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Q04207

- TF65_MOUSE

UniProt

Q04207 - TF65_MOUSE

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Protein

Transcription factor p65

Gene

Rela

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and 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.By similarity2 Publications

GO - Molecular functioni

  1. ankyrin repeat binding Source: UniProtKB
  2. chromatin binding Source: UniProtKB
  3. DNA binding Source: MGI
  4. enzyme binding Source: UniProtKB
  5. phosphate ion binding Source: Ensembl
  6. protein kinase binding Source: UniProtKB
  7. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  8. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: Ensembl
  9. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  10. RNA polymerase II distal enhancer sequence-specific DNA binding Source: Ensembl
  11. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: UniProtKB
  12. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
  13. sequence-specific DNA binding Source: MGI
  14. sequence-specific DNA binding transcription factor activity Source: MGI

GO - Biological processi

  1. acetaldehyde metabolic process Source: Ensembl
  2. aging Source: Ensembl
  3. cellular response to hydrogen peroxide Source: UniProtKB
  4. cellular response to interleukin-1 Source: Ensembl
  5. cellular response to interleukin-6 Source: Ensembl
  6. cellular response to lipopolysaccharide Source: UniProtKB
  7. cellular response to nicotine Source: Ensembl
  8. cellular response to peptide hormone stimulus Source: Ensembl
  9. cellular response to tumor necrosis factor Source: UniProtKB
  10. cytokine-mediated signaling pathway Source: Ensembl
  11. defense response Source: MGI
  12. hair follicle development Source: MGI
  13. inflammatory response Source: Ensembl
  14. liver development Source: UniProtKB
  15. negative regulation of apoptotic process Source: UniProtKB
  16. negative regulation of extrinsic apoptotic signaling pathway Source: MGI
  17. negative regulation of insulin receptor signaling pathway Source: Ensembl
  18. negative regulation of protein catabolic process Source: MGI
  19. nucleotide-binding oligomerization domain containing 2 signaling pathway Source: Ensembl
  20. organ morphogenesis Source: MGI
  21. positive regulation of cell proliferation Source: UniProtKB
  22. positive regulation of chondrocyte differentiation Source: Ensembl
  23. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  24. positive regulation of interleukin-12 biosynthetic process Source: MGI
  25. positive regulation of miRNA metabolic process Source: Ensembl
  26. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  27. positive regulation of Schwann cell differentiation Source: Ensembl
  28. positive regulation of transcription, DNA-templated Source: UniProtKB
  29. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  30. regulation of inflammatory response Source: UniProtKB
  31. response to amino acid Source: Ensembl
  32. response to bacterium Source: MGI
  33. response to cAMP Source: Ensembl
  34. response to cobalamin Source: Ensembl
  35. response to drug Source: Ensembl
  36. response to insulin Source: Ensembl
  37. response to mechanical stimulus Source: Ensembl
  38. response to morphine Source: Ensembl
  39. response to muramyl dipeptide Source: MGI
  40. response to progesterone Source: Ensembl
  41. response to UV-B Source: Ensembl
  42. transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
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 namesi
Name:Rela
Synonyms:Nfkb3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:103290. Rela.

Subcellular locationi

Nucleus 1 Publication. Cytoplasm 1 Publication
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.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: MGI
  3. NF-kappaB complex Source: UniProtKB
  4. nucleus Source: UniProtKB
  5. transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi38 – 381C → S: Abolishes sulfhydration and impairs interaction with RPS3. 1 Publication
Mutagenesisi281 – 2811S → A or E: Abolishes DNA-binding and transcriptional activity. 1 Publication
Mutagenesisi310 – 3101K → R: Abolishes monomethylation by SETD6 and interaction with EHMT1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 549549Transcription factor p65PRO_0000205170Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Cross-linki37 – 37Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3)By similarity
Modified residuei38 – 381Cysteine persulfide; alternate1 Publication
Modified residuei38 – 381S-nitrosocysteine; alternate1 Publication
Modified residuei122 – 1221N6-acetyllysine; by PCAF and EP300; alternateBy similarity
Cross-linki122 – 122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3); alternateBy similarity
Modified residuei123 – 1231N6-acetyllysine; by PCAF and EP300; alternateBy similarity
Cross-linki123 – 123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3); alternateBy similarity
Modified residuei218 – 2181N6-acetyllysineBy similarity
Modified residuei221 – 2211N6-acetyllysineBy similarity
Modified residuei254 – 2541PhosphothreonineBy similarity
Modified residuei276 – 2761Phosphoserine; by RPS6KA4 and RPS6KA5By similarity
Modified residuei310 – 3101N6-acetyllysine; alternate1 Publication
Modified residuei310 – 3101N6-methyllysine; by SETD6; alternate1 Publication
Modified residuei311 – 3111Phosphoserine; by PKC/PRKCZ2 Publications
Modified residuei433 – 4331PhosphothreonineBy similarity
Modified residuei467 – 4671Phosphoserine; by IKKB and IKKEBy similarity
Modified residuei504 – 5041Phosphothreonine; by CHEK1By similarity
Modified residuei527 – 5271Phosphoserine; by CK2By similarity
Modified residuei534 – 5341Phosphoserine; by IKKBBy similarity

Post-translational modificationi

Ubiquitinated, leading to its proteasomal degradation. Degradation is required for termination of NF-kappa-B response (By similarity).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.2 Publications
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.By similarity3 Publications
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).By similarity
S-nitrosylation of Cys-38 inactivates the enzyme activity.1 Publication
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

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

MaxQBiQ04207.
PaxDbiQ04207.
PRIDEiQ04207.

PTM databases

PhosphoSiteiQ04207.

Expressioni

Gene expression databases

BgeeiQ04207.
ExpressionAtlasiQ04207. baseline and differential.
GenevestigatoriQ04207.

Interactioni

Subunit structurei

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.By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Ctnnb1Q022485EBI-644400,EBI-397872
EHMT1Q9H9B15EBI-644400,EBI-766087From a different organism.
Hdac1O091062EBI-644400,EBI-301912
Nfkb1P257995EBI-644400,EBI-643958
NfkbiaQ9Z1E37EBI-644400,EBI-644427
NfkbibQ607788EBI-644400,EBI-644469
Nr0b2Q622273EBI-644400,EBI-4310440
Nr4a2Q062192EBI-644400,EBI-2337255
SETD6Q8TBK24EBI-644400,EBI-3863032From a different organism.
SETD7Q8WTS62EBI-644400,EBI-1268586From a different organism.
UbcP629912EBI-644400,EBI-413074

Protein-protein interaction databases

BioGridi202853. 31 interactions.
DIPiDIP-6219N.
IntActiQ04207. 23 interactions.
MINTiMINT-236104.

Structurei

Secondary structure

1
549
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi20 – 256Combined sources
Beta strandi30 – 323Combined sources
Turni37 – 393Combined sources
Beta strandi48 – 503Combined sources
Beta strandi53 – 553Combined sources
Beta strandi60 – 656Combined sources
Beta strandi71 – 777Combined sources
Beta strandi79 – 824Combined sources
Beta strandi87 – 926Combined sources
Beta strandi99 – 1035Combined sources
Beta strandi109 – 1124Combined sources
Beta strandi117 – 1204Combined sources
Helixi123 – 1253Combined sources
Helixi126 – 13510Combined sources
Turni145 – 1484Combined sources
Beta strandi156 – 16611Combined sources
Beta strandi168 – 1747Combined sources
Beta strandi178 – 1847Combined sources
Beta strandi186 – 1883Combined sources
Turni189 – 1913Combined sources
Beta strandi196 – 2005Combined sources
Beta strandi202 – 2054Combined sources
Beta strandi211 – 2177Combined sources
Helixi221 – 2233Combined sources
Beta strandi225 – 2306Combined sources
Beta strandi233 – 2364Combined sources
Helixi241 – 2433Combined sources
Beta strandi248 – 2536Combined sources
Beta strandi266 – 2749Combined sources
Turni275 – 2784Combined sources
Beta strandi284 – 2896Combined sources
Helixi294 – 30411Combined sources
Helixi306 – 31510Combined sources
Helixi433 – 4397Combined sources
Beta strandi444 – 4474Combined sources
Turni450 – 4534Combined sources
Helixi459 – 4613Combined sources
Helixi465 – 4673Combined sources
Helixi471 – 4777Combined sources
Beta strandi480 – 4845Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
DisProtiDP00129.
ProteinModelPortaliQ04207.
SMRiQ04207. Positions 20-325, 425-490.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04207.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 306288RHDPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi301 – 3044Nuclear localization signalSequence Analysis

Sequence similaritiesi

Contains 1 RHD (Rel-like) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG119056.
HOGENOMiHOG000230474.
HOVERGENiHBG017916.
InParanoidiQ04207.
KOiK04735.
OMAiEFSPMVF.
OrthoDBiEOG7VHSWT.
PhylomeDBiQ04207.
TreeFamiTF325632.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProiIPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR000451. NF_Rel_Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view]
PfamiPF00554. RHD. 1 hit.
[Graphical view]
PRINTSiPR00057. NFKBTNSCPFCT.
SMARTiSM00429. IPT. 1 hit.
[Graphical view]
SUPFAMiSSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform p65 (identifier: Q04207-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDDLFPLIFP SEPAQASGPY VEIIEQPKQR GMRFRYKCEG RSAGSIPGER
60 70 80 90 100
STDTTKTHPT IKINGYTGPG TVRISLVTKD PPHRPHPHEL VGKDCRDGYY
110 120 130 140 150
EADLCPDRSI HSFQNLGIQC VKKRDLEQAI SQRIQTNNNP FHVPIEEQRG
160 170 180 190 200
DYDLNAVRLC FQVTVRDPAG RPLLLTPVLS HPIFDNRAPN TAELKICRVN
210 220 230 240 250
RNSGSCLGGD EIFLLCDKVQ KEDIEVYFTG PGWEARGSFS QADVHRQVAI
260 270 280 290 300
VFRTPPYADP SLQAPVRVSM QLRRPSDREL SEPMEFQYLP DTDDRHRIEE
310 320 330 340 350
KRKRTYETFK SIMKKSPFNG PTEPRPPTRR IAVPTRNSTS VPKPAPQPYT
360 370 380 390 400
FPASLSTINF DEFSPMLLPS GQISNQALAL APSSAPVLAQ TMVPSSAMVP
410 420 430 440 450
LAQPPAPAPV LTPGPPQSLS APVPKSTQAG EGTLSEALLH LQFDADEDLG
460 470 480 490 500
ALLGNSTDPG VFTDLASVDN SEFQQLLNQG VSMSHSTAEP MLMEYPEAIT
510 520 530 540
RLVTGSQRPP DPAPTPLGTS GLPNGLSGDE DFSSIADMDF SALLSQISS
Length:549
Mass (Da):60,212
Last modified:October 1, 1993 - v1
Checksum:iBDF1673D2FE398B9
GO
Isoform p65 delta (identifier: Q04207-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:539
Mass (Da):59,061
Checksum:iF834FD0302D351BD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281K → N in AAB00795. (PubMed:8918242)Curated
Sequence conflicti61 – 611I → IQKD in AAB00795. (PubMed:8918242)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei222 – 23110Missing in isoform p65 delta. CuratedVSP_005589

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61909 mRNA. Translation: AAA39811.1.
BC003818 mRNA. Translation: AAH03818.1.
L77155 Genomic DNA. Translation: AAB00795.1.
Z22952 Genomic DNA. Translation: CAA80528.1.
CCDSiCCDS29473.1. [Q04207-1]
PIRiA37932.
PC4233.
S48113.
RefSeqiNP_033071.1. NM_009045.4. [Q04207-1]
UniGeneiMm.249966.

Genome annotation databases

EnsembliENSMUST00000025867; ENSMUSP00000025867; ENSMUSG00000024927. [Q04207-1]
GeneIDi19697.
KEGGimmu:19697.
UCSCiuc008gee.1. mouse. [Q04207-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61909 mRNA. Translation: AAA39811.1 .
BC003818 mRNA. Translation: AAH03818.1 .
L77155 Genomic DNA. Translation: AAB00795.1 .
Z22952 Genomic DNA. Translation: CAA80528.1 .
CCDSi CCDS29473.1. [Q04207-1 ]
PIRi A37932.
PC4233.
S48113.
RefSeqi NP_033071.1. NM_009045.4. [Q04207-1 ]
UniGenei Mm.249966.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
2LWW NMR - B 425-490 [» ]
2RAM X-ray 2.40 A/B 19-291 [» ]
DisProti DP00129.
ProteinModelPortali Q04207.
SMRi Q04207. Positions 20-325, 425-490.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202853. 31 interactions.
DIPi DIP-6219N.
IntActi Q04207. 23 interactions.
MINTi MINT-236104.

Chemistry

ChEMBLi CHEMBL5902.

PTM databases

PhosphoSitei Q04207.

Proteomic databases

MaxQBi Q04207.
PaxDbi Q04207.
PRIDEi Q04207.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000025867 ; ENSMUSP00000025867 ; ENSMUSG00000024927 . [Q04207-1 ]
GeneIDi 19697.
KEGGi mmu:19697.
UCSCi uc008gee.1. mouse. [Q04207-1 ]

Organism-specific databases

CTDi 5970.
MGIi MGI:103290. Rela.

Phylogenomic databases

eggNOGi NOG119056.
HOGENOMi HOG000230474.
HOVERGENi HBG017916.
InParanoidi Q04207.
KOi K04735.
OMAi EFSPMVF.
OrthoDBi EOG7VHSWT.
PhylomeDBi Q04207.
TreeFami TF325632.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSi Rela. mouse.
EvolutionaryTracei Q04207.
NextBioi 297048.
PROi Q04207.
SOURCEi Search...

Gene expression databases

Bgeei Q04207.
ExpressionAtlasi Q04207. baseline and differential.
Genevestigatori Q04207.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProi IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR000451. NF_Rel_Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view ]
Pfami PF00554. RHD. 1 hit.
[Graphical view ]
PRINTSi PR00057. NFKBTNSCPFCT.
SMARTi SM00429. IPT. 1 hit.
[Graphical view ]
SUPFAMi SSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEi PS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view ]
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Publicationsi

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  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. 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).

Entry informationi

Entry nameiTF65_MOUSE
AccessioniPrimary (citable) accession number: Q04207
Secondary accession number(s): Q62025
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: November 26, 2014
This is version 164 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3