: P25799-2) [UniParc]FASTAAdd to basket
Also known as: p84

The sequence of this isoform differs from the canonical sequence as follows:
     780-971: VFDILNGKPY...GQEGPIEGKI → GT

Show »
Length:781
Mass (Da):84,817
Checksum:i51B98D66F21BF5EC
GO
Isoform 3 (identifier: P25799-3) [UniParc]FASTAAdd to basket
Also known as: p98

The sequence of this isoform differs from the canonical sequence as follows:
     860-971: VSGGTIKELM...GQEGPIEGKI → MNSGIVTASVTVVWRHPSANSALQSLLLETAHCYL

Show »
Length:894
Mass (Da):97,413
Checksum:i8445F5C4CA02D7E4
GO
Isoform 4 (identifier: P25799-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     353-356: DKEE → GTWV
     357-971: Missing.

Show »
Length:356
Mass (Da):39,756
Checksum:i09E32E7A3B63F46A
GO
Isoform 5 (identifier: P25799-5) [UniParc]FASTAAdd to basket
Also known as: P70, I-kappa-B gamma

The sequence of this isoform differs from the canonical sequence as follows:
     1-364: Missing.

Show »
Length:607
Mass (Da):64,782
Checksum:i1B79975F022DF4E2
GO
Isoform 6 (identifier: P25799-6) [UniParc]FASTAAdd to basket
Also known as: p63, I-kappa-B gamma-1

The sequence of this isoform differs from the canonical sequence as follows:
     1-364: Missing.
     860-971: VSGGTIKELM...GQEGPIEGKI → MNSGIVTASVTVVWRHPSANSALQSLLLETAHCYL

Show »
Length:530
Mass (Da):56,580
Checksum:iC7384490B44048FC
GO
Isoform 7 (identifier: P25799-7) [UniParc]FASTAAdd to basket
Also known as: p55, I-kappa-B gamma-2

The sequence of this isoform differs from the canonical sequence as follows:
     1-364: Missing.
     780-971: VFDILNGKPY...GQEGPIEGKI → GT

Note: Inhibits the activity of the p50 NF-kappa-B subunit.
Show »
Length:417
Mass (Da):43,983
Checksum:iDEA2D2B56CDDC6D3
GO

Sequence cautioni

The sequence BAC35117 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti111L → P in AAR00341 (Ref. 9) Curated1
Sequence conflicti265E → G in BAC35117 (PubMed:16141072).Curated1
Sequence conflicti530H → D in BAE34261 (PubMed:16141072).Curated1
Sequence conflicti546A → G in BAE34261 (PubMed:16141072).Curated1
Sequence conflicti684A → P in AAA40415 (PubMed:2203532).Curated1
Sequence conflicti684A → P in AAB21851 (PubMed:1339305).Curated1
Sequence conflicti684A → P in AAB28573 (PubMed:8398903).Curated1
Sequence conflicti732A → T in BAE34261 (PubMed:16141072).Curated1
Sequence conflicti950P → A in BAE43399 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0172361 – 364Missing in isoform 5, isoform 6 and isoform 7. 2 PublicationsAdd BLAST364
Alternative sequenceiVSP_017237353 – 356DKEE → GTWV in isoform 4. 2 Publications4
Alternative sequenceiVSP_017238357 – 971Missing in isoform 4. 2 PublicationsAdd BLAST615
Alternative sequenceiVSP_005583780 – 971VFDIL…IEGKI → GT in isoform 2 and isoform 7. 1 PublicationAdd BLAST192
Alternative sequenceiVSP_005584860 – 971VSGGT…IEGKI → MNSGIVTASVTVVWRHPSAN SALQSLLLETAHCYL in isoform 3 and isoform 6. 1 PublicationAdd BLAST112

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.
CCDSiCCDS17858.1. [P25799-1]
PIRiA35697.
RefSeqiNP_032715.2. NM_008689.2. [P25799-1]
XP_006501169.1. XM_006501106.2. [P25799-3]
UniGeneiMm.256765.

Genome annotation databases

EnsembliENSMUST00000029812; ENSMUSP00000029812; ENSMUSG00000028163. [P25799-1]
ENSMUST00000164430; ENSMUSP00000128345; ENSMUSG00000028163. [P25799-1]
GeneIDi18033.
KEGGimmu:18033.
UCSCiuc008rlw.1. mouse. [P25799-1]
uc008rly.1. mouse. [P25799-4]
uc012cyf.1. mouse. [P25799-6]

Keywords - Coding sequence diversityi

Alternative splicing

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.
CCDSiCCDS17858.1. [P25799-1]
PIRiA35697.
RefSeqiNP_032715.2. NM_008689.2. [P25799-1]
XP_006501169.1. XM_006501106.2. [P25799-3]
UniGeneiMm.256765.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BFSX-ray2.20A245-350[»]
1IKNX-ray2.30C245-363[»]
1LE5X-ray2.75B/F39-350[»]
1LE9X-ray3.00B/F39-350[»]
1LEIX-ray2.70B39-350[»]
1NFKX-ray2.30A/B39-363[»]
1OOAX-ray2.45A/B39-363[»]
1U36X-ray1.89A245-350[»]
1U3JX-ray1.90A245-350[»]
1U3YX-ray1.90A245-350[»]
1U3ZX-ray1.90A245-350[»]
1U41X-ray2.20A/B/C/D245-350[»]
1U42X-ray2.70A245-350[»]
1VKXX-ray2.90B39-350[»]
2I9TX-ray2.80B39-350[»]
2V2TX-ray3.05B38-363[»]
3JV4X-ray3.15B/D/F245-359[»]
ProteinModelPortaliP25799.
SMRiP25799.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201751. 13 interactors.
DIPiDIP-85N.
IntActiP25799. 15 interactors.
MINTiMINT-236136.
STRINGi10090.ENSMUSP00000029812.

Chemistry databases

ChEMBLiCHEMBL1949489.

PTM databases

iPTMnetiP25799.
PhosphoSitePlusiP25799.

Proteomic databases

EPDiP25799.
MaxQBiP25799.
PaxDbiP25799.
PeptideAtlasiP25799.
PRIDEiP25799.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029812; ENSMUSP00000029812; ENSMUSG00000028163. [P25799-1]
ENSMUST00000164430; ENSMUSP00000128345; ENSMUSG00000028163. [P25799-1]
GeneIDi18033.
KEGGimmu:18033.
UCSCiuc008rlw.1. mouse. [P25799-1]
uc008rly.1. mouse. [P25799-4]
uc012cyf.1. mouse. [P25799-6]

Organism-specific databases

CTDi4790.
MGIiMGI:97312. Nfkb1.

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00500000044765.
HOVERGENiHBG052613.
InParanoidiP25799.
KOiK02580.
OMAiHEQMFHL.
OrthoDBiEOG091G03PF.
TreeFamiTF325632.

Enzyme and pathway databases

ReactomeiR-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-2559582. Senescence-Associated Secretory Phenotype (SASP).
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-933542. TRAF6 mediated NF-kB activation.

Miscellaneous databases

ChiTaRSiNfkb1. mouse.
EvolutionaryTraceiP25799.
PROiP25799.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000028163.
ExpressionAtlasiP25799. baseline and differential.
GenevisibleiP25799. MM.

Family and domain databases

CDDicd01177. IPT_NFkappaB. 1 hit.
Gene3Di1.10.533.10. 1 hit.
1.25.40.20. 1 hit.
2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
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.
[Graphical view]
PANTHERiPTHR24169. PTHR24169. 2 hits.
PTHR24169:SF9. PTHR24169:SF9. 2 hits.
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 1 hit.
PF00531. Death. 1 hit.
PF16179. RHD_dimer. 1 hit.
PF00554. RHD_DNA_bind. 1 hit.
[Graphical view]
PRINTSiPR00057. NFKBTNSCPFCT.
SMARTiSM00248. ANK. 6 hits.
SM00005. DEATH. 1 hit.
SM00429. IPT. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNFKB1_MOUSE
AccessioniPrimary (citable) accession number: P25799
Secondary accession number(s): B2RRQ6
, Q3TZE8, Q3V2V6, Q6TDG8, Q75ZL1, Q80Y21, Q8C712
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 191 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.