UniProt ID | PSD10_HUMAN | |
---|---|---|
UniProt AC | O75832 | |
Protein Name | 26S proteasome non-ATPase regulatory subunit 10 | |
Gene Name | PSMD10 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 226 | |
Subcellular Localization | Cytoplasm . Nucleus . | |
Protein Description | Acts as a chaperone during the assembly of the 26S proteasome, specifically of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD10:PSMC4:PSMC5:PAAF1 module which probably assembles with a PSMD5:PSMC2:PSMC1:PSMD2 module. Independently of the proteasome, regulates EGF-induced AKT activation through inhibition of the RHOA/ROCK/PTEN pathway, leading to prolonged AKT activation. Plays an important role in RAS-induced tumorigenesis.; Acts as an proto-oncoprotein by being involved in negative regulation of tumor suppressors RB1 and p53/TP53. Overexpression is leading to phosphorylation of RB1 and proteasomal degradation of RB1. Regulates CDK4-mediated phosphorylation of RB1 by competing with CDKN2A for binding with CDK4. Facilitates binding of MDM2 to p53/TP53 and the mono- and polyubiquitination of p53/TP53 by MDM2 suggesting a function in targeting the TP53:MDM2 complex to the 26S proteasome. Involved in p53-independent apoptosis. Involved in regulation of NF-kappa-B by retaining it in the cytoplasm. Binds to the NF-kappa-B component RELA and accelerates its XPO1/CRM1-mediated nuclear export.. | |
Protein Sequence | MEGCVSNLMVCNLAYSGKLEELKESILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKALLGKGAQVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYEATAMHRAAAKGNLKMIHILLYYKASTNIQDTEGNTPLHLACDEERVEEAKLLVSQGASIYIENKEEKTPLQVAKGGLGLILKRMVEG | |
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 |
---|---|---|---|---|---|
1 | Acetylation | -------MEGCVSNL -------CCCHHHCE | 10.10 | - | |
6 | Phosphorylation | --MEGCVSNLMVCNL --CCCHHHCEEHHHH | 28.46 | 23401153 | |
15 | Phosphorylation | LMVCNLAYSGKLEEL EEHHHHHHCCCHHHH | 22.56 | 23401153 | |
18 | Ubiquitination | CNLAYSGKLEELKES HHHHHCCCHHHHHHH | 46.95 | 22817900 | |
23 | Ubiquitination | SGKLEELKESILADK CCCHHHHHHHHHCCC | 53.33 | 22817900 | |
23 | Ubiquitination | SGKLEELKESILADK CCCHHHHHHHHHCCC | 53.33 | 21890473 | |
23 | Ubiquitination | SGKLEELKESILADK CCCHHHHHHHHHCCC | 53.33 | 21890473 | |
25 | Phosphorylation | KLEELKESILADKSL CHHHHHHHHHCCCCH | 22.70 | 29396449 | |
30 | Ubiquitination | KESILADKSLATRTD HHHHHCCCCHHCCCC | 41.59 | 21890473 | |
30 | Ubiquitination | KESILADKSLATRTD HHHHHCCCCHHCCCC | 41.59 | 23000965 | |
30 | Ubiquitination | KESILADKSLATRTD HHHHHCCCCHHCCCC | 41.59 | 21890473 | |
30 | Acetylation | KESILADKSLATRTD HHHHHCCCCHHCCCC | 41.59 | 25953088 | |
30 | 2-Hydroxyisobutyrylation | KESILADKSLATRTD HHHHHCCCCHHCCCC | 41.59 | - | |
75 | Phosphorylation | DKDDAGWSPLHIAAS CCCCCCCCHHHHHHH | 19.37 | 20873877 | |
90 | Ubiquitination | AGRDEIVKALLGKGA CCCHHHHHHHHCCCC | 38.69 | 23000965 | |
90 | Ubiquitination | AGRDEIVKALLGKGA CCCHHHHHHHHCCCC | 38.69 | 21890473 | |
90 | Ubiquitination | AGRDEIVKALLGKGA CCCHHHHHHHHCCCC | 38.69 | 21890473 | |
90 | 2-Hydroxyisobutyrylation | AGRDEIVKALLGKGA CCCHHHHHHHHCCCC | 38.69 | - | |
95 | Ubiquitination | IVKALLGKGAQVNAV HHHHHHCCCCCCEEE | 51.55 | 23000965 | |
112 | Phosphorylation | NGCTPLHYAASKNRH CCCCHHHHHHCCCCC | 16.14 | 28857561 | |
115 | Phosphorylation | TPLHYAASKNRHEIA CHHHHHHCCCCCHHE | 23.45 | 26437602 | |
116 | Acetylation | PLHYAASKNRHEIAV HHHHHHCCCCCHHEE | 53.96 | 25953088 | |
116 | Malonylation | PLHYAASKNRHEIAV HHHHHHCCCCCHHEE | 53.96 | 26320211 | |
116 | Ubiquitination | PLHYAASKNRHEIAV HHHHHHCCCCCHHEE | 53.96 | 32015554 | |
138 | Phosphorylation | NPDAKDHYEATAMHR CCCHHHHHHHHHHHH | 19.86 | 24927040 | |
138 | Nitration | NPDAKDHYEATAMHR CCCHHHHHHHHHHHH | 19.86 | - | |
143 | Sulfoxidation | DHYEATAMHRAAAKG HHHHHHHHHHHHHHC | 1.59 | 30846556 | |
149 | Ubiquitination | AMHRAAAKGNLKMIH HHHHHHHHCCCEEEE | 43.54 | 22817900 | |
153 | Ubiquitination | AAAKGNLKMIHILLY HHHHCCCEEEEEEEH | 39.55 | 21906983 | |
193 | Phosphorylation | EEAKLLVSQGASIYI HHHHHHHHCCCCEEE | 23.90 | 29396449 | |
197 | Phosphorylation | LLVSQGASIYIENKE HHHHCCCCEEEECCC | 23.81 | 29396449 | |
199 | Phosphorylation | VSQGASIYIENKEEK HHCCCCEEEECCCCC | 10.33 | 29396449 | |
207 | Phosphorylation | IENKEEKTPLQVAKG EECCCCCCCCCHHCC | 32.29 | 20068231 | |
213 | Ubiquitination | KTPLQVAKGGLGLIL CCCCCHHCCCHHHHH | 55.44 | 21890473 | |
213 | Ubiquitination | KTPLQVAKGGLGLIL CCCCCHHCCCHHHHH | 55.44 | 22817900 | |
221 | 2-Hydroxyisobutyrylation | GGLGLILKRMVEG-- CCHHHHHHHHHCC-- | 31.30 | - | |
221 | Ubiquitination | GGLGLILKRMVEG-- CCHHHHHHHHHCC-- | 31.30 | 21906983 | |
221 | Ubiquitination | GGLGLILKRMVEG-- CCHHHHHHHHHCC-- | 31.30 | 21890473 | |
221 | Acetylation | GGLGLILKRMVEG-- CCHHHHHHHHHCC-- | 31.30 | 25953088 |
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 PSD10_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PSD10_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 PSD10_HUMAN !! |
Kegg Disease | ||||||
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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 |
"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. |