Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Proto-oncogene c-Rel  

UniProtKB / Swiss-Prot ID :  REL_HUMAN

Gene Name (Synonyms) : 
REL  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus (By similarity). 

Protein Function :  Proto-oncogene that may play a role in differentiation and lymphopoiesis. 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. 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. The NF-kappa-B heterodimer RELA/p65-c-Rel is a transcriptional activator. 

Protein Sequence MASGAYNPYIEIIEQPRQRGMRFRYKCEGRSAGSIPGEHSTDNNRTYPSIQIMNYYGKGKVRITLVTKND...
Predicted Secondary Structure CCCCCCCCEEEEEECCCCCCEEEEEEECCCCCCCCCCCCCCCCCCCCCEEEEECCCCCEEEEEEEEECCC...
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
359PhosphotyrosineGEGRYFKKE
CCCCCCCCC
30.52Phosphositeplus
Link-
492PhosphoserinePNMLSNCSV
HHHHCCCHH
25.64PhosphoELM
Link-
492PhosphoserinePNMLSNCSV
HHHHCCCHH
25.64Phosphositeplus
Link-
503PhosphoserineMTTSSDSMG
HHHHHHCCC
31.45Phosphositeplus
Link-
503Phosphoserine.MTTSSDSMG
HHHHHHCCC
31.45UniProtKB
Link-
523PhosphoserineLENPSCNSV
CCCCCCCEE
37.20Phosphositeplus
Link-
526PhosphoserinePSCNSVLDP
CCCCEEECC
28.52Phosphositeplus
Link-
557PhosphoserineTVFVSQSDA
CCCCCCCHH
16.71Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
NFKB1_HUMANphysical interactionMINT-47884MINT14743216
NFKB1_HUMANphysical interactionMINT-48548MINT14743216
NFKB1_HUMANphysical interactionMINT-48666MINT14743216
M3K8_HUMANphysical interactionMINT-47831MINT14743216
PAPOA_HUMANphysical interactionMINT-47832MINT14743216
NFKB2_HUMANphysical interactionMINT-47915MINT14743216
NFKB2_HUMANphysical interactionMINT-48733MINT14743216
IKBB_HUMANphysical interactionDIP:44783EDIP14743216
NFKB2_HUMANphysical interactionDIP:44823EDIP14743216
NFKB1_HUMANphysical interactionDIP:44832EDIP14743216
NFKB2_HUMANphysical interactionDIP:44844EDIP14743216
IKBE_HUMANphysical interactionDIP:44807EDIP14743216
REL_HUMANphysical interactionEBI-360804
intact14743216
TNIP2_HUMANphysical interactionEBI-365233
intact14743216
Q8NFZ5_HUMANphysical interactionEBI-365233
intact14743216
M3K8_HUMANphysical interactionEBI-365237
intact14743216
PAPOA_HUMANphysical interactionEBI-365241
intact14743216
HS71L_HUMANphysical interactionEBI-360765
intact14743216
UACA_HUMANphysical interactionEBI-360828
intact14743216
FKBP5_HUMANphysical interactionEBI-360831
intact14743216
TBA3C_HUMANphysical interactionEBI-360837
intact14743216
GRP78_HUMANphysical interactionEBI-360768
intact14743216
HSP7C_HUMANphysical interactionEBI-360771
intact14743216
GRP75_HUMANphysical interactionEBI-360774
intact14743216
HSP76_HUMANphysical interactionEBI-360780
intact14743216
HNRH1_HUMANphysical interactionEBI-360783
intact14743216
C1QBP_HUMANphysical interactionEBI-360786
intact14743216
ACTG_HUMANphysical interactionEBI-360798
intact14743216
NFKB1_HUMANphysical interactionEBI-360795
intact14743216
CLH1_HUMANphysical interactionEBI-360801
intact14743216
WDR37_HUMANphysical interactionEBI-360807
intact14743216
Q9UQC1_HUMANphysical interactionEBI-360810
intact14743216
TBB5_HUMANphysical interactionEBI-360816
intact14743216
TBB4_HUMANphysical interactionEBI-360819
intact14743216
G3P_HUMANphysical interactionEBI-360834
intact14743216
CALM_HUMANphysical interactionEBI-360813
intact14743216
CCNE1_HUMANin vitroHPRD:01286HPRD9731206
REL_HUMANin vitro
yeast 2-hybrid
HPRD:01286HPRD11967310
M3K8_HUMANin vitro
in vivo
HPRD:01286HPRD9950430
14743216
IKBB_HUMANin vitro
in vivo
HPRD:01286HPRD14743216
9135156
BCL3_HUMANENSP00000295025STRING
IKBA_HUMANENSP00000295025STRING
CCL2_HUMANENSP00000295025STRING
IL2_HUMANENSP00000295025STRING
IFNG_HUMANENSP00000295025STRING
TBP_HUMANENSP00000295025STRING
IL6_HUMANENSP00000295025STRING
SYT1_HUMANENSP00000295025STRING
IL1A_HUMANENSP00000295025STRING
IKBE_HUMANENSP00000295025STRING
PP4C_HUMANENSP00000295025STRING
CCL5_HUMANENSP00000295025STRING
NFAC3_HUMANENSP00000295025STRING
BCLX_HUMANENSP00000295025STRING
TF65_HUMANENSP00000295025STRING
TF65_HUMANENSP00000295025STRING
IKBB_HUMANENSP00000295025STRING
CD28_HUMANENSP00000295025STRING
SP1_HUMANENSP00000295025STRING
IKKB_HUMANENSP00000295025STRING
MK08_HUMANENSP00000295025STRING
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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
Phosphorylation
ReferencePubMed
"Tumor necrosis factor-alpha activation of NF-kappa B requires thephosphorylation of Ser-471 in the transactivation domain of c-Rel.";
Martin A.G., Fresno M.;
J. Biol. Chem. 275:24383-24391(2000).
Cited for: PHOSPHORYLATION AT SER-503.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures