UniProt ID | PSA1_HUMAN | |
---|---|---|
UniProt AC | P25786 | |
Protein Name | Proteasome subunit alpha type-1 | |
Gene Name | PSMA1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 263 | |
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 | MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQRKAQPAQPADEPAEKADEPMEH | |
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 |
---|---|---|---|---|---|
1 | Acetylation | -------MFRNQYDN -------CCCCCCCC | 6.85 | - | |
6 | Phosphorylation | --MFRNQYDNDVTVW --CCCCCCCCCCEEE | 21.91 | 28152594 | |
11 | Phosphorylation | NQYDNDVTVWSPQGR CCCCCCCEEECCCCC | 21.08 | 29978859 | |
14 | Phosphorylation | DNDVTVWSPQGRIHQ CCCCEEECCCCCCHH | 11.74 | 25159151 | |
26 | Sulfoxidation | IHQIEYAMEAVKQGS CHHHHHHHHHHHCCC | 3.13 | 30846556 | |
30 | Ubiquitination | EYAMEAVKQGSATVG HHHHHHHHCCCCEEE | 56.86 | 21890473 | |
30 (in isoform 1) | Ubiquitination | - | 56.86 | 21890473 | |
33 | Phosphorylation | MEAVKQGSATVGLKS HHHHHCCCCEEECCC | 20.48 | 26437602 | |
36 (in isoform 2) | Ubiquitination | - | 9.39 | 21890473 | |
39 | Ubiquitination | GSATVGLKSKTHAVL CCCEEECCCHHHHHH | 43.93 | 21906983 | |
39 (in isoform 1) | Ubiquitination | - | 43.93 | 21890473 | |
40 | Phosphorylation | SATVGLKSKTHAVLV CCEEECCCHHHHHHH | 48.07 | 22673903 | |
41 | Ubiquitination | ATVGLKSKTHAVLVA CEEECCCHHHHHHHH | 42.62 | 21890473 | |
41 (in isoform 1) | Ubiquitination | - | 42.62 | 21890473 | |
42 | Phosphorylation | TVGLKSKTHAVLVAL EEECCCHHHHHHHHH | 23.35 | 22673903 | |
45 (in isoform 2) | Ubiquitination | - | 3.24 | 21890473 | |
47 (in isoform 2) | Ubiquitination | - | 4.75 | 21890473 | |
50 | Methylation | HAVLVALKRAQSELA HHHHHHHHHHHHHHH | 35.63 | 24709217 | |
50 | Ubiquitination | HAVLVALKRAQSELA HHHHHHHHHHHHHHH | 35.63 | - | |
54 | Phosphorylation | VALKRAQSELAAHQK HHHHHHHHHHHHHHH | 33.33 | 20068231 | |
56 (in isoform 2) | Ubiquitination | - | 6.55 | - | |
61 (in isoform 1) | Ubiquitination | - | 31.73 | 21890473 | |
61 | Ubiquitination | SELAAHQKKILHVDN HHHHHHHHHHEEECC | 31.73 | 21906983 | |
67 (in isoform 2) | Ubiquitination | - | 30.18 | 21890473 | |
85 | Glutathionylation | TADARLLCNFMRQEC CCCHHHHHHHHHHHH | 4.34 | 22555962 | |
106 | Phosphorylation | FDRPLPVSRLVSLIG CCCCCCHHHHHHHHC | 20.25 | 23186163 | |
110 | Phosphorylation | LPVSRLVSLIGSKTQ CCHHHHHHHHCCCCC | 20.89 | 30266825 | |
110 | O-linked_Glycosylation | LPVSRLVSLIGSKTQ CCHHHHHHHHCCCCC | 20.89 | UniProtKB CARBOHYD | |
114 | Phosphorylation | RLVSLIGSKTQIPTQ HHHHHHCCCCCCCCC | 26.07 | 30266825 | |
115 | Ubiquitination | LVSLIGSKTQIPTQR HHHHHCCCCCCCCCC | 38.96 | - | |
115 | Acetylation | LVSLIGSKTQIPTQR HHHHHCCCCCCCCCC | 38.96 | 25953088 | |
115 | Malonylation | LVSLIGSKTQIPTQR HHHHHCCCCCCCCCC | 38.96 | 26320211 | |
115 (in isoform 1) | Ubiquitination | - | 38.96 | 21890473 | |
115 | Ubiquitination | LVSLIGSKTQIPTQR HHHHHCCCCCCCCCC | 38.96 | 21890473 | |
116 | Phosphorylation | VSLIGSKTQIPTQRY HHHHCCCCCCCCCCC | 33.17 | 24719451 | |
116 (in isoform 2) | Phosphorylation | - | 33.17 | 24719451 | |
121 (in isoform 2) | Ubiquitination | - | 31.10 | 21890473 | |
122 (in isoform 2) | Phosphorylation | - | 38.05 | 24719451 | |
150 | Phosphorylation | HIFQTCPSANYFDCR HHHCCCCCCCCCCCE | 31.15 | - | |
153 | Phosphorylation | QTCPSANYFDCRAMS CCCCCCCCCCCEECC | 10.66 | - | |
160 | Phosphorylation | YFDCRAMSIGARSQS CCCCEECCCCCCCHH | 19.52 | 24670416 | |
165 | Phosphorylation | AMSIGARSQSARTYL ECCCCCCCHHHHHHH | 28.14 | 26437602 | |
170 | Phosphorylation | ARSQSARTYLERHMS CCCHHHHHHHHHHHH | 31.98 | 26437602 | |
176 | Sulfoxidation | RTYLERHMSEFMECN HHHHHHHHHHHHHCC | 5.27 | 30846556 | |
177 | Phosphorylation | TYLERHMSEFMECNL HHHHHHHHHHHHCCH | 22.89 | 22617229 | |
180 | Sulfoxidation | ERHMSEFMECNLNEL HHHHHHHHHCCHHHH | 5.15 | 30846556 | |
182 | Glutathionylation | HMSEFMECNLNELVK HHHHHHHCCHHHHHH | 4.75 | 22555962 | |
183 (in isoform 2) | Phosphorylation | - | 32.37 | 27251275 | |
189 | Ubiquitination | CNLNELVKHGLRALR CCHHHHHHHHHHHHH | 44.58 | - | |
189 | Acetylation | CNLNELVKHGLRALR CCHHHHHHHHHHHHH | 44.58 | 26051181 | |
195 (in isoform 2) | Ubiquitination | - | 4.03 | - | |
207 | Phosphorylation | PAEQDLTTKNVSIGI CCCCCCCCCCEEEEE | 28.11 | 26437602 | |
207 | O-linked_Glycosylation | PAEQDLTTKNVSIGI CCCCCCCCCCEEEEE | 28.11 | 30379171 | |
208 | Ubiquitination | AEQDLTTKNVSIGIV CCCCCCCCCEEEEEE | 50.55 | 21890473 | |
208 (in isoform 1) | Ubiquitination | - | 50.55 | 21890473 | |
208 | Ubiquitination | AEQDLTTKNVSIGIV CCCCCCCCCEEEEEE | 50.55 | 18781797 | |
211 | Phosphorylation | DLTTKNVSIGIVGKD CCCCCCEEEEEECCC | 25.21 | 21406692 | |
214 (in isoform 2) | Ubiquitination | - | 3.35 | 21890473 | |
230 | Phosphorylation | IYDDDDVSPFLEGLE EECCCCCHHHHHCHH | 19.54 | 25159151 | |
243 | Ubiquitination | LEERPQRKAQPAQPA HHHCCCHHCCCCCCC | 46.24 | 21906983 | |
243 (in isoform 1) | Ubiquitination | - | 46.24 | 21890473 | |
243 | Sumoylation | LEERPQRKAQPAQPA HHHCCCHHCCCCCCC | 46.24 | - | |
243 | Sumoylation | LEERPQRKAQPAQPA HHHCCCHHCCCCCCC | 46.24 | - | |
249 (in isoform 2) | Ubiquitination | - | 43.73 | 21890473 | |
256 | Acetylation | PADEPAEKADEPMEH CCCCCHHHCCCCCCC | 64.34 | 23236377 | |
256 | Ubiquitination | PADEPAEKADEPMEH CCCCCHHHCCCCCCC | 64.34 | 2190698 | |
256 (in isoform 1) | Ubiquitination | - | 64.34 | 21890473 | |
261 | Sulfoxidation | AEKADEPMEH----- HHHCCCCCCC----- | 7.44 | 21406390 | |
262 (in isoform 2) | Ubiquitination | - | 58.10 | 21890473 |
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 PSA1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PSA1_HUMAN !! |
* 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 PSA1_HUMAN !! |
Kegg Disease | ||||||
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OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Mass spectrometric characterization of the affinity-purified human26S proteasome complex."; Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.; Biochemistry 46:3553-3565(2007). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASSSPECTROMETRY. | |
Ubiquitylation | |
Reference | PubMed |
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry."; Meierhofer D., Wang X., Huang L., Kaiser P.; J. Proteome Res. 7:4566-4576(2008). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-115 AND LYS-208, AND MASSSPECTROMETRY. |