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Q04207 (TF65_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 157. 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:
Transcription factor p65
Alternative name(s):
Nuclear factor NF-kappa-B p65 subunit
Nuclear factor of kappa light polypeptide gene enhancer in B-cells 3
Gene names
Name:Rela
Synonyms:Nfkb3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length549 AA.
Sequence statusComplete.
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 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. Ref.14 Ref.15

Subunit structure

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. Ref.5 Ref.6 Ref.7 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16

Subcellular location

Nucleus. Cytoplasm. 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. Ref.14

Post-translational modification

Ubiquitinated, leading to its proteasomal degradation. Degradation is required for termination of NF-kappa-B response By similarity.

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. Ref.14

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. Ref.8 Ref.14

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.

S-nitrosylation of Cys-38 inactivates the enzyme activity.

Sulfhydration at Cys-38 mediates the anti-apoptotic activity by promoting the interaction with RPS3 and activating the transcription factor activity.

Sumoylation by PIAS3 negatively regulates DNA-bound activated NF-kappa-B By similarity.

Sequence similarities

Contains 1 RHD (Rel-like) domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandDNA-binding
   Molecular functionActivator
   PTMAcetylation
Isopeptide bond
Methylation
Phosphoprotein
S-nitrosylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacetaldehyde metabolic process

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from electronic annotation. Source: Ensembl

cellular response to hydrogen peroxide

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to interleukin-1

Inferred from electronic annotation. Source: Ensembl

cellular response to lipopolysaccharide

Inferred from expression pattern PubMed 20547752. Source: UniProtKB

cellular response to tumor necrosis factor

Inferred from sequence or structural similarity. Source: UniProtKB

cytokine-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

defense response

Inferred from mutant phenotype PubMed 9120401. Source: MGI

hair follicle development

Inferred from mutant phenotype PubMed 16481354. Source: MGI

inflammatory response

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from mutant phenotype PubMed 7603567. Source: UniProtKB

negative regulation of apoptotic process

Inferred from direct assay Ref.15. Source: UniProtKB

negative regulation of extrinsic apoptotic signaling pathway

Inferred from direct assay Ref.15. Source: MGI

negative regulation of insulin receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein catabolic process

Inferred from mutant phenotype PubMed 15923614. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

nucleotide-binding oligomerization domain containing 2 signaling pathway

Inferred from electronic annotation. Source: Ensembl

organ morphogenesis

Inferred from mutant phenotype PubMed 9120401. Source: MGI

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from direct assay Ref.15. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from direct assay Ref.15. Source: UniProtKB

positive regulation of Schwann cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of chondrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-12 biosynthetic process

Inferred from direct assay PubMed 14568984. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.14. Source: UniProtKB

regulation of inflammatory response

Inferred from direct assay Ref.14. Source: UniProtKB

response to UV-B

Inferred from electronic annotation. Source: Ensembl

response to amino acid

Inferred from electronic annotation. Source: Ensembl

response to bacterium

Inferred from direct assay PubMed 15661922. Source: MGI

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to cobalamin

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to insulin

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to morphine

Inferred from electronic annotation. Source: Ensembl

response to muramyl dipeptide

Inferred from direct assay PubMed 12527755. Source: MGI

response to progesterone

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 8289784. Source: GOC

   Cellular_componentNF-kappaB complex

Traceable author statement Ref.15. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.14. Source: UniProtKB

cytosol

Inferred from direct assay Ref.7. Source: MGI

nucleus

Inferred from direct assay Ref.14Ref.15. Source: UniProtKB

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Inferred from direct assay PubMed 10227969PubMed 14961764PubMed 15684432PubMed 15845452PubMed 15944286PubMed 16207754PubMed 16260493PubMed 18505784. Source: MGI

RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 8289784. Source: UniProtKB

ankyrin repeat binding

Inferred from physical interaction Ref.14. Source: UniProtKB

chromatin binding

Inferred from direct assay Ref.14. Source: UniProtKB

enzyme binding

Inferred from physical interaction Ref.15. Source: UniProtKB

phosphate ion binding

Inferred from electronic annotation. Source: Ensembl

protein kinase binding

Inferred from physical interaction Ref.14. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 14568984. Source: MGI

transcription regulatory region DNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform p65 (identifier: Q04207-1)

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 p65 delta (identifier: Q04207-2)

The sequence of this isoform differs from the canonical sequence as follows:
     222-231: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 549549Transcription factor p65
PRO_0000205170

Regions

Domain19 – 306288RHD
Motif301 – 3044Nuclear localization signal Potential

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue381Cysteine persulfide; alternate Ref.15
Modified residue381S-nitrosocysteine; alternate Ref.15
Modified residue1221N6-acetyllysine; by PCAF and EP300; alternate By similarity
Modified residue1231N6-acetyllysine; by PCAF and EP300; alternate By similarity
Modified residue2181N6-acetyllysine By similarity
Modified residue2211N6-acetyllysine By similarity
Modified residue2541Phosphothreonine By similarity
Modified residue2761Phosphoserine; by RPS6KA4 and RPS6KA5 By similarity
Modified residue3101N6-acetyllysine; alternate Ref.17
Modified residue3101N6-methyllysine; by SETD6; alternate Ref.14
Modified residue3111Phosphoserine; by PKC/PRKCZ Ref.8 Ref.14
Modified residue4331Phosphothreonine By similarity
Modified residue4671Phosphoserine; by IKKB and IKKE By similarity
Modified residue5041Phosphothreonine; by CHEK1 By similarity
Modified residue5271Phosphoserine; by CK2 By similarity
Modified residue5341Phosphoserine; by IKKB By similarity
Cross-link37Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3) By similarity
Cross-link122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3); alternate By similarity
Cross-link123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3); alternate By similarity

Natural variations

Alternative sequence222 – 23110Missing in isoform p65 delta.
VSP_005589

Experimental info

Mutagenesis381C → S: Abolishes sulfhydration and impairs interaction with RPS3. Ref.15
Mutagenesis2811S → A or E: Abolishes DNA-binding and transcriptional activity. Ref.9
Mutagenesis3101K → R: Abolishes monomethylation by SETD6 and interaction with EHMT1. Ref.14
Sequence conflict281K → N in AAB00795. Ref.3
Sequence conflict611I → IQKD in AAB00795. Ref.3

Secondary structure

.............................................................................. 549
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform p65 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: BDF1673D2FE398B9

FASTA54960,212
        10         20         30         40         50         60 
MDDLFPLIFP SEPAQASGPY VEIIEQPKQR GMRFRYKCEG RSAGSIPGER STDTTKTHPT 

        70         80         90        100        110        120 
IKINGYTGPG TVRISLVTKD PPHRPHPHEL VGKDCRDGYY EADLCPDRSI HSFQNLGIQC 

       130        140        150        160        170        180 
VKKRDLEQAI SQRIQTNNNP FHVPIEEQRG DYDLNAVRLC FQVTVRDPAG RPLLLTPVLS 

       190        200        210        220        230        240 
HPIFDNRAPN TAELKICRVN RNSGSCLGGD EIFLLCDKVQ KEDIEVYFTG PGWEARGSFS 

       250        260        270        280        290        300 
QADVHRQVAI VFRTPPYADP SLQAPVRVSM QLRRPSDREL SEPMEFQYLP DTDDRHRIEE 

       310        320        330        340        350        360 
KRKRTYETFK SIMKKSPFNG PTEPRPPTRR IAVPTRNSTS VPKPAPQPYT FPASLSTINF 

       370        380        390        400        410        420 
DEFSPMLLPS GQISNQALAL APSSAPVLAQ TMVPSSAMVP LAQPPAPAPV LTPGPPQSLS 

       430        440        450        460        470        480 
APVPKSTQAG EGTLSEALLH LQFDADEDLG ALLGNSTDPG VFTDLASVDN SEFQQLLNQG 

       490        500        510        520        530        540 
VSMSHSTAEP MLMEYPEAIT RLVTGSQRPP DPAPTPLGTS GLPNGLSGDE DFSSIADMDF 


SALLSQISS 

« Hide

Isoform p65 delta [UniParc].

Checksum: F834FD0302D351BD
Show »

FASTA53959,061

References

« Hide 'large scale' references
[1]"DNA binding and I kappa B inhibition of the cloned p65 subunit of NF-kappa B, a rel-related polypeptide."
Nolan G.P., Ghosh S., Liou H.C., Tempst P., Baltimore D.
Cell 64:961-969(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P65).
[2]"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] (ISOFORM P65).
Strain: C57BL/6J.
Tissue: Mammary gland.
[3]"Cloning of the murine relA (p65 NF-kappa B) gene and comparison to the human gene reveals a distinct first intron."
Linker R.A., Baeuerle P.A., Kaltschmidt C.
Gene 176:119-124(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-114.
Strain: BALB/c.
[4]"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."
Deloukas P., van Loon A.P.G.M.
Hum. Mol. Genet. 2:1895-1900(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 188-252, ALTERNATIVE SPLICING.
Strain: BALB/c.
[5]"Role of unphosphorylated, newly synthesized IkappaB beta in persistent activation of NF-kappaB."
Suyang H., Phillips R.J., Douglas I., Ghosh S.
Mol. Cell. Biol. 16:5444-5449(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NFKBIB.
[6]"Signal-induced ubiquitination of IkappaBalpha by the F-box protein Slimb/beta-TrCP."
Spencer E., Jiang J., Chen Z.J.
Genes Dev. 13:284-294(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NFKBIA.
[7]"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.
[8]"Essential role of RelA Ser311 phosphorylation by zetaPKC in NF-kappaB transcriptional activation."
Duran A., Diaz-Meco M.T., Moscat J.
EMBO J. 22:3910-3918(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-311.
[9]"Critical role of RelB serine 368 for dimerization and p100 stabilization."
Maier H.J., Marienfeld R., Wirth T., Baumann B.
J. Biol. Chem. 278:39242-39250(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF SER-281.
[10]"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, IDENTIFICATION IN THE NF-KAPPA-B P65-P65 COMPLEX.
[11]"Tumor necrosis factor alpha induction of NF-kappaB requires the novel coactivator SIMPL."
Kwon H.-J., Breese E.H., Vig-Varga E., Luo Y., Lee Y., Goebl M.G., Harrington M.A.
Mol. Cell. Biol. 24:9317-9326(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IRAK1BP1.
[12]"Arginine methyltransferase CARM1 is a promoter-specific regulator of NF-kappaB-dependent gene expression."
Covic M., Hassa P.O., Saccani S., Buerki C., Meier N.I., Lombardi C., Imhof R., Bedford M.T., Natoli G., Hottiger M.O.
EMBO J. 24:85-96(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CARM1.
[13]"The association of Notch2 and NF-kappaB accelerates RANKL-induced osteoclastogenesis."
Fukushima H., Nakao A., Okamoto F., Shin M., Kajiya H., Sakano S., Bigas A., Jimi E., Okabe K.
Mol. Cell. Biol. 28:6402-6412(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NOTCH2.
[14]"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."
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. expand/collapse author list , Lee K., Garcia B.A., Bedford M.T., Tarakhovsky A., Cheng X., Gozani O.
Nat. Immunol. 12:29-36(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, METHYLATION AT LYS-310, PHOSPHORYLATION AT SER-311, INTERACTION WITH EHMT1, MUTAGENESIS OF LYS-310.
[15]"Hydrogen sulfide-linked sulfhydration of NF-kappaB mediates its antiapoptotic actions."
Sen N., Paul B.D., Gadalla M.M., Mustafa A.K., Sen T., Xu R., Kim S., Snyder S.H.
Mol. Cell 45:13-24(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SULFHYDRATION AT CYS-38, S-NITROSYLATION AT CYS-38, MUTAGENESIS OF CYS-38.
[16]"Core circadian protein CLOCK is a positive regulator of NF-kappaB-mediated transcription."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:E2457-E2465(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CLOCK.
[17]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
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.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[18]"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 19-291.
[19]"A novel DNA recognition mode by the NF-kappa B p65 homodimer."
Chen Y.Q., Ghosh S., Ghosh G.
Nat. Struct. Biol. 5:67-73(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 19-291.
[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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M61909 mRNA. Translation: AAA39811.1.
BC003818 mRNA. Translation: AAH03818.1.
L77155 Genomic DNA. Translation: AAB00795.1.
Z22952 Genomic DNA. Translation: CAA80528.1.
PIRA37932.
PC4233.
S48113.
RefSeqNP_033071.1. NM_009045.4.
UniGeneMm.249966.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BFTX-ray2.00A/B191-291[»]
1IKNX-ray2.30A19-304[»]
1K3ZX-ray2.50A/B191-326[»]
1LE5X-ray2.75A/E20-291[»]
1LE9X-ray3.00A/E20-291[»]
1LEIX-ray2.70A20-291[»]
1MY5X-ray1.80A/B191-304[»]
1MY7X-ray1.49A/B191-304[»]
1OY3X-ray2.05B/C191-326[»]
1RAMX-ray2.70A/B19-291[»]
1VKXX-ray2.90A20-291[»]
2I9TX-ray2.80A19-291[»]
2LWWNMR-B425-490[»]
2RAMX-ray2.40A/B19-291[»]
DisProtDP00129.
ProteinModelPortalQ04207.
SMRQ04207. Positions 20-325, 425-490.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202853. 31 interactions.
DIPDIP-6219N.
IntActQ04207. 23 interactions.
MINTMINT-236104.

Chemistry

ChEMBLCHEMBL5902.

PTM databases

PhosphoSiteQ04207.

Proteomic databases

PaxDbQ04207.
PRIDEQ04207.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025867; ENSMUSP00000025867; ENSMUSG00000024927. [Q04207-1]
GeneID19697.
KEGGmmu:19697.
UCSCuc008gee.1. mouse. [Q04207-1]

Organism-specific databases

CTD5970.
MGIMGI:103290. Rela.

Phylogenomic databases

eggNOGNOG119056.
HOGENOMHOG000230474.
HOVERGENHBG017916.
InParanoidQ04207.
KOK04735.
OMAEFSPMVF.
OrthoDBEOG7VHSWT.
PhylomeDBQ04207.
TreeFamTF325632.

Gene expression databases

ArrayExpressQ04207.
BgeeQ04207.
GenevestigatorQ04207.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProIPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR000451. NF_Rel_Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view]
PfamPF00554. RHD. 1 hit.
[Graphical view]
PRINTSPR00057. NFKBTNSCPFCT.
SMARTSM00429. IPT. 1 hit.
[Graphical view]
SUPFAMSSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEPS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRELA. mouse.
EvolutionaryTraceQ04207.
NextBio297048.
PROQ04207.
SOURCESearch...

Entry information

Entry nameTF65_MOUSE
AccessionPrimary (citable) accession number: Q04207
Secondary accession number(s): Q62025
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 157 of the entry and version 1 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