STX17_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: STX17_HUMAN
• UniProt AC: P56962
• Protein Name: Syntaxin-17 {ECO:0000303|PubMed:21545355}
• Gene Name: STX17 {ECO:0000312|HGNC:HGNC:11432}
• Organism: Homo sapiens (Human).
• Sequence Length: 302
• Subcellular Localization: Endoplasmic reticulum membrane ; Multi-pass membrane protein . Smooth endoplasmic reticulum membrane ; Multi-pass membrane protein . Endoplasmic reticulum-Golgi intermediate compartment membrane ; Multi-pass membrane protein . Cytoplasmic vesicle, autopha
• Protein Description: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. STX17 is a SNARE of the autophagosome involved in autophagy through the direct control of autophagosome membrane fusion with the lysosome membrane. [PubMed: 23217709]
• Protein Sequence: MSEDEEKVKLRRLEPAIQKFIKIVIPTDLERLRKHQINIEKYQRCRIWDKLHEEHINAGRTVQQLRSNIREIEKLCLKVRKDDLVLLKRMIDPVKEEASAATAEFLQLHLESVEELKKQFNDEETLLQPPLTRSMTVGGAFHTTEAEASSQSLTQIYALPEIPQDQNAAESWETLEADLIELSQLVTDFSLLVNSQQEKIDSIADHVNSAAVNVEEGTKNLGKAAKYKLAALPVAGALIGGMVGGPIGLLAGFKVAGIAAALGGGVLGFTGGKLIQRKKQKMMEKLTSSCPDLPSQTDKKCS

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
2	Phosphorylation	------MSEDEEKVK ------CCHHHHHHH	54.47	24719451
2	Acetylation	------MSEDEEKVK ------CCHHHHHHH	54.47	22814378
7	Ubiquitination	-MSEDEEKVKLRRLE -CCHHHHHHHHHHHH	42.49	24816145
19	Ubiquitination	RLEPAIQKFIKIVIP HHHHHHHHHHHHHCC	42.83	29967540
22	Ubiquitination	PAIQKFIKIVIPTDL HHHHHHHHHHCCCCH	33.77	-
34	Ubiquitination	TDLERLRKHQINIEK CCHHHHHHCCCCHHH	44.44	29967540
41	Acetylation	KHQINIEKYQRCRIW HCCCCHHHHHHHCHH	42.77	19608861
41	Ubiquitination	KHQINIEKYQRCRIW HCCCCHHHHHHHCHH	42.77	19608861
88	Ubiquitination	KDDLVLLKRMIDPVK HHHHHHHHHHCHHHH	35.44	29967540
99	Phosphorylation	DPVKEEASAATAEFL HHHHHHHHHHHHHHH	23.01	-
102	Phosphorylation	KEEASAATAEFLQLH HHHHHHHHHHHHHHH	26.83	-
117	Ubiquitination	LESVEELKKQFNDEE HHHHHHHHHHCCCCC	48.05	29967540
134	Phosphorylation	LQPPLTRSMTVGGAF CCCCCCCCEEECCCC	17.36	24275569
157	Phosphorylation	SQSLTQIYALPEIPQ CCCCHHHHCCCCCCC	7.71	-
184	Ubiquitination	ADLIELSQLVTDFSL HHHHHHHHHHHHHHH	53.21	21890473
189	Ubiquitination	LSQLVTDFSLLVNSQ HHHHHHHHHHHHCCC	3.96	22817900
202	Phosphorylation	SQQEKIDSIADHVNS CCHHHHHHHHHHHHH	24.13	25849741
209	Phosphorylation	SIADHVNSAAVNVEE HHHHHHHHHCCCHHH	19.27	22199227
219	Ubiquitination	VNVEEGTKNLGKAAK CCHHHHCCCHHHHHH	62.12	29967540
227	Phosphorylation	NLGKAAKYKLAALPV CHHHHHHHHHHHHHH	13.40	-
273	Ubiquitination	VLGFTGGKLIQRKKQ CHHHCCHHHHHHHHH	43.70	21890473
278	Ubiquitination	GGKLIQRKKQKMMEK CHHHHHHHHHHHHHH	43.08	22817900
287	Phosphorylation	QKMMEKLTSSCPDLP HHHHHHHHHCCCCCC	29.66	27794612
288	Phosphorylation	KMMEKLTSSCPDLPS HHHHHHHHCCCCCCC	40.14	23401153
289	Phosphorylation	MMEKLTSSCPDLPSQ HHHHHHHCCCCCCCC	25.16	19664994
295	Phosphorylation	SSCPDLPSQTDKKCS HCCCCCCCCCCCCCC	53.67	23403867
297	Phosphorylation	CPDLPSQTDKKCS-- CCCCCCCCCCCCC--	54.87	23403867
299	Ubiquitination	DLPSQTDKKCS---- CCCCCCCCCCC----	60.10	33845483

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
157	Y	Phosphorylation	Kinase	ABL	P00519	PSP
202	S	Phosphorylation	Kinase	TBK1	Q9UHD2	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of STX17_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of STX17_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SNP29_HUMAN	SNAP29	physical	9852078
VP33A_HUMAN	VPS33A	physical	24554770
VPS16_HUMAN	VPS16	physical	24554770
VPS11_HUMAN	VPS11	physical	24554770
VPS18_HUMAN	VPS18	physical	24554770
VPS39_HUMAN	VPS39	physical	24554770
VPS41_HUMAN	VPS41	physical	24554770

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-41, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND MASSSPECTROMETRY.
PubMed: 19413330