SUH_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SUH_MOUSE
• UniProt AC: P31266
• Protein Name: Recombining binding protein suppressor of hairless
• Gene Name: Rbpj {ECO:0000312|MGI:MGI:96522}
• Organism: Mus musculus (Mouse).
• Sequence Length: 526
• Subcellular Localization: Nucleus. Cytoplasm. Mainly nuclear, upon interaction with RITA1, translocates to the cytoplasm, down-regulating the Notch signaling pathway..
• Protein Description: 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. [PubMed: 7566092 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. Binds to the oxygen responsive element of COX4I2 and activates its transcription under hypoxia conditions (4% oxygen) (By similarity Negatively regulates the phagocyte oxidative burst in response to bacterial infection by repressing transcription of NADPH oxidase subunits]
• Protein Sequence: MPSGFPQSPRTSPRARPKTRITGALPMDYSEGLSAEERPAHAPSAGKFGERPPPKRLTREAMRNYLKERGDQTVLILHAKVAQKSYGNEKRFFCPPPCVYLMGSGWKKKKEQMERDGCSEQESQPCAFIGIGNSDQEMQQLNLEGKNYCTAKTLYISDSDKRKHFMLSVKMFYGNSDDIGVFLSKRIKVISKPSKKKQSLKNADLCIASGTKVALFNRLRSQTVSTRYLHVEGGNFHASSQQWGAFYIHLLDDDESEGEEFTVRDGYIHYGQTVKLVCSVTGMALPRLIIRKVDKQTALLDADDPVSQLHKCAFYLKDTERMYLCLSQERIIQFQATPCPKEQNKEMINDGASWTIISTDKAEYTFYEGMGPVLAPVTPVPVVESLQLNGGGDVAMLELTGQNFTPNLRVWFGDVEAETMYRCGESMLCVVPDISAFREGWRWVRQPVQVPVTLVRNDGVIYSTSLTFTYTPEPGPRPHCSAAGAILRANSSQVPSNESNTNSEGNYTNASTNSTSVTSSTATVVS

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MPSGFPQSPRTSPRA CCCCCCCCCCCCCCC	19.31	25266776
8 (in isoform 2)	Acetylation	-	19.31	-
11	Phosphorylation	GFPQSPRTSPRARPK CCCCCCCCCCCCCCC	46.60	29514104
12	Phosphorylation	FPQSPRTSPRARPKT CCCCCCCCCCCCCCC	17.42	25338131
152	Acetylation	GKNYCTAKTLYISDS CCCCEEEEEEEEECC	22.40	7609865
194	Phosphorylation	IKVISKPSKKKQSLK EEEECCCCCCCHHHC	61.92	29176673
201	Acetylation	SKKKQSLKNADLCIA CCCCHHHCCCCEEEE	56.17	23806337
209	Phosphorylation	NADLCIASGTKVALF CCCEEEECCCHHHHH	27.38	-
211	Phosphorylation	DLCIASGTKVALFNR CEEEECCCHHHHHHH	21.61	-
221	Phosphorylation	ALFNRLRSQTVSTRY HHHHHHHCCCCCEEE	34.49	25338131
256	Phosphorylation	HLLDDDESEGEEFTV EEECCCCCCCCEEEE	58.87	21082442
267	Phosphorylation	EFTVRDGYIHYGQTV EEEEECCEEECCCEE	6.71	25367039
341	Ubiquitination	FQATPCPKEQNKEMI EECCCCCHHHCHHHC	77.86	22790023
453	Phosphorylation	QPVQVPVTLVRNDGV CCCCCEEEEEECCCE	17.29	-
480	Glutathionylation	EPGPRPHCSAAGAIL CCCCCCCCCHHHHHH	3.07	24333276

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SUH_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SUH_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SUH_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMRD3_MOUSE	Smarcd3	physical	17210915
NOTC1_MOUSE	Notch1	physical	17210915
NOTC1_MOUSE	Notch1	physical	11518718
NOTC2_MOUSE	Notch2	physical	11518718
NOTC3_MOUSE	Notch3	physical	11518718
NOTC4_MOUSE	Notch4	physical	11518718

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.