SUMO2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SUMO2_MOUSE
• UniProt AC: P61957
• Protein Name: Small ubiquitin-related modifier 2 {ECO:0000305}
• Gene Name: Sumo2 {ECO:0000312|MGI:MGI:2158813}
• Organism: Mus musculus (Mouse).
• Sequence Length: 95
• Subcellular Localization: Nucleus. Nucleus, PML body.
• Protein Description: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. Plays a role in the regulation of sumoylation status of SETX (By similarity)..
• Protein Sequence: MADEKPKEGVKTENNDHINLKVAGQDGSVVQFKIKRHTPLSKLMKAYCERQGLSMRQIRFRFDGQPINETDTPAQLEMEDEDTIDVFQQQTGGVY

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
5	Sumoylation	---MADEKPKEGVKT ---CCCCCCCCCCCC	63.03	28289178
11	Acetylation	EKPKEGVKTENNDHI CCCCCCCCCCCCCCE	62.06	23806337
11	Ubiquitination	EKPKEGVKTENNDHI CCCCCCCCCCCCCCE	62.06	22790023
21	Ubiquitination	NNDHINLKVAGQDGS CCCCEEEEECCCCCC	26.08	22790023
28	Phosphorylation	KVAGQDGSVVQFKIK EECCCCCCEEEEEEE	27.66	26824392
33	Ubiquitination	DGSVVQFKIKRHTPL CCCEEEEEEEECCHH	30.17	27667366
33	Acetylation	DGSVVQFKIKRHTPL CCCEEEEEEEECCHH	30.17	23806337
33	Succinylation	DGSVVQFKIKRHTPL CCCEEEEEEEECCHH	30.17	23806337
35	Ubiquitination	SVVQFKIKRHTPLSK CEEEEEEEECCHHHH	38.42	-
38	Phosphorylation	QFKIKRHTPLSKLMK EEEEEECCHHHHHHH	29.92	22817900
42	Ubiquitination	KRHTPLSKLMKAYCE EECCHHHHHHHHHHH	61.35	27667366
45	Ubiquitination	TPLSKLMKAYCERQG CHHHHHHHHHHHHCC	46.79	-
45	Malonylation	TPLSKLMKAYCERQG CHHHHHHHHHHHHCC	46.79	26320211
48	Glutathionylation	SKLMKAYCERQGLSM HHHHHHHHHHCCCCC	4.09	24333276

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

Oops, there are no upstream regulatory protein records of SUMO2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
6	K	ubiquitylation	Polymeric SUMO2 chains undergo 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4 (By similarity).	-
11	K	ubiquitylation	Polymeric SUMO2 chains undergo 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4 (By similarity).	23806337
48	K	ubiquitylation	Polymeric SUMO2 chains undergo 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4 (By similarity).	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of SUMO2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of SUMO2_MOUSE !!

Drug and Disease Associations

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