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Protein Page:
RBPJ (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
RBPJ Transcriptional regulator that plays a central role in Notch signaling, a signaling pathway involved in cell-cell communication that regulates a broad spectrum of cell-fate determinations. Acts as a transcriptional repressor when it is not associated with Notch proteins. When associated with some NICD product of Notch proteins (Notch intracellular domain), it acts as a transcriptional activator that activates transcription of Notch target genes. Probably represses or activates transcription via the recruitment of chromatin remodeling complexes containing histone deacetylase or histone acetylase proteins, respectively. Specifically binds to the immunoglobulin kappa-type J segment recombination signal sequence. Binds specifically to methylated DNA. Interacts with activated NOTCH1, NOTCH2 or NOTCH3. Interacts with MINT/SHARP. This interaction may mediate the recruitment of large corepressor complexes containing proteins such as HDAC1, HDAC2, NCOR2, SAP30, FHL1/KYOT2 and CIR1. Interacts with EP300, MAML1 and PTF1A. Interacts with Epstein-Barr virus EBNA2, EBNA3, EBNA4 and EBNA6. Interacts with RITA/C12orf52, leading to nuclear export, prevent the interaction between RBPJ and NICD product and subsequent down-regulation of the Notch signaling pathway. Belongs to the Su(H) family. 7 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Cell development/differentiation; Transcription factor
Chromosomal Location of Human Ortholog: 4p15.2
Cellular Component: cytoplasm; nucleolus; nucleoplasm; nucleus
Molecular Function: DNA binding; protein binding; sequence-specific DNA binding; transcription factor activity; transcription factor binding
Biological Process: activation of Notch receptor target transcription factor; angiogenesis; epithelial to mesenchymal transition; negative regulation of ossification; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; Notch signaling pathway; positive regulation of BMP signaling pathway; positive regulation of cardiac muscle cell proliferation; positive regulation of transcription from RNA polymerase II promoter; transcription initiation from RNA polymerase II promoter
Disease: Adams-oliver Syndrome 3
Reference #:  Q06330 (UniProtKB)
Alt. Names/Synonyms: CBF-1; CBF1; csl; H-2K binding factor-2; IGKJRB; IGKJRB1; immunoglobulin kappa J region recombination signal binding protein 1; J kappa-recombination signal-binding protein; KBF2; MGC61669; RBP-J; RBP-J kappa; RBP-JK; RBPJ; RBPJK; RBPSUH; recombination signal binding protein for immunoglobulin kappa J region; Recombining binding protein suppressor of hairless; Renal carcinoma antigen NY-REN-30; SUH; suppressor of hairless homolog
Gene Symbols: RBPJ
Molecular weight: 55,637 Da
Basal Isoelectric point: 6.8  Predict pI for various phosphorylation states
CST Pathways:  Notch Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RBPJ

Protein Structure Not Found.
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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment



 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 3 S7‑p _MDHTEGsPAEEPPA
0 6 S18‑p EPPAHAPsPGKFGER
0 1 Y122‑p LNLEGKNyCtAkTLy
0 1 T124‑p LEGKNyCtAkTLyIs
0 3 K126‑ac GKNyCtAkTLyIsDs
0 2 Y129‑p yCtAkTLyIsDsDKR
0 1 S131‑p tAkTLyIsDsDKRKH
0 1 S133‑p kTLyIsDsDKRKHFM
0 1 K175‑ub SKKKQSLkNADLCIA
0 1 S183 NADLCIASGTKVALF
0 1 T185 DLCIASGTKVALFNR
0 4 S230‑p HLLDDDEsEGEEFTV
0 1 T255‑p VKLVCSVtGMALPRL
0 1 K266‑ac LPRLIIRkVDKQTAL
0 4 K315 FQATPCPKEPNKEMI
1 0 T339‑p STDKAEYtFYEGMGP
0 1 T427 QPVQVPVTLVRNDGI
  RBPJ iso7  
- gap
V5 ___MAPVVTGKFGER
Y109 LNLEGKNYCTAKTLY
T111 LEGKNYCTAKTLYIS
K113 GKNYCTAKTLYISDS
Y116 YCTAKTLYISDSDKR
S118 TAKTLYISDSDKRKH
S120 KTLYISDSDKRKHFM
K162 SKKKQSLKNADLCIA
S170 NADLCIASGTKVALF
T172 DLCIASGTKVALFNR
S217 HLLDDDESEGEEFTV
T242 VKLVCSVTGMALPRL
K253 LPRLIIRKVDKQTAL
K302 FQATPCPKEPNKEMI
T326 STDKAEYTFYEGMGP
T414 QPVQVPVTLVRNDGI
  mouse

 
L33 PMDYSEGLSAEERPA
S44 ERPAHAPSAGKFGER
Y148 LNLEGKNYCTAkTLY
T150 LEGKNYCTAkTLYIS
K152‑ac GKNYCTAkTLYISDS
Y155 YCTAkTLYISDSDKR
S157 TAkTLYISDSDKRKH
S159 kTLYISDSDKRKHFM
K201 SKKKQSLKNADLCIA
S209‑p NADLCIAsGtKVALF
T211‑p DLCIAsGtKVALFNR
S256 HLLDDDESEGEEFTV
T281 VKLVCSVTGMALPRL
K292 LPRLIIRKVDKQTAL
K341‑ub FQATPCPkEQNKEMI
T365 STDKAEYTFYEGMGP
T453‑p QPVQVPVtLVRNDGV
  rat

 
- gap
- gap
Y87 LNLEGKNYCTAKTLY
T89 LEGKNYCTAKTLYIS
K91 GKNYCTAKTLYISDS
Y94 YCTAKTLYISDSDKR
S96 TAKTLYISDSDKRKH
S98 KTLYISDSDKRKHFM
K140 SKKKQSLKNADLCIA
S148 NADLCIASGTKVALF
T150 DLCIASGTKVALFNR
S195 HLLDDDESEGEEFTV
T220 VKLVCSVTGMALPRL
K231 LPRLIIRKVDKQTAL
K280 FQATPCPKEQNKEMI
T304 STDKAEYTFYEGMGP
T392 QPVQVPVTLVRNDGI
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