dbPTM

MSL6_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MSL6_ARATH
UniProt AC	Q9SYM1
Protein Name	Mechanosensitive ion channel protein 6
Gene Name	MSL6
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	856
Subcellular Localization	Membrane Multi-pass membrane protein .
Protein Description	Mechanosensitive channel that opens in response to stretch forces in the membrane lipid bilayer..
Protein Sequence	MAVDAADRREVIVKIDGENGNNNGVSGETVGKIWRDGSYDFWTDGEGNLNKGHNAAAVDSDRSAATTGEQQKDEGFEFRRGEDPPTKLIGQFLHKQQASGEICLDMDLGMDELQSRGLTPVSESPRVSTKRDPVGRRDSRSNTNNNDDGEVVKCSGNNAPIQRSSSTLLKMRTRSRLSDPPTPQLPPQTADMKSGRIPKSGQMKSGFFGKSPKTQGEEEEDDPFAAEDLPEEYRKDKLSLWIVLEWLSLILIIAGFVCTLAIPSLRKKKLWELQLWKWESMVLVLICGRLVSSWIVKIVVFFIERNFLLRKRVLYFVYGVRKAVQNCLWLGLVLLAWHFLFDEKVAKAANTKALRVVTKIFVCLLVGFLLWLVKTLLVKVLASSFHMSTYFDRIQESLFTQYVIETLSGPPLIEIQKNEEEEERISVEVKKFQNPGGVEIQSGAQKSPMKTGKSPFLSHVLSNGGGGGGENKGITIDSLHKLNPKNVSAWKMKRLMNIIRNGSLTTLDEQLQDPSLDDDKGNQIRSEFEAKLAARKIFHNVAKPGSKFIYANDIMRFLPDDEALKTLSLFEGASETNRISKSSLKNWVVNAFRERRALALTLNDTKTAVNRLHKMVNIVVGIIILVIWLIILGITSTKFLVVMSSQVVVVAFIFGNMCKIVFESIIYLFVIHPFDVGDRCEIDGVQMVVEEMNILTTVFLRFDNQKVVYPNSLLWTKSIGNYYRSPDMGDGIEFSIHITTPAEKIILIKQRITSYIEGKKDHWYPAPMIVFKDMESLNSVRIAVWPTHRMNHQDMGEKWARRSQLVEEIAKICRELDIEYRLYPLDINVRNLPTSTALPVSDRLPPNWSAPASGSN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
38	Phosphorylation	GKIWRDGSYDFWTDG CCCCCCCCCCEEECC	26.31	15308754
39	Phosphorylation	KIWRDGSYDFWTDGE CCCCCCCCCEEECCC	22.23	23776212
43	Phosphorylation	DGSYDFWTDGEGNLN CCCCCEEECCCCCCC	33.83	23776212
119	Phosphorylation	ELQSRGLTPVSESPR HHHHCCCCCCCCCCC	25.19	30407730
122	Phosphorylation	SRGLTPVSESPRVST HCCCCCCCCCCCCCC	33.29	15308754
124	Phosphorylation	GLTPVSESPRVSTKR CCCCCCCCCCCCCCC	15.53	17317660
128	Phosphorylation	VSESPRVSTKRDPVG CCCCCCCCCCCCCCC	29.50	15308754
129	Phosphorylation	SESPRVSTKRDPVGR CCCCCCCCCCCCCCC	27.52	19880383
165	Phosphorylation	NAPIQRSSSTLLKMR CCCCCCCHHHHHHHH	29.54	28011693
166	Phosphorylation	APIQRSSSTLLKMRT CCCCCCHHHHHHHHH	25.07	19880383
167	Phosphorylation	PIQRSSSTLLKMRTR CCCCCHHHHHHHHHH	37.75	28011693
175	Phosphorylation	LLKMRTRSRLSDPPT HHHHHHHCCCCCCCC	36.64	15308754
178	Phosphorylation	MRTRSRLSDPPTPQL HHHHCCCCCCCCCCC	47.14	15308754
211	Phosphorylation	KSGFFGKSPKTQGEE CCCCCCCCCCCCCCC	31.82	25561503
442	Phosphorylation	PGGVEIQSGAQKSPM CCCCEECCCCCCCCC	41.58	17317660
447	Phosphorylation	IQSGAQKSPMKTGKS ECCCCCCCCCCCCCC	20.39	17317660
458	Phosphorylation	TGKSPFLSHVLSNGG CCCCCHHHHHHHCCC	16.36	15308754
462	Phosphorylation	PFLSHVLSNGGGGGG CHHHHHHHCCCCCCC	32.13	15308754

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of MSL6_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MSL6_ARATH !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of MSL6_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of MSL6_ARATH !!

Drug and Disease Associations

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

Regulatory Network of MSL6_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomics of early elicitor signaling inArabidopsis."; Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M.,Menke F.L.H.; Mol. Cell. Proteomics 6:1198-1214(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND THR-129, ANDMASS SPECTROMETRY.	17317660 [Abstract]
"Phosphoproteomics of the Arabidopsis plasma membrane and a newphosphorylation site database."; Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.; Plant Cell 16:2394-2405(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND SER-128, AND MASSSPECTROMETRY.	15308754 [Abstract]
"Large-scale analysis of in vivo phosphorylated membrane proteins byimmobilized metal ion affinity chromatography and mass spectrometry."; Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.; Mol. Cell. Proteomics 2:1234-1243(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122; SER-124 ANDSER-128, AND MASS SPECTROMETRY.	14506206 [Abstract]