Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Transcription factor p65  

UniProtKB / Swiss-Prot ID :  TF65_HUMAN

Gene Name (Synonyms) : 
RELA, NFKB3  

Species :  Homo sapiens (Human). 

Subcellular Localization :  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 sti 

Protein Function :  NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed 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. 

Protein Sequence MDELFPLIFPAEPAQASGPYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINGYTGPG...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCEEEEEEECCCCCCEEEEEECCCCCCCCCCCCCCCCCCCCCEEEEECCCCCE...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
37N6-methyllysineRFRYKCEGR
EEEEEECCC
22.89Phosphositeplus
Link
38S-nitrosocysteineFRYKCEGRS
EEEEECCCC
5.06dbSNO
Link
56Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TDTTKTHPT
CCCCCCCCE
47.10Phosphositeplus
Link
62Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)HPTIKINGY
CCEEEEECC
32.37Phosphositeplus
Link
66Nitrated tyrosineKINGYTGPG
EEECCCCCE
12.20HPRD
Link
79Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SLVTKDPPH
EEEECCCCC
61.84Phosphositeplus
Link
122Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IQCVKKRDL
EEECCCCCH
50.12Phosphositeplus
Link
122N6-acetyllysineIQCVKKRDL
EEECCCCCH
50.12HPRD
Link
122N6-acetyllysineIQCVKKRDL
EEECCCCCH
50.12HPRD
Link
122N6-acetyllysineIQCVKKRDL
EEECCCCCH
50.12Phosphositeplus
Link
122N6-acetyllysine; by PCAF and EP300.IQCVKKRDL
EEECCCCCH
50.12UniProtKB
Link
123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QCVKKRDLE
EECCCCCHH
30.65Phosphositeplus
Link
123N6-acetyllysineQCVKKRDLE
EECCCCCHH
30.65HPRD
Link
123N6-acetyllysineQCVKKRDLE
EECCCCCHH
30.65HPRD
Link
123N6-acetyllysineQCVKKRDLE
EECCCCCHH
30.65Phosphositeplus
Link
123N6-acetyllysine; by PCAF and EP300.QCVKKRDLE
EECCCCCHH
30.65UniProtKB
Link
152Nitrated tyrosineQRGDYDLNA
CCCCCCEEE
25.75HPRD
Link
195Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TAELKICRV
CCCCEEEEE
31.12Phosphositeplus
Link
205PhosphoserineRNSGSCLGG
CCCCCCCCC
13.14Phosphositeplus
Link
218N6-acetyllysineLLCDKVQKE
EEECEECCC
45.64HPRD
Link
218N6-acetyllysineLLCDKVQKE
EEECEECCC
45.64HPRD
Link
218N6-acetyllysineLLCDKVQKE
EEECEECCC
45.64Phosphositeplus
Link
221N6-acetyllysineDKVQKEDIE
CEECCCCEE
61.41HPRD
Link
221N6-acetyllysineDKVQKEDIE
CEECCCCEE
61.41HPRD
Link
221N6-acetyllysineDKVQKEDIE
CEECCCCEE
61.41Phosphositeplus
Link
254PhosphothreonineIVFRTPPYA
EEEECCCCC
19.70PhosphoELM
Link
254PhosphothreonineIVFRTPPYA
EEEECCCCC
19.70Phosphositeplus
Link
254Phosphothreonine.IVFRTPPYA
EEEECCCCC
19.70UniProtKB
Link
276PhosphoserineLRRPSDREL
EEECCCCCC
47.70Phosphositeplus
Link
276Phosphoserine (PRKACA)LRRPSDREL
EEECCCCCC
47.70HPRD
Link
276Phosphoserine (RSK-5)LRRPSDREL
EEECCCCCC
47.70PhosphoELM
Link
276Phosphoserine; by RPS6KA4 and RPS6KA5.LRRPSDREL
EEECCCCCC
47.70UniProtKB
Link
281PhosphoserineDRELSEPME
CCCCCCCCC
34.60Phosphositeplus
Link
310DeacetyllysineYETFKSIMK
CHHHHHHHC
46.63HPRD
Link
310Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YETFKSIMK
CHHHHHHHC
46.63Phosphositeplus
Link
310N6-acetyllysineYETFKSIMK
CHHHHHHHC
46.63HPRD
Link
310N6-acetyllysineYETFKSIMK
CHHHHHHHC
46.63HPRD
Link
310N6-acetyllysineYETFKSIMK
CHHHHHHHC
46.63Phosphositeplus
Link
310N6-acetyllysine; alternate.YETFKSIMK
CHHHHHHHC
46.63UniProtKB
Link
310N6-methyllysineYETFKSIMK
CHHHHHHHC
46.63Phosphositeplus
Link
311PhosphoserineETFKSIMKK
HHHHHHHCC
24.59Phosphositeplus
Link
311Phosphoserine (PKC_zeta)ETFKSIMKK
HHHHHHHCC
24.59PhosphoELM
Link
311Phosphoserine (PRKCZ)ETFKSIMKK
HHHHHHHCC
24.59HPRD
Link
314Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KSIMKKSPF
HHHHCCCCC
48.72Phosphositeplus
Link-
314N6-acetyllysineKSIMKKSPF
HHHHCCCCC
48.72Phosphositeplus
Link-
314N6-methyllysineKSIMKKSPF
HHHHCCCCC
48.72Phosphositeplus
Link-
315Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SIMKKSPFS
HHHCCCCCC
46.08Phosphositeplus
Link-
315N6-acetyllysineSIMKKSPFS
HHHCCCCCC
46.08Phosphositeplus
Link-
315N6-methyllysineSIMKKSPFS
HHHCCCCCC
46.08Phosphositeplus
Link-
322O-linked (GlcNAc)FSGPTDPRP
CCCCCCCCC
63.26Phosphositeplus
Link-
352O-linked (GlcNAc)PYPFTSSLS
CCCCCCCCC
16.95Phosphositeplus
Link-
435PhosphothreonineAGEGTLSEA
CCCCCCCCC
23.86Phosphositeplus
Link-
435Phosphothreonine (MAPK1)AGEGTLSEA
CCCCCCCCC
23.86PhosphoELM
Link-
435Phosphothreonine.AGEGTLSEA
CCCCCCCCC
23.86UniProtKB
Link-
468PhosphoserineTDLASVDNS
CCCCCCCCC
36.98Phosphositeplus
Link-
468Phosphoserine (GSK-3_beta)TDLASVDNS
CCCCCCCCC
36.98PhosphoELM
Link-
468Phosphoserine; by IKKB and IKKE.TDLASVDNS
CCCCCCCCC
36.98UniProtKB
Link-
505PhosphothreonineTRLVTGAQR
CCCCCCCCC
31.24PhosphoELM
Link-
505PhosphothreonineTRLVTGAQR
CCCCCCCCC
31.24Phosphositeplus
Link-
505Phosphothreonine; by CHEK1.TRLVTGAQR
CCCCCCCCC
31.24UniProtKB
Link-
529PhosphoserineNGLLSGDED
CCCCCCCCC
49.60Phosphositeplus
Link-
529Phosphoserine (CK2_group;CK2_alpha)NGLLSGDED
CCCCCCCCC
49.60PhosphoELM
Link-
529Phosphoserine; by CK2.NGLLSGDED
CCCCCCCCC
49.60UniProtKB
Link-
536PhosphoserineEDFSSIADM
CCCCCHHHH
23.07Phosphositeplus
Link-
536Phosphoserine (CHUK)EDFSSIADM
CCCCCHHHH
23.07HPRD
Link-
536Phosphoserine (IKK_group;IKK_beta;IKK_beta;IKK_alpha;IKK_epsilon;)EDFSSIADM
CCCCCHHHH
23.07PhosphoELM
Link-
536Phosphoserine; by IKKB.EDFSSIADM
CCCCCHHHH
23.07UniProtKB
Link-
543Phosphoserine (CSNK2A1)DMDFSALLS
HHHHHHHHH
17.47HPRD
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SOCS1_HUMANphysical interactionMINT-4140922MINT17183367
SOCS1_HUMANphysical interactionMINT-4140944MINT17183367
KS6A5_HUMANphysical interactionMINT-50068MINT12628924
GCR_HUMANphysical interactionMINT-17323MINT8290595
NCF1_HUMANphysical interactionMINT-58635MINT12618429
KAPCA_HUMANphosphorylation reactionMINT-50026MINT9150141
IKBA_HUMANphysical interactionMINT-15640MINT9566883
UBIQ_HUMANphysical interactionMINT-4140700MINT17183367
UBIQ_HUMANphysical interactionMINT-4140715MINT17183367
CSK21_HUMANphysical interactionMINT-50090MINT10938077
CSK21_HUMANphosphorylation reactionMINT-50130MINT10938077
TF2B_HUMANphysical interactionMINT-62399MINT15013781
EP300_HUMANphysical interactionMINT-14250MINT9096323
ASPP2_HUMANphysical interactionMINT-15956MINT10498867
ASPP2_HUMANphysical interactionMINT-15955MINT10498867
ASPP2_HUMANphysical interactionMINT-15958MINT10498867
ASPP2_HUMANphysical interactionMINT-15957MINT10498867
CBP_HUMANphysical interactionMINT-16221MINT9096323
CBP_HUMANphysical interactionMINT-17007MINT9660950
CBP_HUMANphysical interactionMINT-14853MINT9096323
CBP_HUMANphysical interactionMINT-16220MINT9096323
CBP_HUMANphysical interactionMINT-17005MINT9660950
CBP_HUMANphysical interactionMINT-17006MINT9660950
PCAF_HUMANphysical interactionMINT-50175MINT11931769
NCOR2_HUMANphysical interactionMINT-15036MINT10777532
NCOA3_HUMANphysical interactionMINT-2834593MINT16456540
MEN1_HUMANphysical interaction
physical interaction
DIP:40178EDIP11526476
11526476
NFKB2_HUMANphysical interactionDIP:44826EDIP14743216
NFKB1_HUMANphysical interactionDIP:44841EDIP14743216
IKBE_HUMANphysical interactionDIP:44878EDIP14743216
REL_HUMANphysical interactionDIP:44767EDIP14743216
IKBA_HUMANphysical interactionDIP:44779EDIP14743216
AKP8L_HUMANphysical interactionDIP:44929EDIP14743216
TF65_HUMANphysical interactionEBI-697798
intact8246997
KS6A5_HUMANphysical interactionEBI-73901
intact12628924
COMD1_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical int
EBI-1551238
EBI-1551147
EBI-1
intact14685242
14685242
15799966
15799966
15799966
15799966
15799966
IKBB_HUMANphysical interaction
physical interaction
EBI-1551167
EBI-1551147
intact14685242
14685242
NFKB1_HUMANphysical interactionEBI-1550577
intact15799966
AATF_HUMANphysical interaction
physical interaction
physical interaction
EBI-1181003
EBI-1180984
EBI-1
intact17157788
17157788
17157788
RS3_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
physical interaction
physical interaction
EBI-1566406
EBI-1566520
EBI-1
intact18045535
18045535
18045535
18045535
18045535
18045535
HDAC1_HUMANdirect interaction
direct interaction
physical interaction
physical interaction
physical interaction
EBI-904590
EBI-904570
EBI-904
intact11931769
11931769
11931769
11931769
16291753
ATF3_HUMANdirect interaction
direct interaction
physical interaction
physical interaction
EBI-981345
EBI-981395
EBI-981
intact16291753
16291753
16291753
16291753
CBP_HUMANdirect interaction
physical interaction
physical interaction
EBI-981475
EBI-981537
EBI-981
intact16291753
16291753
16291753
EP300_HUMANphysical interactionEBI-981234
intact16291753
RRP5_HUMANphysical interactionEBI-300049
intact14624448
RFC1_HUMANin vitro
in vivo
HPRD:01241HPRD12509469
STAT3_HUMANin vitro
in vivo
HPRD:01241HPRD12057007
PML_HUMANin vitro
in vivo
HPRD:01241HPRD12540841
BRCA1_HUMANin vitro
in vivo
HPRD:01241HPRD12700228
CEBPD_HUMANin vivoHPRD:01241HPRD9570146
MEN1_HUMANin vitro
in vivo
HPRD:01241HPRD11526476
EGR1_HUMANin vitroHPRD:01241HPRD10671503
GCR_HUMANin vitro
in vivo
HPRD:01241HPRD10995388
7659084
8290595
FUS_HUMANin vitro
in vivo
HPRD:01241HPRD11278855
IRF1_HUMANin vivoHPRD:01241HPRD8746784
IRF2_HUMANin vitroHPRD:01241HPRD8550813
HMGB1_HUMANin vitro
in vivo
HPRD:01241HPRD12665595
IKBA_HUMANin vivoHPRD:01241HPRD9566883
NFKB2_HUMANin vivoHPRD:01241HPRD8413211
REL_HUMANin vitroHPRD:01241HPRD8152812
1740106
M3K8_HUMANin vitro
in vivo
HPRD:01241HPRD9950430
14743216
BTK_HUMANin vitroHPRD:01241HPRD15849198
STAT1_HUMANin vivoHPRD:01241HPRD16481475
MP2K6_HUMANin vitroHPRD:01241HPRD16498455
STAT6_HUMANin vitroHPRD:01241HPRD9584180
M3K7_HUMANin vitroHPRD:01241HPRD16498455
IRF3_HUMANin vivoHPRD:01241HPRD14557267
FAF1_HUMANin vitro
in vivo
HPRD:01241HPRD14600157
IKBE_HUMANin vitro
in vivo
HPRD:01241HPRD9315679
14743216
AKAP8_HUMANin vitroHPRD:01241HPRD14743216
TBK1_HUMANin vitroHPRD:01241HPRD14560022
ACL6A_HUMANin vitroHPRD:01241HPRD14743216
RELB_HUMANin vitroHPRD:01241HPRD14743216
DHX9_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:01241HPRD15355351
TNR1A_HUMANENSP00000311508STRING
TNR1A_HUMANENSP00000311508STRING
BCL3_HUMANENSP00000311508STRING
BCL3_HUMANENSP00000311508STRING
SIRT1_HUMANENSP00000311508STRING
SIRT1_HUMANENSP00000311508STRING
GA45B_HUMANENSP00000311508STRING
GA45B_HUMANENSP00000311508STRING
IKBA_HUMANENSP00000311508STRING
IKBA_HUMANENSP00000311508STRING
IL2_HUMANENSP00000311508STRING
IL2_HUMANENSP00000311508STRING
BIRC2_HUMANENSP00000311508STRING
BIRC2_HUMANENSP00000311508STRING
TBP_HUMANENSP00000311508STRING
TBP_HUMANENSP00000311508STRING
AHR_HUMANENSP00000311508STRING
AHR_HUMANENSP00000311508STRING
IL6_HUMANENSP00000311508STRING
IL6_HUMANENSP00000311508STRING
SYT1_HUMANENSP00000311508STRING
SYT1_HUMANENSP00000311508STRING
HDAC9_HUMANENSP00000311508STRING
HDAC9_HUMANENSP00000311508STRING
CBP_HUMANENSP00000311508STRING
CBP_HUMANENSP00000311508STRING
M3K8_HUMANENSP00000311508STRING
M3K8_HUMANENSP00000311508STRING
EP300_HUMANENSP00000311508STRING
EP300_HUMANENSP00000311508STRING
IL1A_HUMANENSP00000311508STRING
IL1A_HUMANENSP00000311508STRING
IL1B_HUMANENSP00000311508STRING
IL1B_HUMANENSP00000311508STRING
BIRC3_HUMANENSP00000311508STRING
BIRC3_HUMANENSP00000311508STRING
PCAF_HUMANENSP00000311508STRING
PCAF_HUMANENSP00000311508STRING
ICAM1_HUMANENSP00000311508STRING
ICAM1_HUMANENSP00000311508STRING
AKT1_HUMANENSP00000311508STRING
AKT1_HUMANENSP00000311508STRING
IKBE_HUMANENSP00000311508STRING
IKBE_HUMANENSP00000311508STRING
CHK1_HUMANENSP00000311508STRING
CHK1_HUMANENSP00000311508STRING
PP4C_HUMANENSP00000311508STRING
PP4C_HUMANENSP00000311508STRING
ETHE1_HUMANENSP00000311508STRING
ETHE1_HUMANENSP00000311508STRING
REL_HUMANENSP00000311508STRING
REL_HUMANENSP00000311508STRING
SNIP1_HUMANENSP00000311508STRING
SNIP1_HUMANENSP00000311508STRING
BCLX_HUMANENSP00000311508STRING
BCLX_HUMANENSP00000311508STRING
HDAC3_HUMANENSP00000311508STRING
HDAC3_HUMANENSP00000311508STRING
CEBPB_HUMANENSP00000311508STRING
CEBPB_HUMANENSP00000311508STRING
CXL10_HUMANENSP00000311508STRING
CXL10_HUMANENSP00000311508STRING
IL8_HUMANENSP00000311508STRING
IL8_HUMANENSP00000311508STRING
IRF2_HUMANENSP00000311508STRING
IRF2_HUMANENSP00000311508STRING
IKBB_HUMANENSP00000311508STRING
IKBB_HUMANENSP00000311508STRING
TRAF6_HUMANENSP00000311508STRING
TRAF6_HUMANENSP00000311508STRING
SP1_HUMANENSP00000311508STRING
SP1_HUMANENSP00000311508STRING
MEN1_HUMANENSP00000311508STRING
MEN1_HUMANENSP00000311508STRING
IKKB_HUMANENSP00000311508STRING
IKKB_HUMANENSP00000311508STRING
RINI_HUMANENSP00000311508STRING
RINI_HUMANENSP00000311508STRING
NCOR2_HUMANENSP00000311508STRING
NCOR2_HUMANENSP00000311508STRING
MK08_HUMANENSP00000311508STRING
MK08_HUMANENSP00000311508STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Acetylation of RelA at discrete sites regulates distinct nuclearfunctions of NF-kappaB.";
Chen L.F., Mu Y., Greene W.C.;
EMBO J. 21:6539-6548(2002).
Cited for: ACETYLATION AT LYS-218; LYS-221 AND LYS-310.
"Post-activation turn-off of NF-kappa B-dependent transcription isregulated 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).
Cited for: ACETYLATION AT LYS-122 AND LYS-123.
"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).
Cited for: ACETYLATION AT LYS-310.
"Breast cancer metastasis suppressor 1 functions as a corepressor byenhancing histone deacetylase 1-mediated deacetylation of RelA/p65 andpromoting apoptosis.";
Liu Y., Smith P.W., Jones D.R.;
Mol. Cell. Biol. 26:8683-8696(2006).
Cited for: INTERACTION WITH BRMS1, FUNCTION, AND ACETYLATION AT LYS-310.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-310, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"IkappaB kinases phosphorylate NF-kappaB p65 subunit on serine 536 inthe transactivation domain.";
Sakurai H., Chiba H., Miyoshi H., Sugita T., Toriumi W.;
J. Biol. Chem. 274:30353-30356(1999).
Cited for: PHOSPHORYLATION AT SER-536.
"Tumor necrosis factor alpha-induced phosphorylation of RelA/p65 onSer529 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).
Cited for: PHOSPHORYLATION AT SER-529.
"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).
Cited for: INTERACTION WITH RPS6KA5, MUTAGENESIS OF SER-276, AND PHOSPHORYLATIONAT SER-276.
"Regulation of NF-kappaB signaling by Pin1-dependent prolylisomerization 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).
Cited for: PHOSPHORYLATION AT THR-254, INTERACTION WITH PIN1 AND SOCS1, ANDMUTAGENESIS OF THR-254.
"Suppression of MEK/ERK signaling pathway enhances cisplatin-inducedNF-kappaB activation by protein phosphatase 4-mediated NF-kappaB p65Thr dephosphorylation.";
Yeh P.Y., Yeh K.H., Chuang S.E., Song Y.C., Cheng A.L.;
J. Biol. Chem. 279:26143-26148(2004).
Cited for: PHOSPHORYLATION AT THR-435.
"Regulation of NF-kappaB and p53 through activation of ATR and Chk1 bythe ARF tumour suppressor.";
Rocha S., Garrett M.D., Campbell K.J., Schumm K., Perkins N.D.;
EMBO J. 24:1157-1169(2005).
Cited for: PHOSPHORYLATION AT THR-505.
"IKKbeta phosphorylates p65 at S468 in transactivaton domain 2.";
Schwabe R.F., Sakurai H.;
FASEB J. 19:1758-1760(2005).
Cited for: PHOSPHORYLATION AT SER-468.
"Inducible phosphorylation of NF-kappa B p65 at serine 468 by T cellcostimulation 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).
Cited for: PHOSPHORYLATION AT SER-468.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures