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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
  • chromatin binding Source: UniProtKB
  • chromatin DNA binding Source: UniProtKB
  • 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 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 core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: NTNU_SB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
  • RNA polymerase II distal enhancer sequence-specific DNA binding Source: NTNU_SB
  • RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: UniProtKB
  • sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • transcription regulatory region DNA binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_12555. Downstream TCR signaling.
REACT_13443. Regulated proteolysis of p75NTR.
REACT_13696. NF-kB is activated and signals survival.
REACT_163773. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
REACT_163994. FCERI mediated NF-kB activation.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_188323. CLEC7A (Dectin-1) signaling.
REACT_188330. Dectin-1 mediated noncanonical NF-kB signaling.
REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_23950. Interleukin-1 processing.
REACT_24969. TRAF6 mediated NF-kB activation.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
REACT_355196. IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (EDA-ID) (via TLR).
REACT_355226. IkBA variant leads to EDA-ID.
REACT_355503. CD209 (DC-SIGN) signaling.
REACT_355550. CLEC7A/inflammasome pathway.
SABIO-RKQ04206.
SignaLinkiQ04206.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 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 complex Source: InterPro
  • nucleoplasm Source: GO_Central
  • 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).

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi254 – 2541T → A: Abolishes interaction with PIN1. 1 Publication
Mutagenesisi276 – 2761S → C: Loss of phosphorylation. 1 Publication

Organism-specific databases

Orphaneti251636. Ependymoma.
PharmGKBiPA296.

Polymorphism and mutation databases

BioMutaiRELA.
DMDMi62906901.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 551551Transcription factor p65PRO_0000205169Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Cross-linki37 – 37Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3)
Modified residuei38 – 381Cysteine persulfide; alternateBy similarity
Modified residuei38 – 381S-nitrosocysteine; alternateBy similarity
Modified residuei122 – 1221N6-acetyllysine; by PCAF and EP300; alternate1 Publication
Cross-linki122 – 122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3); alternate
Modified residuei123 – 1231N6-acetyllysine; by PCAF and EP300; alternate1 Publication
Cross-linki123 – 123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO3); alternate
Modified residuei218 – 2181N6-acetyllysine1 Publication
Modified residuei221 – 2211N6-acetyllysine1 Publication
Modified residuei254 – 2541Phosphothreonine1 Publication
Modified residuei276 – 2761Phosphoserine; by RPS6KA4 and RPS6KA51 Publication
Modified residuei281 – 2811Phosphoserine1 Publication
Modified residuei310 – 3101N6-acetyllysine; alternate5 Publications
Modified residuei310 – 3101N6-methyllysine; by SETD6; alternateBy similarity
Modified residuei311 – 3111Phosphoserine; by PKC/PRKCZBy similarity
Modified residuei435 – 4351Phosphothreonine1 Publication
Modified residuei468 – 4681Phosphoserine; by IKKB and IKKE2 Publications
Modified residuei505 – 5051Phosphothreonine; by CHEK11 Publication
Modified residuei529 – 5291Phosphoserine; by CK21 Publication
Modified residuei536 – 5361Phosphoserine; by IKKB1 Publication

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

Keywords - PTMi

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

Proteomic databases

MaxQBiQ04206.
PaxDbiQ04206.
PRIDEiQ04206.

PTM databases

PhosphoSiteiQ04206.

Expressioni

Gene expression databases

BgeeiQ04206.
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 with FOXP3.By similarity1 Publication

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 a different organism.
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 a different organism.
GFI1Q996842EBI-73886,EBI-949368
HDAC1Q135476EBI-73886,EBI-301834
IER3P466956EBI-73886,EBI-1748945
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
NFKB1P198389EBI-73886,EBI-300010
NFKBIAP2596319EBI-73886,EBI-307386
NFKBIBQ156536EBI-73886,EBI-352889
OGTO152942EBI-73886,EBI-539828
P/VP0C7743EBI-73886,EBI-3650423From a different organism.
PDCD4Q53EL66EBI-73886,EBI-935824
PPP2CAP677756EBI-73886,EBI-712311
PPP2R1AP301532EBI-73886,EBI-302388
RELQ048643EBI-10223388,EBI-307352
RELBQ012012EBI-73886,EBI-357837
RPS3P233967EBI-73886,EBI-351193
RPS6KA5O755822EBI-73886,EBI-73869
SETD7Q8WTS610EBI-73886,EBI-1268586
SIRT1Q96EB65EBI-73886,EBI-1802965
SIRT2Q8IXJ62EBI-73886,EBI-477232
SIRT6Q8N6T74EBI-73886,EBI-712415
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 a different organism.
UXTQ9UBK95EBI-73886,EBI-357355

Protein-protein interaction databases

BioGridi111902. 251 interactions.
DIPiDIP-24238N.
IntActiQ04206. 120 interactions.
MINTiMINT-106444.
STRINGi9606.ENSP00000384273.

Structurei

Secondary structure

1
551
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi21 – 255Combined sources
Beta strandi30 – 323Combined sources
Beta strandi39 – 413Combined sources
Beta strandi53 – 553Combined sources
Beta strandi60 – 634Combined sources
Beta strandi68 – 8013Combined sources
Beta strandi87 – 926Combined sources
Beta strandi97 – 1048Combined sources
Beta strandi109 – 1124Combined sources
Beta strandi117 – 1193Combined sources
Helixi123 – 1253Combined sources
Helixi126 – 1294Combined sources
Turni130 – 1378Combined sources
Turni145 – 1484Combined sources
Beta strandi156 – 16611Combined sources
Beta strandi168 – 1736Combined sources
Beta strandi183 – 1886Combined sources
Beta strandi196 – 2005Combined sources
Beta strandi202 – 2054Combined sources
Beta strandi211 – 2177Combined sources
Beta strandi225 – 2306Combined sources
Beta strandi233 – 2386Combined sources
Helixi241 – 2433Combined sources
Turni246 – 2483Combined sources
Beta strandi249 – 2535Combined sources
Beta strandi258 – 2603Combined sources
Beta strandi266 – 2738Combined sources
Turni275 – 2773Combined sources
Beta strandi284 – 2896Combined sources
Helixi294 – 3029Combined sources
Helixi309 – 3113Combined sources
Helixi492 – 4987Combined sources
Turni499 – 5013Combined sources
Beta strandi505 – 5073Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
DisProtiDP00085.
ProteinModelPortaliQ04206.
SMRiQ04206. Positions 20-319, 427-491.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04206.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni415 – 45945Activation domainAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi301 – 3044Nuclear localization signalSequence Analysis
Motifi536 – 54499aaTAD

Domaini

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

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG119056.
GeneTreeiENSGT00500000044765.
HOGENOMiHOG000230474.
HOVERGENiHBG017916.
InParanoidiQ04206.
KOiK04735.
OMAiEFSPMVF.
OrthoDBiEOG7VHSWT.
PhylomeDBiQ04206.
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. NFkB/Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR030495. RelA.
IPR011539. RHD.
IPR030492. RHD_CS.
[Graphical view]
PANTHERiPTHR24169. PTHR24169. 1 hit.
PTHR24169:SF1. PTHR24169:SF1. 1 hit.
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 (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.

« Hide

        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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 491E → R in CAA80524 (PubMed:8281153).Curated
Sequence conflicti180 – 1801S → P in AAA36408 (PubMed:2006423).Curated
Sequence conflicti372 – 3809QISQASALA → RSARPRLG in CAA80524 (PubMed:8281153).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei13 – 2513Missing in isoform 2. 1 PublicationVSP_005587Add
BLAST
Alternative sequencei143 – 1453Missing in isoform 4. 1 PublicationVSP_031245
Alternative sequencei222 – 23110Missing in isoform 3. 1 PublicationVSP_012031
Alternative sequencei506 – 5061Missing in isoform 2. 1 PublicationVSP_005588

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.
GeneIDi5970.
KEGGihsa:5970.
UCSCiuc001off.3. human. [Q04206-1]
uc001ofh.3. human. [Q04206-4]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
SeattleSNPs

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
DisProtiDP00085.
ProteinModelPortaliQ04206.
SMRiQ04206. Positions 20-319, 427-491.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111902. 251 interactions.
DIPiDIP-24238N.
IntActiQ04206. 120 interactions.
MINTiMINT-106444.
STRINGi9606.ENSP00000384273.

Chemistry

BindingDBiQ04206.
ChEMBLiCHEMBL5533.

PTM databases

PhosphoSiteiQ04206.

Polymorphism and mutation databases

BioMutaiRELA.
DMDMi62906901.

Proteomic databases

MaxQBiQ04206.
PaxDbiQ04206.
PRIDEiQ04206.

Protocols and materials databases

DNASUi5970.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000308639; ENSP00000311508; ENSG00000173039. [Q04206-4]
ENST00000406246; ENSP00000384273; ENSG00000173039.
GeneIDi5970.
KEGGihsa:5970.
UCSCiuc001off.3. human. [Q04206-1]
uc001ofh.3. human. [Q04206-4]

Organism-specific databases

CTDi5970.
GeneCardsiGC11M065421.
HGNCiHGNC:9955. RELA.
HPAiCAB004264.
CAB005030.
HPA063461.
MIMi164014. gene.
neXtProtiNX_Q04206.
Orphaneti251636. Ependymoma.
PharmGKBiPA296.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG119056.
GeneTreeiENSGT00500000044765.
HOGENOMiHOG000230474.
HOVERGENiHBG017916.
InParanoidiQ04206.
KOiK04735.
OMAiEFSPMVF.
OrthoDBiEOG7VHSWT.
PhylomeDBiQ04206.
TreeFamiTF325632.

Enzyme and pathway databases

ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_12555. Downstream TCR signaling.
REACT_13443. Regulated proteolysis of p75NTR.
REACT_13696. NF-kB is activated and signals survival.
REACT_163773. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
REACT_163994. FCERI mediated NF-kB activation.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_188323. CLEC7A (Dectin-1) signaling.
REACT_188330. Dectin-1 mediated noncanonical NF-kB signaling.
REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_23950. Interleukin-1 processing.
REACT_24969. TRAF6 mediated NF-kB activation.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
REACT_355196. IKBKG deficiency causes anhidrotic ectodermal dysplasia with immunodeficiency (EDA-ID) (via TLR).
REACT_355226. IkBA variant leads to EDA-ID.
REACT_355503. CD209 (DC-SIGN) signaling.
REACT_355550. CLEC7A/inflammasome pathway.
SABIO-RKQ04206.
SignaLinkiQ04206.

Miscellaneous databases

ChiTaRSiRELA. human.
EvolutionaryTraceiQ04206.
GeneWikiiRELA.
GenomeRNAii5970.
NextBioi23241.
PROiQ04206.
SOURCEiSearch...

Gene expression databases

BgeeiQ04206.
CleanExiHS_RELA.
ExpressionAtlasiQ04206. baseline and differential.
GenevisibleiQ04206. HS.

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. NFkB/Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR030495. RelA.
IPR011539. RHD.
IPR030492. RHD_CS.
[Graphical view]
PANTHERiPTHR24169. PTHR24169. 1 hit.
PTHR24169:SF1. PTHR24169:SF1. 1 hit.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: INTERACTION WITH COMMD1, SUBCELLULAR LOCATION.
  37. Cited for: ACETYLATION AT LYS-310.
  38. "Foxp3 interacts with nuclear factor of activated T cells and NF-kappa B to repress cytokine gene expression and effector functions of T helper cells."
    Bettelli E., Dastrange M., Oukka M.
    Proc. Natl. Acad. Sci. U.S.A. 102:5138-5143(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FOXP3.
  39. "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.
  40. "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.
  41. "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.
  42. "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.
  43. "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.
  44. "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.
  45. "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.
  46. "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.
  47. "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.
  48. "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.
  49. "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.
  50. "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.
  51. "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.
  52. "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.
  53. "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].
  54. "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.
  55. "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.
  56. "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.
  57. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  58. "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.
  59. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  60. Cited for: CHROMOSOMAL TRANSLOCATION WITH C11ORF95.
  61. "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).

Entry informationi

Entry nameiTF65_HUMAN
AccessioniPrimary (citable) accession number: Q04206
Secondary accession number(s): Q6GTV1, Q6SLK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: April 26, 2005
Last modified: July 22, 2015
This is version 187 of the entry and version 2 of the sequence. [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
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.