dbPTM

SY122_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SY122_ARATH
UniProt AC	Q9SVC2
Protein Name	Syntaxin-122
Gene Name	SYP122
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	341
Subcellular Localization	Membrane Single-pass type IV membrane protein.
Protein Description	Vesicle trafficking protein that functions in the secretory pathway..
Protein Sequence	MNDLLSGSFKTSVADGSSPPHSHNIEMSKAKVSGGSCHGGNNLDTFFLDVEVVNEDLKELDRLCHNLRSSNEQSKTLHNANAVKELKKKMDADVTAALKTARRLKGNLEALDRANEVNRSLPESGPGSSSDRQRTSVVNGLRKKLKDEMEKFSRVRETITNEYKETVGRMCFTVTGEYPDEATLERLISTGESETFLQKAIQEQGRGRILDTINEIQERHDAVKDIEKSLNELHQVFLDMAVLVEHQGAQLDDIEGNVKRANSLVRSGADRLVKARFYQKNTRKWTCFAILLLLIIVVLIVVFTVKPWESNGGGGGGAPRQATPVQAQPPPPPAVNRRLLR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MNDLLSGS -------CCCCCCCC	8.75	22223895
6	Phosphorylation	--MNDLLSGSFKTSV --CCCCCCCCCCCCC	39.42	27643528
8	Phosphorylation	MNDLLSGSFKTSVAD CCCCCCCCCCCCCCC	21.86	15308754
11	Phosphorylation	LLSGSFKTSVADGSS CCCCCCCCCCCCCCC	26.82	23776212
12	Phosphorylation	LSGSFKTSVADGSSP CCCCCCCCCCCCCCC	18.85	23776212
17	Phosphorylation	KTSVADGSSPPHSHN CCCCCCCCCCCCCCC	39.97	27532006
18	Phosphorylation	TSVADGSSPPHSHNI CCCCCCCCCCCCCCC	48.24	27532006
22	Phosphorylation	DGSSPPHSHNIEMSK CCCCCCCCCCCCCCC	24.81	17317660
28	Phosphorylation	HSHNIEMSKAKVSGG CCCCCCCCCCEECCC	19.37	23776212
33	Phosphorylation	EMSKAKVSGGSCHGG CCCCCEECCCCCCCC	36.41	23776212
36	Phosphorylation	KAKVSGGSCHGGNNL CCEECCCCCCCCCCC	13.38	23776212
45	Phosphorylation	HGGNNLDTFFLDVEV CCCCCCCCEEEEHHH	21.32	26811356
189	Phosphorylation	ATLERLISTGESETF HHHHHHHHCCCCHHH	34.64	17317660
263	Phosphorylation	GNVKRANSLVRSGAD CHHHHHHHHHHCCCH	27.53	17586839

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 SY122_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SY122_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 SY122_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PLST4_ARATH	PGLCT	physical	22737156
PUP3_ARATH	PUP3	physical	22737156
SYP71_ARATH	SYP71	physical	24556609
HIR3_ARATH	AT3G01290	physical	24556609
RL312_ARATH	AT4G26230	physical	24556609
VA721_ARATH	VAMP721	physical	24556609
IF2B_ARATH	EIF2 BETA	physical	24556609
ADT1_ARATH	AAC1	physical	24556609
RL171_ARATH	AT1G27400	physical	24556609
SY121_ARATH	SYP121	physical	24556609
NPS13_ARATH	NPSN13	physical	24556609
VAP42_ARATH	AT4G21450	physical	24556609
R27AA_ARATH	AT1G23410	physical	24556609
RL92_ARATH	AT4G10450	physical	24556609
RS241_ARATH	AT3G04920	physical	24556609
RL354_ARATH	AT5G02610	physical	24556609
ACT12_ARATH	ACT12	physical	24556609
RS41_ARATH	AT2G17360	physical	24556609
NPS11_ARATH	NPSN11	physical	24556609
ANXD4_ARATH	ANNAT4	physical	24556609
RH5_ARATH	STRS1	physical	24556609
RS91_ARATH	AT5G15200	physical	24556609
MD36B_ARATH	FIB1	physical	24556609
RS30_ARATH	AT2G19750	physical	24556609
RS191_ARATH	AT3G02080	physical	24556609
RL81_ARATH	EMB2296	physical	24556609
RL281_ARATH	AT2G19730	physical	24556609
RL4B_ARATH	AT5G02870	physical	24556609
MKS1_ARATH	MKS1	physical	24556609
EXPB3_ARATH	EXPB3	physical	24556609

Drug and Disease Associations

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

Regulatory Network of SY122_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Temporal analysis of sucrose-induced phosphorylation changes inplasma membrane proteins of Arabidopsis."; Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B.,Schulze W.X.; Mol. Cell. Proteomics 6:1711-1726(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND MASSSPECTROMETRY.	17586839 [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-8, 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-8, AND MASSSPECTROMETRY.	14506206 [Abstract]