dbPTM

PSMD9_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PSMD9_MOUSE
UniProt AC	Q9CR00
Protein Name	26S proteasome non-ATPase regulatory subunit 9
Gene Name	Psmd9
Organism	Mus musculus (Mouse).
Sequence Length	222
Subcellular Localization
Protein Description	Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). During the base subcomplex assembly is part of an intermediate PSMD9:PSMC6:PSMC3 module, also known as modulator trimer complex; PSMD9 is released during the further base assembly process (By similarity)..
Protein Sequence	MSGEDVPHRAESSEARAAAVSDIQDLMRRKEEIEAEIKANYDVLESQKGIGMNEPLVDCEGYPRADVDLYQVRTARHNIICLQNDHKALMKQVEEALHQLHARDKEKQARDMAEAREEAMNRRLASNSPVLPQAFARVNSISPGSPASIAGLQVDDEIVEFGSVNTQNFQSVQNVGTVVQHSEGKPLNVTVIRRGEKHQLRLIPTRWAGKGLLGCNIIPLQR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSGEDVPHR ------CCCCCCCCC	51.38	26824392
12	Phosphorylation	DVPHRAESSEARAAA CCCCCHHCHHHHHHH	32.28	30352176
13	Phosphorylation	VPHRAESSEARAAAV CCCCHHCHHHHHHHH	27.12	26643407
41	Phosphorylation	EAEIKANYDVLESQK HHHHHHCHHHHHHCC	16.58	29514104
59	S-nitrosocysteine	MNEPLVDCEGYPRAD CCCCCCCCCCCCCCC	3.22	-
59	Glutathionylation	MNEPLVDCEGYPRAD CCCCCCCCCCCCCCC	3.22	24333276
59	S-nitrosylation	MNEPLVDCEGYPRAD CCCCCCCCCCCCCCC	3.22	21278135
81	S-nitrosocysteine	TARHNIICLQNDHKA ECCCCEEEEECHHHH	2.57	-
81	S-nitrosylation	TARHNIICLQNDHKA ECCCCEEEEECHHHH	2.57	21278135
91	Ubiquitination	NDHKALMKQVEEALH CHHHHHHHHHHHHHH	52.63	-
126	Phosphorylation	AMNRRLASNSPVLPQ HHHHHHHHCCCCHHH	42.29	25521595
128	Phosphorylation	NRRLASNSPVLPQAF HHHHHHCCCCHHHHH	17.56	25521595
210	Ubiquitination	IPTRWAGKGLLGCNI EECCCCCCCCCCCEE	38.34	-
215	S-nitrosocysteine	AGKGLLGCNIIPLQR CCCCCCCCEEEECCC	3.14	-
215	S-nitrosylation	AGKGLLGCNIIPLQR CCCCCCCCEEEECCC	3.14	21278135
215	S-palmitoylation	AGKGLLGCNIIPLQR CCCCCCCCEEEECCC	3.14	28526873

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 PSMD9_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PSMD9_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 PSMD9_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PSMD9_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PSMD9_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128, AND MASSSPECTROMETRY.	19131326 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128, AND MASSSPECTROMETRY.	17242355 [Abstract]