dbPTM

PSME3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PSME3_MOUSE
UniProt AC	P61290
Protein Name	Proteasome activator complex subunit 3
Gene Name	Psme3
Organism	Mus musculus (Mouse).
Sequence Length	254
Subcellular Localization	Nucleus . Cytoplasm . Localizes to the cytoplasm during mitosis following nuclear envelope breakdown at this distinct stage of the cell cycle which allows its interaction with MAP3K3 kinase.
Protein Description	Subunit of the 11S REG-gamma (also called PA28-gamma) proteasome regulator, a doughnut-shaped homoheptamer which associates with the proteasome. 11S REG-gamma activates the trypsin-like catalytic subunit of the proteasome but inhibits the chymotrypsin-like and postglutamyl-preferring (PGPH) subunits. Facilitates the MDM2-p53/TP53 interaction which promotes ubiquitination- and MDM2-dependent proteasomal degradation of p53/TP53, limiting its accumulation and resulting in inhibited apoptosis after DNA damage. May also be involved in cell cycle regulation. Mediates CCAR2 and CHEK2-dependent SIRT1 inhibition (By similarity)..
Protein Sequence	MASLLKVDQEVKLKVDSFRERITSEAEDLVANFFPKKLLELDSFLKEPILNIHDLTQIHSDMNLPVPDPILLTNSHDGLDGPTYKKRRLDECEEAFQGTKVFVMPNGMLKSNQQLVDIIEKVKPEIRLLIEKCNTVKMWVQLLIPRIEDGNNFGVSIQEETVAELRTVESEAASYLDQISRYYITRAKLVSKIAKYPHVEDYRRTVTEIDEKEYISLRLIISELRNQYVTLHDMILKNIEKIKRPRSSNAETLY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASLLKVDQ ------CCCCCCCCH	14.64	-
14	Ubiquitination	VDQEVKLKVDSFRER CCHHHHHHHHHHHHH	37.97	22790023
17	Phosphorylation	EVKLKVDSFRERITS HHHHHHHHHHHHHHH	29.23	-
23	Phosphorylation	DSFRERITSEAEDLV HHHHHHHHHHHHHHH	27.08	23984901
24	Phosphorylation	SFRERITSEAEDLVA HHHHHHHHHHHHHHH	32.22	26824392
36	Ubiquitination	LVANFFPKKLLELDS HHHHHCCHHHHCHHH	51.39	22790023
37	Ubiquitination	VANFFPKKLLELDSF HHHHCCHHHHCHHHH	59.55	22790023
86	Ubiquitination	LDGPTYKKRRLDECE CCCCCCCCCCHHHHH	32.13	22790023
92	Glutathionylation	KKRRLDECEEAFQGT CCCCHHHHHHHHCCC	5.98	24333276
121	Ubiquitination	QLVDIIEKVKPEIRL HHHHHHHHHCHHHHH	45.19	22790023
132	Acetylation	EIRLLIEKCNTVKMW HHHHHHHHCCHHHHH	26.28	22826441
195	Acetylation	KLVSKIAKYPHVEDY HHHHHHHCCCCHHHH	63.89	-
205	Phosphorylation	HVEDYRRTVTEIDEK CHHHHCCCEEECCHH	23.84	17203969
207	Phosphorylation	EDYRRTVTEIDEKEY HHHCCCEEECCHHHH	26.98	17203969
247	Phosphorylation	EKIKRPRSSNAETLY HHHCCCCCCCCCCCC	30.54	30635358
248	Phosphorylation	KIKRPRSSNAETLY- HHCCCCCCCCCCCC-	41.14	30635358

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
247	S	Phosphorylation	Kinase	CHEK2	Q9Z265	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
195	K	Acetylation	-
Acetylation at the major site Lys-195 is important for oligomerization and ability to degrade its target substrates.
247	S	Phosphorylation	12650640
Phosphorylation at Ser-247 promotes its association with CCAR2 (By similarity).

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 PSME3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
MAFA_MOUSE	Mafa	physical	21646385

Drug and Disease Associations

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

Regulatory Network of PSME3_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205 AND THR-207, ANDMASS SPECTROMETRY.	17203969 [Abstract]