PIAS2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PIAS2_MOUSE
• UniProt AC: Q8C5D8
• Protein Name: E3 SUMO-protein ligase PIAS2
• Gene Name: Pias2
• Organism: Mus musculus (Mouse).
• Sequence Length: 621
• 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. Isoform PIASx-beta, but not isoform PIASx-alpha, promotes MDM2 sumoylation. Isoform PIASx-alpha promotes PARK7 sumoylation. Isoform PIASx-beta promotes NCOA2 sumoylation more efficiently than isoform PIASx-alpha (By similarity). Sumoylates PML at'Lys-65' and 'Lys-160' (By similarity)..
• Protein Sequence: MADFEELRNMVSSFRVSELQVLLGFAGRNKSGRKHDLLMRALHLLKSGCSPAVQIKIRELYRRRYPRTLEGLCDLSTIKSSVFSLDGSSSPVEPDLPVAGIHSLPSTSITPHSPSSPVGSVLLQDTKPTFEMQQPSPPIPPVHPDVQLKNLPFYDVLDVLIKPTSLVQSSIQRFQEKFFIFALTPQQVREICISRDFLPGGRRDYTVQVQLRLCLAETSCPQEDNYPNSLCIKVNGKLFPLPGYAPPPKNGIEQKRPGRPLNITSLVRLSSAVPNQISISWASEIGKNYSMSVYLVRQLTSAMLLQRLKMKGIRNPDHSRALIKEKLTADPDSEIATTSLRVSLMCPLGKMRLTIPCRAVTCTHLQCFDAALYLQMNEKKPTWICPVCDKKAAYESLILDGLFMEILNDCSDVDEIKFQEDGSWCPMRPKKEAMKVTSQPCTKVESSSVFSKPCSVTVASDASKKKIDVIDLTIESSSDEEEDPPAKRKCIFMSETQSSPTKGVLMYQPSSVRVPSVTSVDPAAIPPSLTDYSVPFHHTPVSSMSSDLPGLDFLSLIPVDPQYCPPMFLDSLTSPLTASSTSVTTTSPHESSTHVSSSSSRSETGVITSSGRNIPDIISLD

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
47	Phosphorylation	RALHLLKSGCSPAVQ HHHHHHHCCCCHHHH	45.03	23140645
50	Phosphorylation	HLLKSGCSPAVQIKI HHHHCCCCHHHHHHH	21.30	23140645
473	Phosphorylation	KIDVIDLTIESSSDE CEEEEEEEECCCCCC	20.96	21743459
476	Phosphorylation	VIDLTIESSSDEEED EEEEEECCCCCCCCC	31.15	21743459
477	Phosphorylation	IDLTIESSSDEEEDP EEEEECCCCCCCCCC	29.08	21743459
478	Phosphorylation	DLTIESSSDEEEDPP EEEECCCCCCCCCCC	59.32	21743459
494	Phosphorylation	KRKCIFMSETQSSPT CCEEEEEECCCCCCC	27.09	28833060
496	Phosphorylation	KCIFMSETQSSPTKG EEEEEECCCCCCCCC	26.83	28833060
498	Phosphorylation	IFMSETQSSPTKGVL EEEECCCCCCCCCEE	45.78	28833060
499	Phosphorylation	FMSETQSSPTKGVLM EEECCCCCCCCCEEE	27.11	27087446
501	Phosphorylation	SETQSSPTKGVLMYQ ECCCCCCCCCEEEEC	42.24	28833060
592	Phosphorylation	TTSPHESSTHVSSSS ECCCCCCCCCCCCCC	21.39	-
593	Phosphorylation	TSPHESSTHVSSSSS CCCCCCCCCCCCCCC	35.26	-
610	Phosphorylation	ETGVITSSGRNIPDI CCEEECCCCCCCCCC	32.87	-

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	Huwe1	Q4JG03	PMID:23699408

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PIAS2_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 PIAS2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NFKB1_MOUSE	Nfkb1	physical	20211142
PPARG_MOUSE	Pparg	physical	15123625

Drug and Disease Associations

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