BSL2_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BSL2_ARATH
• UniProt AC: Q9SJF0
• Protein Name: Serine/threonine-protein phosphatase BSL2
• Gene Name: BSL2
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 1018
• Subcellular Localization: Cytoplasm . Cell membrane . Nucleus. Mainly cytoplasmic. Colocalizes with BSK8 at the plasma membrane.
• Protein Description: Phosphatase involved in elongation process, probably by acting as a regulator of brassinolide signaling..
• Protein Sequence: MDEDSSMVADNDQDREFQSLDGGQSPSPMERETPQQMNDQSPPPEGGSVPTPPPSDPNPATSQQQAAAVVGQEQQPALVVGPRCAPTYSVVDAMMDKKEDGPGPRCGHTLTAVPAVGDEGTPGYIGPRLVLFGGATALEGNSGGTGTPTSAGSAGIRLAGATADVHCYDVLSNKWTRLTPFGEPPTPRAAHVATAVGTMVVIQGGIGPAGLSAEDLHVLDLTQQRPRWHRVVVQGPGPGPRYGHVMALVGQRYLMAIGGNDGKRPLADVWALDTAAKPYEWRKLEPEGEGPPPCMYATASARSDGLLLLCGGRDANSVPLASAYGLAKHRDGRWEWAIAPGVSPSSRYQHAAVFVNARLHVSGGALGGGRMVEDSSSVAVLDTAAGVWCDTKSVVTSPRTGRYSADAAGGDASVELTRRCRHAAAAVGDLIFIYGGLRGGVLLDDLLVAEDLAAAETTYAASHAAAAAATNSPPGRLPGRYGFSDERNRELSESAADGAVVLGSPVAPPVNGDMHTDISPENALLPGTRRTNKGVEYLVEASAAEAEAISATLAAAKARQVNGEVELPDRDCGAEATPSGKPTFSLIKPDSMGSMSVTPAGIRLHHRAVVVAAETGGALGGMVRQLSIDQFENEGRRVSYGTPESATAARKLLDRQMSINSVPKKVIAHLLKPRGWKPPVRRQFFLDCNEIADLCDSAERIFASEPTVLQLKAPIKIFGDLHGQFGDLMRLFDEYGSPSTAGDISYIDYLFLGDYVDRGQHSLETISLLLALKVEYQHNVHLIRGNHEAADINALFGFRIECIERMGERDGIWVWHRINRLFNWLPLAASIEKKIICMHGGIGRSINHVEQIENIQRPITMEAGSIVLMDLLWSDPTENDSVEGLRPNARGPGLVTFGPDRVMEFCNNNDLQLIVRAHECVMDGFERFAQGHLITLFSATNYCGTANNAGAILVLGRDLVVVPKLIHPLPPALSSPETSPERHIEDTWMQELNANRPATPTRGRPQNSNDRGGSLAWM

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
25	Phosphorylation	QSLDGGQSPSPMERE HHCCCCCCCCCCCCC	30.53	23111157
136	Phosphorylation	LVLFGGATALEGNSG EEEECCCEEECCCCC	34.74	30407730
142	Phosphorylation	ATALEGNSGGTGTPT CEEECCCCCCCCCCC	49.83	19880383
145	Phosphorylation	LEGNSGGTGTPTSAG ECCCCCCCCCCCCCC	41.21	30407730
147	Phosphorylation	GNSGGTGTPTSAGSA CCCCCCCCCCCCCCC	24.19	30291188
149	Phosphorylation	SGGTGTPTSAGSAGI CCCCCCCCCCCCCCC	30.92	30407730
150	Phosphorylation	GGTGTPTSAGSAGIR CCCCCCCCCCCCCCE	31.66	19880383
153	Phosphorylation	GTPTSAGSAGIRLAG CCCCCCCCCCCEECC	24.04	30407730
396	Phosphorylation	CDTKSVVTSPRTGRY ECCCCEECCCCCCCC	30.75	23776212
397	Phosphorylation	DTKSVVTSPRTGRYS CCCCEECCCCCCCCC	10.77	23776212
400	Phosphorylation	SVVTSPRTGRYSADA CEECCCCCCCCCCCC	29.42	29797451
404	Phosphorylation	SPRTGRYSADAAGGD CCCCCCCCCCCCCCC	20.50	30291188
552	Phosphorylation	EAEAISATLAAAKAR HHHHHHHHHHHHHHH	15.33	29654922
591	Phosphorylation	FSLIKPDSMGSMSVT EEEECCCCCCCCCCC	33.30	25561503
627	Phosphorylation	GGMVRQLSIDQFENE HHHHEEECHHHCCCC	18.77	30291188
642	Phosphorylation	GRRVSYGTPESATAA CCCCCCCCHHHHHHH	18.69	22631563
645	Phosphorylation	VSYGTPESATAARKL CCCCCHHHHHHHHHH	31.93	19880383
647	Phosphorylation	YGTPESATAARKLLD CCCHHHHHHHHHHHH	30.08	19880383
658	Phosphorylation	KLLDRQMSINSVPKK HHHHHCCCCCCCCHH	15.41	30291188
661	Phosphorylation	DRQMSINSVPKKVIA HHCCCCCCCCHHHHH	37.82	23776212
974	Phosphorylation	HPLPPALSSPETSPE CCCCCCCCCCCCCCC	46.05	24601666
975	Phosphorylation	PLPPALSSPETSPER CCCCCCCCCCCCCCH	27.83	24601666
978	Phosphorylation	PALSSPETSPERHIE CCCCCCCCCCCHHCH	53.63	24601666
979	Phosphorylation	ALSSPETSPERHIED CCCCCCCCCCHHCHH	24.09	24601666
999	Phosphorylation	LNANRPATPTRGRPQ HHCCCCCCCCCCCCC	28.07	23111157
1001	Phosphorylation	ANRPATPTRGRPQNS CCCCCCCCCCCCCCC	41.21	24601666

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

Oops, there are no upstream regulatory protein records of BSL2_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BSL2_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 BSL2_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of BSL2_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-975 AND THR-978, ANDMASS SPECTROMETRY.
PubMed: 19376835