dbPTM

PSMD2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PSMD2_MOUSE
UniProt AC	Q8VDM4
Protein Name	26S proteasome non-ATPase regulatory subunit 2
Gene Name	Psmd2
Organism	Mus musculus (Mouse).
Sequence Length	908
Subcellular Localization
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.; Binds to the intracellular domain of tumor necrosis factor type 1 receptor. The binding domain of TRAP1 and TRAP2 resides outside the death domain of TNFR1..
Protein Sequence	MEEGGRDKTPVQSQQPSATTPSGADEKSSGKERRDAGEKDKEQELSEEDKQLQDELEMLVERLGEKDTSLYRPALEELRRQIRSSTTSMTSVPKPLKFLRPHYGKLKEIYENMAPGENKCFAADIISVLAMTMSGERECLKYRLVGSQEELASWGHEYVRHLAGEVAKEWQELDDAEKAQREPLLTLVKEIVPYNMAHNAEHEACDLLMEIEQVDMLEKDIDENAYAKVCLYLTSCVNYVPEPENSALLRCALGVFRKFSRFPEALRLALMLNDMELVEDIFTSCKDVVVQKQMAFMLGRHGVFLELSEDVEEYEDLTEIMSNVQLNSNFLALARELDIMEPKVPDDIYKTHLENNRFGGSGSQVDSARMNLASSFVNGFVNAAFGQDKLLTDDGNKWLYKNKDHGMLSAAASLGMILLWDVDGGLTQIDKYLYSSEDYIKSGALLACGIVNSGVRNECDPALALLSDYVLHNSNTMRLGSIFGLGLAYAGSNREDVLTLLLPVMGDSKSSMEVAGVTALACGMIAVGSCNGDVTSTILQTIMEKSETELKDTYARWLPLGLGLNHLGKGEAIEAILAALEVVSEPFRSFANTLVDVCAYAGSGNVLKVQQLLHICSEHFDSKEKEEDKDKKEKKDKDKKEAPADMGAHQGVAVLGIALIAMGEEIGAEMALRTFGHLLRYGEPTLRRAVPLALALISVSNPRLNILDTLSKFSHDADPEVSYNSIFAMGMVGSGTNNARLAAMLRQLAQYHAKDPNNLFMVRLAQGLTHLGKGTLTLCPYHSDRQLMSQVAVAGLLTVLVSFLDVRNIILGKSHYVLYGLVAAMQPRMLVTFDEELRPLPVSVRVGQAVDVVGQAGKPKTITGFQTHTTPVLLAHGERAELATEEFLPVTPILEGFVILRKNPNYDL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEEGGRDK -------CCCCCCCC	10.77	17242355
1	Oxidation	-------MEEGGRDK -------CCCCCCCC	10.77	17242355
9	Phosphorylation	EEGGRDKTPVQSQQP CCCCCCCCCCCCCCC	32.74	25521595
13	Phosphorylation	RDKTPVQSQQPSATT CCCCCCCCCCCCCCC	30.89	25619855
17	Phosphorylation	PVQSQQPSATTPSGA CCCCCCCCCCCCCCC	33.63	25521595
19	Phosphorylation	QSQQPSATTPSGADE CCCCCCCCCCCCCCC	43.51	24925903
20	Phosphorylation	SQQPSATTPSGADEK CCCCCCCCCCCCCCC	18.38	25521595
22	Phosphorylation	QPSATTPSGADEKSS CCCCCCCCCCCCCCC	44.51	24925903
27	Ubiquitination	TPSGADEKSSGKERR CCCCCCCCCCCCCCC	50.93	-
28	Phosphorylation	PSGADEKSSGKERRD CCCCCCCCCCCCCCC	42.13	23684622
29	Phosphorylation	SGADEKSSGKERRDA CCCCCCCCCCCCCCC	66.02	-
39	Ubiquitination	ERRDAGEKDKEQELS CCCCCCHHHHHHHHC	73.51	-
41	Ubiquitination	RDAGEKDKEQELSEE CCCCHHHHHHHHCHH	72.81	-
46	Phosphorylation	KDKEQELSEEDKQLQ HHHHHHHCHHHHHHH	37.88	30352176
50	Ubiquitination	QELSEEDKQLQDELE HHHCHHHHHHHHHHH	57.07	-
66	Ubiquitination	LVERLGEKDTSLYRP HHHHHCCCCCHHHHH	65.59	-
94	Ubiquitination	TSMTSVPKPLKFLRP CCCCCCCCCCHHHHC	61.91	-
107	Ubiquitination	RPHYGKLKEIYENMA HCCCHHHHHHHHCCC	45.62	-
107	Acetylation	RPHYGKLKEIYENMA HCCCHHHHHHHHCCC	45.62	23806337
132	Phosphorylation	IISVLAMTMSGEREC HHHHHHHHHCCCHHH	11.54	26745281
134	Phosphorylation	SVLAMTMSGERECLK HHHHHHHCCCHHHHH	28.47	26745281
147	Phosphorylation	LKYRLVGSQEELASW HHHEECCCHHHHHHH	27.26	26643407
158	Phosphorylation	LASWGHEYVRHLAGE HHHHHHHHHHHHHHH	9.34	-
168	Ubiquitination	HLAGEVAKEWQELDD HHHHHHHHHHHHCCH	65.74	-
178	Ubiquitination	QELDDAEKAQREPLL HHCCHHHHHHHCHHH	52.09	-
189	Ubiquitination	EPLLTLVKEIVPYNM CHHHHHHHHHHCCCC	44.85	-
194	Phosphorylation	LVKEIVPYNMAHNAE HHHHHHCCCCCCCCH	13.48	-
286	Ubiquitination	EDIFTSCKDVVVQKQ HHHHHHCHHHHHHHH	54.01	-
292	Ubiquitination	CKDVVVQKQMAFMLG CHHHHHHHHHHHHHH	30.36	-
343	Ubiquitination	ELDIMEPKVPDDIYK HHCCCCCCCCCCHHH	53.76	-
343	Acetylation	ELDIMEPKVPDDIYK HHCCCCCCCCCCHHH	53.76	23236377
350	Malonylation	KVPDDIYKTHLENNR CCCCCHHHHHCCCCC	29.78	26320211
350	Ubiquitination	KVPDDIYKTHLENNR CCCCCHHHHHCCCCC	29.78	-
350	Acetylation	KVPDDIYKTHLENNR CCCCCHHHHHCCCCC	29.78	23236377
361	Phosphorylation	ENNRFGGSGSQVDSA CCCCCCCCCHHHHHH	35.33	25521595
363	Phosphorylation	NRFGGSGSQVDSARM CCCCCCCHHHHHHHH	28.82	25521595
367	Phosphorylation	GSGSQVDSARMNLAS CCCHHHHHHHHHHHH	20.93	28833060
397	Ubiquitination	LLTDDGNKWLYKNKD EECCCCCEEEEECCC	44.07	-
397	Acetylation	LLTDDGNKWLYKNKD EECCCCCEEEEECCC	44.07	23236377
441	Ubiquitination	YSSEDYIKSGALLAC HCCCHHHHCCHHHHH	36.29	-
448	S-palmitoylation	KSGALLACGIVNSGV HCCHHHHHCCCCCCC	3.74	28526873
459	S-palmitoylation	NSGVRNECDPALALL CCCCCCCCCHHHHHH	9.67	28526873
459	Glutathionylation	NSGVRNECDPALALL CCCCCCCCCHHHHHH	9.67	24333276
499	Phosphorylation	SNREDVLTLLLPVMG CCHHHHHHHHHHHHC	18.40	21454597
508	Phosphorylation	LLPVMGDSKSSMEVA HHHHHCCCCCHHHHH	28.80	21454597
551	Acetylation	EKSETELKDTYARWL HHCCCHHHHHHHHHH	41.62	23806337
551	Ubiquitination	EKSETELKDTYARWL HHCCCHHHHHHHHHH	41.62	-
551	Succinylation	EKSETELKDTYARWL HHCCCHHHHHHHHHH	41.62	23954790
598	S-palmitoylation	ANTLVDVCAYAGSGN HHHHHHHHHHCCCCC	1.76	28526873
754	Acetylation	QLAQYHAKDPNNLFM HHHHHHCCCCCCEEE	61.48	23954790
754	Ubiquitination	QLAQYHAKDPNNLFM HHHHHHCCCCCCEEE	61.48	-
779	Glutathionylation	GKGTLTLCPYHSDRQ CCCEEEECCCCCCHH	2.37	24333276
843	Phosphorylation	ELRPLPVSVRVGQAV CCCCCCEEEEECCEE	11.41	28725479
858	Ubiquitination	DVVGQAGKPKTITGF EEECCCCCCCEECEE	46.48	-
860	Ubiquitination	VGQAGKPKTITGFQT ECCCCCCCEECEEEC	56.92	-

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 PSMD2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PSMD2_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 PSMD2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PSMD2_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of PSMD2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-17, AND MASSSPECTROMETRY.	17242355 [Abstract]
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20 AND SER-22, AND MASSSPECTROMETRY.	17114649 [Abstract]
"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 THR-20, AND MASSSPECTROMETRY.	19131326 [Abstract]