Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Transcription factor p65 (Nuclear factor NF-kappa-B p65 subunit) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3)

 TF65_MOUSE              Reviewed;         549 AA.
Q04207; Q62025;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
27-SEP-2017, entry version 192.
RecName: Full=Transcription factor p65;
AltName: Full=Nuclear factor NF-kappa-B p65 subunit;
AltName: Full=Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3;
Name=Rela; Synonyms=Nfkb3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P65).
PubMed=2001591; DOI=10.1016/0092-8674(91)90320-X;
Nolan G.P., Ghosh S., Liou H.C., Tempst P., Baltimore D.;
"DNA binding and I kappa B inhibition of the cloned p65 subunit of NF-
kappa B, a rel-related polypeptide.";
Cell 64:961-969(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P65).
STRAIN=C57BL/6J; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-114.
STRAIN=BALB/cJ;
PubMed=8918242; DOI=10.1016/0378-1119(96)00231-4;
Linker R.A., Baeuerle P.A., Kaltschmidt C.;
"Cloning of the murine relA (p65 NF-kappa B) gene and comparison to
the human gene reveals a distinct first intron.";
Gene 176:119-124(1996).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 188-252, AND ALTERNATIVE
SPLICING.
STRAIN=BALB/cJ;
PubMed=8281153; DOI=10.1093/hmg/2.11.1895;
Deloukas P., van Loon A.P.G.M.;
"Genomic organization of the gene encoding the p65 subunit of NF-kappa
B: multiple variants of the p65 protein may be generated by
alternative splicing.";
Hum. Mol. Genet. 2:1895-1900(1993).
[5]
INTERACTION WITH NFKBIB.
PubMed=8816457; DOI=10.1128/MCB.16.10.5444;
Suyang H., Phillips R.J., Douglas I., Ghosh S.;
"Role of unphosphorylated, newly synthesized IkappaB beta in
persistent activation of NF-kappaB.";
Mol. Cell. Biol. 16:5444-5449(1996).
[6]
INTERACTION WITH NFKBIA.
PubMed=9990853; DOI=10.1101/gad.13.3.284;
Spencer E., Jiang J., Chen Z.J.;
"Signal-induced ubiquitination of IkappaBalpha by the F-box protein
Slimb/beta-TrCP.";
Genes Dev. 13:284-294(1999).
[7]
INTERACTION WITH NFKBID.
PubMed=11931770; DOI=10.1016/S1097-2765(02)00469-0;
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.;
"Peptide-induced negative selection of thymocytes activates
transcription of an NF-kappa B inhibitor.";
Mol. Cell 9:637-648(2002).
[8]
PHOSPHORYLATION AT SER-311.
PubMed=12881425; DOI=10.1093/emboj/cdg370;
Duran A., Diaz-Meco M.T., Moscat J.;
"Essential role of RelA Ser311 phosphorylation by zetaPKC in NF-kappaB
transcriptional activation.";
EMBO J. 22:3910-3918(2003).
[9]
MUTAGENESIS OF SER-281.
PubMed=12874295; DOI=10.1074/jbc.M301521200;
Maier H.J., Marienfeld R., Wirth T., Baumann B.;
"Critical role of RelB serine 368 for dimerization and p100
stabilization.";
J. Biol. Chem. 278:39242-39250(2003).
[10]
IDENTIFICATION IN THE NF-KAPPA-B P65-P50 COMPLEX, AND IDENTIFICATION
IN THE NF-KAPPA-B P65-P65 COMPLEX.
PubMed=15051764; DOI=10.1084/jem.20031272;
Goriely S., Van Lint C., Dadkhah R., Libin M., De Wit D., Demonte D.,
Willems F., Goldman M.;
"A defect in nucleosome remodeling prevents IL-12(p35) gene
transcription in neonatal dendritic cells.";
J. Exp. Med. 199:1011-1016(2004).
[11]
INTERACTION WITH IRAK1BP1.
PubMed=15485901; DOI=10.1128/MCB.24.21.9317-9326.2004;
Kwon H.-J., Breese E.H., Vig-Varga E., Luo Y., Lee Y., Goebl M.G.,
Harrington M.A.;
"Tumor necrosis factor alpha induction of NF-kappaB requires the novel
coactivator SIMPL.";
Mol. Cell. Biol. 24:9317-9326(2004).
[12]
INTERACTION WITH CARM1.
PubMed=15616592; DOI=10.1038/sj.emboj.7600500;
Covic M., Hassa P.O., Saccani S., Buerki C., Meier N.I., Lombardi C.,
Imhof R., Bedford M.T., Natoli G., Hottiger M.O.;
"Arginine methyltransferase CARM1 is a promoter-specific regulator of
NF-kappaB-dependent gene expression.";
EMBO J. 24:85-96(2005).
[13]
INTERACTION WITH NOTCH2.
PubMed=18710934; DOI=10.1128/MCB.00299-08;
Fukushima H., Nakao A., Okamoto F., Shin M., Kajiya H., Sakano S.,
Bigas A., Jimi E., Okabe K.;
"The association of Notch2 and NF-kappaB accelerates RANKL-induced
osteoclastogenesis.";
Mol. Cell. Biol. 28:6402-6412(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-176, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[15]
FUNCTION, SUBCELLULAR LOCATION, METHYLATION AT LYS-310,
PHOSPHORYLATION AT SER-311, INTERACTION WITH EHMT1, AND MUTAGENESIS OF
LYS-310.
PubMed=21131967; DOI=10.1038/ni.1968;
Levy D., Kuo A.J., Chang Y., Schaefer U., Kitson C., Cheung P.,
Espejo A., Zee B.M., Liu C.L., Tangsombatvisit S., Tennen R.I.,
Kuo A.Y., Tanjing S., Cheung R., Chua K.F., Utz P.J., Shi X.,
Prinjha R.K., Lee K., Garcia B.A., Bedford M.T., Tarakhovsky A.,
Cheng X., Gozani O.;
"Lysine methylation of the NF-kappaB subunit RelA by SETD6 couples
activity of the histone methyltransferase GLP at chromatin to tonic
repression of NF-kappaB signaling.";
Nat. Immunol. 12:29-36(2011).
[16]
FUNCTION, SULFHYDRATION AT CYS-38, S-NITROSYLATION AT CYS-38, AND
MUTAGENESIS OF CYS-38.
PubMed=22244329; DOI=10.1016/j.molcel.2011.10.021;
Sen N., Paul B.D., Gadalla M.M., Mustafa A.K., Sen T., Xu R., Kim S.,
Snyder S.H.;
"Hydrogen sulfide-linked sulfhydration of NF-kappaB mediates its
antiapoptotic actions.";
Mol. Cell 45:13-24(2012).
[17]
INTERACTION WITH CLOCK.
PubMed=22895791; DOI=10.1073/pnas.1206274109;
Spengler M.L., Kuropatwinski K.K., Comas M., Gasparian A.V.,
Fedtsova N., Gleiberman A.S., Gitlin I.I., Artemicheva N.M.,
Deluca K.A., Gudkov A.V., Antoch M.P.;
"Core circadian protein CLOCK is a positive regulator of NF-kappaB-
mediated transcription.";
Proc. Natl. Acad. Sci. U.S.A. 109:E2457-E2465(2012).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-310, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[19]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 19-291.
PubMed=9865694; DOI=10.1016/S0092-8674(00)81699-2;
Huxford T., Huang D.B., Malek S., Ghosh G.;
"The crystal structure of the IkappaBalpha/NF-kappaB complex reveals
mechanisms of NF-kappaB inactivation.";
Cell 95:759-770(1998).
[20]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 19-291.
PubMed=9437432; DOI=10.1038/nsb0198-67;
Chen Y.Q., Ghosh S., Ghosh G.;
"A novel DNA recognition mode by the NF-kappa B p65 homodimer.";
Nat. Struct. Biol. 5:67-73(1998).
[21]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
PubMed=9450761; DOI=10.1038/34956;
Chen F.E., Huang D.B., Chen Y.Q., Ghosh G.;
"Crystal structure of p50/p65 heterodimer of transcription factor NF-
kappaB bound to DNA.";
Nature 391:410-413(1998).
-!- 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
p65-c-Rel complexes are transcriptional activators. The NF-kappa-B
p65-p65 complex appears to be involved in invasin-mediated
activation of IL-8 expression (By similarity). The inhibitory
effect of I-kappa-B upon NF-kappa-B the cytoplasm is exerted
primarily through the interaction with p65. p65 shows a weak DNA-
binding site which could contribute directly to DNA binding in the
NF-kappa-B complex. Associates with chromatin at the NF-kappa-B
promoter region via association with DDX1. Essential for cytokine
gene expression in T-cells (By similarity).
{ECO:0000250|UniProtKB:Q04206, ECO:0000269|PubMed:21131967,
ECO:0000269|PubMed:22244329}.
-!- SUBUNIT: Component of the NF-kappa-B p65-p50 complex. Component of
the NF-kappa-B p65-c-Rel complex. Homodimer; component of the NF-
kappa-B p65-p65 complex. Component of the NF-kappa-B p65-p52
complex. May interact with ETHE1. Binds AES and TLE1. Interacts
with TP53BP2. Binds to and is phosphorylated by the activated form
of either RPS6KA4 or RPS6KA5. Interacts with ING4 and this
interaction may be indirect. Interacts with CARM1, USP48 and
UNC5CL. Interacts with IRAK1BP1. Interacts with NFKBIA. Interacts
with GSK3B. Interacts with NFKBIB. Interacts with NFKBIE.
Interacts with NFKBIZ. Part of a 70-90 kDa complex at least
consisting of CHUK, IKBKB, NFKBIA, RELA, IKBKAP and MAP3K14.
Interacts with HDAC3; HDAC3 mediates the deacetylation of RELA.
Interacts with HDAC1; the interaction requires non-phosphorylated
RELA. Interacts with CBP; the interaction requires phosphorylated
RELA. Interacts (phosphorylated at 'Thr-254') with PIN1; the
interaction inhibits p65 binding to NFKBIA. Interacts with SOCS1.
Interacts with MTDH and PHF11. Interacts with NFKBID. Interacts
with ARRB2. Interacts with NFKBIA (when phosphorylated), the
interaction is direct; phosphorylated NFKBIA is associated with a
SCF(BTRC)-like complex lacking CUL1. Interacts with RNF25.
Interacts (via C-terminus) with DDX1 (By similarity). Interacts
with UFL1 and COMMD1 (By similarity). Interacts with BRMS1; this
promotes deacetylation of 'Lys-310'. Interacts (when acetylated at
Lys-310) with BRD4; leading to activation of the NF-kappa-B
pathway (By similarity). Interacts with EHMT1 (via ANK repeats).
Interacts with NOTCH2. Directly interacts with MEN1; this
interaction represses NFKB-mediated transactivation (By
similarity). Interacts with AKIP1, which promotes the
phosphorylation and nuclear retention of RELA (By similarity).
Interacts (via the RHD) with GFI1; the interaction, after
bacterial lipopolysaccharide (LPS) stimulation, inhibits the
transcriptional activity by interfering with the DNA-binding
activity to target gene promoter DNA. Interacts with MEFV (By
similarity). Interacts with CLOCK. Interacts with FOXP3 (By
similarity). Interacts (via N-terminus) with CPEN1; this
interaction induces proteolytic cleavage of p65/RELA subunit and
inhibition of NF-kappa-B transcriptional activity (By similarity).
Interacts with CDK5RAP3; stimulates the interaction of RELA with
HDAC1, HDAC2 and HDAC3 thereby inhibiting NF-kappa-B
transcriptional activity (By similarity). Interacts with DHX9;
this interaction is direct and activates NF-kappa-B-mediated
transcription (By similarity). {ECO:0000250|UniProtKB:Q04206,
ECO:0000269|PubMed:11931770, ECO:0000269|PubMed:15051764,
ECO:0000269|PubMed:15485901, ECO:0000269|PubMed:15616592,
ECO:0000269|PubMed:18710934, ECO:0000269|PubMed:21131967,
ECO:0000269|PubMed:22895791, ECO:0000269|PubMed:8816457,
ECO:0000269|PubMed:9990853}.
-!- INTERACTION:
Q02248:Ctnnb1; NbExp=5; IntAct=EBI-644400, EBI-397872;
Q9H9B1:EHMT1 (xeno); NbExp=5; IntAct=EBI-644400, EBI-766087;
O09106:Hdac1; NbExp=2; IntAct=EBI-644400, EBI-301912;
P25799:Nfkb1; NbExp=6; IntAct=EBI-644400, EBI-643958;
Q9Z1E3:Nfkbia; NbExp=7; IntAct=EBI-644400, EBI-644427;
Q60778:Nfkbib; NbExp=8; IntAct=EBI-644400, EBI-644469;
Q62227:Nr0b2; NbExp=3; IntAct=EBI-644400, EBI-4310440;
Q06219:Nr4a2; NbExp=2; IntAct=EBI-644400, EBI-2337255;
Q8TBK2:SETD6 (xeno); NbExp=4; IntAct=EBI-644400, EBI-3863032;
Q8WTS6:SETD7 (xeno); NbExp=2; IntAct=EBI-644400, EBI-1268586;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21131967}.
Cytoplasm {ECO:0000269|PubMed:21131967}. Note=Colocalized with
DDX1 in the nucleus upon TNF-alpha induction (By similarity).
Nuclear, but also found in the cytoplasm in an inactive form
complexed to an inhibitor (I-kappa-B). Colocalizes with GFI1 in
the nucleus after lipopolysaccharide (LPS) stimulation.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=p65;
IsoId=Q04207-1; Sequence=Displayed;
Name=p65 delta;
IsoId=Q04207-2; Sequence=VSP_005589;
-!- PTM: Ubiquitinated, leading to its proteasomal degradation.
Degradation is required for termination of NF-kappa-B response (By
similarity). {ECO:0000250}.
-!- PTM: Monomethylated at Lys-310 by SETD6. Monomethylation at Lys-
310 is recognized by the ANK repeats of EHMT1 and promotes the
formation of repressed chromatin at target genes, leading to down-
regulation of NF-kappa-B transcription factor activity.
Phosphorylation at Ser-311 disrupts the interaction with EHMT1
without preventing monomethylation at Lys-310 and relieves the
repression of target genes. {ECO:0000269|PubMed:12881425,
ECO:0000269|PubMed:21131967}.
-!- PTM: Phosphorylation on Ser-534 stimulates acetylation on Lys-310
and interaction with CBP; the phosphorylated and acetylated forms
show enhanced transcriptional activity (By similarity).
Phosphorylation at Ser-311 disrupts the interaction with EHMT1 and
promotes transcription factor activity. Phosphorylation at Ser-276
by RPS6KA4 and RPS6KA5 promotes its transactivation and
transcriptional activities. {ECO:0000250,
ECO:0000269|PubMed:12881425, ECO:0000269|PubMed:21131967}.
-!- PTM: Reversibly acetylated; the acetylation seems to be mediated
by CBP, the deacetylation by HDAC3 and SIRT2. Acetylation at Lys-
122 enhances DNA binding and impairs association with NFKBIA.
Acetylation at Lys-310 is required for full transcriptional
activity in the absence of effects on DNA binding and NFKBIA
association. Acetylation at Lys-310 promotes interaction with
BRD4. Acetylation can also lower DNA-binding and results in
nuclear export. Interaction with BRMS1 promotes deacetylation of
Lys-310. Lys-310 is deacetylated by SIRT2 (By similarity).
{ECO:0000250}.
-!- PTM: S-nitrosylation of Cys-38 inactivates the enzyme activity.
{ECO:0000269|PubMed:22244329}.
-!- PTM: Sulfhydration at Cys-38 mediates the anti-apoptotic activity
by promoting the interaction with RPS3 and activating the
transcription factor activity.
-!- PTM: Sumoylation by PIAS3 negatively regulates DNA-bound activated
NF-kappa-B. {ECO:0000250}.
-!- PTM: Proteolytically cleaved within a conserved N-terminus region
required for base-specific contact with DNA in a CPEN1-mediated
manner, and hence inhibits NF-kappa-B transcriptional activity.
{ECO:0000250|UniProtKB:Q04206}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M61909; AAA39811.1; -; mRNA.
EMBL; BC003818; AAH03818.1; -; mRNA.
EMBL; L77155; AAB00795.1; -; Genomic_DNA.
EMBL; Z22952; CAA80528.1; -; Genomic_DNA.
CCDS; CCDS29473.1; -. [Q04207-1]
PIR; A37932; A37932.
PIR; PC4233; PC4233.
PIR; S48113; S48113.
RefSeq; NP_033071.1; NM_009045.4. [Q04207-1]
UniGene; Mm.249966; -.
PDB; 1BFT; X-ray; 2.00 A; A/B=191-291.
PDB; 1IKN; X-ray; 2.30 A; A=19-304.
PDB; 1K3Z; X-ray; 2.50 A; A/B=191-326.
PDB; 1LE5; X-ray; 2.75 A; A/E=20-291.
PDB; 1LE9; X-ray; 3.00 A; A/E=20-291.
PDB; 1LEI; X-ray; 2.70 A; A=20-291.
PDB; 1MY5; X-ray; 1.80 A; A/B=191-304.
PDB; 1MY7; X-ray; 1.49 A; A/B=191-304.
PDB; 1OY3; X-ray; 2.05 A; B/C=191-326.
PDB; 1RAM; X-ray; 2.70 A; A/B=19-291.
PDB; 1VKX; X-ray; 2.90 A; A=20-291.
PDB; 2I9T; X-ray; 2.80 A; A=19-291.
PDB; 2LWW; NMR; -; B=425-490.
PDB; 2RAM; X-ray; 2.40 A; A/B=19-291.
PDBsum; 1BFT; -.
PDBsum; 1IKN; -.
PDBsum; 1K3Z; -.
PDBsum; 1LE5; -.
PDBsum; 1LE9; -.
PDBsum; 1LEI; -.
PDBsum; 1MY5; -.
PDBsum; 1MY7; -.
PDBsum; 1OY3; -.
PDBsum; 1RAM; -.
PDBsum; 1VKX; -.
PDBsum; 2I9T; -.
PDBsum; 2LWW; -.
PDBsum; 2RAM; -.
DisProt; DP00129; -.
ProteinModelPortal; Q04207; -.
SMR; Q04207; -.
BioGrid; 202853; 31.
CORUM; Q04207; -.
DIP; DIP-6219N; -.
IntAct; Q04207; 22.
MINT; MINT-236104; -.
STRING; 10090.ENSMUSP00000025867; -.
ChEMBL; CHEMBL5902; -.
iPTMnet; Q04207; -.
PhosphoSitePlus; Q04207; -.
EPD; Q04207; -.
PaxDb; Q04207; -.
PeptideAtlas; Q04207; -.
PRIDE; Q04207; -.
Ensembl; ENSMUST00000025867; ENSMUSP00000025867; ENSMUSG00000024927. [Q04207-1]
GeneID; 19697; -.
KEGG; mmu:19697; -.
UCSC; uc008gee.1; mouse. [Q04207-1]
CTD; 5970; -.
MGI; MGI:103290; Rela.
eggNOG; ENOG410IG8F; Eukaryota.
eggNOG; ENOG410XT64; LUCA.
GeneTree; ENSGT00500000044765; -.
HOGENOM; HOG000230474; -.
HOVERGEN; HBG017916; -.
InParanoid; Q04207; -.
KO; K04735; -.
OMA; EFSPMVF; -.
OrthoDB; EOG091G08JD; -.
PhylomeDB; Q04207; -.
TreeFam; TF325632; -.
Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
Reactome; R-MMU-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-MMU-193692; Regulated proteolysis of p75NTR.
Reactome; R-MMU-202424; Downstream TCR signaling.
Reactome; R-MMU-209560; NF-kB is activated and signals survival.
Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
Reactome; R-MMU-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
Reactome; R-MMU-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-MMU-446652; Interleukin-1 family signaling.
Reactome; R-MMU-448706; Interleukin-1 processing.
Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-MMU-933542; TRAF6 mediated NF-kB activation.
ChiTaRS; Rela; mouse.
EvolutionaryTrace; Q04207; -.
PRO; PR:Q04207; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000024927; -.
ExpressionAtlas; Q04207; baseline and differential.
Genevisible; Q04207; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0033256; C:I-kappaB/NF-kappaB complex; IBA:GO_Central.
GO; GO:0071159; C:NF-kappaB complex; TAS:UniProtKB.
GO; GO:0035525; C:NF-kappaB p50/p65 complex; ISO:MGI.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; ISO:MGI.
GO; GO:0042805; F:actinin binding; IPI:UniProtKB.
GO; GO:0033613; F:activating transcription factor binding; ISO:MGI.
GO; GO:0071532; F:ankyrin repeat binding; IPI:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0031490; F:chromatin DNA binding; ISO:MGI.
GO; GO:0001046; F:core promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0051059; F:NF-kappaB binding; ISO:MGI.
GO; GO:0042301; F:phosphate ion binding; ISO:MGI.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
GO; GO:0070491; F:repressing transcription factor binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; ISO:MGI.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; ISO:MGI.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0000983; F:transcription factor activity, RNA polymerase II core promoter sequence-specific; ISO:MGI.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IDA:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISO:MGI.
GO; GO:0001205; F:transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific binding; ISO:MGI.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:BHF-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0006117; P:acetaldehyde metabolic process; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IDA:MGI.
GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
GO; GO:0071347; P:cellular response to interleukin-1; ISO:MGI.
GO; GO:0071354; P:cellular response to interleukin-6; ISO:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:UniProtKB.
GO; GO:0071223; P:cellular response to lipoteichoic acid; ISO:MGI.
GO; GO:0071316; P:cellular response to nicotine; ISO:MGI.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; ISO:MGI.
GO; GO:0071224; P:cellular response to peptidoglycan; ISO:MGI.
GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:MGI.
GO; GO:0006952; P:defense response; IMP:MGI.
GO; GO:0001942; P:hair follicle development; IMP:MGI.
GO; GO:0006954; P:inflammatory response; ISO:MGI.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0001889; P:liver development; IMP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IDA:MGI.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IEA:Ensembl.
GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; ISO:MGI.
GO; GO:0042177; P:negative regulation of protein catabolic process; IMP:MGI.
GO; GO:0033234; P:negative regulation of protein sumoylation; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0038061; P:NIK/NF-kappaB signaling; IBA:GO_Central.
GO; GO:0070431; P:nucleotide-binding oligomerization domain containing 2 signaling pathway; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IEA:Ensembl.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0045084; P:positive regulation of interleukin-12 biosynthetic process; IDA:MGI.
GO; GO:2000630; P:positive regulation of miRNA metabolic process; ISO:MGI.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:MGI.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0014040; P:positive regulation of Schwann cell differentiation; IEA:Ensembl.
GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0043620; P:regulation of DNA-templated transcription in response to stress; ISO:MGI.
GO; GO:0050727; P:regulation of inflammatory response; IDA:UniProtKB.
GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; ISO:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
GO; GO:0009617; P:response to bacterium; IDA:MGI.
GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
GO; GO:0033590; P:response to cobalamin; IEA:Ensembl.
GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
GO; GO:0070555; P:response to interleukin-1; ISO:MGI.
GO; GO:0043278; P:response to morphine; IEA:Ensembl.
GO; GO:0032495; P:response to muramyl dipeptide; IDA:MGI.
GO; GO:0035994; P:response to muscle stretch; IDA:MGI.
GO; GO:0010033; P:response to organic substance; ISO:MGI.
GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
GO; GO:0010224; P:response to UV-B; ISO:MGI.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:MGI.
CDD; cd01177; IPT_NFkappaB; 1.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 2.60.40.340; -; 1.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR014756; Ig_E-set.
InterPro; IPR002909; IPT.
InterPro; IPR033926; IPT_NFkappaB.
InterPro; IPR000451; NFkB/Dor.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR030495; RelA.
InterPro; IPR030492; RHD_CS.
InterPro; IPR032397; RHD_dimer.
InterPro; IPR011539; RHD_DNA_bind_dom.
PANTHER; PTHR24169; PTHR24169; 1.
PANTHER; PTHR24169:SF23; PTHR24169:SF23; 1.
Pfam; PF16179; RHD_dimer; 1.
Pfam; PF00554; RHD_DNA_bind; 1.
PRINTS; PR00057; NFKBTNSCPFCT.
SMART; SM00429; IPT; 1.
SUPFAM; SSF49417; SSF49417; 1.
SUPFAM; SSF81296; SSF81296; 1.
PROSITE; PS01204; REL_1; 1.
PROSITE; PS50254; REL_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Complete proteome; Cytoplasm; DNA-binding; Isopeptide bond;
Methylation; Nucleus; Phosphoprotein; Reference proteome;
S-nitrosylation; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 549 Transcription factor p65.
/FTId=PRO_0000205170.
DOMAIN 19 306 RHD. {ECO:0000255|PROSITE-
ProRule:PRU00265}.
MOTIF 301 304 Nuclear localization signal.
{ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q04206}.
MOD_RES 38 38 Cysteine persulfide; alternate.
{ECO:0000269|PubMed:22244329}.
MOD_RES 38 38 S-nitrosocysteine; alternate.
{ECO:0000269|PubMed:22244329}.
MOD_RES 122 122 N6-acetyllysine; by PCAF and EP300;
alternate.
{ECO:0000250|UniProtKB:Q04206}.
MOD_RES 123 123 N6-acetyllysine; by PCAF and EP300;
alternate.
{ECO:0000250|UniProtKB:Q04206}.
MOD_RES 176 176 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 218 218 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q04206}.
MOD_RES 221 221 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q04206}.
MOD_RES 254 254 Phosphothreonine.
{ECO:0000250|UniProtKB:Q04206}.
MOD_RES 276 276 Phosphoserine; by RPS6KA4 and RPS6KA5.
{ECO:0000250|UniProtKB:Q04206}.
MOD_RES 310 310 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 310 310 N6-methyllysine; by SETD6; alternate.
{ECO:0000269|PubMed:21131967}.
MOD_RES 311 311 Phosphoserine; by PKC/PRKCZ.
{ECO:0000269|PubMed:12881425,
ECO:0000269|PubMed:21131967}.
MOD_RES 433 433 Phosphothreonine.
{ECO:0000250|UniProtKB:Q04206}.
MOD_RES 467 467 Phosphoserine; by IKKB and IKKE.
{ECO:0000250|UniProtKB:Q04206}.
MOD_RES 504 504 Phosphothreonine; by CHEK1.
{ECO:0000250|UniProtKB:Q04206}.
MOD_RES 527 527 Phosphoserine; by CK2.
{ECO:0000250|UniProtKB:Q04206}.
MOD_RES 534 534 Phosphoserine; by IKKB.
{ECO:0000250|UniProtKB:Q04206}.
CROSSLNK 37 37 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO3).
{ECO:0000250}.
CROSSLNK 122 122 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO3);
alternate. {ECO:0000250}.
CROSSLNK 123 123 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO3);
alternate. {ECO:0000250}.
VAR_SEQ 222 231 Missing (in isoform p65 delta).
{ECO:0000305}.
/FTId=VSP_005589.
MUTAGEN 38 38 C->S: Abolishes sulfhydration and impairs
interaction with RPS3.
{ECO:0000269|PubMed:22244329}.
MUTAGEN 281 281 S->A,E: Abolishes DNA-binding and
transcriptional activity.
{ECO:0000269|PubMed:12874295}.
MUTAGEN 310 310 K->R: Abolishes monomethylation by SETD6
and interaction with EHMT1.
{ECO:0000269|PubMed:21131967}.
CONFLICT 28 28 K -> N (in Ref. 3; AAB00795).
{ECO:0000305}.
CONFLICT 61 61 I -> IQKD (in Ref. 3; AAB00795).
{ECO:0000305}.
STRAND 20 25 {ECO:0000244|PDB:1IKN}.
STRAND 30 32 {ECO:0000244|PDB:1RAM}.
TURN 37 39 {ECO:0000244|PDB:1IKN}.
STRAND 48 50 {ECO:0000244|PDB:1VKX}.
STRAND 53 55 {ECO:0000244|PDB:2RAM}.
STRAND 60 65 {ECO:0000244|PDB:1IKN}.
STRAND 71 77 {ECO:0000244|PDB:1IKN}.
STRAND 79 82 {ECO:0000244|PDB:1IKN}.
STRAND 87 92 {ECO:0000244|PDB:1IKN}.
STRAND 99 103 {ECO:0000244|PDB:1IKN}.
STRAND 109 112 {ECO:0000244|PDB:1IKN}.
STRAND 117 120 {ECO:0000244|PDB:1IKN}.
HELIX 123 125 {ECO:0000244|PDB:1IKN}.
HELIX 126 135 {ECO:0000244|PDB:1IKN}.
TURN 145 148 {ECO:0000244|PDB:2RAM}.
STRAND 156 166 {ECO:0000244|PDB:1IKN}.
STRAND 168 174 {ECO:0000244|PDB:1IKN}.
STRAND 178 184 {ECO:0000244|PDB:1LEI}.
STRAND 186 188 {ECO:0000244|PDB:1VKX}.
TURN 189 191 {ECO:0000244|PDB:2RAM}.
STRAND 196 200 {ECO:0000244|PDB:1MY7}.
STRAND 202 205 {ECO:0000244|PDB:1MY7}.
STRAND 211 217 {ECO:0000244|PDB:1MY7}.
HELIX 221 223 {ECO:0000244|PDB:1BFT}.
STRAND 225 230 {ECO:0000244|PDB:1MY7}.
STRAND 233 236 {ECO:0000244|PDB:1MY7}.
HELIX 241 243 {ECO:0000244|PDB:1MY7}.
STRAND 248 253 {ECO:0000244|PDB:1MY7}.
STRAND 266 274 {ECO:0000244|PDB:1MY7}.
TURN 275 278 {ECO:0000244|PDB:1MY7}.
STRAND 284 289 {ECO:0000244|PDB:1MY7}.
HELIX 294 304 {ECO:0000244|PDB:1OY3}.
HELIX 306 315 {ECO:0000244|PDB:1OY3}.
HELIX 433 439 {ECO:0000244|PDB:2LWW}.
STRAND 444 447 {ECO:0000244|PDB:2LWW}.
TURN 450 453 {ECO:0000244|PDB:2LWW}.
HELIX 459 461 {ECO:0000244|PDB:2LWW}.
HELIX 465 467 {ECO:0000244|PDB:2LWW}.
HELIX 471 477 {ECO:0000244|PDB:2LWW}.
STRAND 480 484 {ECO:0000244|PDB:2LWW}.
SEQUENCE 549 AA; 60212 MW; BDF1673D2FE398B9 CRC64;
MDDLFPLIFP SEPAQASGPY VEIIEQPKQR GMRFRYKCEG RSAGSIPGER STDTTKTHPT
IKINGYTGPG TVRISLVTKD PPHRPHPHEL VGKDCRDGYY EADLCPDRSI HSFQNLGIQC
VKKRDLEQAI SQRIQTNNNP FHVPIEEQRG DYDLNAVRLC FQVTVRDPAG RPLLLTPVLS
HPIFDNRAPN TAELKICRVN RNSGSCLGGD EIFLLCDKVQ KEDIEVYFTG PGWEARGSFS
QADVHRQVAI VFRTPPYADP SLQAPVRVSM QLRRPSDREL SEPMEFQYLP DTDDRHRIEE
KRKRTYETFK SIMKKSPFNG PTEPRPPTRR IAVPTRNSTS VPKPAPQPYT FPASLSTINF
DEFSPMLLPS GQISNQALAL APSSAPVLAQ TMVPSSAMVP LAQPPAPAPV LTPGPPQSLS
APVPKSTQAG EGTLSEALLH LQFDADEDLG ALLGNSTDPG VFTDLASVDN SEFQQLLNQG
VSMSHSTAEP MLMEYPEAIT RLVTGSQRPP DPAPTPLGTS GLPNGLSGDE DFSSIADMDF
SALLSQISS


Related products :

Catalog number Product name Quantity
E0616m ELISA Mouse,Mus musculus,Nfkb3,Nuclear factor NF-kappa-B p65 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3,Rela,Transcription factor p65 96T
U0616m CLIA Mouse,Mus musculus,Nfkb3,Nuclear factor NF-kappa-B p65 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3,Rela,Transcription factor p65 96T
E0616m ELISA kit Mouse,Mus musculus,Nfkb3,Nuclear factor NF-kappa-B p65 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3,Rela,Transcription factor p65 96T
U0616h CLIA Homo sapiens,Human,NFKB3,Nuclear factor NF-kappa-B p65 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3,RELA,Transcription factor p65 96T
E0616h ELISA kit Homo sapiens,Human,NFKB3,Nuclear factor NF-kappa-B p65 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3,RELA,Transcription factor p65 96T
E0616h ELISA Homo sapiens,Human,NFKB3,Nuclear factor NF-kappa-B p65 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3,RELA,Transcription factor p65 96T
U1824m CLIA DNA-binding factor KBF1,EBP-1,Mouse,Mus musculus,NF-kappa-B1 p84_NF-kappa-B1 p98,Nfkb1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 96T
E1824m ELISA DNA-binding factor KBF1,EBP-1,Mouse,Mus musculus,NF-kappa-B1 p84_NF-kappa-B1 p98,Nfkb1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 96T
EIAAB27080 DNA-binding factor KBF2,Mouse,Mus musculus,Nfkb2,Nuclear factor NF-kappa-B p100 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 2
U1824r CLIA DNA-binding factor KBF1,EBP-1,Nfkb1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1,Rat,Rattus norvegicus 96T
E1824r ELISA DNA-binding factor KBF1,EBP-1,Nfkb1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1,Rat,Rattus norvegicus 96T
U1824r CLIA kit DNA-binding factor KBF1,EBP-1,Nfkb1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1,Rat,Rattus norvegicus 96T
E1824r ELISA kit DNA-binding factor KBF1,EBP-1,Nfkb1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1,Rat,Rattus norvegicus 96T
E1824h ELISA kit DNA-binding factor KBF1,EBP-1,Homo sapiens,Human,NFKB1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 96T
E1824h ELISA DNA-binding factor KBF1,EBP-1,Homo sapiens,Human,NFKB1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 96T
U1824h CLIA DNA-binding factor KBF1,EBP-1,Homo sapiens,Human,NFKB1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 96T
U1824h CLIA kit DNA-binding factor KBF1,EBP-1,Homo sapiens,Human,NFKB1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 96T
E1824m ELISA kit DNA-binding factor KBF1,EBP-1,Mouse,Mus musculus,NF-kappa-B1 p84_NF-kappa-B1 p98,Nfkb1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-ce 96T
U1824m CLIA kit DNA-binding factor KBF1,EBP-1,Mouse,Mus musculus,NF-kappa-B1 p84_NF-kappa-B1 p98,Nfkb1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cel 96T
EIAAB27078 Chicken,DNA-binding factor KBF2,Gallus gallus,Lyt-10,NFKB2,Nuclear factor NF-kappa-B p100 subunit,Nuclear factor NF-kappa-B p97 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cel
U1824c CLIA kit Chicken,Gallus gallus,NFKB1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 96T
E1824c ELISA kit Chicken,Gallus gallus,NFKB1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 96T
U1824c CLIA Chicken,Gallus gallus,NFKB1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 96T
E1824c ELISA Chicken,Gallus gallus,NFKB1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 96T
U1824c CLIA Canis familiaris,Canis lupus familiaris,Dog,NFKB1,Nuclear factor NF-kappa-B p105 subunit,Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur