dbPTM

PSA3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PSA3_MOUSE
UniProt AC	O70435
Protein Name	Proteasome subunit alpha type-3
Gene Name	Psma3
Organism	Mus musculus (Mouse).
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	MSSIGTGYDLSASTFSPDGRVFQVEYAMKAVENSSTAIGIRCKDGVVFGVEKLVLSKLYEEGSNKRLFNVDRHVGMAVAGLLADARSLADIAREEASNFRSNFGYNIPLKHLADRVAMYVHAYTLYSAVRPFGCSFMLGSYSANDGAQLYMIDPSGVSYGYWGCAIGKARQAAKTEIEKLQMKEMTCRDVVKEVAKIIYIVHDEVKDKAFELELSWVGELTKGRHEIVPKDIREEAEKYAKESLKEEDESDDDNM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSSIGTGYD ------CCCCCCCCC	30.57	26643407
2	Acetylation	------MSSIGTGYD ------CCCCCCCCC	30.57	16857966
3	Phosphorylation	-----MSSIGTGYDL -----CCCCCCCCCC	24.60	26643407
6	Phosphorylation	--MSSIGTGYDLSAS --CCCCCCCCCCCCC	30.79	26643407
8	Phosphorylation	MSSIGTGYDLSASTF CCCCCCCCCCCCCEE	17.35	30635358
11	Phosphorylation	IGTGYDLSASTFSPD CCCCCCCCCCEECCC	19.78	28066266
13	Phosphorylation	TGYDLSASTFSPDGR CCCCCCCCEECCCCC	26.98	28066266
14	Phosphorylation	GYDLSASTFSPDGRV CCCCCCCEECCCCCE	28.05	28066266
16	Phosphorylation	DLSASTFSPDGRVFQ CCCCCEECCCCCEEE	23.36	26643407
35	Phosphorylation	MKAVENSSTAIGIRC HHHHHCCCCEEEEEE	33.18	28464351
52	Acetylation	GVVFGVEKLVLSKLY CEEEEEEHHHHHHHH	41.30	22826441
57	Malonylation	VEKLVLSKLYEEGSN EEHHHHHHHHHCCCC	51.43	26320211
57	Ubiquitination	VEKLVLSKLYEEGSN EEHHHHHHHHHCCCC	51.43	-
57	Acetylation	VEKLVLSKLYEEGSN EEHHHHHHHHHCCCC	51.43	23806337
65	Succinylation	LYEEGSNKRLFNVDR HHHCCCCCCCCEECH	52.77	23954790
110	Acetylation	FGYNIPLKHLADRVA CCCCCCHHHHHHHHH	31.08	22826441
110	Ubiquitination	FGYNIPLKHLADRVA CCCCCCHHHHHHHHH	31.08	22790023
155	Phosphorylation	QLYMIDPSGVSYGYW EEEEECCCCCCCCCH	48.34	-
158	Phosphorylation	MIDPSGVSYGYWGCA EECCCCCCCCCHHHH	19.16	-
159	Phosphorylation	IDPSGVSYGYWGCAI ECCCCCCCCCHHHHH	16.30	-
179	Acetylation	AAKTEIEKLQMKEMT HHHHHHHHHHHHHCC	50.08	22826441
179	Ubiquitination	AAKTEIEKLQMKEMT HHHHHHHHHHHHHCC	50.08	22790023
183	Acetylation	EIEKLQMKEMTCRDV HHHHHHHHHCCHHHH	31.22	22826441
183	Ubiquitination	EIEKLQMKEMTCRDV HHHHHHHHHCCHHHH	31.22	22790023
186	Phosphorylation	KLQMKEMTCRDVVKE HHHHHHCCHHHHHHH	12.89	18579562
196	Acetylation	DVVKEVAKIIYIVHD HHHHHHHHHHEEECH	34.51	22826441
206	Malonylation	YIVHDEVKDKAFELE EEECHHHCCCCEEEE	52.01	26320211
206	Acetylation	YIVHDEVKDKAFELE EEECHHHCCCCEEEE	52.01	23236377
206	Ubiquitination	YIVHDEVKDKAFELE EEECHHHCCCCEEEE	52.01	-
222	Ubiquitination	SWVGELTKGRHEIVP EECCHHHCCCCEECC	67.58	-
230	Acetylation	GRHEIVPKDIREEAE CCCEECCHHHHHHHH	55.69	22826441
230	Ubiquitination	GRHEIVPKDIREEAE CCCEECCHHHHHHHH	55.69	22790023
238	Acetylation	DIREEAEKYAKESLK HHHHHHHHHHHHHHH	58.52	22826441
239	Phosphorylation	IREEAEKYAKESLKE HHHHHHHHHHHHHHH	17.89	25367039
243	Phosphorylation	AEKYAKESLKEEDES HHHHHHHHHHHCCCC	43.99	22942356
250	Phosphorylation	SLKEEDESDDDNM-- HHHHCCCCCCCCC--	59.67	27087446

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 PSA3_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PSA3_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 PSA3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PSA3_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of PSA3_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASSSPECTROMETRY.	19131326 [Abstract]
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASSSPECTROMETRY.	19144319 [Abstract]
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis."; Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; J. Proteome Res. 7:3957-3967(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASSSPECTROMETRY.	18630941 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243 AND SER-250, ANDMASS SPECTROMETRY.	17242355 [Abstract]
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND MASSSPECTROMETRY.	17203969 [Abstract]