UniProt ID | PSB4_HUMAN | |
---|---|---|
UniProt AC | P28070 | |
Protein Name | Proteasome subunit beta type-4 | |
Gene Name | PSMB4 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 264 | |
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). SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1.. | |
Protein Sequence | MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE | |
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 | -------MEAFLGSR -------CCCCCCCC | 8.27 | 22223895 | |
9 | Phosphorylation | EAFLGSRSGLWAGGP CCCCCCCCCCCCCCC | 39.68 | 24114839 | |
22 | Phosphorylation | GPAPGQFYRIPSTPD CCCCCCEEECCCCCC | 10.35 | 20068231 | |
26 | Phosphorylation | GQFYRIPSTPDSFMD CCEEECCCCCCCCCC | 50.64 | 25106551 | |
27 | Phosphorylation | QFYRIPSTPDSFMDP CEEECCCCCCCCCCH | 26.26 | 25106551 | |
30 | Phosphorylation | RIPSTPDSFMDPASA ECCCCCCCCCCHHHH | 24.55 | 28450419 | |
44 | Phosphorylation | ALYRGPITRTQNPMV HHHCCCCCCCCCCCC | 30.69 | 22210691 | |
46 | Phosphorylation | YRGPITRTQNPMVTG HCCCCCCCCCCCCCC | 24.85 | 20068231 | |
50 | Sulfoxidation | ITRTQNPMVTGTSVL CCCCCCCCCCCEEEE | 5.74 | 21406390 | |
52 | Phosphorylation | RTQNPMVTGTSVLGV CCCCCCCCCEEEEEE | 28.61 | 21406692 | |
54 | Phosphorylation | QNPMVTGTSVLGVKF CCCCCCCEEEEEEEE | 13.29 | 20068231 | |
55 | Phosphorylation | NPMVTGTSVLGVKFE CCCCCCEEEEEEEEC | 19.38 | 20068231 | |
74 | Phosphorylation | IAADMLGSYGSLARF EEEEHHCCCHHHHHH | 23.51 | 28348404 | |
75 | Phosphorylation | AADMLGSYGSLARFR EEEHHCCCHHHHHHH | 14.67 | 20090780 | |
77 | Phosphorylation | DMLGSYGSLARFRNI EHHCCCHHHHHHHCC | 15.60 | 28348404 | |
85 | Phosphorylation | LARFRNISRIMRVNN HHHHHCCHHHEEECC | 21.21 | 24719451 | |
93 | Phosphorylation | RIMRVNNSTMLGASG HHEEECCCCCCCCCC | 15.25 | 21712546 | |
94 | Phosphorylation | IMRVNNSTMLGASGD HEEECCCCCCCCCCC | 20.66 | 24719451 | |
99 | Phosphorylation | NSTMLGASGDYADFQ CCCCCCCCCCHHHHH | 30.33 | 28102081 | |
102 | Phosphorylation | MLGASGDYADFQYLK CCCCCCCHHHHHHHH | 16.17 | 7918633 | |
107 | Phosphorylation | GDYADFQYLKQVLGQ CCHHHHHHHHHHHCC | 18.83 | 20090780 | |
109 | Sumoylation | YADFQYLKQVLGQMV HHHHHHHHHHHCCHH | 33.17 | - | |
109 | Ubiquitination | YADFQYLKQVLGQMV HHHHHHHHHHHCCHH | 33.17 | - | |
115 | Sulfoxidation | LKQVLGQMVIDEELL HHHHHCCHHCCHHHC | 2.43 | 30846556 | |
127 | Phosphorylation | ELLGDGHSYSPRAIH HHCCCCCCCCHHHHH | 32.60 | 24719451 | |
128 | Phosphorylation | LLGDGHSYSPRAIHS HCCCCCCCCHHHHHH | 19.61 | 27080861 | |
129 | Phosphorylation | LGDGHSYSPRAIHSW CCCCCCCCHHHHHHH | 15.78 | 27282143 | |
147 | Ubiquitination | AMYSRRSKMNPLWNT HHHHCHHHCCCCCCE | 40.67 | - | |
186 | Phosphorylation | APSLATGYGAYLAQP CCCHHCCHHHHHHHH | 8.33 | - | |
189 | Phosphorylation | LATGYGAYLAQPLLR HHCCHHHHHHHHHHH | 9.75 | - | |
201 | Acetylation | LLREVLEKQPVLSQT HHHHHHHHCCCCCHH | 56.60 | 23236377 | |
201 | Ubiquitination | LLREVLEKQPVLSQT HHHHHHHHCCCCCHH | 56.60 | 21906983 | |
206 | Phosphorylation | LEKQPVLSQTEARDL HHHCCCCCHHHHHHH | 34.98 | 23663014 | |
208 | Phosphorylation | KQPVLSQTEARDLVE HCCCCCHHHHHHHHH | 28.39 | 23663014 | |
222 | Phosphorylation | ERCMRVLYYRDARSY HHHHHHHHHHCCCCC | 8.13 | 28152594 | |
223 | Phosphorylation | RCMRVLYYRDARSYN HHHHHHHHHCCCCCC | 9.61 | 28152594 | |
228 | Phosphorylation | LYYRDARSYNRFQIA HHHHCCCCCCCEEEE | 28.60 | - | |
236 | Phosphorylation | YNRFQIATVTEKGVE CCCEEEEEEECCCEE | 29.59 | - | |
238 | Phosphorylation | RFQIATVTEKGVEIE CEEEEEEECCCEEEE | 27.85 | - | |
240 | Ubiquitination | QIATVTEKGVEIEGP EEEEEECCCEEEECC | 59.91 | 21906983 | |
249 | Phosphorylation | VEIEGPLSTETNWDI EEEECCCCCCCCHHH | 27.60 | 22817900 | |
250 | Phosphorylation | EIEGPLSTETNWDIA EEECCCCCCCCHHHH | 55.29 | 28348404 | |
252 | Phosphorylation | EGPLSTETNWDIAHM ECCCCCCCCHHHHHH | 41.52 | 28348404 | |
259 | Sulfoxidation | TNWDIAHMISGFE-- CCHHHHHHHHCCC-- | 1.60 | 30846556 | |
261 | Phosphorylation | WDIAHMISGFE---- HHHHHHHHCCC---- | 29.83 | 27251275 |
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 PSB4_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PSB4_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 PSB4_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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Phosphorylation | |
Reference | PubMed |
"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-102, AND MASSSPECTROMETRY. |