PIAS4_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PIAS4_MOUSE
• UniProt AC: Q9JM05
• Protein Name: E3 SUMO-protein ligase PIAS4
• Gene Name: Pias4
• Organism: Mus musculus (Mouse).
• Sequence Length: 507
• Subcellular Localization: Nucleus, PML body . Colocalizes with SUMO1 and TCF7L2/TCF4 and LEF1 in a subset of PML (promyelocytic leukemia) nuclear bodies. Accumulates in the cytoplasm upon treatment with UVB and TNF-alpha.
• Protein Description: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53/TP53 pathway, the Wnt pathway and the steroid hormone signaling pathway. Involved in gene silencing. Mediates sumoylation of CEBPA, PARK7, HERC2, MYB, TCF4 and RNF168. In Wnt signaling, represses LEF1 and enhances TCF4 transcriptional activities through promoting their sumoylations. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation (By similarity)..
• Protein Sequence: MAAELVEAKNMVMSFRVSDLQMLLGFVGRSKSGLKHELVTRALQLVQFDCSPELFKKIKELYETRYAKKSAEPGPQAPRPLDPLALHSMPRTPLSGPTVDYPVLYGKYLNGLGRLPTKTLKPEVRLVKLPFFNMLDELLKPTELVPQSAEKLQESPCIFALTPRQVEMIRNSRELQPGVKAVQVVLRICYSDTSCPQEDQYPPNIAVKVNHSYCSVPGYYPSNKPGVEPKRPCRPINLTHLMYLSSATNRITVTWGNYGKSYSVALYLVRQLTSSDLLQRLKTIGVKHPELCKALVKEKLRLDPDSEIATTGVRVSLICPLVKMRLSVPCRAETCAHLQCFDAVFYLQMNEKKPTWMCPVCDKPAAYDQLIIDGLLSKILSECEGADEIEFLAEGSWRPIRAEKEPSCSPQGPILVLGTSDANGLAPASSTPGIGSGLSGPGSAGSGAGAAGSLENGKTGADVVDLTLDSSSSSEDEDEDEDDDEDEDEGPRPKRRCPFQKGLVPAC

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	Acetylation	------MAAELVEAK ------CCHHHHHHH	15.05	-
31	Ubiquitination	LGFVGRSKSGLKHEL HHHHCCCCCCCCHHH	47.37	-
92	Phosphorylation	ALHSMPRTPLSGPTV HHCCCCCCCCCCCCC	23.78	25293948
95	Phosphorylation	SMPRTPLSGPTVDYP CCCCCCCCCCCCCCH	43.88	25293948
107	Acetylation	DYPVLYGKYLNGLGR CCHHHHHHHHCCCCC	32.76	-
118	Acetylation	GLGRLPTKTLKPEVR CCCCCCCCCCCCCEE	50.34	23806337
239	Phosphorylation	PCRPINLTHLMYLSS CCCCCCCHHHEHHHC	14.42	25293948
243	Phosphorylation	INLTHLMYLSSATNR CCCHHHEHHHCCCCE	15.14	25293948
245	Phosphorylation	LTHLMYLSSATNRIT CHHHEHHHCCCCEEE	10.63	25293948
246	Phosphorylation	THLMYLSSATNRITV HHHEHHHCCCCEEEE	36.20	25293948
248	Phosphorylation	LMYLSSATNRITVTW HEHHHCCCCEEEEEE	27.29	25293948
467	Phosphorylation	GADVVDLTLDSSSSS CCEEEEEEECCCCCC	24.85	25293948
470	Phosphorylation	VVDLTLDSSSSSEDE EEEEEECCCCCCCCC	34.92	25293948
471	Phosphorylation	VDLTLDSSSSSEDED EEEEECCCCCCCCCC	33.63	25293948
472	Phosphorylation	DLTLDSSSSSEDEDE EEEECCCCCCCCCCC	41.66	25293948
473	Phosphorylation	LTLDSSSSSEDEDED EEECCCCCCCCCCCC	39.43	25293948
474	Phosphorylation	TLDSSSSSEDEDEDE EECCCCCCCCCCCCC	51.52	25293948

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
-	K	Ubiquitination	E3 ubiquitin ligase	Trim32	Q8CH72	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
35	K	Sumoylation	Lys-35 is the main site of sumoylation.	11731474

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PIAS4_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TF65_MOUSE	Rela	physical	20054338

Drug and Disease Associations

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