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P25799 (NFKB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Nuclear factor NF-kappa-B p50 subunit
Gene names
Name:Nfkb1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length971 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.13 Ref.14 Ref.15 Ref.16

Subcellular location

Nucleus Ref.2 Ref.11. Cytoplasm Ref.2 Ref.11. Note: Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B). Ref.2 Ref.11

Isoform 5: Cytoplasm Ref.2 Ref.11.

Isoform 6: Nucleus Ref.2 Ref.11. Cytoplasm Ref.2 Ref.11.

Isoform 7: Nucleus Ref.2 Ref.11.

Induction

By phorbol ester and TNF-alpha.

Domain

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.

Post-translational modification

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.

Sequence similarities

Contains 7 ANK repeats.

Contains 1 death domain.

Contains 1 RHD (Rel-like) domain.

Sequence caution

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

Ontologies

Keywords
   Biological processApoptosis
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainANK repeat
Repeat
   LigandDNA-binding
   Molecular functionActivator
   PTMAcetylation
Hydroxylation
Lipoprotein
Phosphoprotein
S-nitrosylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to interleukin-1

Inferred from electronic annotation. Source: Ensembl

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

lymph node development

Traceable author statement PubMed 10687308. Source: MGI

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of calcidiol 1-monooxygenase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of cytokine production

Inferred from mutant phenotype PubMed 18566389. Source: BHF-UCL

negative regulation of inflammatory response

Inferred from mutant phenotype PubMed 18270204. Source: MGI

negative regulation of interleukin-12 biosynthetic process

Inferred from direct assay PubMed 14568984. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 14568984. Source: MGI

positive regulation of canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of hyaluronan biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 16081776PubMed 19666510. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

response to bacterium

Inferred from electronic annotation. Source: Ensembl

response to copper ion

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

signal transduction

Inferred from electronic annotation. Source: InterPro

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Inferred from direct assay Ref.14. Source: MGI

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 10395695Ref.14PubMed 12970181PubMed 15220916PubMed 15728238PubMed 15817708PubMed 19404405PubMed 19734906PubMed 21982707. Source: MGI

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Inferred from direct assay PubMed 10395695PubMed 11976687PubMed 12618484PubMed 15845452PubMed 15944286PubMed 16081776PubMed 19734906. Source: MGI

double-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

nucleic acid binding transcription factor activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 15220916. Source: MGI

regulatory region DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

sequence-specific DNA binding

Inferred from direct assay PubMed 19404405. Source: MGI

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: InterPro

transcription regulatory region sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P25799-1)

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.
Isoform 2 (identifier: P25799-2)

Also known as: p84;

The sequence of this isoform differs from the canonical sequence as follows:
     780-971: VFDILNGKPY...GQEGPIEGKI → GT
Isoform 3 (identifier: P25799-3)

Also known as: p98;

The sequence of this isoform differs from the canonical sequence as follows:
     860-971: VSGGTIKELM...GQEGPIEGKI → MNSGIVTASVTVVWRHPSANSALQSLLLETAHCYL
Isoform 4 (identifier: P25799-4)

The sequence of this isoform differs from the canonical sequence as follows:
     353-356: DKEE → GTWV
     357-971: Missing.
Isoform 5 (identifier: P25799-5)

Also known as: P70; I-kappa-B gamma;

The sequence of this isoform differs from the canonical sequence as follows:
     1-364: Missing.
Isoform 6 (identifier: P25799-6)

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
Isoform 7 (identifier: P25799-7)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 971971Nuclear factor NF-kappa-B p105 subunit
PRO_0000030312
Chain1 – 431431Nuclear factor NF-kappa-B p50 subunit By similarity
PRO_0000030313

Regions

Domain40 – 365326RHD
Repeat538 – 56730ANK 1
Repeat577 – 60630ANK 2
Repeat610 – 63930ANK 3
Repeat646 – 67530ANK 4
Repeat680 – 71031ANK 5
Repeat714 – 74330ANK 6
Repeat767 – 79731ANK 7
Domain801 – 88888Death
Region370 – 39223GRR
Region433 – 971539Interaction with CFLAR By similarity
Region646 – 68035Essential for interaction with HIF1AN By similarity
Motif358 – 3636Nuclear localization signal Potential
Compositional bias373 – 43159Gly-rich

Sites

Site431 – 4322Cleavage (when cotranslationally processed) By similarity

Amino acid modifications

Modified residue591S-nitrosocysteine; alternate By similarity
Modified residue3351Phosphoserine; by PKA Potential
Modified residue4381N6-acetyllysine; by EP300 By similarity
Modified residue6741(3S)-3-hydroxyasparagine; by HIF1AN By similarity
Modified residue9101Phosphoserine; by GSK3-beta; in vitro By similarity
Modified residue9301Phosphoserine; by IKKB By similarity
Modified residue9351Phosphoserine; by IKKB By similarity
Modified residue9401Phosphoserine By similarity
Lipidation591S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternate By similarity

Natural variations

Alternative sequence1 – 364364Missing in isoform 5, isoform 6 and isoform 7.
VSP_017236
Alternative sequence353 – 3564DKEE → GTWV in isoform 4.
VSP_017237
Alternative sequence357 – 971615Missing in isoform 4.
VSP_017238
Alternative sequence780 – 971192VFDIL…IEGKI → GT in isoform 2 and isoform 7.
VSP_005583
Alternative sequence860 – 971112VSGGT…IEGKI → MNSGIVTASVTVVWRHPSAN SALQSLLLETAHCYL in isoform 3 and isoform 6.
VSP_005584

Experimental info

Sequence conflict1111L → P in AAR00341. Ref.9
Sequence conflict2651E → G in BAC35117. Ref.10
Sequence conflict5301H → D in BAE34261. Ref.10
Sequence conflict5461A → G in BAE34261. Ref.10
Sequence conflict6841A → P in AAA40415. Ref.1
Sequence conflict6841A → P in AAB21851. Ref.2
Sequence conflict6841A → P in AAB28573. Ref.3
Sequence conflict7321A → T in BAE34261. Ref.10
Sequence conflict9501P → A in BAE43399. Ref.10

Secondary structure

........................................................................... 971
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (p105) [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 91EA9C595E375C30

FASTA971105,615
        10         20         30         40         50         60 
MADDDPYGTG QMFHLNTALT HSIFNAELYS PEIPLSTDGP YLQILEQPKQ RGFRFRYVCE 

        70         80         90        100        110        120 
GPSHGGLPGA SSEKNKKSYP QVKICNYVGP AKVIVQLVTN GKNIHLHAHS LVGKHCEDGV 

       130        140        150        160        170        180 
CTVTAGPKDM VVGFANLGIL HVTKKKVFET LEARMTEACI RGYNPGLLVH SDLAYLQAEG 

       190        200        210        220        230        240 
GGDRQLTDRE KEIIRQAAVQ QTKEMDLSVV RLMFTAFLPD STGSFTRRLE PVVSDAIYDS 

       250        260        270        280        290        300 
KAPNASNLKI VRMDRTAGCV TGGEEIYLLC DKVQKDDIQI RFYEEEENGG VWEGFGDFSP 

       310        320        330        340        350        360 
TDVHRQFAIV FKTPKYKDVN ITKPASVFVQ LRRKSDLETS EPKPFLYYPE IKDKEEVQRK 

       370        380        390        400        410        420 
RQKLMPNFSD SFGGGSGAGA GGGGMFGSGG GGGSTGSPGP GYGYSNYGFP PYGGITFHPG 

       430        440        450        460        470        480 
VTKSNAGVTH GTINTKFKNG PKDCAKSDDE ESLTLPEKET EGEGPSLPMA CTKTEPIALA 

       490        500        510        520        530        540 
STMEDKEQDM GFQDNLFLEK ALQLARRHAN ALFDYAVTGD VKMLLAVQRH LTAVQDENGD 

       550        560        570        580        590        600 
SVLHLAIIHL HAQLVRDLLE VTSGLISDDI INMRNDLYQT PLHLAVITKQ EDVVEDLLRV 

       610        620        630        640        650        660 
GADLSLLDRW GNSVLHLAAK EGHDRILSIL LKSRKAAPLI DHPNGEGLNA IHIAVMSNSL 

       670        680        690        700        710        720 
PCLLLLVAAG AEVNAQEQKS GRTALHLAVE YDNISLAGCL LLEGDAHVDS TTYDGTTPLH 

       730        740        750        760        770        780 
IAAGRGSTRL AALLKAAGAD PLVENFEPLY DLDDSWEKAG EDEGVVPGTT PLDMAANWQV 

       790        800        810        820        830        840 
FDILNGKPYE PVFTSDDILP QGDMKQLTED TRLQLCKLLE IPDPDKNWAT LAQKLGLGIL 

       850        860        870        880        890        900 
NNAFRLSPAP SKTLMDNYEV SGGTIKELME ALQQMGYTEA IEVIQAAFRT PATTASSPVT 

       910        920        930        940        950        960 
TAQVHCLPLS SSSTRQHIDE LRDSDSVCDS GVETSFRKLS FTESLTGDSP LLSLNKMPHG 

       970 
YGQEGPIEGK I 

« Hide

Isoform 2 (p84) [UniParc].

Checksum: 51B98D66F21BF5EC
Show »

FASTA78184,817
Isoform 3 (p98) [UniParc].

Checksum: 8445F5C4CA02D7E4
Show »

FASTA89497,413
Isoform 4 [UniParc].

Checksum: 09E32E7A3B63F46A
Show »

FASTA35639,756
Isoform 5 (P70) (I-kappa-B gamma) [UniParc].

Checksum: 1B79975F022DF4E2
Show »

FASTA60764,782
Isoform 6 (p63) (I-kappa-B gamma-1) [UniParc].

Checksum: C7384490B44048FC
Show »

FASTA53056,580
Isoform 7 (p55) (I-kappa-B gamma-2) [UniParc].

Checksum: DEA2D2B56CDDC6D3
Show »

FASTA41743,983

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA35697.
RefSeqNP_032715.2. NM_008689.2.
XP_006501169.1. XM_006501106.1.
UniGeneMm.256765.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP25799.
SMRP25799. Positions 39-350, 460-786, 802-885.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201751. 13 interactions.
DIPDIP-85N.
IntActP25799. 9 interactions.
MINTMINT-236136.

Chemistry

ChEMBLCHEMBL1949489.

PTM databases

PhosphoSiteP25799.

Proteomic databases

PaxDbP25799.
PRIDEP25799.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029812; ENSMUSP00000029812; ENSMUSG00000028163. [P25799-1]
ENSMUST00000164430; ENSMUSP00000128345; ENSMUSG00000028163. [P25799-1]
GeneID18033.
KEGGmmu:18033.
UCSCuc008rlw.1. mouse. [P25799-1]
uc008rly.1. mouse. [P25799-4]
uc012cyf.1. mouse. [P25799-6]

Organism-specific databases

CTD4790.
MGIMGI:97312. Nfkb1.

Phylogenomic databases

eggNOGCOG0666.
GeneTreeENSGT00500000044765.
HOVERGENHBG052613.
InParanoidB2RRQ6.
KOK02580.
OMAPGYGFPH.
OrthoDBEOG7W154S.
TreeFamTF325632.

Gene expression databases

BgeeP25799.
GenevestigatorP25799.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
1.25.40.20. 1 hit.
2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProIPR002110. 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]
PfamPF00023. Ank. 2 hits.
PF12796. Ank_2. 1 hit.
PF00531. Death. 1 hit.
PF00554. RHD. 1 hit.
[Graphical view]
PRINTSPR00057. NFKBTNSCPFCT.
SMARTSM00248. ANK. 6 hits.
SM00005. DEATH. 1 hit.
SM00429. IPT. 1 hit.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNFKB1. mouse.
EvolutionaryTraceP25799.
NextBio293121.
PROP25799.
SOURCESearch...

Entry information

Entry nameNFKB1_MOUSE
AccessionPrimary (citable) accession number: P25799
Secondary accession number(s): B2RRQ6 expand/collapse secondary AC list , Q3TZE8, Q3V2V6, Q6TDG8, Q75ZL1, Q80Y21, Q8C712
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot