dbPTM

PSB1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PSB1_MOUSE
UniProt AC	O09061
Protein Name	Proteasome subunit beta type-1
Gene Name	Psmb1
Organism	Mus musculus (Mouse).
Sequence Length	240
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	MLSTAAYRDVERELGMGPHGSAGPVQLRFSPYAFNGGTVLAIAGEDFSIVASDTRLSEGFSIHTRDSPKCYKLTDKTVIGCSGFHGDCLTLTKIIEARLKMYKHSNNKAMTTGAIAAMLSTILYSRRFFPYYVYNIIGGLDEEGKGAVYSFDPVGSYQRDSFKAGGSASAMLQPLLDNQVGFKNMQNVEHVPLTLDRAMRLVKDVFISAAERDVYTGDALRICIVTKEGIREETVPLRKD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MLSTAAYR -------CCCCHHHH	6.35	-
48	Phosphorylation	AIAGEDFSIVASDTR EECCCCEEEEEECCC	28.60	-
52	Phosphorylation	EDFSIVASDTRLSEG CCEEEEEECCCCCCC	28.72	-
57	O-linked_Glycosylation	VASDTRLSEGFSIHT EEECCCCCCCEEEEE	32.17	22556278
61	Phosphorylation	TRLSEGFSIHTRDSP CCCCCCEEEEECCCC	25.07	28066266
64	Phosphorylation	SEGFSIHTRDSPKCY CCCEEEEECCCCCCE	34.21	28066266
67	Phosphorylation	FSIHTRDSPKCYKLT EEEEECCCCCCEECC	23.98	25338131
81	S-nitrosocysteine	TDKTVIGCSGFHGDC CCCEEEECCCCCCHH	2.18	-
81	S-nitrosylation	TDKTVIGCSGFHGDC CCCEEEECCCCCCHH	2.18	20925432
88	S-nitrosylation	CSGFHGDCLTLTKII CCCCCCHHHHHHHHH	3.56	20925432
88	S-nitrosocysteine	CSGFHGDCLTLTKII CCCCCCHHHHHHHHH	3.56	-
149	Phosphorylation	EEGKGAVYSFDPVGS CCCCCCEEEECCCCC	11.77	22817900
150	Phosphorylation	EGKGAVYSFDPVGSY CCCCCEEEECCCCCC	19.30	20415495
157	Phosphorylation	SFDPVGSYQRDSFKA EECCCCCCCCCCCCC	11.13	20531401
161	Phosphorylation	VGSYQRDSFKAGGSA CCCCCCCCCCCCCCH	30.73	-
163	Ubiquitination	SYQRDSFKAGGSASA CCCCCCCCCCCCHHH	50.50	22790023
167	Phosphorylation	DSFKAGGSASAMLQP CCCCCCCCHHHHHHH	20.38	18579562
194	Phosphorylation	NVEHVPLTLDRAMRL CCEECCCCHHHHHHH	22.12	29899451
203	Acetylation	DRAMRLVKDVFISAA HHHHHHHHHHHHHHH	53.41	23806337
203	Ubiquitination	DRAMRLVKDVFISAA HHHHHHHHHHHHHHH	53.41	-
203	Malonylation	DRAMRLVKDVFISAA HHHHHHHHHHHHHHH	53.41	26320211
208	O-linked_Glycosylation	LVKDVFISAAERDVY HHHHHHHHHHHCCCC	15.23	22556278
208	Phosphorylation	LVKDVFISAAERDVY HHHHHHHHHHHCCCC	15.23	23737553
215	Phosphorylation	SAAERDVYTGDALRI HHHHCCCCCCCCEEE	14.86	22817900
227	Acetylation	LRICIVTKEGIREET EEEEEEECCCCCCCC	42.95	22826441

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
Oops, there are no upstream regulatory protein records of PSB1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PSB1_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of PSB1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PSB1_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of PSB1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-149, AND MASSSPECTROMETRY.	18034455 [Abstract]