BGL38_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BGL38_ARATH
• UniProt AC: P37702
• Protein Name: Myrosinase 1
• Gene Name: TGG1
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 541
• Subcellular Localization: Vacuole.
• Protein Description: Degradation of glucosinolates (glucose residue linked by a thioglucoside bound to an amino acid derivative) to glucose, sulfate and any of the products: thiocyanates, isothiocyanates, nitriles, epithionitriles or oxazolidine-2-thiones. These toxic degradation products can deter insect herbivores. Seems to function in abscisic acid (ABA) and methyl jasmonate (MeJA) signaling in guard cells. Functionally redundant with TGG2. Hydrolyzes sinigrin and, with lower efficiency, p-nitrophenyl beta-D-glucoside..
• Protein Sequence: MKLLMLAFVFLLALATCKGDEFVCEENEPFTCNQTKLFNSGNFEKGFIFGVASSAYQVEGGRGRGLNVWDSFTHRFPEKGGADLGNGDTTCDSYTLWQKDIDVMDELNSTGYRFSIAWSRLLPKGKRSRGVNPGAIKYYNGLIDGLVAKNMTPFVTLFHWDLPQTLQDEYNGFLNKTIVDDFKDYADLCFELFGDRVKNWITINQLYTVPTRGYALGTDAPGRCSPKIDVRCPGGNSSTEPYIVAHNQLLAHAAAVDVYRTKYKDDQKGMIGPVMITRWFLPFDHSQESKDATERAKIFFHGWFMGPLTEGKYPDIMREYVGDRLPEFSETEAALVKGSYDFLGLNYYVTQYAQNNQTIVPSDVHTALMDSRTTLTSKNATGHAPGPPFNAASYYYPKGIYYVMDYFKTTYGDPLIYVTENGFSTPGDEDFEKATADYKRIDYLCSHLCFLSKVIKEKNVNVKGYFAWSLGDNYEFCNGFTVRFGLSYVDFANITGDRDLKASGKWFQKFINVTDEDSTNQDLLRSSVSSKNRDRKSLADA

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
33	N-linked_Glycosylation	ENEPFTCNQTKLFNS CCCCCCCCCEEEECC	49.88	-
40	Phosphorylation	NQTKLFNSGNFEKGF CCEEEECCCCCCCCE	27.98	25561503
108	N-linked_Glycosylation	IDVMDELNSTGYRFS CHHHHHHHHCCCCEE	35.16	-
128	Phosphorylation	LLPKGKRSRGVNPGA HCCCCCCCCCCCHHH	36.55	24894044
175	N-linked_Glycosylation	DEYNGFLNKTIVDDF HHHCCCCCCHHHHCH	36.84	-
236	N-linked_Glycosylation	DVRCPGGNSSTEPYI EEECCCCCCCCCCEE	38.41	-
356	N-linked_Glycosylation	VTQYAQNNQTIVPSD EEEHHHHCCEECCCH	28.43	-
376	Phosphorylation	MDSRTTLTSKNATGH HCCCCEECCCCCCCC	35.25	26811356
377	Phosphorylation	DSRTTLTSKNATGHA CCCCEECCCCCCCCC	27.33	26811356
379	N-linked_Glycosylation	RTTLTSKNATGHAPG CCEECCCCCCCCCCC	42.37	-
381	Phosphorylation	TLTSKNATGHAPGPP EECCCCCCCCCCCCC	38.60	26811356
396	Phosphorylation	FNAASYYYPKGIYYV CCCHHHCCCCCEEEE	7.10	26811356
404	Sulfoxidation	PKGIYYVMDYFKTTY CCCEEEEEHHHHCCC	1.68	25693801
493	N-linked_Glycosylation	LSYVDFANITGDRDL CEEEEEECCCCCCCH	32.14	-
512	N-linked_Glycosylation	KWFQKFINVTDEDST CCHHHHHCCCCCCCC	33.49	-

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

Oops, there are no upstream regulatory protein records of BGL38_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BGL38_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 BGL38_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of BGL38_ARATH !!

Drug and Disease Associations

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