| UniProt ID | PSA2_HUMAN | |
|---|---|---|
| UniProt AC | P25787 | |
| Protein Name | Proteasome subunit alpha type-2 | |
| Gene Name | PSMA2 | |
| Organism | Homo sapiens (Human). | |
| 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 | MAERGYSFSLTTFSPSGKLVQIEYALAAVAGGAPSVGIKAANGVVLATEKKQKSILYDERSVHKVEPITKHIGLVYSGMGPDYRVLVHRARKLAQQYYLVYQEPIPTAQLVQRVASVMQEYTQSGGVRPFGVSLLICGWNEGRPYLFQSDPSGAYFAWKATAMGKNYVNGKTFLEKRYNEDLELEDAIHTAILTLKESFEGQMTEDNIEVGICNEAGFRRLTPTEVKDYLAAIA | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MAERGYSFS ------CCCCCCEEE | 18.39 | 19413330 | |
| 6 | Phosphorylation | --MAERGYSFSLTTF --CCCCCCEEEEEEE | 16.86 | 21044959 | |
| 7 | Phosphorylation | -MAERGYSFSLTTFS -CCCCCCEEEEEEEC | 15.93 | 25159151 | |
| 9 | Phosphorylation | AERGYSFSLTTFSPS CCCCCEEEEEEECCC | 20.90 | 28102081 | |
| 11 | Phosphorylation | RGYSFSLTTFSPSGK CCCEEEEEEECCCCC | 25.29 | 30108239 | |
| 12 | Phosphorylation | GYSFSLTTFSPSGKL CCEEEEEEECCCCCE | 27.66 | 28102081 | |
| 14 | Phosphorylation | SFSLTTFSPSGKLVQ EEEEEEECCCCCEEE | 18.96 | 25159151 | |
| 16 | Phosphorylation | SLTTFSPSGKLVQIE EEEEECCCCCEEEEH | 47.57 | 21712546 | |
| 24 | Phosphorylation | GKLVQIEYALAAVAG CCEEEEHHHHHHHHC | 14.45 | 20090780 | |
| 35 | Phosphorylation | AVAGGAPSVGIKAAN HHHCCCCCCEEEHHC | 32.23 | 21712546 | |
| 39 | Ubiquitination | GAPSVGIKAANGVVL CCCCCEEEHHCCEEE | 35.20 | - | |
| 50 | Ubiquitination | GVVLATEKKQKSILY CEEEEECCCCCCCCC | 57.03 | 21906983 | |
| 50 | 2-Hydroxyisobutyrylation | GVVLATEKKQKSILY CEEEEECCCCCCCCC | 57.03 | - | |
| 50 | Acetylation | GVVLATEKKQKSILY CEEEEECCCCCCCCC | 57.03 | 23749302 | |
| 51 | Ubiquitination | VVLATEKKQKSILYD EEEEECCCCCCCCCC | 57.64 | - | |
| 53 | Acetylation | LATEKKQKSILYDER EEECCCCCCCCCCCC | 48.63 | 23749302 | |
| 53 | Ubiquitination | LATEKKQKSILYDER EEECCCCCCCCCCCC | 48.63 | 21890473 | |
| 53 | Malonylation | LATEKKQKSILYDER EEECCCCCCCCCCCC | 48.63 | 26320211 | |
| 54 | Phosphorylation | ATEKKQKSILYDERS EECCCCCCCCCCCCC | 18.48 | 26437602 | |
| 57 | Phosphorylation | KKQKSILYDERSVHK CCCCCCCCCCCCCCC | 17.68 | 25159151 | |
| 64 | Acetylation | YDERSVHKVEPITKH CCCCCCCCCCCCHHH | 46.25 | 25953088 | |
| 64 | Succinylation | YDERSVHKVEPITKH CCCCCCCCCCCCHHH | 46.25 | 23954790 | |
| 64 | Sumoylation | YDERSVHKVEPITKH CCCCCCCCCCCCHHH | 46.25 | - | |
| 64 | Sumoylation | YDERSVHKVEPITKH CCCCCCCCCCCCHHH | 46.25 | - | |
| 64 | Ubiquitination | YDERSVHKVEPITKH CCCCCCCCCCCCHHH | 46.25 | - | |
| 70 | Acetylation | HKVEPITKHIGLVYS CCCCCCHHHEEEEEC | 33.66 | 19608861 | |
| 70 | Ubiquitination | HKVEPITKHIGLVYS CCCCCCHHHEEEEEC | 33.66 | 21906983 | |
| 76 | Phosphorylation | TKHIGLVYSGMGPDY HHHEEEEECCCCCCH | 12.44 | 21082442 | |
| 77 | Phosphorylation | KHIGLVYSGMGPDYR HHEEEEECCCCCCHH | 18.15 | 28450419 | |
| 79 | Sulfoxidation | IGLVYSGMGPDYRVL EEEEECCCCCCHHHH | 6.07 | 30846556 | |
| 83 | Phosphorylation | YSGMGPDYRVLVHRA ECCCCCCHHHHHHHH | 13.02 | 26356563 | |
| 92 | Ubiquitination | VLVHRARKLAQQYYL HHHHHHHHHHHHHHE | 47.38 | 21890473 | |
| 92 | Malonylation | VLVHRARKLAQQYYL HHHHHHHHHHHHHHE | 47.38 | 26320211 | |
| 92 | Acetylation | VLVHRARKLAQQYYL HHHHHHHHHHHHHHE | 47.38 | 23954790 | |
| 97 | Phosphorylation | ARKLAQQYYLVYQEP HHHHHHHHHEEECCC | 6.15 | 28152594 | |
| 98 | Phosphorylation | RKLAQQYYLVYQEPI HHHHHHHHEEECCCC | 5.83 | 20090780 | |
| 101 | Phosphorylation | AQQYYLVYQEPIPTA HHHHHEEECCCCCHH | 12.45 | 18180459 | |
| 121 | Phosphorylation | VASVMQEYTQSGGVR HHHHHHHHHHCCCCC | 8.00 | - | |
| 165 | Ubiquitination | WKATAMGKNYVNGKT EEEEECCCCCCCCEE | 31.83 | 21906983 | |
| 167 | Phosphorylation | ATAMGKNYVNGKTFL EEECCCCCCCCEEHH | 9.97 | 22817900 | |
| 171 | Ubiquitination | GKNYVNGKTFLEKRY CCCCCCCEEHHHHHH | 30.79 | 21906983 | |
| 171 | Acetylation | GKNYVNGKTFLEKRY CCCCCCCEEHHHHHH | 30.79 | 19608861 | |
| 171 | 2-Hydroxyisobutyrylation | GKNYVNGKTFLEKRY CCCCCCCEEHHHHHH | 30.79 | - | |
| 176 | Ubiquitination | NGKTFLEKRYNEDLE CCEEHHHHHHCCCCC | 63.43 | 21906983 | |
| 178 | Phosphorylation | KTFLEKRYNEDLELE EEHHHHHHCCCCCHH | 33.69 | 29496907 | |
| 190 | Phosphorylation | ELEDAIHTAILTLKE CHHHHHHHHHHHHHH | 14.85 | - | |
| 222 | Phosphorylation | EAGFRRLTPTEVKDY CCCCCCCCHHHHHHH | 26.76 | 28985074 | |
| 224 | Phosphorylation | GFRRLTPTEVKDYLA CCCCCCHHHHHHHHH | 48.45 | 24719451 | |
| 227 | Ubiquitination | RLTPTEVKDYLAAIA CCCHHHHHHHHHHHC | 34.13 | 21906983 | |
| 229 | Phosphorylation | TPTEVKDYLAAIA-- CHHHHHHHHHHHC-- | 7.79 | 29496907 | |
| 229 | Nitration | TPTEVKDYLAAIA-- CHHHHHHHHHHHC-- | 7.79 | - | |
| 229 | Nitrated tyrosine | TPTEVKDYLAAIA-- CHHHHHHHHHHHC-- | 7.79 | - |
| 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_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PSA2_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 PSA2_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY. | |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-171, AND MASSSPECTROMETRY. | |
| Nitration | |
| Reference | PubMed |
| "Nitroproteins from a human pituitary adenoma tissue discovered with anitrotyrosine affinity column and tandem mass spectrometry."; Zhan X., Desiderio D.M.; Anal. Biochem. 354:279-289(2006). Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-229, AND MASS SPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASSSPECTROMETRY. | |
| "Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-57 AND TYR-76, AND MASSSPECTROMETRY. | |
| "Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-24 AND TYR-98, AND MASSSPECTROMETRY. | |
