SY132_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SY132_ARATH
• UniProt AC: Q8VZU2
• Protein Name: Syntaxin-132
• Gene Name: SYP132
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 304
• Subcellular Localization: Membrane; Single-pass type IV membrane protein.
• Protein Description: Vesicle trafficking protein that functions in the secretory pathway..
• Protein Sequence: MNDLLKGSFELPRGQSSREGDVELGEQQGGDQGLEDFFKKVQVIDKQYDKLDKLLKKLQASHEESKSVTKAPAMKAIKKTMEKDVDEVGSIARFIKGKLEELDRENLANRQKPGCAKGSGVDRSRTATTLSLKKKLKDKMAEFQVLRENIQQEYRDVVDRRVYTVTGERADEDTIDELIETGNSEQIFQKAIQEQGRGQVMDTLAEIQERHDAVRDLEKKLLDLQQIFLDMAVLVDAQGEMLDNIESQVSSAVDHVQSGNTALQRAKSLQKNSRKWMCIAIIILLIVVAVIVVGVLKPWKNKSA

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
1	Acetylation	-------MNDLLKGS -------CCCHHCCC	8.75	-
8	Phosphorylation	MNDLLKGSFELPRGQ CCCHHCCCCCCCCCC	17.60	17317660
16	Phosphorylation	FELPRGQSSREGDVE CCCCCCCCCCCCCCC	33.90	19880383
17	Phosphorylation	ELPRGQSSREGDVEL CCCCCCCCCCCCCCH	26.85	23776212

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

Oops, there are no upstream regulatory protein records of SY132_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SY132_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 SY132_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SYP71_ARATH	SYP71	physical	24556609
JAL34_ARATH	AT3G16460	physical	24556609
PME17_ARATH	AT2G45220	physical	24556609
PIP12_ARATH	PIP1B	physical	24556609
HIR3_ARATH	AT3G01290	physical	24556609
BGL22_ARATH	BGLU22	physical	24556609
PMA2_ARATH	HA2	physical	24556609
PIP11_ARATH	PIP1A	physical	24556609
PIP24_ARATH	PIP2;4	physical	24556609
VA721_ARATH	VAMP721	physical	24556609
PIP22_ARATH	PIP2B	physical	24556609
RS41_ARATH	AT2G17360	physical	24556609
VCS_ARATH	VCS	physical	24556609
SY122_ARATH	SYP122	physical	24556609
PIP27_ARATH	PIP3	physical	24556609
SY123_ARATH	SYP123	physical	24556609
RS3A1_ARATH	AT3G04840	physical	24556609
ENPL_ARATH	SHD	physical	24556609
RS131_ARATH	AT3G60770	physical	24556609
RL51_ARATH	ATL5	physical	24556609
VAP42_ARATH	AT4G21450	physical	24556609
RL31_ARATH	RP1	physical	24556609
RS111_ARATH	EMB1080	physical	24556609
RL171_ARATH	AT1G27400	physical	24556609
RS232_ARATH	AT5G02960	physical	24556609
NPS11_ARATH	NPSN11	physical	24556609
TBB2_ARATH	TUB2	physical	24556609
TBB3_ARATH	TUB2	physical	24556609
RL81_ARATH	EMB2296	physical	24556609
RS163_ARATH	AT5G18380	physical	24556609
R27AA_ARATH	AT1G23410	physical	24556609
RS241_ARATH	AT3G04920	physical	24556609
RL301_ARATH	AT1G36240	physical	24556609
RL7A2_ARATH	AT3G62870	physical	24556609
NPS13_ARATH	NPSN13	physical	24556609
JAL20_ARATH	AT2G25980	physical	24556609
CAMT4_ARATH	CCoAOMT1	physical	24556609
RS91_ARATH	AT5G15200	physical	24556609
RL312_ARATH	AT4G26230	physical	24556609

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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.
PubMed: 15308754

"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.
PubMed: 14506206