U2AFA_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: U2AFA_ARATH
• UniProt AC: Q9S709
• Protein Name: Splicing factor U2af small subunit A
• Gene Name: U2AF35A
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 296
• Subcellular Localization: Nucleus speckle .
• Protein Description: Necessary for the splicing of pre-mRNA (By similarity). Probably active at the 3' splice sites..
• Protein Sequence: MAEHLASIFGTEKDRVNCPFYFKIGACRHGDRCSRLHNRPTISPTLLLSNMYQRPDMITPGVDAQGQPLDPRKIQEHFEDFFEDLFEELGKFGEIESLNICDNLADHMIGNVYVQFKEEDQAAAALQALQGRFYSGRPIIADFSPVTDFREATCRQYEENNCNRGGYCNFMHVKLVSRELRRKLFGRYRRSYRRGSRSRSRSRSISPRNKRDNDRRDPSHREFSHRDRDREFYRHGSGKRSSERSERQERDGSRGRRQASPKRGGSPGGGREGSEERRARIEQWNREREEKEEGGA

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
260	Phosphorylation	SRGRRQASPKRGGSP CCCCCCCCCCCCCCC	23.71	23776212
266	Phosphorylation	ASPKRGGSPGGGREG CCCCCCCCCCCCCCC	24.16	23776212
274	Phosphorylation	PGGGREGSEERRARI CCCCCCCHHHHHHHH	31.37	23776212

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

Oops, there are no upstream regulatory protein records of U2AFA_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of U2AFA_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 U2AFA_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
U2AFA_ARATH	ATU2AF35A	physical	22563826
U2AFB_ARATH	U2AF35B	physical	22563826
RU17_ARATH	U1-70K	physical	22563826

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-266 AND SER-274, ANDMASS SPECTROMETRY.
PubMed: 19376835