UniProt ID | PSA2_MOUSE | |
---|---|---|
UniProt AC | P49722 | |
Protein Name | Proteasome subunit alpha type-2 | |
Gene Name | Psma2 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 234 | |
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 | MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVRDYLAAIA | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MAERGYSFS ------CCCCCCEEE | 15.39 | 16857966 | |
6 | Phosphorylation | --MAERGYSFSLTTF --CCCCCCEEEEEEE | 15.58 | 25521595 | |
7 | Phosphorylation | -MAERGYSFSLTTFS -CCCCCCEEEEEEEC | 15.93 | 25521595 | |
9 | Phosphorylation | AERGYSFSLTTFSPS CCCCCEEEEEEECCC | 20.90 | 26745281 | |
11 | Phosphorylation | RGYSFSLTTFSPSGK CCCEEEEEEECCCCC | 25.29 | 26745281 | |
12 | Phosphorylation | GYSFSLTTFSPSGKL CCEEEEEEECCCCCE | 27.66 | 26745281 | |
14 | Phosphorylation | SFSLTTFSPSGKLVQ EEEEEEECCCCCEEE | 18.96 | 26239621 | |
16 | Phosphorylation | SLTTFSPSGKLVQIE EEEEECCCCCEEEEH | 47.57 | 26745281 | |
24 | Phosphorylation | GKLVQIEYALAAVAG CCEEEEHHHHHHHHC | 14.45 | - | |
50 | Ubiquitination | GVVLATEKKQKSILY CEEEEECCCCCCCCC | 57.03 | - | |
53 | Ubiquitination | LATEKKQKSILYDER EEECCCCCCCCCCCC | 48.63 | - | |
53 | Malonylation | LATEKKQKSILYDER EEECCCCCCCCCCCC | 48.63 | 26320211 | |
57 | Phosphorylation | KKQKSILYDERSVHK CCCCCCCCCCCCCCC | 17.68 | 26032504 | |
70 | Acetylation | HKVEPITKHIGLVYS CCCCCCHHHEEEEEC | 33.66 | - | |
70 | Ubiquitination | HKVEPITKHIGLVYS CCCCCCHHHEEEEEC | 33.66 | 27667366 | |
76 | Phosphorylation | TKHIGLVYSGMGPDY HHHEEEEECCCCCCH | 12.44 | 25177544 | |
77 | Phosphorylation | KHIGLVYSGMGPDYR HHEEEEECCCCCCHH | 18.15 | 17242355 | |
92 | Phosphoglycerylation | VLVHRARKLAQQYYL HHHHHHHHHHHHHHE | 47.38 | - | |
92 | Ubiquitination | VLVHRARKLAQQYYL HHHHHHHHHHHHHHE | 47.38 | 27667366 | |
92 | Acetylation | VLVHRARKLAQQYYL HHHHHHHHHHHHHHE | 47.38 | 23806337 | |
92 | Malonylation | VLVHRARKLAQQYYL HHHHHHHHHHHHHHE | 47.38 | 26320211 | |
97 | Phosphorylation | ARKLAQQYYLVYQEP HHHHHHHHHEEECCC | 6.15 | - | |
98 | Phosphorylation | RKLAQQYYLVYQEPI HHHHHHHHEEECCCC | 5.83 | 18563927 | |
101 | Phosphorylation | AQQYYLVYQEPIPTA HHHHHEEECCCCCHH | 12.45 | 17242355 | |
121 | Phosphorylation | VASVMQEYTQSGGVR HHHHHHHHHHCCCCC | 8.00 | - | |
165 | Ubiquitination | WKATAMGKNYVNGKT EEEEECCCCCCCCEE | 31.83 | - | |
167 | Phosphorylation | ATAMGKNYVNGKTFL EEECCCCCCCCEEHH | 9.97 | - | |
171 | Succinylation | GKNYVNGKTFLEKRY CCCCCCCEEHHHHHH | 30.79 | 23954790 | |
171 | Acetylation | GKNYVNGKTFLEKRY CCCCCCCEEHHHHHH | 30.79 | 23806337 | |
171 | Ubiquitination | GKNYVNGKTFLEKRY CCCCCCCEEHHHHHH | 30.79 | - | |
176 | Ubiquitination | NGKTFLEKRYNEDLE CCEEHHHHHHCCCCC | 63.43 | 27667366 | |
198 | Phosphorylation | AILTLKESFEGQMTE HHHHHHHHHCCCCCC | 27.32 | 18579562 |
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 PSA2_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PSA2_MOUSE !! |
* 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 PSA2_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ADRM1_HUMAN | ADRM1 | physical | 17139257 | |
TBA1A_HUMAN | TUBA1A | physical | 17139257 | |
HSP74_HUMAN | HSPA4 | physical | 17139257 | |
HSP7C_HUMAN | HSPA8 | physical | 17139257 | |
GRP78_HUMAN | HSPA5 | physical | 17139257 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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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-76, AND MASSSPECTROMETRY. |