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P25799

- NFKB1_MOUSE

UniProt

P25799 - NFKB1_MOUSE

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Protein

Nuclear factor NF-kappa-B p105 subunit

Gene

Nfkb1

Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei431 – 4322Cleavage (when cotranslationally processed)By similarity

GO - Molecular functioni

  1. DNA binding Source: MGI
  2. double-stranded DNA binding Source: Ensembl
  3. nucleic acid binding transcription factor activity Source: UniProtKB
  4. protein homodimerization activity Source: MGI
  5. regulatory region DNA binding Source: UniProtKB
  6. sequence-specific DNA binding Source: MGI
  7. sequence-specific DNA binding transcription factor activity Source: InterPro
  8. transcription regulatory region sequence-specific DNA binding Source: Ensembl

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cellular response to interleukin-1 Source: Ensembl
  3. cellular response to interleukin-6 Source: Ensembl
  4. cellular response to lipopolysaccharide Source: MGI
  5. cellular response to mechanical stimulus Source: Ensembl
  6. cellular response to nicotine Source: Ensembl
  7. cellular response to peptide hormone stimulus Source: Ensembl
  8. lymph node development Source: MGI
  9. negative regulation of apoptotic process Source: Ensembl
  10. negative regulation of calcidiol 1-monooxygenase activity Source: Ensembl
  11. negative regulation of cytokine production Source: BHF-UCL
  12. negative regulation of inflammatory response Source: MGI
  13. negative regulation of interleukin-12 biosynthetic process Source: MGI
  14. negative regulation of transcription, DNA-templated Source: MGI
  15. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  16. positive regulation of canonical Wnt signaling pathway Source: Ensembl
  17. positive regulation of hyaluronan biosynthetic process Source: Ensembl
  18. positive regulation of miRNA metabolic process Source: Ensembl
  19. positive regulation of transcription, DNA-templated Source: UniProtKB
  20. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  21. response to copper ion Source: Ensembl
  22. response to oxidative stress Source: Ensembl
  23. signal transduction Source: InterPro
  24. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_198700. Interleukin-1 processing.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_202898. TRAF6 mediated NF-kB activation.
REACT_205561. FCERI mediated NF-kB activation.
REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
REACT_218614. Regulated proteolysis of p75NTR.
REACT_218887. NF-kB is activated and signals survival.
REACT_219800. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_222971. RIP-mediated NFkB activation via ZBP1.
REACT_224208. Interleukin-1 signaling.
REACT_225145. Downstream TCR signaling.

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
ProteomesiUP000000589: 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

  1. cytosol Source: MGI
  2. mitochondrion Source: Ensembl
  3. nucleus Source: MGI
  4. protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 971971Nuclear factor NF-kappa-B p105 subunitPRO_0000030312Add
BLAST
Chaini1 – 431431Nuclear factor NF-kappa-B p50 subunitBy similarityPRO_0000030313Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591S-nitrosocysteine; alternateBy similarity
Lipidationi59 – 591S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternateBy similarity
Modified residuei335 – 3351Phosphoserine; by PKASequence Analysis
Modified residuei438 – 4381N6-acetyllysine; by EP300By similarity
Modified residuei674 – 6741(3S)-3-hydroxyasparagine; by HIF1ANBy similarity
Modified residuei910 – 9101Phosphoserine; by GSK3-beta; in vitroBy similarity
Modified residuei930 – 9301Phosphoserine; by IKKBBy similarity
Modified residuei935 – 9351Phosphoserine; by IKKBBy similarity
Modified residuei940 – 9401PhosphoserineBy similarity

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

Keywords - PTMi

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

Proteomic databases

MaxQBiP25799.
PaxDbiP25799.
PRIDEiP25799.

PTM databases

PhosphoSiteiP25799.

Expressioni

Inductioni

By phorbol ester and TNF-alpha.

Gene expression databases

BgeeiP25799.
GenevestigatoriP25799.

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
Hdac1O091062EBI-643958,EBI-301912
NCOA1Q157882EBI-643958,EBI-455189From a different organism.
RelaQ042075EBI-643958,EBI-644400
RelbQ048632EBI-1209141,EBI-1209145

Protein-protein interaction databases

BioGridi201751. 13 interactions.
DIPiDIP-85N.
IntActiP25799. 9 interactions.
MINTiMINT-236136.

Structurei

Secondary structure

1
971
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi41 – 466
Beta strandi50 – 523
Helixi58 – 603
Beta strandi62 – 643
Beta strandi74 – 763
Beta strandi81 – 855
Beta strandi92 – 987
Beta strandi100 – 1034
Beta strandi108 – 1136
Beta strandi117 – 1193
Beta strandi120 – 1245
Beta strandi131 – 1333
Beta strandi138 – 1403
Helixi144 – 1463
Helixi147 – 16014
Beta strandi162 – 1643
Helixi165 – 1695
Helixi171 – 1733
Beta strandi179 – 1824
Helixi188 – 20316
Beta strandi209 – 21911
Beta strandi221 – 2233
Beta strandi225 – 2284
Beta strandi232 – 2398
Beta strandi240 – 2423
Turni243 – 2464
Beta strandi250 – 2545
Beta strandi256 – 2594
Beta strandi265 – 2717
Turni275 – 2773
Beta strandi279 – 2846
Helixi287 – 2893
Beta strandi292 – 2954
Helixi300 – 3023
Turni305 – 3073
Beta strandi308 – 3125
Beta strandi325 – 3328
Turni334 – 3363
Beta strandi343 – 3486
Beta strandi351 – 3544

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 39-350, 460-786, 802-885.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25799.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 365326RHDPROSITE-ProRule annotationAdd
BLAST
Repeati538 – 56730ANK 1Add
BLAST
Repeati577 – 60630ANK 2Add
BLAST
Repeati610 – 63930ANK 3Add
BLAST
Repeati646 – 67530ANK 4Add
BLAST
Repeati680 – 71031ANK 5Add
BLAST
Repeati714 – 74330ANK 6Add
BLAST
Repeati767 – 79731ANK 7Add
BLAST
Domaini801 – 88888DeathAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni370 – 39223GRRAdd
BLAST
Regioni433 – 971539Interaction with CFLARBy similarityAdd
BLAST
Regioni646 – 68035Essential for interaction with HIF1ANBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi358 – 3636Nuclear localization signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi373 – 43159Gly-richAdd
BLAST

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

eggNOGiCOG0666.
GeneTreeiENSGT00500000044765.
HOVERGENiHBG052613.
InParanoidiP25799.
KOiK02580.
OMAiPGYGFPH.
OrthoDBiEOG7W154S.
TreeFamiTF325632.

Family and domain databases

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.
IPR000451. NF_Rel_Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view]
PfamiPF00023. Ank. 2 hits.
PF12796. Ank_2. 1 hit.
PF00531. Death. 1 hit.
PF00554. RHD. 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. Align

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 BAC35117.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 1111L → P in AAR00341. 1 PublicationCurated
Sequence conflicti265 – 2651E → G in BAC35117. (PubMed:16141072)Curated
Sequence conflicti530 – 5301H → D in BAE34261. (PubMed:16141072)Curated
Sequence conflicti546 – 5461A → G in BAE34261. (PubMed:16141072)Curated
Sequence conflicti684 – 6841A → P in AAA40415. (PubMed:2203532)Curated
Sequence conflicti684 – 6841A → P in AAB21851. (PubMed:1339305)Curated
Sequence conflicti684 – 6841A → P in AAB28573. (PubMed:8398903)Curated
Sequence conflicti732 – 7321A → T in BAE34261. (PubMed:16141072)Curated
Sequence conflicti950 – 9501P → A in BAE43399. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 364364Missing in isoform 5, isoform 6 and isoform 7. 2 PublicationsVSP_017236Add
BLAST
Alternative sequencei353 – 3564DKEE → GTWV in isoform 4. 2 PublicationsVSP_017237
Alternative sequencei357 – 971615Missing in isoform 4. 2 PublicationsVSP_017238Add
BLAST
Alternative sequencei780 – 971192VFDIL…IEGKI → GT in isoform 2 and isoform 7. 1 PublicationVSP_005583Add
BLAST
Alternative sequencei860 – 971112VSGGT…IEGKI → MNSGIVTASVTVVWRHPSAN SALQSLLLETAHCYL in isoform 3 and isoform 6. 1 PublicationVSP_005584Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006501106.1. [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:
EMBL
GenBank
DDBJ
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_006501106.1. [P25799-3 ]
UniGenei Mm.256765.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P25799.
SMRi P25799. Positions 39-350, 460-786, 802-885.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 201751. 13 interactions.
DIPi DIP-85N.
IntActi P25799. 9 interactions.
MINTi MINT-236136.

Chemistry

ChEMBLi CHEMBL1949489.

PTM databases

PhosphoSitei P25799.

Proteomic databases

MaxQBi P25799.
PaxDbi P25799.
PRIDEi P25799.

Protocols and materials databases

Structural Biology Knowledgebase Search...

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.

Phylogenomic databases

eggNOGi COG0666.
GeneTreei ENSGT00500000044765.
HOVERGENi HBG052613.
InParanoidi P25799.
KOi K02580.
OMAi PGYGFPH.
OrthoDBi EOG7W154S.
TreeFami TF325632.

Enzyme and pathway databases

Reactomei REACT_198700. Interleukin-1 processing.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_202898. TRAF6 mediated NF-kB activation.
REACT_205561. FCERI mediated NF-kB activation.
REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
REACT_218614. Regulated proteolysis of p75NTR.
REACT_218887. NF-kB is activated and signals survival.
REACT_219800. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_222971. RIP-mediated NFkB activation via ZBP1.
REACT_224208. Interleukin-1 signaling.
REACT_225145. Downstream TCR signaling.

Miscellaneous databases

ChiTaRSi NFKB1. mouse.
EvolutionaryTracei P25799.
NextBioi 293121.
PROi P25799.
SOURCEi Search...

Gene expression databases

Bgeei P25799.
Genevestigatori P25799.

Family and domain databases

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 IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR000451. NF_Rel_Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view ]
Pfami PF00023. Ank. 2 hits.
PF12796. Ank_2. 1 hit.
PF00531. Death. 1 hit.
PF00554. RHD. 1 hit.
[Graphical view ]
PRINTSi PR00057. NFKBTNSCPFCT.
SMARTi SM00248. ANK. 6 hits.
SM00005. DEATH. 1 hit.
SM00429. IPT. 1 hit.
[Graphical view ]
SUPFAMi SSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the p50 DNA binding subunit of NF-kappa B: homology to rel and dorsal."
    Ghosh S., Gifford A.M., Riviere L.R., Tempst P., Nolan G.P., Baltimore D.
    Cell 62:1019-1029(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Lung and Spleen.
  2. "I kappa B gamma, a 70 kd protein identical to the C-terminal half of p110 NF-kappa B: a new member of the I kappa B family."
    Inoue J., Kerr L.D., Kakizuka A., Verma I.M.
    Cell 68:1109-1120(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), SUBCELLULAR LOCATION.
  3. "The activity of a 70 kilodalton I kappa B molecule identical to the carboxyl terminus of the p105 NF-kappa B precursor is modulated by protein kinase A."
    Gerondakis S., Morrice N., Richardson I.B., Wettenhall R., Fecondo J., Grumont R.J.
    Cell Growth Differ. 4:617-627(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), PARTIAL PROTEIN SEQUENCE.
  4. "Alternate RNA splicing of murine nfkb1 generates a nuclear isoform of the p50 precursor NF-kappa B1 that can function as a transactivator of NF-kappa B-regulated transcription."
    Grumont R.J., Fecondo J., Gerondakis S.
    Mol. Cell. Biol. 14:8460-8470(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
  5. "Mus musculus transcription factor NF-kappa-B DNA binding subunit(p105) mRNA, complete cds."
    Ohara O., Kitamura H., Nakagawa T.
    Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6CrSlc.
    Tissue: Spleen.
  6. Bleich A., Hedrich H.J., Schlegelberger B., Maehler M.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C3H/HeJBir and C57BL/6J.
  7. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
    Tissue: Brain and Embryo.
  9. Gerhauser I., Ulrich R., Baumgartner W.
    Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 54-129.
    Strain: C57BL/6.
    Tissue: Lung carcinoma.
  10. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-971 (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 376-971 (ISOFORM 1).
    Strain: C57BL/6J and NOD.
    Tissue: Inner ear, Kidney and Spleen.
  11. "Alternative splicing of RNA transcripts encoded by the murine p105 NF-kappa B gene generates I kappa B gamma isoforms with different inhibitory activities."
    Grumont R.J., Gerondakis S.
    Proc. Natl. Acad. Sci. U.S.A. 91:4367-4371(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORMS 6 AND 7), SUBCELLULAR LOCATION.
  12. "Cotranslational biogenesis of NF-kappaB p50 by the 26S proteasome."
    Lin L., DeMartino G.N., Greene W.C.
    Cell 92:819-828(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: COTRANSLATIONAL FOLDING OF P105.
  13. "A novel IkappaB protein, IkappaB-zeta, induced by proinflammatory stimuli, negatively regulates nuclear factor-kappaB in the nuclei."
    Yamazaki S., Muta T., Takeshige K.
    J. Biol. Chem. 276:27657-27662(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NFKBIZ.
  14. "Peptide-induced negative selection of thymocytes activates transcription of an NF-kappa B inhibitor."
    Fiorini E., Schmitz I., Marissen W.E., Osborn S.L., Touma M., Sasada T., Reche P.A., Tibaldi E.V., Hussey R.E., Kruisbeek A.M., Reinherz E.L., Clayton L.K.
    Mol. Cell 9:637-648(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NFKBID.
  15. "A defect in nucleosome remodeling prevents IL-12(p35) gene transcription in neonatal dendritic cells."
    Goriely S., Van Lint C., Dadkhah R., Libin M., De Wit D., Demonte D., Willems F., Goldman M.
    J. Exp. Med. 199:1011-1016(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NF-KAPPA-B P65-P50 COMPLEX.
  16. "Regulation of Toll/IL-1-receptor-mediated gene expression by the inducible nuclear protein IkappaBzeta."
    Yamamoto M., Yamazaki S., Uematsu S., Sato S., Hemmi H., Hoshino K., Kaisho T., Kuwata H., Takeuchi O., Takeshige K., Saitoh T., Yamaoka S., Yamamoto N., Yamamoto S., Muta T., Takeda K., Akira S.
    Nature 430:218-222(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NFKBIZ.
  17. "Structure of NF-kappa B p50 homodimer bound to a kappa B site."
    Ghosh G., van Duyne G., Ghosh S., Sigler P.B.
    Nature 373:303-310(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 39-364.
  18. "The role of DNA in the mechanism of NFkappaB dimer formation: crystal structures of the dimerization domains of the p50 and p65 subunits."
    Huang D.B., Huxford T., Chen Y.Q., Ghosh G.
    Structure 5:1427-1436(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 245-350.
  19. "The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation."
    Huxford T., Huang D.B., Malek S., Ghosh G.
    Cell 95:759-770(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 245-363.
  20. "Crystal structure of p50/p65 heterodimer of transcription factor NF-kappaB bound to DNA."
    Chen F.E., Huang D.B., Chen Y.Q., Ghosh G.
    Nature 391:410-413(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 39-350.
  21. "The X-ray crystal structure of the NF-kappa B p50.p65 heterodimer bound to the interferon beta -kappa B site."
    Berkowitz B., Huang D.B., Chen-Park F.E., Sigler P.B., Ghosh G.
    J. Biol. Chem. 277:24694-24700(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 39-350.
  22. "The kappa B DNA sequence from the HIV long terminal repeat functions as an allosteric regulator of HIV transcription."
    Chen-Park F.E., Huang D.B., Noro B., Thanos D., Ghosh G.
    J. Biol. Chem. 277:24701-24708(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 39-350.
  23. "Crystal structure of NF-kappaB (p50)2 complexed to a high-affinity RNA aptamer."
    Huang D.B., Vu D., Cassiday L.A., Zimmerman J.M., Maher L.J. III, Ghosh G.
    Proc. Natl. Acad. Sci. U.S.A. 100:9268-9273(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 38-351 HOMODIMER COMPLEXED WITH RNA APTAMER.
  24. "X-ray structure of a NF-kappaB p50/RelB/DNA complex reveals assembly of multiple dimers on tandem kappaB sites."
    Moorthy A.K., Huang D.B., Wang V.Y., Vu D., Ghosh G.
    J. Mol. Biol. 373:723-734(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 91-378 IN COMPLEX WITH RELB.

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: October 29, 2014
This is version 168 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

External Data

Dasty 3