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Q04206 (TF65_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 172. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length551 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. 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.15 Ref.25 Ref.42 Ref.46 Ref.50 Ref.51 Ref.55

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 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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.22 Ref.23 Ref.25 Ref.26 Ref.27 Ref.28 Ref.31 Ref.32 Ref.36 Ref.38 Ref.39 Ref.40 Ref.42 Ref.43 Ref.44 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.53 Ref.55

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 LPS stimulation. Ref.25 Ref.36 Ref.50 Ref.55

Domain

the 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors. Ref.6 Ref.45

Post-translational modification

Ubiquitinated, leading to its proteasomal degradation. Degradation is required for termination of NF-kappa-B response. Ref.30

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.

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. Ref.13 Ref.17 Ref.22 Ref.23 Ref.27 Ref.29 Ref.33 Ref.34 Ref.35 Ref.41

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. Ref.19 Ref.21 Ref.24 Ref.37 Ref.42 Ref.51 Ref.54

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. Ref.57

Sequence similarities

Contains 1 RHD (Rel-like) domain.

Ontologies

Keywords
   Biological processHost-virus interaction
Transcription
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_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-independent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

T cell receptor signaling pathway

Traceable author statement. Source: Reactome

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

acetaldehyde metabolic process

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from electronic annotation. Source: Ensembl

cellular defense response

Non-traceable author statement PubMed 8717528. Source: UniProtKB

cellular response to hydrogen peroxide

Inferred from direct assay PubMed 21830064. Source: UniProtKB

cellular response to interleukin-1

Inferred from direct assay PubMed 18073330. Source: UniProtKB

cellular response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

cellular response to tumor necrosis factor

Inferred from direct assay PubMed 18073330PubMed 23091055. Source: UniProtKB

cytokine-mediated signaling pathway

Inferred from direct assay PubMed 15876188. Source: UniProtKB

defense response to virus

Non-traceable author statement PubMed 8717528. Source: UniProtKB

hair follicle development

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Inferred from direct assay PubMed 12924514. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

liver development

Inferred from electronic annotation. Source: Ensembl

membrane protein intracellular domain proteolysis

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Inferred from direct assay PubMed 10747850PubMed 23091055. Source: UniProtKB

negative regulation of extrinsic apoptotic signaling pathway

Inferred from mutant phenotype PubMed 21310825. Source: BHF-UCL

negative regulation of insulin receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein catabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 17350185. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

nucleotide-binding oligomerization domain containing 2 signaling pathway

Inferred from direct assay PubMed 12527755. Source: MGI

organ morphogenesis

Inferred from electronic annotation. Source: Ensembl

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

Inferred from expression pattern PubMed 12761501. Source: UniProtKB

positive regulation of NF-kappaB transcription factor activity

Inferred from direct assay PubMed 15790681. Source: MGI

positive regulation of Schwann cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from direct assay PubMed 23091055. Source: UniProtKB

positive regulation of chondrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-12 biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 17350185PubMed 23091055. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 17350185PubMed 18073330. Source: UniProtKB

positive regulation of type I interferon production

Traceable author statement. Source: Reactome

regulation of inflammatory response

Inferred from sequence or structural similarity. Source: UniProtKB

response to UV-B

Inferred from direct assay PubMed 15616591. Source: UniProtKB

response to amino acid

Inferred from electronic annotation. Source: Ensembl

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 interleukin-1

Inferred from genetic interaction PubMed 15489227. Source: BHF-UCL

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 electronic annotation. Source: Ensembl

response to organic substance

Inferred from direct assay PubMed 10747850. Source: UniProtKB

response to progesterone

Inferred from electronic annotation. Source: Ensembl

toll-like receptor 10 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 5 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 3091258. Source: GOC

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 21830064PubMed 3140380. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 21474709. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 17350185Ref.50PubMed 21474709PubMed 21830064PubMed 3140380. Source: UniProtKB

transcription factor complex

Inferred from direct assay PubMed 12048232. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay PubMed 18073330PubMed 23091055. Source: UniProtKB

NF-kappaB binding

Inferred from physical interaction PubMed 8441377. Source: UniProtKB

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

Inferred from direct assay PubMed 3091258. Source: UniProtKB

activating transcription factor binding

Inferred from physical interaction PubMed 15489227. Source: BHF-UCL

chromatin binding

Inferred from direct assay Ref.50. Source: UniProtKB

identical protein binding

Inferred from direct assay PubMed 9437432. Source: UniProtKB

phosphate ion binding

Inferred from direct assay Ref.13. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction PubMed 7739562. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.13PubMed 15465828. Source: UniProtKB

repressing transcription factor binding

Inferred from physical interaction Ref.16. Source: BHF-UCL

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 12048232. Source: UniProtKB

transcription factor binding

Inferred from physical interaction PubMed 10849440. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from direct assay PubMed 17350185. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction Ref.25. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q04206-1)

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.
Isoform 2 (identifier: Q04206-2)

Also known as: p65 delta 2;

The sequence of this isoform differs from the canonical sequence as follows:
     13-25: Missing.
     506-506: Missing.
Isoform 3 (identifier: Q04206-3)

Also known as: p65 delta;

The sequence of this isoform differs from the canonical sequence as follows:
     222-231: Missing.
Isoform 4 (identifier: Q04206-4)

The sequence of this isoform differs from the canonical sequence as follows:
     143-145: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 551551Transcription factor p65
PRO_0000205169

Regions

Domain19 – 306288RHD
Region415 – 45945Activation domain
Motif301 – 3044Nuclear localization signal Potential
Motif536 – 54499aaTAD

Amino acid modifications

Modified residue11N-acetylmethionine Ref.58
Modified residue381Cysteine persulfide; alternate By similarity
Modified residue381S-nitrosocysteine; alternate By similarity
Modified residue1221N6-acetyllysine; by PCAF and EP300; alternate Ref.24
Modified residue1231N6-acetyllysine; by PCAF and EP300; alternate Ref.24
Modified residue2181N6-acetyllysine Ref.21
Modified residue2211N6-acetyllysine Ref.21
Modified residue2541Phosphothreonine Ref.27
Modified residue2761Phosphoserine; by RPS6KA4 and RPS6KA5 Ref.23
Modified residue2811Phosphoserine Probable
Modified residue3101N6-acetyllysine; alternate Ref.21 Ref.37 Ref.42 Ref.51 Ref.52
Modified residue3101N6-methyllysine; by SETD6; alternate By similarity
Modified residue3111Phosphoserine; by PKC/PRKCZ By similarity
Modified residue4351Phosphothreonine Ref.29
Modified residue4681Phosphoserine; by IKKB and IKKE Ref.34 Ref.41
Modified residue5051Phosphothreonine; by CHEK1 Ref.33
Modified residue5291Phosphoserine; by CK2 Ref.17
Modified residue5361Phosphoserine; by IKKB Ref.13
Cross-link37Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3) Ref.57
Cross-link122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3); alternate Ref.57
Cross-link123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3); alternate Ref.57

Natural variations

Alternative sequence13 – 2513Missing in isoform 2.
VSP_005587
Alternative sequence143 – 1453Missing in isoform 4.
VSP_031245
Alternative sequence222 – 23110Missing in isoform 3.
VSP_012031
Alternative sequence5061Missing in isoform 2.
VSP_005588

Experimental info

Mutagenesis2541T → A: Abolishes interaction with PIN1. Ref.27
Mutagenesis2761S → C: Loss of phosphorylation. Ref.23
Sequence conflict491E → R in CAA80524. Ref.2
Sequence conflict1801S → P in AAA36408. Ref.1
Sequence conflict372 – 3809QISQASALA → RSARPRLG in CAA80524. Ref.2

Secondary structure

............................................................ 551
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (p65) [UniParc].

Last modified April 26, 2005. Version 2.
Checksum: 8147A6AF9F2445C6

FASTA55160,219
        10         20         30         40         50         60 
MDELFPLIFP AEPAQASGPY VEIIEQPKQR GMRFRYKCEG RSAGSIPGER STDTTKTHPT 

        70         80         90        100        110        120 
IKINGYTGPG TVRISLVTKD PPHRPHPHEL VGKDCRDGFY EAELCPDRCI HSFQNLGIQC 

       130        140        150        160        170        180 
VKKRDLEQAI SQRIQTNNNP FQVPIEEQRG DYDLNAVRLC FQVTVRDPSG RPLRLPPVLS 

       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 SIMKKSPFSG PTDPRPPPRR IAVPSRSSAS VPKPAPQPYP FTSSLSTINY 

       370        380        390        400        410        420 
DEFPTMVFPS GQISQASALA PAPPQVLPQA PAPAPAPAMV SALAQAPAPV PVLAPGPPQA 

       430        440        450        460        470        480 
VAPPAPKPTQ AGEGTLSEAL LQLQFDDEDL GALLGNSTDP AVFTDLASVD NSEFQQLLNQ 

       490        500        510        520        530        540 
GIPVAPHTTE PMLMEYPEAI TRLVTGAQRP PDPAPAPLGA PGLPNGLLSG DEDFSSIADM 

       550 
DFSALLSQIS S 

« Hide

Isoform 2 (p65 delta 2) [UniParc].

Checksum: A1F26DF2F53E662E
Show »

FASTA53758,807
Isoform 3 (p65 delta) [UniParc].

Checksum: 49F0493E19798AD1
Show »

FASTA54159,068
Isoform 4 [UniParc].

Checksum: ED40EF8B91F0A19A
Show »

FASTA54859,910

References

« Hide 'large scale' references
[1]"Isolation of a rel-related human cDNA that potentially encodes the 65-kD subunit of NF-kappa B."
Ruben S.M., Dillon P.J., Schreck R., Henkel T., Chen C.-H., Maher M., Baeuerle P.A., Rosen C.A.
Science 251:1490-1493(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"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], ALTERNATIVE SPLICING.
[3]"An alternatively spliced transcript, p65 delta 2, of the gene encoding the p65 subunit of the transcription factor NF-kappa B."
Lyle R., Valleley E.M., Sharpe P.T., Hewitt J.E.
Gene 138:265-266(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Bone.
[4]"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 4).
Tissue: Colon.
[5]SeattleSNPs variation discovery resource
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 4-551.
[6]"Functional characterization of the NF-kappa B p65 transcriptional activator and an alternatively spliced derivative."
Ruben S.M., Narayanan R., Klement J.F., Chen C.-H., Rosen C.A.
Mol. Cell. Biol. 12:444-454(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 214-239 (ISOFORMS 1/2 AND 3), ACTIVATION DOMAIN.
[7]"A novel complex between the p65 subunit of NF-kappa B and c-Rel binds to a DNA element involved in the phorbol ester induction of the human urokinase gene."
Hansen S.K., Nerlov C., Zabel U., Verde P., Johnsen M., Baeuerle P.A., Blasi F.
EMBO J. 11:205-213(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE NF-KAPPA-B P65-P50 COMPLEX, IDENTIFICATION IN THE NF-KAPPA-B P65-C-REL COMPLEX.
[8]"I kappa B/MAD-3 masks the nuclear localization signal of NF-kappa B p65 and requires the transactivation domain to inhibit NF-kappa B p65 DNA binding."
Ganchi P.A., Sun S.C., Greene W.C., Ballard D.W.
Mol. Biol. Cell 3:1339-1352(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NFKBIA.
[9]"Activation of multiple NF-kappa B/Rel DNA-binding complexes by tumor necrosis factor."
Beg A.A., Baldwin A.S. Jr.
Oncogene 9:1487-1492(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE NF-KAPPA-B P65-C-REL COMPLEX, IDENTIFICATION IN THE NF-KAPPA-B P65-P52 COMPLEX.
[10]"Regulation of intercellular adhesion molecule-1 gene by tumor necrosis factor-alpha is mediated by the nuclear factor-kappaB heterodimers p65/p65 and p65/c-Rel in the absence of p50."
Aoudjit F., Brochu N., Belanger B., Stratowa C., Hiscott J., Audette M.
Cell Growth Differ. 8:335-342(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE NF-KAPPA-B P65-P65 COMPLEX, IDENTIFICATION IN THE NF-KAPPA-B P65-C-REL COMPLEX.
[11]"A new member of the IkappaB protein family, IkappaB epsilon, inhibits RelA (p65)-mediated NF-kappaB transcription."
Li Z., Nabel G.J.
Mol. Cell. Biol. 17:6184-6190(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NFKBIE.
[12]"IKAP is a scaffold protein of the IkappaB kinase complex."
Cohen L., Henzel W.J., Baeuerle P.A.
Nature 395:292-296(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH CHUK; IKBKB; NFKBIA; IKBKAP AND MAP3K14.
[13]"IkappaB kinases phosphorylate NF-kappaB p65 subunit on serine 536 in the transactivation domain."
Sakurai H., Chiba H., Miyoshi H., Sugita T., Toriumi W.
J. Biol. Chem. 274:30353-30356(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-536.
[14]"NF-kappaB subunit p65 binds to 53BP2 and inhibits cell death induced by 53BP2."
Yang J.-P., Hori M., Takahashi N., Kawabe T., Kato H., Okamoto T.
Oncogene 18:5177-5186(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INTERACTION WITH TP53BP2.
[15]"Yersinia enterocolitica invasin protein triggers IL-8 production in epithelial cells via activation of Rel p65-p65 homodimers."
Schulte R., Grassl G.A., Preger S., Fessele S., Jacobi C.A., Schaller M., Nelson P.J., Autenrieth I.B.
FASEB J. 14:1471-1484(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE NF-KAPPA-B P65-P65 COMPLEX.
[16]"Inhibition of nuclear factor-kappaB-mediated transcription by association with the amino-terminal enhancer of split, a Groucho-related protein lacking WD40 repeats."
Tetsuka T., Uranishi H., Imai H., Ono T., Sonta S., Takahashi N., Asamitsu K., Okamoto T.
J. Biol. Chem. 275:4383-4390(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AES AND TLE1.
[17]"Tumor necrosis factor alpha-induced phosphorylation of RelA/p65 on Ser529 is controlled by casein kinase II."
Wang D., Westerheide S.D., Hanson J.L., Baldwin A.S. Jr.
J. Biol. Chem. 275:32592-32597(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-529.
[18]"The tumor suppressor protein menin interacts with NF-kappaB proteins and inhibits NF-kappaB-mediated transactivation."
Heppner C., Bilimoria K.Y., Agarwal S.K., Kester M., Whitty L.J., Guru S.C., Chandrasekharappa S.C., Collins F.S., Spiegel A.M., Marx S.J., Burns A.L.
Oncogene 20:4917-4925(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MEN1.
[19]"Duration of nuclear NF-kappaB action regulated by reversible acetylation."
Chen L.F., Fischle W., Verdin E., Greene W.C.
Science 293:1653-1657(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION, INTERACTION WITH HDAC3.
[20]"A novel protein overexpressed in hepatoma accelerates export of NF-kappa B from the nucleus and inhibits p53-dependent apoptosis."
Higashitsuji H., Higashitsuji H., Nagao T., Nonoguchi K., Fujii S., Itoh K., Fujita J.
Cancer Cell 2:335-346(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ETHE1.
[21]"Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB."
Chen L.F., Mu Y., Greene W.C.
EMBO J. 21:6539-6548(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-218; LYS-221 AND LYS-310.
[22]"The phosphorylation status of nuclear NF-kappa B determines its association with CBP/p300 or HDAC-1."
Zhong H., May M.J., Jimi E., Ghosh S.
Mol. Cell 9:625-636(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBP AND HDAC1, PHOSPHORYLATION.
[23]"Transcriptional activation of the NF-kappaB p65 subunit by mitogen- and stress-activated protein kinase-1 (MSK1)."
Vermeulen L., De Wilde G., Van Damme P., Vanden Berghe W., Haegeman G.
EMBO J. 22:1313-1324(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RPS6KA5, MUTAGENESIS OF SER-276, PHOSPHORYLATION AT SER-276.
[24]"Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65."
Kiernan R., Bres V., Ng R.W., Coudart M.-P., El Messaoudi S., Sardet C., Jin D.-Y., Emiliani S., Benkirane M.
J. Biol. Chem. 278:2758-2766(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-122 AND LYS-123.
[25]"RING finger protein AO7 supports NF-kappaB-mediated transcription by interacting with the transactivation domain of the p65 subunit."
Asamitsu K., Tetsuka T., Kanazawa S., Okamoto T.
J. Biol. Chem. 278:26879-26887(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RNF25.
[26]"Glycogen synthase kinase-3 beta regulates NF-kappa B1/p105 stability."
Demarchi F., Bertoli C., Sandy P., Schneider C.
J. Biol. Chem. 278:39583-39590(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GSK3B.
[27]"Regulation of NF-kappaB signaling by Pin1-dependent prolyl isomerization and ubiquitin-mediated proteolysis of p65/RelA."
Ryo A., Suizu F., Yoshida Y., Perrem K., Liou Y.C., Wulf G., Rottapel R., Yamaoka S., Lu K.P.
Mol. Cell 12:1413-1426(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-254, INTERACTION WITH PIN1 AND SOCS1, MUTAGENESIS OF THR-254.
[28]"Identification of a ZU5 and death domain-containing inhibitor of NF-kappaB."
Zhang J., Xu L.-G., Han K.-J., Shu H.-B.
J. Biol. Chem. 279:17819-17825(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UNC5CL.
[29]"Suppression of MEK/ERK signaling pathway enhances cisplatin-induced NF-kappaB activation by protein phosphatase 4-mediated NF-kappaB p65 Thr dephosphorylation."
Yeh P.Y., Yeh K.H., Chuang S.E., Song Y.C., Cheng A.L.
J. Biol. Chem. 279:26143-26148(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-435.
[30]"Degradation of promoter-bound p65/RelA is essential for the prompt termination of the nuclear factor kappaB response."
Saccani S., Marazzi I., Beg A.A., Natoli G.
J. Exp. Med. 200:107-113(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[31]"Identification of beta-arrestin2 as a G protein-coupled receptor-stimulated regulator of NF-kappaB pathways."
Gao H., Sun Y., Wu Y., Luan B., Wang Y., Qu B., Pei G.
Mol. Cell 14:303-317(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARRB2.
[32]"The candidate tumour suppressor protein ING4 regulates brain tumour growth and angiogenesis."
Garkavtsev I., Kozin S.V., Chernova O., Xu L., Winkler F., Brown E., Barnett G.H., Jain R.K.
Nature 428:328-332(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ING4.
[33]"Regulation of NF-kappaB and p53 through activation of ATR and Chk1 by the ARF tumour suppressor."
Rocha S., Garrett M.D., Campbell K.J., Schumm K., Perkins N.D.
EMBO J. 24:1157-1169(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-505.
[34]"IKKbeta phosphorylates p65 at S468 in transactivation domain 2."
Schwabe R.F., Sakurai H.
FASEB J. 19:1758-1760(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-468.
[35]"cis-acting, element-specific transcriptional activity of differentially phosphorylated nuclear factor-kappa B."
Anrather J., Racchumi G., Iadecola C.
J. Biol. Chem. 280:244-252(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-281.
[36]"COMMD proteins, a novel family of structural and functional homologs of MURR1."
Burstein E., Hoberg J.E., Wilkinson A.S., Rumble J.M., Csomos R.A., Komarck C.M., Maine G.N., Wilkinson J.C., Mayo M.W., Duckett C.S.
J. Biol. Chem. 280:22222-22232(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COMMD1, SUBCELLULAR LOCATION.
[37]"NF-kappaB RelA phosphorylation regulates RelA acetylation."
Chen L.F., Williams S.A., Mu Y., Nakano H., Duerr J.M., Buckbinder L., Greene W.C.
Mol. Cell. Biol. 25:7966-7975(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-310.
[38]"Respiratory syncytial virus M2-1 protein induces the activation of nuclear factor kappa B."
Reimers K., Buchholz K., Werchau H.
Virology 331:260-268(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HRSV PROTEIN M2-1.
[39]"Activation of the nuclear factor kappaB pathway by astrocyte elevated gene-1: implications for tumor progression and metastasis."
Emdad L., Sarkar D., Su Z.-Z., Randolph A., Boukerche H., Valerie K., Fisher P.B.
Cancer Res. 66:1509-1516(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MTDH.
[40]"Human ubiquitin specific protease 31 is a deubiquitinating enzyme implicated in activation of nuclear factor-kappaB."
Tzimas C., Michailidou G., Arsenakis M., Kieff E., Mosialos G., Hatzivassiliou E.G.
Cell. Signal. 18:83-92(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH USP48.
[41]"Inducible phosphorylation of NF-kappa B p65 at serine 468 by T cell costimulation is mediated by IKK epsilon."
Mattioli I., Geng H., Sebald A., Hodel M., Bucher C., Kracht M., Schmitz M.L.
J. Biol. Chem. 281:6175-6183(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-468.
[42]"Breast cancer metastasis suppressor 1 functions as a corepressor by enhancing histone deacetylase 1-mediated deacetylation of RelA/p65 and promoting apoptosis."
Liu Y., Smith P.W., Jones D.R.
Mol. Cell. Biol. 26:8683-8696(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BRMS1, FUNCTION, ACETYLATION AT LYS-310.
[43]"Coactivator-associated arginine methyltransferase-1 enhances nuclear factor-kappaB-mediated gene transcription through methylation of histone H3 at arginine 17."
Miao F., Li S., Chavez V., Lanting L., Natarajan R.
Mol. Endocrinol. 20:1562-1573(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CARM1.
[44]"IL-1 receptor-associated kinase 1 is critical for latent membrane protein 1-induced p65/RelA serine 536 phosphorylation and NF-kappaB activation."
Song Y.J., Jen K.Y., Soni V., Kieff E., Cahir-McFarland E.
Proc. Natl. Acad. Sci. U.S.A. 103:2689-2694(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE NF-KAPPA-B P65-P52 COMPLEX.
[45]"Nine-amino-acid transactivation domain: establishment and prediction utilities."
Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M.
Genomics 89:756-768(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN.
[46]"UXT is a novel and essential cofactor in the NF-kappaB transcriptional enhanceosome."
Sun S., Tang Y., Lou X., Zhu L., Yang K., Zhang B., Shi H., Wang C.
J. Cell Biol. 178:231-244(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH UXT.
[47]"The familial Mediterranean fever protein, pyrin, is cleaved by caspase-1 and activates NF-kappaB through its N-terminal fragment."
Chae J.J., Wood G., Richard K., Jaffe H., Colburn N.T., Masters S.L., Gumucio D.L., Shoham N.G., Kastner D.L.
Blood 112:1794-1803(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MEFV.
[48]"Functional characterization of the atopy-associated gene PHF11."
Clarke E., Rahman N., Page N., Rolph M.S., Stewart G.J., Jones G.J.
J. Allergy Clin. Immunol. 121:1148-1154(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PHF11.
[49]"AKIP1 enhances NF-kappaB-dependent gene expression by promoting the nuclear retention and phosphorylation of p65."
Gao N., Asamitsu K., Hibi Y., Ueno T., Okamoto T.
J. Biol. Chem. 283:7834-7843(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AKIP1.
[50]"The DEAD-box RNA helicase DDX1 interacts with RelA and enhances nuclear factor kappaB-mediated transcription."
Ishaq M., Ma L., Wu X., Mu Y., Pan J., Hu J., Hu T., Fu Q., Guo D.
J. Cell. Biochem. 106:296-305(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DDX1, SUBCELLULAR LOCATION.
[51]"Brd4 coactivates transcriptional activation of NF-kappaB via specific binding to acetylated RelA."
Huang B., Yang X.D., Zhou M.M., Ozato K., Chen L.F.
Mol. Cell. Biol. 29:1375-1387(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BRD4, ACETYLATION AT LYS-310.
[52]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[53]"A novel LZAP-binding protein, NLBP, inhibits cell invasion."
Kwon J., Cho H.J., Han S.H., No J.G., Kwon J.Y., Kim H.
J. Biol. Chem. 285:12232-12240(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UFL1.
[54]"SIRT2 regulates NF-kappaB dependent gene expression through deacetylation of p65 Lys310."
Rothgiesser K.M., Erener S., Waibel S., Luscher B., Hottiger M.O.
J. Cell Sci. 123:4251-4258(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: DEACETYLATION BY SIRT2.
[55]"Zinc finger protein Gfi1 controls the endotoxin-mediated Toll-like receptor inflammatory response by antagonizing NF-kappaB p65."
Sharif-Askari E., Vassen L., Kosan C., Khandanpour C., Gaudreau M.C., Heyd F., Okayama T., Jin J., Rojas M.E., Grimes H.L., Zeng H., Moroy T.
Mol. Cell. Biol. 30:3929-3942(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GFI1, SUBCELLULAR LOCATION, INDUCTION, FUNCTION.
[56]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[57]"NF-kappaB repression by PIAS3 mediated RelA SUMOylation."
Liu Y., Bridges R., Wortham A., Kulesz-Martin M.
PLoS ONE 7:E37636-E37636(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-37; LYS-122 AND LYS-123 BY PIAS3.
[58]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[59]"Structure of an IkappaBalpha/NF-kappaB complex."
Jacobs M.D., Harrison S.C.
Cell 95:749-758(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M62399 mRNA. Translation: AAA36408.1.
Z22948 expand/collapse EMBL AC list , 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.
PIRA40851.
I53719.
A42017. S51782.
RefSeqNP_001138610.1. NM_001145138.1.
NP_001230913.1. NM_001243984.1.
NP_068810.3. NM_021975.3.
UniGeneHs.502875.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
DisProtDP00085.
ProteinModelPortalQ04206.
SMRQ04206. Positions 20-319, 427-491.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111902. 220 interactions.
DIPDIP-24238N.
IntActQ04206. 99 interactions.
MINTMINT-106444.
STRING9606.ENSP00000384273.

Chemistry

BindingDBQ04206.
ChEMBLCHEMBL5533.

PTM databases

PhosphoSiteQ04206.

Polymorphism databases

DMDM62906901.

Proteomic databases

PaxDbQ04206.
PRIDEQ04206.

Protocols and materials databases

DNASU5970.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308639; ENSP00000311508; ENSG00000173039. [Q04206-4]
ENST00000406246; ENSP00000384273; ENSG00000173039. [Q04206-1]
GeneID5970.
KEGGhsa:5970.
UCSCuc001off.3. human. [Q04206-1]
uc001ofh.3. human. [Q04206-4]

Organism-specific databases

CTD5970.
GeneCardsGC11M065421.
HGNCHGNC:9955. RELA.
HPACAB004264.
CAB005030.
MIM164014. gene.
neXtProtNX_Q04206.
PharmGKBPA296.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG119056.
HOGENOMHOG000230474.
HOVERGENHBG017916.
InParanoidQ04206.
KOK04735.
OMAEFSPMVF.
OrthoDBEOG7VHSWT.
PhylomeDBQ04206.
TreeFamTF325632.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_120956. Cellular responses to stress.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.
SABIO-RKQ04206.
SignaLinkQ04206.

Gene expression databases

ArrayExpressQ04206.
BgeeQ04206.
CleanExHS_RELA.
GenevestigatorQ04206.

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. human.
EvolutionaryTraceQ04206.
GeneWikiRELA.
GenomeRNAi5970.
NextBio23241.
PROQ04206.
SOURCESearch...

Entry information

Entry nameTF65_HUMAN
AccessionPrimary (citable) accession number: Q04206
Secondary accession number(s): Q6GTV1, Q6SLK1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: April 26, 2005
Last modified: April 16, 2014
This is version 172 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM