| UniProt ID | PSDE_HUMAN | |
|---|---|---|
| UniProt AC | O00487 | |
| Protein Name | 26S proteasome non-ATPase regulatory subunit 14 | |
| Gene Name | PSMD14 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 310 | |
| 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. The PSMD14 subunit is a metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains within the complex. Plays a role in response to double-strand breaks (DSBs): acts as a regulator of non-homologous end joining (NHEJ) by cleaving 'Lys-63'-linked polyubiquitin, thereby promoting retention of JMJD2A/KDM4A on chromatin and restricting TP53BP1 accumulation. Also involved in homologous recombination repair by promoting RAD51 loading.. | |
| Protein Sequence | MDRLLRLGGGMPGLGQGPPTDAPAVDTAEQVYISSLALLKMLKHGRAGVPMEVMGLMLGEFVDDYTVRVIDVFAMPQSGTGVSVEAVDPVFQAKMLDMLKQTGRPEMVVGWYHSHPGFGCWLSGVDINTQQSFEALSERAVAVVVDPIQSVKGKVVIDAFRLINANMMVLGHEPRQTTSNLGHLNKPSIQALIHGLNRHYYSITINYRKNELEQKMLLNLHKKSWMEGLTLQDYSEHCKHNESVVKEMLELAKNYNKAVEEEDKMTPEQLAIKNVGKQDPKRHLEEHVDVLMTSNIVQCLAAMLDTVVFK | |
| 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 |
|---|---|---|---|---|---|
| 27 | Phosphorylation | TDAPAVDTAEQVYIS CCCCCCCCHHHHHHH | 26.04 | 28122231 | |
| 32 | Phosphorylation | VDTAEQVYISSLALL CCCHHHHHHHHHHHH | 8.52 | 22817900 | |
| 34 | Phosphorylation | TAEQVYISSLALLKM CHHHHHHHHHHHHHH | 11.12 | 28122231 | |
| 35 | Phosphorylation | AEQVYISSLALLKML HHHHHHHHHHHHHHH | 14.22 | 28122231 | |
| 43 | Ubiquitination | LALLKMLKHGRAGVP HHHHHHHHCCCCCCC | 40.28 | 21906983 | |
| 51 | Sulfoxidation | HGRAGVPMEVMGLML CCCCCCCHHHHHHHH | 5.87 | 30846556 | |
| 54 | Sulfoxidation | AGVPMEVMGLMLGEF CCCCHHHHHHHHHHH | 1.86 | 30846556 | |
| 57 | Sulfoxidation | PMEVMGLMLGEFVDD CHHHHHHHHHHHCCC | 3.61 | 30846556 | |
| 75 | Sulfoxidation | RVIDVFAMPQSGTGV EEEEEEECCCCCCCC | 1.79 | 30846556 | |
| 94 | Ubiquitination | VDPVFQAKMLDMLKQ ECHHHHHHHHHHHHH | 29.25 | 21906983 | |
| 150 | Phosphorylation | VVVDPIQSVKGKVVI EEECCHHHCCCEEEE | 26.90 | 19060867 | |
| 152 | Acetylation | VDPIQSVKGKVVIDA ECCHHHCCCEEEEEH | 59.26 | 25953088 | |
| 152 | Ubiquitination | VDPIQSVKGKVVIDA ECCHHHCCCEEEEEH | 59.26 | 21906983 | |
| 154 | 2-Hydroxyisobutyrylation | PIQSVKGKVVIDAFR CHHHCCCEEEEEHHH | 27.84 | - | |
| 154 | Ubiquitination | PIQSVKGKVVIDAFR CHHHCCCEEEEEHHH | 27.84 | 21906983 | |
| 177 | Phosphorylation | LGHEPRQTTSNLGHL CCCCCCCCCCCCCCC | 33.21 | 20068231 | |
| 178 | Phosphorylation | GHEPRQTTSNLGHLN CCCCCCCCCCCCCCC | 13.79 | 20068231 | |
| 179 | Phosphorylation | HEPRQTTSNLGHLNK CCCCCCCCCCCCCCH | 33.18 | 20068231 | |
| 186 | Ubiquitination | SNLGHLNKPSIQALI CCCCCCCHHHHHHHH | 46.64 | 21906983 | |
| 188 | Phosphorylation | LGHLNKPSIQALIHG CCCCCHHHHHHHHHH | 29.01 | 20068231 | |
| 188 | O-linked_Glycosylation | LGHLNKPSIQALIHG CCCCCHHHHHHHHHH | 29.01 | 30379171 | |
| 209 | Ubiquitination | SITINYRKNELEQKM EEEEECCCCHHHHHH | 44.40 | 21906983 | |
| 215 | Ubiquitination | RKNELEQKMLLNLHK CCCHHHHHHHHHHHH | 23.34 | 21906983 | |
| 216 | Sulfoxidation | KNELEQKMLLNLHKK CCHHHHHHHHHHHHH | 5.27 | 30846556 | |
| 222 | Ubiquitination | KMLLNLHKKSWMEGL HHHHHHHHHCHHCCC | 52.23 | 21906983 | |
| 222 | 2-Hydroxyisobutyrylation | KMLLNLHKKSWMEGL HHHHHHHHHCHHCCC | 52.23 | - | |
| 223 | Ubiquitination | MLLNLHKKSWMEGLT HHHHHHHHCHHCCCC | 38.31 | - | |
| 224 | Phosphorylation | LLNLHKKSWMEGLTL HHHHHHHCHHCCCCH | 36.14 | 22199227 | |
| 226 | Sulfoxidation | NLHKKSWMEGLTLQD HHHHHCHHCCCCHHH | 3.65 | 30846556 | |
| 234 | Phosphorylation | EGLTLQDYSEHCKHN CCCCHHHHHHHHCCC | 11.73 | 27642862 | |
| 239 | Ubiquitination | QDYSEHCKHNESVVK HHHHHHHCCCHHHHH | 51.91 | - | |
| 239 | Acetylation | QDYSEHCKHNESVVK HHHHHHHCCCHHHHH | 51.91 | 21466224 | |
| 246 | Ubiquitination | KHNESVVKEMLELAK CCCHHHHHHHHHHHH | 34.94 | 21906983 | |
| 246 | Acetylation | KHNESVVKEMLELAK CCCHHHHHHHHHHHH | 34.94 | 21466224 | |
| 253 | Ubiquitination | KEMLELAKNYNKAVE HHHHHHHHHHHHHHH | 73.01 | 21906983 | |
| 257 | Acetylation | ELAKNYNKAVEEEDK HHHHHHHHHHHHHHC | 43.37 | 26051181 | |
| 257 | Ubiquitination | ELAKNYNKAVEEEDK HHHHHHHHHHHHHHC | 43.37 | 21906983 | |
| 264 | Ubiquitination | KAVEEEDKMTPEQLA HHHHHHHCCCHHHHH | 48.21 | 21906983 | |
| 264 | Acetylation | KAVEEEDKMTPEQLA HHHHHHHCCCHHHHH | 48.21 | 26051181 | |
| 265 | Sulfoxidation | AVEEEDKMTPEQLAI HHHHHHCCCHHHHHH | 13.46 | 28465586 | |
| 266 | Phosphorylation | VEEEDKMTPEQLAIK HHHHHCCCHHHHHHH | 29.43 | 29255136 | |
| 273 | Acetylation | TPEQLAIKNVGKQDP CHHHHHHHCCCCCCH | 39.72 | 27452117 | |
| 273 | Ubiquitination | TPEQLAIKNVGKQDP CHHHHHHHCCCCCCH | 39.72 | 21906983 | |
| 277 | Ubiquitination | LAIKNVGKQDPKRHL HHHHCCCCCCHHHHH | 47.44 | 21906983 | |
| 306 | Phosphorylation | CLAAMLDTVVFK--- HHHHHHHHHHCC--- | 18.01 | 22210691 |
| 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 PSDE_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PSDE_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 PSDE_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 |
| "Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction."; Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.; Mol. Cell. Proteomics 6:1952-1967(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, AND MASSSPECTROMETRY. | |
| "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, 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-32, AND MASSSPECTROMETRY. | |
