PSD10_MOUSE - dbPTM
PSD10_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSD10_MOUSE
UniProt AC Q9Z2X2
Protein Name 26S proteasome non-ATPase regulatory subunit 10
Gene Name Psmd10
Organism Mus musculus (Mouse).
Sequence Length 231
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 (By similarity). 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 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 (By similarity)..
Protein Sequence MEGCVSNIMICNLAYSGKLDELKERILADKSLATRTDQDSRTALHWACSAGHTEIVEFLLQLGVPVNDKDDAGWSPLHIAASAGRDEIVKALLVKGAHVNAVNQNGCTPLHYAASKNRHEIAVMLLEGGANPDAKDHYDATAMHRAAAKGNLKMVHILLFYKASTNIQDTEGNTPLHLACDEERVEEAKFLVTQGASIYIENKEEKTPLQVAKGGLGLILKRLAESEEASM
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
30UbiquitinationKERILADKSLATRTD
HHHHHCCCCHHCCCC
41.5922790023
30UbiquitinationKERILADKSLATRTD
HHHHHCCCCHHCCCC
41.5922790023
107GlutathionylationNAVNQNGCTPLHYAA
CCCCCCCCCHHHHHH
4.6724333276
112PhosphorylationNGCTPLHYAASKNRH
CCCCHHHHHHCCCCC
16.1422817900
138PhosphorylationNPDAKDHYDATAMHR
CCCHHHHHCHHHHHH
19.8722817900
230PhosphorylationLAESEEASM------
HHHHHHHCC------
28.4528833060

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSD10_MOUSE !!

Disease-associated PTM Sites based on SAP

* 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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRS6B_MOUSEPsmc4physical
17292836

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PSD10_MOUSE

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Related Literatures of Post-Translational Modification

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