PP4R2_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PP4R2_DROME
• UniProt AC: Q9W2U4
• Protein Name: Serine/threonine-protein phosphatase 4 regulatory subunit 2
• Gene Name: PPP4R2r
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 609
• Protein Description: Regulatory subunit of serine/threonine-protein phosphatase 4 (PP4) (By similarity). The probable PP4 complex Pp4-19C-PPP4R2r-flfl (PPP4C-PPP4R2-PPP4R3) is required to prevent caspase induced cell death (in vitro)..
• Protein Sequence: MVTMENSDEIMQILERFTDLKQKEIPKELEEYLQYVAKTGDTIFKWSSLKYLFREKLLSVIKHFNEDSPRLEEIPNYPNVDPFNYETMKSSLLERLDLFNAAPFTVQRLCELLIDPRKQYSRIDKFMRALEKNILVVSTIDPGRKRTESENGDSLDSVVNGDLSMEVNIDIEMENNNGNADEGSSPGAGSAGCAQKASCPRSDDNDQPKAKKAKLEIDGEERSEASDETDTEVATRVKNEKDEKNDNDETDSPHEAAEIEEPDEEVDEADQETKTTKQPAYGSQKEGEQEESFPSSADDEAEDPMVSKSIEAEKELVAQEKKREEDKKVAIEPKEEIVKKEEVVESDKPDGKVAQLGDKAVVKKSTPPADGENQEPVKVKAENEKEEKKHAPIKTEKQDDIDSTETDDAPSAEKPAEEKIASSESKPKTKSEDDPEAETKKSQPEKTETEAAEKSVSDEKQAAEPNAESENRNDLTTSKATEAAQESVEKSPVEDASSPAVEDLAAATTPQSPLGAADSAAETPPAETGDDSQASPLVAAVTPPVLALNDQPMEDTPAEEEARVSPSATVEEVVMAESANAGAMATEEAAKDDPAAMEIDDTSQEVMMQ

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
62	Acetylation	EKLLSVIKHFNEDSP HHHHHHHHHHCCCCC	39.73	21791702
68	Phosphorylation	IKHFNEDSPRLEEIP HHHHCCCCCCHHHCC	13.02	19429919
77	Phosphorylation	RLEEIPNYPNVDPFN CHHHCCCCCCCCCCC	7.28	19429919
223	Phosphorylation	EIDGEERSEASDETD EECCCHHHCCCCCCC	40.57	22817900
226	Phosphorylation	GEERSEASDETDTEV CCHHHCCCCCCCHHH	31.74	25749252
229	Phosphorylation	RSEASDETDTEVATR HHCCCCCCCHHHHHH	53.89	25749252
250	Phosphorylation	EKNDNDETDSPHEAA CCCCCCCCCCHHHHH	44.64	19429919
252	Phosphorylation	NDNDETDSPHEAAEI CCCCCCCCHHHHHCC	35.26	19429919
348	Acetylation	EEVVESDKPDGKVAQ HHHHCCCCCCCCEEE	55.05	21791702
352	Acetylation	ESDKPDGKVAQLGDK CCCCCCCCEEECCCE	41.60	21791702
365	Phosphorylation	DKAVVKKSTPPADGE CEEEEECCCCCCCCC	40.19	19429919
366	Phosphorylation	KAVVKKSTPPADGEN EEEEECCCCCCCCCC	42.02	19429919
454	Acetylation	TETEAAEKSVSDEKQ HHHHHHHHHHCHHHH	51.97	21791702
565	Phosphorylation	AEEEARVSPSATVEE HHHHHCCCCCCCCEE	13.95	29892262
567	Phosphorylation	EEARVSPSATVEEVV HHHCCCCCCCCEEHH	29.12	29892262
569	Phosphorylation	ARVSPSATVEEVVMA HCCCCCCCCEEHHHH	32.56	29892262
602	Phosphorylation	AAMEIDDTSQEVMMQ CCCCCCCCCHHHHCC	28.67	19429919
603	Phosphorylation	AMEIDDTSQEVMMQ- CCCCCCCCHHHHCC-	31.19	19429919

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

Oops, there are no upstream regulatory protein records of PP4R2_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PP4R2_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 PP4R2_DROME !!

Protein-Protein Interaction

Oops, there are no PPI records of PP4R2_DROME !!

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 SER-68; SER-223; SER-226 ANDSER-252, AND MASS SPECTROMETRY.
PubMed: 18327897

"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells.";
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
Mol. Biosyst. 3:275-286(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252; THR-602 ANDSER-603, AND MASS SPECTROMETRY.
PubMed: 17372656