Q04207 (TF65_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	549 AA.
Sequence status	Complete.
Protein existence	Evidence 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' 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. Ref.5 Ref.6 Ref.7 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
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 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 process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	DNA-binding
Molecular function	Activator
PTM	Acetylation Isopeptide bond Methylation Phosphoprotein S-nitrosylation Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	acetaldehyde metabolic process Inferred from electronic annotation. Source: Compara aging Inferred from electronic annotation. Source: Compara cellular response to interleukin-1 Inferred from electronic annotation. Source: Compara cellular response to lipopolysaccharide Inferred from expression pattern PubMed 20547752. Source: UniProtKB cellular response to tumor necrosis factor Inferred from electronic annotation. Source: Compara cytokine-mediated signaling pathway Inferred from electronic annotation. Source: Compara 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: Compara 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 insulin receptor signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of protein catabolic process Inferred from mutant phenotype PubMed 15923614. Source: MGI negative regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara nucleotide-binding oligomerization domain containing 2 signaling pathway Inferred from electronic annotation. Source: Compara organ morphogenesis Inferred from mutant phenotype PubMed 9120401. Source: MGI positive regulation of I-kappaB kinase/NF-kappaB cascade 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: Compara positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of chondrocyte differentiation Inferred from electronic annotation. Source: Compara 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 electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent 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: Compara response to amino acid stimulus Inferred from electronic annotation. Source: Compara response to cAMP Inferred from electronic annotation. Source: Compara response to cobalamin Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to hydrogen peroxide Inferred from electronic annotation. Source: Compara response to insulin stimulus Inferred from electronic annotation. Source: Compara response to mechanical stimulus Inferred from electronic annotation. Source: Compara response to morphine Inferred from electronic annotation. Source: Compara response to muramyl dipeptide Inferred from direct assay PubMed 12527755. Source: MGI response to progesterone stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	NF-kappaB complex Traceable author statement Ref.15. 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: Compara
Molecular_function	DNA 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 chromatin binding Inferred from direct assay Ref.14. Source: UniProtKB phosphate ion binding Inferred from electronic annotation. Source: Compara sequence-specific DNA binding Inferred from electronic annotation. Source: Compara transcription regulatory region DNA binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EHMT1	Q9H9B1	5	EBI-644400,EBI-766087	From a different organism.
Hdac1	O09106	2	EBI-644400,EBI-301912
Nfkb1	P25799	3	EBI-644400,EBI-643958
Nfkbia	Q9Z1E3	3	EBI-644400,EBI-644427
Nfkbib	Q60778	8	EBI-644400,EBI-644469
Nr0b2	Q62227	3	EBI-644400,EBI-4310440
Nr4a2	Q06219	2	EBI-644400,EBI-2337255
SETD6	Q8TBK2	4	EBI-644400,EBI-3863032	From a different organism.
SETD7	Q8WTS6	2	EBI-644400,EBI-1268586	From a different organism.

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 549

549

Transcription factor p65

PRO_0000205170

Regions

Domain

19 – 306

288

RHD

Motif

301 – 304

4

Nuclear localization signal Potential

Amino acid modifications

Modified residue

38

1

Cysteine persulfide; alternate Ref.15

Modified residue

38

1

S-nitrosocysteine; alternate Ref.15

Modified residue

122

1

N6-acetyllysine; by PCAF and EP300; alternate By similarity

Modified residue

123

1

N6-acetyllysine; by PCAF and EP300; alternate By similarity

Modified residue

254

1

Phosphothreonine By similarity

Modified residue

276

1

Phosphoserine; by RPS6KA4 and RPS6KA5 By similarity

Modified residue

310

1

N6-acetyllysine; alternate By similarity

Modified residue

310

1

N6-methyllysine; by SETD6 Ref.14

Modified residue

311

1

Phosphoserine; by PKC/PRKCZ Ref.8 Ref.14

Modified residue

433

1

Phosphothreonine By similarity

Modified residue

467

1

Phosphoserine; by IKKB and IKKE By similarity

Modified residue

504

1

Phosphothreonine; by CHEK1 By similarity

Modified residue

527

1

Phosphoserine; by CK2 By similarity

Modified residue

534

1

Phosphoserine; by IKKB By similarity

Cross-link

37

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3) By similarity

Cross-link

122

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3); alternate By similarity

Cross-link

123

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3); alternate By similarity

Natural variations

Alternative sequence

222 – 231

10

Missing in isoform p65 delta.

VSP_005589

Experimental info

Mutagenesis

38

1

C → S: Abolishes sulfhydration and impairs interaction with RPS3. Ref.15

Mutagenesis

281

1

S → A or E: Abolishes DNA-binding and transcriptional activity. Ref.9

Mutagenesis

310

1

K → R: Abolishes monomethylation by SETD6 and interaction with EHMT1. Ref.14

Sequence conflict

28

1

K → N in AAB00795. Ref.3

Sequence conflict

61

1

I → IQKD in AAB00795. Ref.3

Secondary structure

1

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549

Helix Strand Turn

Details...

Beta strand

20 – 25

6

Beta strand

30 – 32

3

Turn

37 – 39

3

Beta strand

48 – 50

3

Beta strand

53 – 55

3

Beta strand

60 – 65

6

Beta strand

71 – 77

7

Beta strand

79 – 82

4

Beta strand

87 – 92

6

Beta strand

99 – 103

5

Beta strand

109 – 112

4

Beta strand

117 – 120

4

Helix

123 – 125

3

Helix

126 – 135

10

Turn

145 – 148

4

Beta strand

156 – 166

11

Beta strand

168 – 174

7

Beta strand

178 – 184

7

Beta strand

186 – 188

3

Turn

189 – 191

3

Beta strand

196 – 200

5

Beta strand

202 – 205

4

Beta strand

211 – 217

7

Helix

221 – 223

3

Beta strand

225 – 230

6

Beta strand

233 – 236

4

Helix

241 – 243

3

Beta strand

248 – 253

6

Beta strand

266 – 274

9

Turn

275 – 278

4

Beta strand

284 – 289

6

Helix

294 – 304

11

Helix

306 – 315

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform p65 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: BDF1673D2FE398B9	FASTA	549	60,212
	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
	Isoform p65 delta [UniParc]. Checksum: F834FD0302D351BD	FASTA	539	59,061
	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 KGWEARGSFS QADVHRQVAI 250 260 270 280 290 300 VFRTPPYADP SLQAPVRVSM QLRRPSDREL SEPMEFQYLP DTDDRHRIEE KRKRTYETFK 310 320 330 340 350 360 SIMKKSPFNG PTEPRPPTRR IAVPTRNSTS VPKPAPQPYT FPASLSTINF DEFSPMLLPS 370 380 390 400 410 420 GQISNQALAL APSSAPVLAQ TMVPSSAMVP LAQPPAPAPV LTPGPPQSLS APVPKSTQAG 430 440 450 460 470 480 EGTLSEALLH LQFDADEDLG ALLGNSTDPG VFTDLASVDN SEFQQLLNQG VSMSHSTAEP 490 500 510 520 530 MLMEYPEAIT RLVTGSQRPP DPAPTPLGTS GLPNGLSGDE DFSSIADMDF SALLSQISS

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
[17]	"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.
[18]	"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.

IPI

IPI00134188.
IPI00229014.

PIR

A37932.
PC4233.
S48113.

RefSeq

NP_033071.1. NM_009045.4.

UniGene

Mm.249966.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BFT	X-ray	2.00	A/B	191-291	[»]
1IKN	X-ray	2.30	A	19-304	[»]
1K3Z	X-ray	2.50	A/B	191-326	[»]
1LE5	X-ray	2.75	A/E	20-291	[»]
1LE9	X-ray	3.00	A/E	20-291	[»]
1LEI	X-ray	2.70	A	20-291	[»]
1MY5	X-ray	1.80	A/B	191-304	[»]
1MY7	X-ray	1.49	A/B	191-304	[»]
1OY3	X-ray	2.05	B/C	191-326	[»]
1RAM	X-ray	2.70	A/B	19-291	[»]
1VKX	X-ray	2.90	A	20-291	[»]
2I9T	X-ray	2.80	A	19-291	[»]
2RAM	X-ray	2.40	A/B	19-291	[»]

DisProt

DP00129.

ProteinModelPortal

Q04207.

SMR

Q04207. Positions 20-325.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6219N.

IntAct

Q04207. 15 interactions.

MINT

MINT-236104.

PTM databases

PhosphoSite

Q04207.

Proteomic databases

PaxDb

Q04207.

PRIDE

Q04207.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000025867; ENSMUSP00000025867; ENSMUSG00000024927.

GeneID

19697.

KEGG

mmu:19697.

UCSC

uc008gee.1. mouse.

Organism-specific databases

CTD

5970.

MGI

MGI:103290. Rela.

Phylogenomic databases

eggNOG

NOG119056.

HOGENOM

HOG000230474.

HOVERGEN

HBG017916.

InParanoid

Q04207.

KO

K04735.

OMA

EFSPMVF.

OrthoDB

EOG4NVZK2.

Gene expression databases

ArrayExpress

Q04207.

Bgee

Q04207.

Genevestigator

Q04207.

GermOnline

ENSMUSG00000024927. Mus musculus.

Family and domain databases

Gene3D

2.60.40.10. 1 hit.
2.60.40.340. 1 hit.

InterPro

IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT_TIG_rcpt.
IPR000451. NF_Rel_Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view]

Pfam

PF00554. RHD. 1 hit.
[Graphical view]

PRINTS

PR00057. NFKBTNSCPFCT.

SMART

SM00429. IPT. 1 hit.
[Graphical view]

SUPFAM

SSF81296. Ig_E-set. 1 hit.
SSF49417. P53_like_DNA_bnd. 1 hit.

PROSITE

PS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL5902.

ChiTaRS

RELA. mouse.

EvolutionaryTrace

Q04207.

NextBio

297048.

SOURCE

Search...

Entry information

Entry name

TF65_MOUSE

Accession

Primary (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:	May 29, 2013
This is version 148 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program