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UniProtKB - Q04206 (TF65_HUMAN)

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Protein

Transcription factor p65

Gene

RELA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. 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 (PubMed:15790681).8 Publications

GO - Molecular functioni

  • actinin binding Source: UniProtKB
  • activating transcription factor binding Source: BHF-UCL
  • ankyrin repeat binding Source: Ensembl
  • chromatin binding Source: UniProtKB
  • chromatin DNA binding Source: UniProtKB
  • core promoter sequence-specific DNA binding Source: Ensembl
  • DNA binding Source: UniProtKB
  • histone deacetylase binding Source: UniProtKB
  • identical protein binding Source: UniProtKB
  • NF-kappaB binding Source: UniProtKB
  • phosphate ion binding Source: UniProtKB
  • protein complex binding Source: Ensembl
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB
  • repressing transcription factor binding Source: BHF-UCL
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  • RNA polymerase II distal enhancer sequence-specific DNA binding Source: NTNU_SB
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: UniProtKB
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: NTNU_SB
  • transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific binding Source: NTNU_SB
  • transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: NTNU_SB
  • transcription factor activity, RNA polymerase II core promoter sequence-specific Source: BHF-UCL
  • transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • transcription regulatory region DNA binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  • acetaldehyde metabolic process Source: Ensembl
  • aging Source: Ensembl
  • animal organ morphogenesis Source: Ensembl
  • cellular defense response Source: UniProtKB
  • cellular response to hepatocyte growth factor stimulus Source: Ensembl
  • cellular response to hydrogen peroxide Source: UniProtKB
  • cellular response to interleukin-1 Source: UniProtKB
  • cellular response to interleukin-6 Source: BHF-UCL
  • cellular response to lipopolysaccharide Source: Ensembl
  • cellular response to nicotine Source: BHF-UCL
  • cellular response to peptide hormone stimulus Source: BHF-UCL
  • cellular response to peptidoglycan Source: UniProtKB
  • cellular response to tumor necrosis factor Source: UniProtKB
  • cytokine-mediated signaling pathway Source: UniProtKB
  • defense response to virus Source: UniProtKB
  • Fc-epsilon receptor signaling pathway Source: Reactome
  • hair follicle development Source: Ensembl
  • inflammatory response Source: UniProtKB
  • liver development Source: Ensembl
  • membrane protein intracellular domain proteolysis Source: Reactome
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
  • negative regulation of insulin receptor signaling pathway Source: Ensembl
  • negative regulation of NIK/NF-kappaB signaling Source: UniProtKB
  • negative regulation of protein catabolic process Source: Ensembl
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
  • nucleotide-binding oligomerization domain containing 2 signaling pathway Source: MGI
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of chondrocyte differentiation Source: Ensembl
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of interleukin-12 biosynthetic process Source: Ensembl
  • positive regulation of miRNA metabolic process Source: BHF-UCL
  • positive regulation of NF-kappaB transcription factor activity Source: MGI
  • positive regulation of NIK/NF-kappaB signaling Source: CAFA
  • positive regulation of pri-miRNA transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of Schwann cell differentiation Source: Ensembl
  • positive regulation of T cell receptor signaling pathway Source: CAFA
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus Source: UniProtKB
  • positive regulation of type I interferon production Source: Reactome
  • regulation of inflammatory response Source: UniProtKB
  • regulation of NIK/NF-kappaB signaling Source: CAFA
  • regulation of transcription, DNA-templated Source: CAFA
  • response to amino acid Source: Ensembl
  • response to cAMP Source: Ensembl
  • response to cobalamin Source: Ensembl
  • response to drug Source: Ensembl
  • response to insulin Source: Ensembl
  • response to interleukin-1 Source: BHF-UCL
  • response to morphine Source: Ensembl
  • response to muramyl dipeptide Source: Ensembl
  • response to muscle stretch Source: Ensembl
  • response to organic substance Source: UniProtKB
  • response to progesterone Source: Ensembl
  • response to UV-B Source: UniProtKB
  • stimulatory C-type lectin receptor signaling pathway Source: Reactome
  • T cell receptor signaling pathway Source: Reactome
  • tumor necrosis factor-mediated signaling pathway Source: CAFA
  • viral process Source: UniProtKB-KW
Complete GO annotation...

Keywordsi

Molecular functionActivator, DNA-binding
Biological processHost-virus interaction, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1810476. RIP-mediated NFkB activation via ZBP1.
R-HSA-193692. Regulated proteolysis of p75NTR.
R-HSA-202424. Downstream TCR signaling.
R-HSA-209560. NF-kB is activated and signals survival.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-3134963. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
R-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-381340. Transcriptional regulation of white adipocyte differentiation.
R-HSA-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-HSA-446652. Interleukin-1 signaling.
R-HSA-448706. Interleukin-1 processing.
R-HSA-5603027. IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (EDA-ID) (via TLR).
R-HSA-5603029. IkBA variant leads to EDA-ID.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5621575. CD209 (DC-SIGN) signaling.
R-HSA-5660668. CLEC7A/inflammasome pathway.
R-HSA-933542. TRAF6 mediated NF-kB activation.
SABIO-RKiQ04206.
SignaLinkiQ04206.
SIGNORiQ04206.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:9955. RELA.

Subcellular locationi

  • 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 LPS stimulation.By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • I-kappaB/NF-kappaB complex Source: GO_Central
  • NF-kappaB p50/p65 complex Source: CAFA
  • nuclear chromatin Source: BHF-UCL
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • transcription factor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving C11orf95 is found in more than two-thirds of supratentorial ependymomas. Translocation with C11orf95 produces a C11orf95-RELA fusion protein. C11orf95-RELA translocations are potent oncogenes that probably transform neural stem cells by driving an aberrant NF-kappa-B transcription program (PubMed:24553141).1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi254T → A: Abolishes interaction with PIN1. 1 Publication1
Mutagenesisi276S → C: Loss of phosphorylation. 1 Publication1

Organism-specific databases

DisGeNETi5970.
MalaCardsiRELA.
OpenTargetsiENSG00000173039.
Orphaneti251636. Ependymoma.
PharmGKBiPA296.

Chemistry databases

ChEMBLiCHEMBL5533.

Polymorphism and mutation databases

BioMutaiRELA.
DMDMi62906901.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002051691 – 551Transcription factor p65Add BLAST551

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Cross-linki37Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3)1 Publication
Modified residuei38Cysteine persulfide; alternateBy similarity1
Modified residuei38S-nitrosocysteine; alternateBy similarity1
Modified residuei122N6-acetyllysine; by PCAF and EP300; alternate1 Publication1
Cross-linki122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3); alternate
Modified residuei123N6-acetyllysine; by PCAF and EP300; alternate1 Publication1
Cross-linki123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3); alternate
Modified residuei218N6-acetyllysine1 Publication1
Modified residuei221N6-acetyllysine1 Publication1
Modified residuei254Phosphothreonine1 Publication1
Modified residuei276Phosphoserine; by RPS6KA4 and RPS6KA51 Publication1
Modified residuei281Phosphoserine1 Publication1
Modified residuei310N6-acetyllysine; alternateCombined sources4 Publications1
Modified residuei310N6-methyllysine; by SETD6; alternateBy similarity1
Modified residuei311Phosphoserine; by PKC/PRKCZBy similarity1
Modified residuei435Phosphothreonine1 Publication1
Modified residuei468Phosphoserine; by IKKB and IKKE2 Publications1
Modified residuei505Phosphothreonine; by CHEK11 Publication1
Modified residuei529Phosphoserine; by CK21 Publication1
Modified residuei536Phosphoserine; by IKKB2 Publications1

Post-translational modificationi

Ubiquitinated, leading to its proteasomal degradation. Degradation is required for termination of NF-kappa-B response.1 Publication
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 (By similarity).By similarity
Phosphorylation at Ser-311 disrupts the interaction with EHMT1 and promotes transcription factor activity (By similarity). Phosphorylation on Ser-536 stimulates acetylation on Lys-310 and interaction with CBP; the phosphorylated and acetylated forms show enhanced transcriptional activity. Phosphorylation at Ser-276 by RPS6KA4 and RPS6KA5 promotes its transactivation and transcriptional activities.By similarity14 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 SIRT2.5 Publications
S-nitrosylation of Cys-38 inactivates the enzyme activity.By similarity
Sulfhydration at Cys-38 mediates the anti-apoptotic activity by promoting the interaction with RPS3 and activating the transcription factor activity.By similarity
Sumoylation by PIAS3 negatively regulates DNA-bound activated NF-kappa-B.1 Publication
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 (PubMed:18212740).1 Publication

Keywords - PTMi

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

Proteomic databases

EPDiQ04206.
MaxQBiQ04206.
PaxDbiQ04206.
PeptideAtlasiQ04206.
PRIDEiQ04206.

PTM databases

iPTMnetiQ04206.
PhosphoSitePlusiQ04206.
SwissPalmiQ04206.

Expressioni

Gene expression databases

BgeeiENSG00000173039.
CleanExiHS_RELA.
ExpressionAtlasiQ04206. baseline and differential.
GenevisibleiQ04206. HS.

Organism-specific databases

HPAiCAB004264.
CAB005030.
HPA063461.

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 (By similarity). Interacts with NFKBID (By similarity). Interacts with NFKBIA. Interacts with GSK3B. Interacts with NFKBIB (By similarity). Interacts with NFKBIE. Interacts with NFKBIZ. Interacts with EHMT1 (via ANK repeats) (By similarity). 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 UXT. Interacts with MTDH and PHF11. Interacts with ARRB2. Interacts with human respiratory syncytial virus (HRSV) protein M2-1. Interacts with NFKBIA (when phosphorylated), the interaction is direct; phosphorylated NFKBIA is part of a SCF(BTRC)-like complex lacking CUL1. Interacts with RNF25. Interacts (via C-terminus) with DDX1. Interacts with UFL1 and COMMD1. Interacts with BRMS1; this promotes deacetylation of 'Lys-310'. Interacts with NOTCH2 (By similarity). Directly interacts with MEN1; this interaction represses NFKB-mediated transactivation. Interacts with AKIP1, which promotes the phosphorylation and nuclear retention of RELA. 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 (when acetylated at Lys-310) with BRD4; leading to activation of the NF-kappa-B pathway. Interacts with MEFV. Interacts with CLOCK (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 (PubMed:18212740). Interacts with FOXP3. Interacts with CDK5RAP3; stimulates the interaction of RELA with HDAC1, HDAC2 and HDAC3 thereby inhibiting NF-kappa-B transcriptional activity (PubMed:17785205).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-73886,EBI-73886
AATFQ9NY613EBI-73886,EBI-372428
ATF3P18847-35EBI-73886,EBI-9844134
BRD4O608858EBI-73886,EBI-723869
Brd4Q9ESU66EBI-73886,EBI-6260864From Mus musculus.
CDK5RAP3Q96JB54EBI-73886,EBI-718818
CHUKO151112EBI-73886,EBI-81249
COMMD1Q8N6687EBI-73886,EBI-1550112
CREBBPQ927935EBI-73886,EBI-81215
CTNNB1P352222EBI-73886,EBI-491549
DAXXQ9UER75EBI-73886,EBI-77321
DHX9Q082114EBI-73886,EBI-352022
EHMT1Q9H9B13EBI-73886,EBI-766087
ESR1P033727EBI-73886,EBI-78473
GAMMAHV.ORF73O419743EBI-73886,EBI-6933128From Murid herpesvirus 4.
GFI1Q996842EBI-73886,EBI-949368
HDAC1Q135476EBI-73886,EBI-301834
IER3P466956EBI-73886,EBI-1748945
IKBKBO149202EBI-73886,EBI-81266
IRF5Q135684EBI-73886,EBI-3931258
KEAP1Q141454EBI-73886,EBI-751001
KLF6Q996126EBI-73886,EBI-714994
LMO2P257913EBI-73886,EBI-739696
MAPK10P537792EBI-73886,EBI-713543
MEN1O00255-24EBI-73886,EBI-9869387
NFKB1P1983813EBI-73886,EBI-300010
NFKBIAP2596321EBI-73886,EBI-307386
NFKBIBQ156536EBI-73886,EBI-352889
OGTO152942EBI-73886,EBI-539828
P/VP0C7743EBI-73886,EBI-3650423From Measles virus (strain Ichinose-B95a).
PDCD4Q53EL66EBI-73886,EBI-935824
PPP2CAP677756EBI-73886,EBI-712311
PPP2R1AP301532EBI-73886,EBI-302388
RELQ048643EBI-10223388,EBI-307352
RELBQ012012EBI-73886,EBI-357837
RPS3P233968EBI-73886,EBI-351193
RPS6KA5O755822EBI-73886,EBI-73869
SETD7Q8WTS610EBI-73886,EBI-1268586
SIRT1Q96EB65EBI-73886,EBI-1802965
SIRT2Q8IXJ62EBI-73886,EBI-477232
SIRT6Q8N6T74EBI-73886,EBI-712415
SNAI1O958635EBI-73886,EBI-1045459
SOCS1O155242EBI-73886,EBI-968198
STAT3P407634EBI-73886,EBI-518675
TCF4P158843EBI-10223388,EBI-533224
TGM2P219803EBI-73886,EBI-727668
TP53BP2Q136254EBI-73886,EBI-77642
TP53BP2Q13625-26EBI-73886,EBI-287091
UBCP0CG486EBI-73886,EBI-3390054
UL42P102266EBI-73886,EBI-1029310From Human herpesvirus 1 (strain 17).
UXTQ9UBK95EBI-73886,EBI-357355

GO - Molecular functioni

  • actinin binding Source: UniProtKB
  • activating transcription factor binding Source: BHF-UCL
  • ankyrin repeat binding Source: Ensembl
  • histone deacetylase binding Source: UniProtKB
  • identical protein binding Source: UniProtKB
  • NF-kappaB binding Source: UniProtKB
  • protein complex binding Source: Ensembl
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB
  • repressing transcription factor binding Source: BHF-UCL
  • transcription factor binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB
Complete GO annotation...

Protein-protein interaction databases

BioGridi111902. 275 interactors.
DIPiDIP-24238N.
IntActiQ04206. 135 interactors.
MINTiMINT-106444.
STRINGi9606.ENSP00000384273.

Chemistry databases

BindingDBiQ04206.

Structurei

Secondary structure

1551
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi21 – 25Combined sources5
Beta strandi30 – 32Combined sources3
Beta strandi39 – 41Combined sources3
Beta strandi53 – 55Combined sources3
Beta strandi60 – 63Combined sources4
Beta strandi68 – 80Combined sources13
Beta strandi87 – 92Combined sources6
Beta strandi97 – 104Combined sources8
Beta strandi109 – 112Combined sources4
Beta strandi117 – 119Combined sources3
Helixi123 – 125Combined sources3
Helixi126 – 129Combined sources4
Turni130 – 137Combined sources8
Turni145 – 148Combined sources4
Beta strandi156 – 166Combined sources11
Beta strandi168 – 173Combined sources6
Beta strandi183 – 188Combined sources6
Beta strandi196 – 200Combined sources5
Beta strandi202 – 205Combined sources4
Beta strandi211 – 217Combined sources7
Beta strandi225 – 230Combined sources6
Beta strandi233 – 238Combined sources6
Helixi241 – 243Combined sources3
Turni246 – 248Combined sources3
Beta strandi249 – 253Combined sources5
Beta strandi258 – 260Combined sources3
Beta strandi266 – 273Combined sources8
Turni275 – 277Combined sources3
Beta strandi284 – 289Combined sources6
Helixi294 – 302Combined sources9
Helixi309 – 311Combined sources3
Helixi313 – 323Combined sources11
Beta strandi330 – 335Combined sources6
Beta strandi338 – 342Combined sources5
Helixi358 – 360Combined sources3
Helixi361 – 369Combined sources9
Helixi388 – 406Combined sources19
Beta strandi528 – 530Combined sources3
Helixi532 – 536Combined sources5
Helixi537 – 546Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NFIX-ray2.70A/C20-320[»]
2LSPNMR-A304-316[»]
2O61X-ray2.80A20-291[»]
3GUTX-ray3.59A/C/E/G20-291[»]
3QXYX-ray2.09P/Q302-316[»]
3RC0X-ray2.19P/Q302-316[»]
4KV1X-ray1.50C/D308-314[»]
4KV4X-ray2.00B308-314[»]
5U4KNMR-B521-551[»]
5URNNMR-B521-551[»]
DisProtiDP00085.
ProteinModelPortaliQ04206.
SMRiQ04206.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04206.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini19 – 306RHDPROSITE-ProRule annotationAdd BLAST288

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni415 – 459Activation domainAdd BLAST45

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi301 – 304Nuclear localization signalSequence analysis4
Motifi536 – 5449aaTAD9

Domaini

the 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.1 Publication

Phylogenomic databases

eggNOGiENOG410IG8F. Eukaryota.
ENOG410XT64. LUCA.
GeneTreeiENSGT00500000044765.
HOGENOMiHOG000230474.
HOVERGENiHBG017916.
InParanoidiQ04206.
KOiK04735.
OMAiEFSPMVF.
OrthoDBiEOG091G08JD.
PhylomeDBiQ04206.
TreeFamiTF325632.

Family and domain databases

CDDicd01177. IPT_NFkappaB. 1 hit.
Gene3Di2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProiView protein in InterPro
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR033926. IPT_NFkappaB.
IPR000451. NFkB/Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR030495. RelA.
IPR030492. RHD_CS.
IPR032397. RHD_dimer.
IPR011539. RHD_DNA_bind_dom.
PANTHERiPTHR24169. PTHR24169. 1 hit.
PTHR24169:SF23. PTHR24169:SF23. 1 hit.
PfamiView protein in Pfam
PF16179. RHD_dimer. 1 hit.
PF00554. RHD_DNA_bind. 1 hit.
PRINTSiPR00057. NFKBTNSCPFCT.
SMARTiView protein in SMART
SM00429. IPT. 1 hit.
SUPFAMiSSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiView protein in PROSITE
PS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q04206-1) [UniParc]FASTAAdd to basket
Also known as: p65

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.

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        10         20         30         40         50
MDELFPLIFP AEPAQASGPY VEIIEQPKQR GMRFRYKCEG RSAGSIPGER 
        60         70         80         90        100
STDTTKTHPT IKINGYTGPG TVRISLVTKD PPHRPHPHEL VGKDCRDGFY 
       110        120        130        140        150
EAELCPDRCI HSFQNLGIQC VKKRDLEQAI SQRIQTNNNP FQVPIEEQRG 
       160        170        180        190        200
DYDLNAVRLC FQVTVRDPSG RPLRLPPVLS 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 SIMKKSPFSG PTDPRPPPRR IAVPSRSSAS VPKPAPQPYP 
       360        370        380        390        400
FTSSLSTINY DEFPTMVFPS GQISQASALA PAPPQVLPQA PAPAPAPAMV 
       410        420        430        440        450
SALAQAPAPV PVLAPGPPQA VAPPAPKPTQ AGEGTLSEAL LQLQFDDEDL 
       460        470        480        490        500
GALLGNSTDP AVFTDLASVD NSEFQQLLNQ GIPVAPHTTE PMLMEYPEAI 
       510        520        530        540        550
TRLVTGAQRP PDPAPAPLGA PGLPNGLLSG DEDFSSIADM DFSALLSQIS 

S
Length:551
Mass (Da):60,219
Last modified:April 26, 2005 - v2
Checksum:i8147A6AF9F2445C6
GO
Isoform 2 (identifier: Q04206-2) [UniParc]FASTAAdd to basket
Also known as: p65 delta 2

The sequence of this isoform differs from the canonical sequence as follows:
     13-25: Missing.
     506-506: Missing.

Show »
Length:537
Mass (Da):58,807
Checksum:iA1F26DF2F53E662E
GO
Isoform 3 (identifier: Q04206-3) [UniParc]FASTAAdd to basket
Also known as: p65 delta

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

Show »
Length:541
Mass (Da):59,068
Checksum:i49F0493E19798AD1
GO
Isoform 4 (identifier: Q04206-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     143-145: Missing.

Note: No experimental confirmation available.
Show »
Length:548
Mass (Da):59,910
Checksum:iED40EF8B91F0A19A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti49E → R in CAA80524 (PubMed:8281153).Curated1
Sequence conflicti180S → P in AAA36408 (PubMed:2006423).Curated1
Sequence conflicti372 – 380QISQASALA → RSARPRLG in CAA80524 (PubMed:8281153).Curated9

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00558713 – 25Missing in isoform 2. 1 PublicationAdd BLAST13
Alternative sequenceiVSP_031245143 – 145Missing in isoform 4. 1 Publication3
Alternative sequenceiVSP_012031222 – 231Missing in isoform 3. 1 Publication10
Alternative sequenceiVSP_005588506Missing in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62399 mRNA. Translation: AAA36408.1.
Z22948
, Z22949, Z22953, Z22950, Z22951 Genomic DNA. Translation: CAA80524.2.
L19067 mRNA. Translation: AAA20946.1.
BC033522 mRNA. Translation: AAH33522.1.
AY455868 Genomic DNA. Translation: AAR13863.1.
CCDSiCCDS31609.1. [Q04206-1]
CCDS44651.1. [Q04206-4]
PIRiA40851.
I53719.
S51782. A42017.
RefSeqiNP_001138610.1. NM_001145138.1. [Q04206-4]
NP_001230913.1. NM_001243984.1.
NP_068810.3. NM_021975.3. [Q04206-1]
UniGeneiHs.502875.

Genome annotation databases

EnsembliENST00000308639; ENSP00000311508; ENSG00000173039. [Q04206-4]
ENST00000406246; ENSP00000384273; ENSG00000173039. [Q04206-1]
GeneIDi5970.
KEGGihsa:5970.
UCSCiuc001ofg.4. human. [Q04206-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiTF65_HUMAN
AccessioniPrimary (citable) accession number: Q04206
Secondary accession number(s): Q6GTV1, Q6SLK1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: April 26, 2005
Last modified: July 5, 2017
This is version 209 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references