PSB2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PSB2_MOUSE
• UniProt AC: Q9R1P3
• Protein Name: Proteasome subunit beta type-2
• Gene Name: Psmb2
• Organism: Mus musculus (Mouse).
• Sequence Length: 201
• Subcellular Localization: Cytoplasm . Nucleus .
• Protein Description: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex)..
• Protein Sequence: MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRVIDKDGIHNLENIAFPKRDS

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
1	Acetylation	-------MEYLIGIQ -------CCEECCCC	7.43	-
29	Ubiquitination	ASNIVQMKDDHDKMF HHHCEECCCCHHHHH	42.80	-
29	Succinylation	ASNIVQMKDDHDKMF HHHCEECCCCHHHHH	42.80	23954790
37	Ubiquitination	DDHDKMFKMSEKILL CCHHHHHHHCHHHHH	37.71	27667366
39	Phosphorylation	HDKMFKMSEKILLLC HHHHHHHCHHHHHHH	36.01	18579562
62	Ubiquitination	QFAEYIQKNVQLYKM HHHHHHHHHCCCEEC	49.91	-
68	Acetylation	QKNVQLYKMRNGYEL HHHCCCEECCCCCCC	39.72	22826441
68	Ubiquitination	QKNVQLYKMRNGYEL HHHCCCEECCCCCCC	39.72	-
73	Phosphorylation	LYKMRNGYELSPTAA CEECCCCCCCCHHHH	19.76	30635358
76	Phosphorylation	MRNGYELSPTAAANF CCCCCCCCHHHHHHC	14.31	24719451
78	Phosphorylation	NGYELSPTAAANFTR CCCCCCHHHHHHCCH	26.08	30635358
91	S-nitrosylation	TRRNLADCLRSRTPY CHHCHHHHHHHCCCC	2.57	21278135
91	Glutathionylation	TRRNLADCLRSRTPY CHHCHHHHHHHCCCC	2.57	24333276
91	S-nitrosocysteine	TRRNLADCLRSRTPY CHHCHHHHHHHCCCC	2.57	-
162	Malonylation	RAVELLRKCLEELQK HHHHHHHHHHHHHHH	43.04	26320211
162	Ubiquitination	RAVELLRKCLEELQK HHHHHHHHHHHHHHH	43.04	-
177	Phosphorylation	RFILNLPTFSVRVID HHHHCCCCCEEEEEC	31.54	22006019
185	Acetylation	FSVRVIDKDGIHNLE CEEEEECCCCCCCCE	46.89	22826441
201	Phosphorylation	IAFPKRDS------- CCCCCCCC-------	46.27	29514104

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

Oops, there are no upstream regulatory protein records of PSB2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PSB2_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 PSB2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of PSB2_MOUSE !!

Drug and Disease Associations

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