PSD11_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PSD11_MOUSE
• UniProt AC: Q8BG32
• Protein Name: 26S proteasome non-ATPase regulatory subunit 11
• Gene Name: Psmd11
• Organism: Mus musculus (Mouse).
• Sequence Length: 422
• 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. In the complex, PSMD11 is required for proteasome assembly. Plays a key role in increased proteasome activity in embryonic stem cells (ESCs): its high expression in ESCs promotes enhanced assembly of the 26S proteasome, followed by higher proteasome activity..
• Protein Sequence: MAAAAVVEFQRAQSLLSTDREASIDILHSIVKRDIQENDEEAVQVKEQSILELGSLLAKTGQAAELGGLLKYVRPFLNSISKAKAARLVRSLLDLFLDMEAATGQEVELCLECIEWAKSEKRTFLRQALEARLVSLYFDTKRYQEALHLGSQLLRELKKMDDKALLVEVQLLESKTYHALSNLPKARAALTSARTTANAIYCPPKLQATLDMQSGIIHAAEEKDWKTAYSYFYEAFEGYDSIDSPKAITSLKYMLLCKIMLNTPEDVQALVSGKLALRYAGRQTEALKCVAQASKNRSLADFEKALTDYRAELRDDPIISTHLAKLYDNLLEQNLIRVIEPFSRVQIEHISSLIKLSKADVERKLSQMILDKKFHGILDQGEGVLIIFDEPPVDKTYEAALETIQNMSKVVDSLYSKAKKLT

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
2	Acetylation	------MAAAAVVEF ------CCHHHHHHH	13.05	16857966
14	Phosphorylation	VEFQRAQSLLSTDRE HHHHHHHHHHCCCHH	30.23	26824392
17	Phosphorylation	QRAQSLLSTDREASI HHHHHHHCCCHHHHH	33.29	26643407
18	Phosphorylation	RAQSLLSTDREASID HHHHHHCCCHHHHHH	38.76	26643407
23	Phosphorylation	LSTDREASIDILHSI HCCCHHHHHHHHHHH	18.95	28507225
29	Phosphorylation	ASIDILHSIVKRDIQ HHHHHHHHHHHHHHH	26.15	25266776
32	Ubiquitination	DILHSIVKRDIQEND HHHHHHHHHHHHCCC	42.56	-
32	Acetylation	DILHSIVKRDIQEND HHHHHHHHHHHHCCC	42.56	22826441
59	Ubiquitination	ELGSLLAKTGQAAEL HHHHHHHHHCCHHHH	53.83	-
60	Phosphorylation	LGSLLAKTGQAAELG HHHHHHHHCCHHHHH	28.99	-
79	Phosphorylation	YVRPFLNSISKAKAA HHHHHHHHHHHHHHH	30.31	-
141	Acetylation	VSLYFDTKRYQEALH HHHHCCCHHHHHHHH	51.45	23236377
185	Malonylation	HALSNLPKARAALTS HHHCCCHHHHHHHHC	54.38	26320211
202	S-nitrosocysteine	TTANAIYCPPKLQAT HHCCCCCCCHHHHHE	3.67	-
202	S-nitrosylation	TTANAIYCPPKLQAT HHCCCCCCCHHHHHE	3.67	21278135
252	Acetylation	PKAITSLKYMLLCKI HHHHHHHHHHHHHHH	28.51	22826441
272	Phosphorylation	EDVQALVSGKLALRY HHHHHHHHCHHHHHH	30.94	25338131
274	Acetylation	VQALVSGKLALRYAG HHHHHHCHHHHHHCC	24.07	23954790
289	Glutathionylation	RQTEALKCVAQASKN CCHHHHHHHHHHHCC	2.97	24333276
304	Acetylation	RSLADFEKALTDYRA CCHHHHHHHHHHHHH	49.00	23864654
366	Phosphorylation	ADVERKLSQMILDKK HHHHHHHHHHHHHHH	22.27	28418008
413	Phosphorylation	NMSKVVDSLYSKAKK HHHHHHHHHHHHHHH	20.00	25367039
415	Phosphorylation	SKVVDSLYSKAKKLT HHHHHHHHHHHHHCC	16.45	22817900
416	Phosphorylation	KVVDSLYSKAKKLT- HHHHHHHHHHHHCC-	31.28	22345495
417	Acetylation	VVDSLYSKAKKLT-- HHHHHHHHHHHCC--	51.14	22826441
417	Malonylation	VVDSLYSKAKKLT-- HHHHHHHHHHHCC--	51.14	26320211

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
14	S	Phosphorylation	Kinase	PKACA	P17612	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PSD11_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PSD11_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of PSD11_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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-14, AND MASSSPECTROMETRY.
PubMed: 17242355