PATL3_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PATL3_ARATH
• UniProt AC: Q56Z59
• Protein Name: Patellin-3
• Gene Name: PATL3
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 490
• Subcellular Localization: Membrane; Peripheral membrane protein. Cytoplasm. Mainly membrane-associated. Also cytoplasmic (By similarity)..
• Protein Description: Carrier protein that may be involved in membrane-trafficking events associated with cell plate formation during cytokinesis. Binds to some hydrophobic molecules such as phosphoinositides and promotes their transfer between the different cellular sites (By similarity)..
• Protein Sequence: MAEEPTTTTLVTPEKLPSPSLTPSEVSESTQDALPTETETLEKVTETNPPETADTTTKPEEETAAEHHPPTVTETETASTEKQEVKDEASQKEVAEEKKSMIPQNLGSFKEESSKLSDLSNSEKKSLDELKHLVREALDNHQFTNTPEEVKIWGIPLLEDDRSDVVLLKFLRAREFKVKDSFAMLKNTIKWRKEFKIDELVEEDLVDDLDKVVFMHGHDREGHPVCYNVYGEFQNKELYNKTFSDEEKRKHFLRTRIQFLERSIRKLDFSSGGVSTIFQVNDMKNSPGLGKKELRSATKQAVELLQDNYPEFVFKQAFINVPWWYLVFYTVIGPFMTPRSKSKLVFAGPSRSAETLFKYISPEQVPVQYGGLSVDPCDCNPDFSLEDSASEITVKPGTKQTVEIIIYEKCELVWEIRVTGWEVSYKAEFVPEEKDAYTVVIQKPRKMRPSDEPVLTHSFKVNELGKVLLTVDNPTSKKKKLVYRFNVKPL

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	------MAEEPTTTT ------CCCCCCEEE	29.84	22223895
18	Phosphorylation	VTPEKLPSPSLTPSE ECCCCCCCCCCCHHH	37.24	19880383
20	Phosphorylation	PEKLPSPSLTPSEVS CCCCCCCCCCHHHCC	49.57	23660473
22	Phosphorylation	KLPSPSLTPSEVSES CCCCCCCCHHHCCHH	29.16	23660473
24	Phosphorylation	PSPSLTPSEVSESTQ CCCCCCHHHCCHHHH	45.45	23660473
27	Phosphorylation	SLTPSEVSESTQDAL CCCHHHCCHHHHCCC	23.06	23660473
29	Phosphorylation	TPSEVSESTQDALPT CHHHCCHHHHCCCCC	24.70	23660473
30	Phosphorylation	PSEVSESTQDALPTE HHHCCHHHHCCCCCC	26.81	23660473
36	Phosphorylation	STQDALPTETETLEK HHHCCCCCCCHHHHH	57.29	23660473
38	Phosphorylation	QDALPTETETLEKVT HCCCCCCCHHHHHHH	36.43	23660473
100	Phosphorylation	EVAEEKKSMIPQNLG HHHHHHHCCCCCCHH	32.77	23776212
108	Phosphorylation	MIPQNLGSFKEESSK CCCCCHHCHHHHHHH	35.99	30291188
113	Phosphorylation	LGSFKEESSKLSDLS HHCHHHHHHHHHHCC	33.59	24601666
114	Phosphorylation	GSFKEESSKLSDLSN HCHHHHHHHHHHCCH	40.68	24601666
342	Phosphorylation	FMTPRSKSKLVFAGP CCCCCCCCCEEEECC	32.25	24894044

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

Oops, there are no upstream regulatory protein records of PATL3_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PATL3_ARATH !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PATL3_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of PATL3_ARATH !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND MASSSPECTROMETRY.
PubMed: 19376835

"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana.";
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.;
J. Proteomics 72:439-451(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND MASSSPECTROMETRY.
PubMed: 19245862