PSA6_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PSA6_MOUSE
• UniProt AC: Q9QUM9
• Protein Name: Proteasome subunit alpha type-6
• Gene Name: Psma6
• Organism: Mus musculus (Mouse).
• Sequence Length: 246
• Subcellular Localization: Cytoplasm . Nucleus . Colocalizes with TRIM5 in cytoplasmic bodies.
• 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: MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPDKLLDSSTVTHLFKITESIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYTQNAEMRPLGCCMILIGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVETAITCLSTVLSIDFKPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD

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
2	Phosphorylation	------MSRGSSAGF ------CCCCCCCCC	45.40	23527152
5	Phosphorylation	---MSRGSSAGFDRH ---CCCCCCCCCCCE	18.86	25266776
5	O-linked_Glycosylation	---MSRGSSAGFDRH ---CCCCCCCCCCCE	18.86	22556278
6	Phosphorylation	--MSRGSSAGFDRHI --CCCCCCCCCCCEE	34.92	29176673
14	Phosphorylation	AGFDRHITIFSPEGR CCCCCEEEEECCCCC	15.16	28066266
17	Phosphorylation	DRHITIFSPEGRLYQ CCEEEEECCCCCEEE	20.42	28066266
23	Phosphorylation	FSPEGRLYQVEYAFK ECCCCCEEEEEEHHH	14.78	22817900
30	Acetylation	YQVEYAFKAINQGGL EEEEEHHHHHHCCCC	39.94	23954790
45	Ubiquitination	TSVAVRGKDCAVIVT EEEEECCCCEEEEEE	38.78	-
45	Malonylation	TSVAVRGKDCAVIVT EEEEECCCCEEEEEE	38.78	26320211
47	S-nitrosocysteine	VAVRGKDCAVIVTQK EEECCCCEEEEEECC	3.57	-
47	Glutathionylation	VAVRGKDCAVIVTQK EEECCCCEEEEEECC	3.57	24333276
47	S-nitrosylation	VAVRGKDCAVIVTQK EEECCCCEEEEEECC	3.57	20925432
55	Ubiquitination	AVIVTQKKVPDKLLD EEEEECCCCCHHHCC	49.54	22790023
59	Acetylation	TQKKVPDKLLDSSTV ECCCCCHHHCCCCHH	44.90	22826441
63	Phosphorylation	VPDKLLDSSTVTHLF CCHHHCCCCHHHHHH	28.07	22817900
64	Phosphorylation	PDKLLDSSTVTHLFK CHHHCCCCHHHHHHH	26.94	22817900
65	Phosphorylation	DKLLDSSTVTHLFKI HHHCCCCHHHHHHHH	33.12	23984901
73	Phosphorylation	VTHLFKITESIGCVM HHHHHHHHHCCCCEE	25.03	20469934
75	Phosphorylation	HLFKITESIGCVMTG HHHHHHHCCCCEECC	18.68	20469934
78	S-nitrosylation	KITESIGCVMTGMTA HHHHCCCCEECCCCC	1.48	21278135
78	S-nitrosocysteine	KITESIGCVMTGMTA HHHHCCCCEECCCCC	1.48	-
81	Phosphorylation	ESIGCVMTGMTADSR HCCCCEECCCCCCCH	11.91	20469934
84	Phosphorylation	GCVMTGMTADSRSQV CCEECCCCCCCHHHH	28.76	20469934
87	Phosphorylation	MTGMTADSRSQVQRA ECCCCCCCHHHHHHH	31.22	20469934
89	Phosphorylation	GMTADSRSQVQRARY CCCCCCHHHHHHHHH	38.36	20469934
96	Phosphorylation	SQVQRARYEAANWKY HHHHHHHHHHHCCHH	14.67	17242355
102	Ubiquitination	RYEAANWKYKYGYEI HHHHHCCHHHCCCCC	31.50	22790023
102	Acetylation	RYEAANWKYKYGYEI HHHHHCCHHHCCCCC	31.50	22826441
103	Phosphorylation	YEAANWKYKYGYEIP HHHHCCHHHCCCCCC	10.89	-
104	Acetylation	EAANWKYKYGYEIPV HHHCCHHHCCCCCCH	28.59	23806337
104	Malonylation	EAANWKYKYGYEIPV HHHCCHHHCCCCCCH	28.59	26320211
105	Phosphorylation	AANWKYKYGYEIPVD HHCCHHHCCCCCCHH	23.11	25195567
107	Phosphorylation	NWKYKYGYEIPVDML CCHHHCCCCCCHHHH	13.95	25195567
115	Glutathionylation	EIPVDMLCKRIADIS CCCHHHHHHHHHHHH	1.92	24333276
116	Acetylation	IPVDMLCKRIADISQ CCHHHHHHHHHHHHH	42.76	22826441
159	Phosphorylation	YKCDPAGYYCGFKAT EEECCCCCCCCEEEE	9.55	22817900
160	Phosphorylation	KCDPAGYYCGFKATA EECCCCCCCCEEEEE	5.79	22817900
164	Acetylation	AGYYCGFKATAAGVK CCCCCCEEEEECCCC	30.06	22826441
171	Acetylation	KATAAGVKQTESTSF EEEECCCCCCCCCCH	51.05	22826441
171	Ubiquitination	KATAAGVKQTESTSF EEEECCCCCCCCCCH	51.05	22790023
173	Phosphorylation	TAAGVKQTESTSFLE EECCCCCCCCCCHHH	26.62	25338131
175	Phosphorylation	AGVKQTESTSFLEKK CCCCCCCCCCHHHHH	32.51	28066266
176	Phosphorylation	GVKQTESTSFLEKKV CCCCCCCCCHHHHHH	19.77	28066266
177	Phosphorylation	VKQTESTSFLEKKVK CCCCCCCCHHHHHHH	36.79	25521595
181	Acetylation	ESTSFLEKKVKKKFD CCCCHHHHHHHHHCC	66.08	23864654
181	Malonylation	ESTSFLEKKVKKKFD CCCCHHHHHHHHHCC	66.08	26073543
181	Ubiquitination	ESTSFLEKKVKKKFD CCCCHHHHHHHHHCC	66.08	-

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

Oops, there are no upstream regulatory protein records of PSA6_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PSA6_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 PSA6_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of PSA6_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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-159, AND MASSSPECTROMETRY.
PubMed: 18034455