dbPTM

STX10_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	STX10_HUMAN
UniProt AC	O60499
Protein Name	Syntaxin-10
Gene Name	STX10
Organism	Homo sapiens (Human).
Sequence Length	249
Subcellular Localization	Golgi apparatus membrane Single-pass type IV membrane protein .
Protein Description	SNARE involved in vesicular transport from the late endosomes to the trans-Golgi network..
Protein Sequence	MSLEDPFFVVRGEVQKAVNTARGLYQRWCELLQESAAVGREELDWTTNELRNGLRSIEWDLEDLEETIGIVEANPGKFKLPAGDLQERKVFVERMREAVQEMKDHMVSPTAVAFLERNNREILAGKPAAQKSPSDLLDASAVSATSRYIEEQQATQQLIMDEQDQQLEMVSGSIQVLKHMSGRVGEELDEQGIMLDAFAQEMDHTQSRMDGVLRKLAKVSHMTSDRRQWCAIAVLVGVLLLVLILLFSL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSLEDPFFV ------CCCCCCCEE	40.23	22617229
2	Acetylation	------MSLEDPFFV ------CCCCCCCEE	40.23	22814378
16	Ubiquitination	VVRGEVQKAVNTARG EEHHHHHHHHHHHHH	60.52	-
77	Ubiquitination	IVEANPGKFKLPAGD EEECCCCCCCCCCCC	40.35	-
79	Ubiquitination	EANPGKFKLPAGDLQ ECCCCCCCCCCCCHH	57.98	-
83 (in isoform 2)	Phosphorylation	-	33.93	29507054
85 (in isoform 2)	Phosphorylation	-	5.80	29507054
108	Phosphorylation	EMKDHMVSPTAVAFL HHHHHCCCHHHHHHH	14.68	30266825
110	Phosphorylation	KDHMVSPTAVAFLER HHHCCCHHHHHHHHH	26.68	30266825
126	Ubiquitination	NREILAGKPAAQKSP CCHHHCCCCCCCCCH	26.35	-
131	Acetylation	AGKPAAQKSPSDLLD CCCCCCCCCHHHHHH	60.66	26051181
131	Ubiquitination	AGKPAAQKSPSDLLD CCCCCCCCCHHHHHH	60.66	-
132	Phosphorylation	GKPAAQKSPSDLLDA CCCCCCCCHHHHHHH	19.98	25159151
134	Phosphorylation	PAAQKSPSDLLDASA CCCCCCHHHHHHHHH	48.24	25159151
140	Phosphorylation	PSDLLDASAVSATSR HHHHHHHHHHHHHHH	28.95	25159151
143	Phosphorylation	LLDASAVSATSRYIE HHHHHHHHHHHHHHH	26.08	23401153
145	Phosphorylation	DASAVSATSRYIEEQ HHHHHHHHHHHHHHH	13.26	21712546
146	Phosphorylation	ASAVSATSRYIEEQQ HHHHHHHHHHHHHHH	23.85	25159151
148	Phosphorylation	AVSATSRYIEEQQAT HHHHHHHHHHHHHHH	16.67	22210691
155	Phosphorylation	YIEEQQATQQLIMDE HHHHHHHHHHHHCHH	16.71	22210691
171	Phosphorylation	DQQLEMVSGSIQVLK HHHHHHHHHHHHHHH	26.05	22210691
194	Sulfoxidation	ELDEQGIMLDAFAQE HHHHCCCCHHHHHHH	3.38	21406390
223	Phosphorylation	LAKVSHMTSDRRQWC HHHHHCCCCCHHHHH	23.27	24719451
224	Phosphorylation	AKVSHMTSDRRQWCA HHHHCCCCCHHHHHH	22.88	24719451

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 STX10_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of STX10_HUMAN !!

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 STX10_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of STX10_HUMAN !!

Drug and Disease Associations

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

Regulatory Network of STX10_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-140 ANDSER-143, AND MASS SPECTROMETRY.	19690332 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-143, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-140, ANDMASS SPECTROMETRY.	18691976 [Abstract]