PSMD1_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PSMD1_DROME
• UniProt AC: Q9V3P6
• Protein Name: 26S proteasome non-ATPase regulatory subunit 1
• Gene Name: Rpn2
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 1020
• Protein Description: Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins..
• Protein Sequence: MSLTSAAGIISLLDEPMPDLKVFALKKLDNIVDEFWPEISESIEKIEMLHEDRSFPENKLAGMVASKVFYHLGSFEDALTYALGAGDLFDVNARNEYTETIIAKCIDFYIAQRVEFIENPKEASVVDERLEGIVNRMIQRCLDDNQFRQALGIALETRRMDTFKDAIMKSDDVRGMLAYAYNVTMSLIQNRGFRNEVLRCLVSLYRDLGVPDYVNMCQCLIFLEDPFAVAEMLDNLTRSSVETNNLMAYQIAFDLYESATQEFLGNVLQHLKNTAPIPTALPSTFKPQGTTSEDGAKSEGDKSKSDEDITEETPADDKVERTIDSLNEVEKLHQKNIEKLISILSGEVSIDLQLQFLIRSNHADLQVLRGTKEAVRVSICHTATVIANAFMHSGTTSDQFLRDNLDWLARATNWAKLTATASLGVIHRGHEKDSLALMQSYLPKEAGPSSGYSEGGALYALGLIHANHGANIIDYLLQQLKDAQNENVRHGGCLGLGLAGMGTHRQDLYEQLKFNLYQDDAVTGEAAGIAMGMVMLGSKNAQAIEDMVSYAQETQHEKILRGLAVGISLTMFSRLEEADPLVTSLSSDKDPVLRRSGMYTIAMAYNGTGSNKAIRKLLHVAVSDVNDDVRRAAVTAIGFILFRSPEQCPSVVSLLAESYNPHVRYGAAMALGIACAGTGLREAIALLEPMVKFDPVNFVRQGALIASAMILIQHTDQSCPKSTFFRQLYAEVISNKHEDVMAKYGAILAQGIIDAGGRNATLSLQSRTGHTNLQAVVGMLAFTQYWYWFPLAHTLSLAFTPTCVIGLNSDLKMPKMEYKSAAKPSLYAYPAPLEEKKSEEREKVATAVLSIAARQKRRENADKKEDEKMDVDEDSKEGAAVKKDEEAKADEKMVTDEKPKKKDEKEKKKEEDKEKEAAGTSSEKDKDKEKDKKEKKEPEPTSEILQNPARVLRQQLKVLSVIDGQSYEPLKDVTIGGIIVFQHTGKAEDQELVEPVAAFGPMNDEEKEPEPPEPFEYIED

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
124	Phosphorylation	IENPKEASVVDERLE CCCCCCCCHHHHHHH	24.62	22817900
291	Phosphorylation	TFKPQGTTSEDGAKS CCCCCCCCCCCCCCC	36.62	18327897
292	Phosphorylation	FKPQGTTSEDGAKSE CCCCCCCCCCCCCCC	33.26	19429919
298	Phosphorylation	TSEDGAKSEGDKSKS CCCCCCCCCCCCCCC	46.40	19429919
303	Phosphorylation	AKSEGDKSKSDEDIT CCCCCCCCCCCCCCC	41.97	19429919
305	Phosphorylation	SEGDKSKSDEDITEE CCCCCCCCCCCCCCC	54.01	19429919
310	Phosphorylation	SKSDEDITEETPADD CCCCCCCCCCCCCCH	39.84	19429919
313	Phosphorylation	DEDITEETPADDKVE CCCCCCCCCCCHHHH	19.97	19429919
318	Acetylation	EETPADDKVERTIDS CCCCCCHHHHHHHHH	46.68	21791702
325	Phosphorylation	KVERTIDSLNEVEKL HHHHHHHHHHHHHHH	29.28	23607784
846	Phosphorylation	EEREKVATAVLSIAA HHHHHHHHHHHHHHH	21.93	21082442
875	Phosphorylation	KMDVDEDSKEGAAVK CCCCCCCCCCCCCCC	30.47	19429919
922	Phosphorylation	KEAAGTSSEKDKDKE HHHHCCCCHHHHHHH	48.80	22817900

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

Oops, there are no upstream regulatory protein records of PSMD1_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PSMD1_DROME !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PSMD1_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ADRM1_DROME	Rpn13	physical	14605208
ENY2B_DROME	e(y)2b	physical	14605208
MECR_DROME	CG16935	physical	14605208
ADRM1_DROME	Rpn13	physical	22036573
PSA1_DROME	Prosalpha6	physical	22036573
PSA4_DROME	Prosalpha3	physical	22036573
PSDE_DROME	Rpn11	physical	22036573
PSB4_DROME	Prosbeta7	physical	22036573
PSMD3_DROME	Rpn3	physical	22036573
PSA2_DROME	Prosalpha2	physical	22036573

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-291; SER-298; SER-303;SER-305 AND THR-310, AND MASS SPECTROMETRY.
PubMed: 18327897