BSL1_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BSL1_ARATH
• UniProt AC: Q8L7U5
• Protein Name: Serine/threonine-protein phosphatase BSL1
• Gene Name: BSL1
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 881
• Subcellular Localization: Nucleus .
• Protein Description: Phosphatase involved in elongation process, probably by acting as a regulator of brassinolide signaling..
• Protein Sequence: MGSKPWLHPAPQYKTLETFWDDEDDAPGPRCAHTLTAVAATKTHGPRLILFGGATAIEGGSSSVPGIRLAGVTNTVHSYDILTRKWTRLKPAGEPPSPRAAHAAAAVGTMVVFQGGIGPAGHSTDDLYVLDMTNDKFKWHRVVVQGDGPGPRYGHVMDLVSQRYLVTVTGNDGKRALSDAWALDTAQKPYVWQRLNPDGDRPSARMYASGSARSDGMFLLCGGRDTLGAPLGDAYGLLMHRNGQWEWTLAPGVAPSPRYQHAAVFVGARLHVSGGVLRGGRVIDAEASVAVLDTAAGVWLDRNGQVTSARGSKGQIDQDPSFELMRRCRHGAASVGIRIYVHGGLRGDVLLDDFLVAENSTFQSDISSPLLASDRTQQSSTPRFSYAARPPSGSEPSFSMSEGLSLDENSLEKLTEASAAEAEVASSVWRAAQLGAGTLDEEPSTSDASSPIVESTTDGTANEGDVRLHPRAVVVAKETVGSLGGMVRQLSLDQFQNESRRMVPMNNSDVPQPTKKFTRQKSPQGLHKKVIAALLRPRNWKPPGNRKFFLDSYEVGELCYAAEQIFMHEQTVLQLKAPIKVFGDLHGQFGDLMRLFDEYGFPSTAGDITYIDYLFLGDYVDRGQHSLETITLLLALKIEYPENVHLIRGNHEAADINALFGFRLECIERMGENDGIWAWTRFNQLFNYLPLAALIENKIICMHGGIGRSISTVEQIEKIERPITMDAGSLVLMDLLWSDPTENDSIEGLRPNARGPGLVTFGPDRVTEFCKRNKLQLIIRAHECVMDGFERFAQGQLITLFSATNYCGTANNAGAILVVGRGLVIVPKLIHPLPPPILSPENSPEHSGDDAWMQELNIQRPPTPTRGRPQPDFDRSSLAYI

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
97	Phosphorylation	KPAGEPPSPRAAHAA CCCCCCCCHHHHHHH	37.42	25561503
482	Phosphorylation	VAKETVGSLGGMVRQ EEECCHHHHHHHHHH	21.36	25561503
491	Phosphorylation	GGMVRQLSLDQFQNE HHHHHHCCHHHHHHH	22.89	30291188
499	Phosphorylation	LDQFQNESRRMVPMN HHHHHHHCCCCCCCC	32.51	23776212
522	Phosphorylation	KKFTRQKSPQGLHKK HHHCCCCCCCCHHHH	17.70	25561503
839	Phosphorylation	PLPPPILSPENSPEH CCCCCCCCCCCCCCC	30.78	19880383
843	Phosphorylation	PILSPENSPEHSGDD CCCCCCCCCCCCCCC	29.97	19880383
863	Phosphorylation	LNIQRPPTPTRGRPQ CCCCCCCCCCCCCCC	39.72	29654922
865	Phosphorylation	IQRPPTPTRGRPQPD CCCCCCCCCCCCCCC	48.51	24601666

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

Oops, there are no upstream regulatory protein records of BSL1_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BSL1_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 BSL1_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of BSL1_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-491, 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-491, SUBCELLULARLOCATION, AND MASS SPECTROMETRY.
PubMed: 19245862