SET_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SET_RAT
• UniProt AC: Q63945
• Protein Name: Protein SET
• Gene Name: Set
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 289
• Subcellular Localization: Cytoplasm, cytosol. Endoplasmic reticulum. Nucleus, nucleoplasm. In the cytoplasm, found both in the cytosol and associated with the endoplasmic reticulum. The SET complex is associated with the endoplasmic reticulum. Following CTL attack and cleavag
• Protein Description: Multitasking protein, involved in apoptosis, transcription, nucleosome assembly and histone chaperoning. Isoform 2 anti-apoptotic activity is mediated by inhibition of the GZMA-activated DNase, NME1. In the course of cytotoxic T-lymphocyte (CTL)-induced apoptosis, GZMA cleaves SET, disrupting its binding to NME1 and releasing NME1 inhibition. Isoform 1 and isoform 2 are potent inhibitors of protein phosphatase 2A. Isoform 1 and isoform 2 inhibit EP300/CREBBP and PCAF-mediated acetylation of histones (HAT) and nucleosomes, most probably by masking the accessibility of lysines of histones to the acetylases. The predominant target for inhibition is histone H4. HAT inhibition leads to silencing of HAT-dependent transcription and prevents active demethylation of DNA. Both isoforms stimulate DNA replication of the adenovirus genome complexed with viral core proteins; however, isoform 2 specific activity is higher (By similarity)..
• Protein Sequence: MAPKRQSAILPQPKKPRPVAAPKLEDKSASPGLPKGEKEQQEAIEHIDEVQNEIDRLNEQASEEILKVEQKYNKLRQPFFQKRSELIAKIPNFWVTTFVNHPQVSALLGEEDEEALHYLTRVEVTEFEDIKSGYRIDFYFDENPYFENKVLSKEFHLNESGDPSSKSTEIKWKSGKDLTKRSSQTQNKASRKRQHEEPESFFTWFTDHSDAGADELGEVIKDDIWPNPLQYYLVPDMDDEEGEAEDDDDDDEEEEGLEDIDEEGDEDEGEEDDDEDEGEEGEEDEGEDD

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
2	Methylation	------MAPKRQSAI ------CCCCCCCCC	20.51	-
7	Phosphorylation	-MAPKRQSAILPQPK -CCCCCCCCCCCCCC	22.70	23984901
10 (in isoform 2)	Acetylation	-	3.01	-
11 (in isoform 2)	Acetylation	-	42.17	-
15 (in isoform 2)	Phosphorylation	-	53.60	-
23	Acetylation	PRPVAAPKLEDKSAS CCCCCCCCCCCCCCC	60.84	25786129
24 (in isoform 2)	Phosphorylation	-	11.36	-
27	Acetylation	AAPKLEDKSASPGLP CCCCCCCCCCCCCCC	38.25	22902405
28	Phosphorylation	APKLEDKSASPGLPK CCCCCCCCCCCCCCC	46.42	27097102
30	Phosphorylation	KLEDKSASPGLPKGE CCCCCCCCCCCCCCH	26.96	23712012
35	Acetylation	SASPGLPKGEKEQQE CCCCCCCCCHHHHHH	82.07	-
38	Acetylation	PGLPKGEKEQQEAIE CCCCCCHHHHHHHHH	70.28	18530491
62	Phosphorylation	DRLNEQASEEILKVE HHHHHHHHHHHHHHH	35.14	28432305
67	Acetylation	QASEEILKVEQKYNK HHHHHHHHHHHHHHH	49.76	22902405
71	Acetylation	EILKVEQKYNKLRQP HHHHHHHHHHHHHCC	36.97	22902405
82	Acetylation	LRQPFFQKRSELIAK HHCCHHHHHHHHHHH	53.38	22902405
131	Acetylation	VTEFEDIKSGYRIDF EEEEECCCCCEEEEE	50.58	22902405
132	Phosphorylation	TEFEDIKSGYRIDFY EEEECCCCCEEEEEE	41.20	27097102
134	Phosphorylation	FEDIKSGYRIDFYFD EECCCCCEEEEEEEC	16.10	27097102
139	Phosphorylation	SGYRIDFYFDENPYF CCEEEEEEECCCCCH	13.33	-
145	Phosphorylation	FYFDENPYFENKVLS EEECCCCCHHCCEEC	34.80	-
149	Acetylation	ENPYFENKVLSKEFH CCCCHHCCEECEEEE	37.04	22902405
160	Phosphorylation	KEFHLNESGDPSSKS EEEECCCCCCCCCCC	47.63	27097102
166	Acetylation	ESGDPSSKSTEIKWK CCCCCCCCCCEEEEC	66.78	22902405
171	Acetylation	SSKSTEIKWKSGKDL CCCCCEEEECCCCCH	42.19	22902405
176	Acetylation	EIKWKSGKDLTKRSS EEEECCCCCHHHHHH	57.57	22902405

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

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

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
11	K	Acetylation	Isoform 2 is acetylated on Lys-11.	-
15	S	Phosphorylation	Isoform 2 is phosphorylated on Ser-15 and Ser-24.	-
24	S	Phosphorylation	Isoform 2 is phosphorylated on Ser-15 and Ser-24.	-

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of SET_RAT !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS.";
Moser K., White F.M.;
J. Proteome Res. 5:98-104(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASSSPECTROMETRY.
PubMed: 16396499