| UniProt ID | PSMD7_HUMAN | |
|---|---|---|
| UniProt AC | P51665 | |
| Protein Name | 26S proteasome non-ATPase regulatory subunit 7 | |
| Gene Name | PSMD7 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 324 | |
| Subcellular Localization | ||
| Protein Description | Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair.. | |
| Protein Sequence | MPELAVQKVVVHPLVLLSVVDHFNRIGKVGNQKRVVGVLLGSWQKKVLDVSNSFAVPFDEDDKDDSVWFLDHDYLENMYGMFKKVNARERIVGWYHTGPKLHKNDIAINELMKRYCPNSVLVIIDVKPKDLGLPTEAYISVEEVHDDGTPTSKTFEHVTSEIGAEEAEEVGVEHLLRDIKDTTVGTLSQRITNQVHGLKGLNSKLLDIRSYLEKVATGKLPINHQIIYQLQDVFNLLPDVSLQEFVKAFYLKTNDQMVVVYLASLIRSVVALHNLINNKIANRDAEKKEGQEKEESKKDRKEDKEKDKDKEKSDVKKEEKKEKK | |
| 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 |
|---|---|---|---|---|---|
| 28 | Ubiquitination | DHFNRIGKVGNQKRV HHHHHCCCCCCCHHH | 21906983 | ||
| 33 | Ubiquitination | IGKVGNQKRVVGVLL CCCCCCCHHHHEEEE | 22817900 | ||
| 45 | Ubiquitination | VLLGSWQKKVLDVSN EEECHHHHHEECCCC | 21906983 | ||
| 45 | Acetylation | VLLGSWQKKVLDVSN EEECHHHHHEECCCC | 25953088 | ||
| 46 | Ubiquitination | LLGSWQKKVLDVSNS EECHHHHHEECCCCC | 22817900 | ||
| 100 | Ubiquitination | GWYHTGPKLHKNDIA EEEECCCCCCCCCHH | 22817900 | ||
| 100 | Acetylation | GWYHTGPKLHKNDIA EEEECCCCCCCCCHH | 25953088 | ||
| 103 | Ubiquitination | HTGPKLHKNDIAINE ECCCCCCCCCHHHHH | 21906983 | ||
| 112 | Sulfoxidation | DIAINELMKRYCPNS CHHHHHHHHHHCCCC | 21406390 | ||
| 113 | Ubiquitination | IAINELMKRYCPNSV HHHHHHHHHHCCCCE | 22817900 | ||
| 113 | Acetylation | IAINELMKRYCPNSV HHHHHHHHHHCCCCE | 26051181 | ||
| 119 | Phosphorylation | MKRYCPNSVLVIIDV HHHHCCCCEEEEEEC | 20860994 | ||
| 127 | Ubiquitination | VLVIIDVKPKDLGLP EEEEEECCHHHCCCC | 33845483 | ||
| 129 | Ubiquitination | VIIDVKPKDLGLPTE EEEECCHHHCCCCCE | 33845483 | ||
| 138 | Phosphorylation | LGLPTEAYISVEEVH CCCCCEEEEEEEEEC | 27134283 | ||
| 149 | Phosphorylation | EEVHDDGTPTSKTFE EEECCCCCCCCHHHC | 30266825 | ||
| 151 | Phosphorylation | VHDDGTPTSKTFEHV ECCCCCCCCHHHCHH | 30266825 | ||
| 152 | Phosphorylation | HDDGTPTSKTFEHVT CCCCCCCCHHHCHHH | 30266825 | ||
| 180 | Ubiquitination | EHLLRDIKDTTVGTL HHHHHHCCCCCHHHH | 23000965 | ||
| 180 | 2-Hydroxyisobutyrylation | EHLLRDIKDTTVGTL HHHHHHCCCCCHHHH | - | ||
| 180 | Acetylation | EHLLRDIKDTTVGTL HHHHHHCCCCCHHHH | 25953088 | ||
| 182 | Phosphorylation | LLRDIKDTTVGTLSQ HHHHCCCCCHHHHHH | 21406692 | ||
| 183 | Phosphorylation | LRDIKDTTVGTLSQR HHHCCCCCHHHHHHH | 21406692 | ||
| 186 | Phosphorylation | IKDTTVGTLSQRITN CCCCCHHHHHHHHHH | 25850435 | ||
| 188 | Phosphorylation | DTTVGTLSQRITNQV CCCHHHHHHHHHHHH | 21406692 | ||
| 199 | 2-Hydroxyisobutyrylation | TNQVHGLKGLNSKLL HHHHCCCCCCCHHHH | - | ||
| 199 | Malonylation | TNQVHGLKGLNSKLL HHHHCCCCCCCHHHH | 32601280 | ||
| 199 | Acetylation | TNQVHGLKGLNSKLL HHHHCCCCCCCHHHH | 25953088 | ||
| 199 | Ubiquitination | TNQVHGLKGLNSKLL HHHHCCCCCCCHHHH | 23000965 | ||
| 203 | Phosphorylation | HGLKGLNSKLLDIRS CCCCCCCHHHHHHHH | 20068231 | ||
| 204 | Malonylation | GLKGLNSKLLDIRSY CCCCCCHHHHHHHHH | 26320211 | ||
| 204 | Acetylation | GLKGLNSKLLDIRSY CCCCCCHHHHHHHHH | 19608861 | ||
| 204 | Ubiquitination | GLKGLNSKLLDIRSY CCCCCCHHHHHHHHH | 23000965 | ||
| 204 | 2-Hydroxyisobutyrylation | GLKGLNSKLLDIRSY CCCCCCHHHHHHHHH | - | ||
| 209 | Methylation | NSKLLDIRSYLEKVA CHHHHHHHHHHHHHH | 115489477 | ||
| 214 | Ubiquitination | DIRSYLEKVATGKLP HHHHHHHHHHCCCCC | 22817900 | ||
| 214 | 2-Hydroxyisobutyrylation | DIRSYLEKVATGKLP HHHHHHHHHHCCCCC | - | ||
| 214 | Acetylation | DIRSYLEKVATGKLP HHHHHHHHHHCCCCC | 19608861 | ||
| 219 | Ubiquitination | LEKVATGKLPINHQI HHHHHCCCCCCCHHH | 22817900 | ||
| 228 | Phosphorylation | PINHQIIYQLQDVFN CCCHHHHHHHHHHHH | 24043423 | ||
| 241 | Phosphorylation | FNLLPDVSLQEFVKA HHCCCCCCHHHHHHH | 24043423 | ||
| 253 | Phosphorylation | VKAFYLKTNDQMVVV HHHHCCCCCCHHHHH | 21406692 | ||
| 261 | Phosphorylation | NDQMVVVYLASLIRS CCHHHHHHHHHHHHH | 21406692 | ||
| 264 | Phosphorylation | MVVVYLASLIRSVVA HHHHHHHHHHHHHHH | 21406692 | ||
| 268 | Phosphorylation | YLASLIRSVVALHNL HHHHHHHHHHHHHHH | - | ||
| 279 | Acetylation | LHNLINNKIANRDAE HHHHHHHCHHCCHHH | 25825284 | ||
| 279 | Ubiquitination | LHNLINNKIANRDAE HHHHHHHCHHCCHHH | 23000965 | ||
| 293 | Ubiquitination | EKKEGQEKEESKKDR HHHHHHHHHHHHHHH | 24816145 | ||
| 304 | Ubiquitination | KKDRKEDKEKDKDKE HHHHHHHHHHHHHHH | - | ||
| 308 | Acetylation | KEDKEKDKDKEKSDV HHHHHHHHHHHHHHH | 7675241 | ||
| 310 | Acetylation | DKEKDKDKEKSDVKK HHHHHHHHHHHHHHH | 7675251 | ||
| 316 | Acetylation | DKEKSDVKKEEKKEK HHHHHHHHHHHHHHH | - | ||
| 317 | Acetylation | KEKSDVKKEEKKEKK HHHHHHHHHHHHHHC | - |
| 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 PSMD7_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PSMD7_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 PSMD7_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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