dbPTM

PSA3_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PSA3_RAT
UniProt AC	P18422
Protein Name	Proteasome subunit alpha type-3
Gene Name	Psma3
Organism	Rattus norvegicus (Rat).
Sequence Length	255
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). Binds to the C-terminus of CDKN1A and thereby mediates its degradation. Negatively regulates the membrane trafficking of the cell-surface thromboxane A2 receptor (TBXA2R) isoform 2..
Protein Sequence	MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSVNDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDVVKEVAKIIYIVHDEVKDKAFELELSWVGELTKGRHEIVPKDVREEAEKYAKESLKEEDESDDDNM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSSIGTGYD ------CCCCCCCCC	30.57	2335242
57	Acetylation	VEKLVLSKLYEEGSN EEHHHHHHHHHCCCC	51.43	22902405
179	Acetylation	AAKTEIEKLQMKEMT HHHHHHHHHHHHHCC	50.08	22902405
192	Acetylation	MTCRDVVKEVAKIIY CCHHHHHHHHHHHHE	46.44	72613897
206	Acetylation	YIVHDEVKDKAFELE EEECHHHCCCCEEEE	52.01	22902405
230	Acetylation	GRHEIVPKDVREEAE CCCCCCCHHHHHHHH	58.94	-
238	Acetylation	DVREEAEKYAKESLK HHHHHHHHHHHHHHH	58.52	22902405
239	Phosphorylation	VREEAEKYAKESLKE HHHHHHHHHHHHHHH	17.89	-
243	Phosphorylation	AEKYAKESLKEEDES HHHHHHHHHHHCCCC	43.99	23712012
250	Phosphorylation	SLKEEDESDDDNM-- HHHHCCCCCCCCC--	59.67	19700791

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
243	S	Phosphorylation	Kinase	CK2A1	P68400	PSP
243	S	Phosphorylation	Kinase	CSNK2A1	P19139	GPS
250	S	Phosphorylation	Kinase	CK2A1	P68400	PSP
250	S	Phosphorylation	Kinase	CSNK2A1	P19139	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PSA3_RAT !!

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 PSA3_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PSA3_RAT !!

Drug and Disease Associations

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

Regulatory Network of PSA3_RAT

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"The NH2-terminal residues of rat liver proteasome (multicatalyticproteinase complex) subunits, C2, C3 and C8, are N alpha-acetylated."; Tokunaga F., Aruga R., Iwanaga S., Tanaka K., Ichihara A., Takao T.,Shimonishi Y.; FEBS Lett. 263:373-375(1990). Cited for: PROTEIN SEQUENCE OF 2-29.	2335242 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:regulation of aquaporin-2 phosphorylation at two sites."; Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.; Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASSSPECTROMETRY.	16641100 [Abstract]