SNP33_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SNP33_ARATH
• UniProt AC: Q9S7P9
• Protein Name: SNAP25 homologous protein SNAP33 {ECO:0000303|PubMed:12746539}
• Gene Name: SNAP33 {ECO:0000303|PubMed:12746539}
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 300
• Subcellular Localization: Membrane. Plasma membrane, some endomembrane compartment and cell plate in dividing cells.
• Protein Description: t-SNARE involved in diverse vesicle trafficking and membrane fusion processes, including cell plate formation. May function in the secretory pathway..
• Protein Sequence: MFGLRKSPANLPKHNSVDLKSSKPNPFDSDDESDNKHTLNPSKRTTSEPSLADMTNPFGGERVQKGDSSSSKQSLFSNSKYQYKNNFRDSGGIENQSVQELEGYAVYKAEETTKSVQGCLKVAEDIRSDATRTLVMLHDQGEQITRTHHKAVEIDHDLSRGEKLLGSLGGMFSKTWKPKKTRPINGPVVTRDDSPTRRVNHLEKREKLGLNSAPRGQSRTREPLPESADAYQRVEMEKAKQDDGLSDLSDILGELKNMAVDMGSEIEKQNKGLDHLHDDVDELNFRVQQSNQRGRRLLGK

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
7	Phosphorylation	-MFGLRKSPANLPKH -CCCCCCCCCCCCCC	23.86	19880383
16	Phosphorylation	ANLPKHNSVDLKSSK CCCCCCCCCCCCCCC	19.41	23776212
21	Phosphorylation	HNSVDLKSSKPNPFD CCCCCCCCCCCCCCC	51.39	23776212
22	Phosphorylation	NSVDLKSSKPNPFDS CCCCCCCCCCCCCCC	51.01	23776212
29	Phosphorylation	SKPNPFDSDDESDNK CCCCCCCCCCCCCCC	47.54	30291188
33	Phosphorylation	PFDSDDESDNKHTLN CCCCCCCCCCCCCCC	54.18	23776212
38	Phosphorylation	DESDNKHTLNPSKRT CCCCCCCCCCCHHCC	29.82	23776212
42	Phosphorylation	NKHTLNPSKRTTSEP CCCCCCCHHCCCCCC	33.42	23776212
45	Phosphorylation	TLNPSKRTTSEPSLA CCCCHHCCCCCCCHH	38.11	24601666
46	Phosphorylation	LNPSKRTTSEPSLAD CCCHHCCCCCCCHHH	34.82	24601666
47	Phosphorylation	NPSKRTTSEPSLADM CCHHCCCCCCCHHHC	47.07	30291188
50	Phosphorylation	KRTTSEPSLADMTNP HCCCCCCCHHHCCCC	31.94	23776212
55	Phosphorylation	EPSLADMTNPFGGER CCCHHHCCCCCCCCC	40.04	19376835
70	Phosphorylation	VQKGDSSSSKQSLFS CCCCCCCCCCHHHHC	45.57	23572148
71	Phosphorylation	QKGDSSSSKQSLFSN CCCCCCCCCHHHHCC	36.34	23572148
173	Phosphorylation	GSLGGMFSKTWKPKK HHHCCCCCCCCCCCC	21.93	25561503
190	Phosphorylation	PINGPVVTRDDSPTR CCCCCEECCCCCCCC	28.72	19880383
194	Phosphorylation	PVVTRDDSPTRRVNH CEECCCCCCCCCCCH	32.24	19880383
246	Phosphorylation	AKQDDGLSDLSDILG HHCCCCCCHHHHHHH	41.87	29797451

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

Oops, there are no upstream regulatory protein records of SNP33_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SNP33_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 SNP33_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SY121_ARATH	SYP121	physical	18678865
SY111_ARATH	SYP111	physical	11591731
SY111_ARATH	SYP111	physical	23515225
VA721_ARATH	VAMP721	physical	23515225
VA722_ARATH	SAR1	physical	23515225
E70B1_ARATH	EXO70B1	physical	25617755
VA721_ARATH	VAMP721	physical	18273019
VA722_ARATH	SAR1	physical	18273019
SY121_ARATH	SYP121	physical	18273019

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-16 AND SER-29, AND MASSSPECTROMETRY.
PubMed: 19376835