PIAS2_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PIAS2_RAT
• UniProt AC: Q6AZ28
• Protein Name: E3 SUMO-protein ligase PIAS2
• Gene Name: Pias2
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 572
• Subcellular Localization: Nucleus speckle . Nucleus, PML body . Nucleus . Colocalizes at least partially with promyelocytic leukemia nuclear bodies (PML NBs) (By similarity). Colocalizes with SUMO1 in nuclear granules (PubMed:12077349).
• 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 pathway and the steroid hormone signaling pathway. The effects of this transcriptional coregulation, transactivation or silencing may vary depending upon the biological context and PIAS2 isoform studied. However, it seems to be mostly involved in gene silencing. Binds to sumoylated ELK1 and enhances its transcriptional activity by preventing recruitment of HDAC2 by ELK1, thus reversing SUMO-mediated repression of ELK1 transactivation activity (By similarity). Sumoylates PML at'Lys-65' and 'Lys-160' (By similarity)..
• Protein Sequence: MADFEELRNMVSSFRVSELQVLLGFAGRNKSGRKHDLLMRALHLLKSGCTPAVQIKIRELYRRRYPRTLEGLSDLSTIKSSVFSLDGSSSPVEPDLAVAGIHSLPSTSIAPHSPSSPVASVLLQDTKPTFEMQQPSPPIPPVHPDVQLKTLPFYDVLDVLIKPTSLVQSSIQRFQEKFFIFALTPQQVREICISRDFLPGGRRDYTVQVQLRLCLAETSCPQEDNYPNSLCIKVNGKLFPLPGYAPPPKNGIEQKRPGRPLNITSLVRLSSAVPNQISISWASEIGKNYSMSVYLVRQLTSAMLLQRLKMKGIRNPDHSRALIKEKLTADPDSEIATTSLRVSLMCPLGKMRLTIPCRAVTCTHLQCFDAALYLQMNEKKPTWICPVCDKKAAYESLILDGLFMEILNDCSDVDEIKFQEDGSWCPMRPKKEAMKVTSQPCTKVESSSVFSKPCSVTVASDASKKKIDVIDLTIESSSDEEEDPPAKRKCIFMSETQSSPTKGVLMYQPSSVRVPSVTSVDPAAIPPSLTDYSVPFHHTPVSSMSSDLPGEQRRNDINNEVQLGTSSDTVQQ

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
113	Phosphorylation	STSIAPHSPSSPVAS CCCCCCCCCCCCCHH	25.97	16713578
116	Phosphorylation	IAPHSPSSPVASVLL CCCCCCCCCCHHHHC	27.12	16713578
476	Phosphorylation	VIDLTIESSSDEEED EEEEEECCCCCCCCC	31.15	27097102
477	Phosphorylation	IDLTIESSSDEEEDP EEEEECCCCCCCCCC	29.08	27097102
478	Phosphorylation	DLTIESSSDEEEDPP EEEECCCCCCCCCCC	59.32	27097102
494	Phosphorylation	KRKCIFMSETQSSPT CCEEEEEECCCCCCC	27.09	23984901
496	Phosphorylation	KCIFMSETQSSPTKG EEEEEECCCCCCCCC	26.83	23984901
498	Phosphorylation	IFMSETQSSPTKGVL EEEECCCCCCCCCEE	45.78	27097102
499	Phosphorylation	FMSETQSSPTKGVLM EEECCCCCCCCCEEE	27.11	27097102
501	Phosphorylation	SETQSSPTKGVLMYQ ECCCCCCCCCEEEEC	42.24	27097102

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
113	S	Phosphorylation	Kinase	MAPK11	Q15759	GPS
116	S	Phosphorylation	Kinase	MAPK11	Q15759	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PIAS2_RAT !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PIAS2_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of PIAS2_RAT !!

Drug and Disease Associations

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