dbPTM

STX1A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	STX1A_HUMAN
UniProt AC	Q16623
Protein Name	Syntaxin-1A
Gene Name	STX1A
Organism	Homo sapiens (Human).
Sequence Length	288
Subcellular Localization	Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane Single-pass type IV membrane protein . Cell junction, synapse, synaptosome . Cell membrane . Colocalizes with KCNB1 at the cell membrane. Isoform 2: Secreted .
Protein Description	Plays a role in hormone and neurotransmitter exocytosis (By similarity). Potentially involved in docking of synaptic vesicles at presynaptic active zones. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm..
Protein Sequence	MKDRTQELRTAKDSDDDDDVAVTVDRDRFMDEFFEQVEEIRGFIDKIAENVEEVKRKHSAILASPNPDEKTKEELEELMSDIKKTANKVRSKLKSIEQSIEQEEGLNRSSADLRIRKTQHSTLSRKFVEVMSEYNATQSDYRERCKGRIQRQLEITGRTTTSEELEDMLESGNPAIFASGIIMDSSISKQALSEIETRHSEIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHAVDYVERAVSDTKKAVKYQSKARRKKIMIIICCVILGIVIASTVGGIFA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	DRTQELRTAKDSDDD HHHHHHHHCCCCCCC	51.16	23403867
14	Phosphorylation	ELRTAKDSDDDDDVA HHHHCCCCCCCCCEE	42.08	28355574
23	Phosphorylation	DDDDVAVTVDRDRFM CCCCEEEEECHHHHH	13.62	23403867
59	Phosphorylation	EEVKRKHSAILASPN HHHHHHHHHHHCCCC	21.75	25332170
64	Phosphorylation	KHSAILASPNPDEKT HHHHHHCCCCCCHHH	23.05	18510355
80	Phosphorylation	EELEELMSDIKKTAN HHHHHHHHHHHHHHH	49.13	30108239
95	Phosphorylation	KVRSKLKSIEQSIEQ HHHHHHHHHHHHHHH	41.62	25307156
99	Phosphorylation	KLKSIEQSIEQEEGL HHHHHHHHHHHHHCC	18.46	24719451
109	Phosphorylation	QEEGLNRSSADLRIR HHHCCCCCHHHHHHH	28.89	23312004
110	Phosphorylation	EEGLNRSSADLRIRK HHCCCCCHHHHHHHH	23.67	23312004
118	O-linked_Glycosylation	ADLRIRKTQHSTLSR HHHHHHHHHCCHHHH	22.97	30059200
118	Phosphorylation	ADLRIRKTQHSTLSR HHHHHHHHHCCHHHH	22.97	22985185
122	Phosphorylation	IRKTQHSTLSRKFVE HHHHHCCHHHHHHHH	26.99	22985185
145	S-nitrosocysteine	QSDYRERCKGRIQRQ HHHHHHHHHHHHHHH	4.73	-
145	S-nitrosylation	QSDYRERCKGRIQRQ HHHHHHHHHHHHHHH	4.73	22178444
160	Phosphorylation	LEITGRTTTSEELED HHHHCCCCCHHHHHH	27.28	24076635
188	Phosphorylation	IIMDSSISKQALSEI EEECCCHHHHHHHHH	22.21	9003414
225	Phosphorylation	DMAMLVESQGEMIDR HHHHHHHCCCCHHHH	35.69	29083192
225 (in isoform 3)	Phosphorylation	-	35.69	22210691
227 (in isoform 3)	Phosphorylation	-	35.40	22210691
234 (in isoform 2)	Phosphorylation	-	31.76	-
243	Phosphorylation	NVEHAVDYVERAVSD CHHHHHHHHHHHHHH	9.52	27196784
249	Phosphorylation	DYVERAVSDTKKAVK HHHHHHHHHHHHHHH	38.28	26657352
257	Phosphorylation	DTKKAVKYQSKARRK HHHHHHHHHHHHHHH	16.06	29116813
259	Phosphorylation	KKAVKYQSKARRKKI HHHHHHHHHHHHHHH	25.78	22468782
281	Phosphorylation	ILGIVIASTVGGIFA HHHHHHHHHHCCCCC	16.70	-
282	Phosphorylation	LGIVIASTVGGIFA- HHHHHHHHHCCCCC-	17.72	-

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
14	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
14	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
14	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
188	S	Phosphorylation	Kinase	DAPK1	P53355	Uniprot
188	S	Phosphorylation	Kinase	DAPK-FAMILY	-	GPS
188	S	Phosphorylation	Kinase	DAPK_GROUP	-	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	RNF40	O75150	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
188	S	Phosphorylation		12730201
Phosphorylation at Ser-188 by DAPK1 significantly decreases its interaction with STXBP1.

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 STX1A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SCNNA_HUMAN	SCNN1A	physical	14996668
SCNNG_HUMAN	SCNN1G	physical	14996668
SCNNB_HUMAN	SCNN1B	physical	14996668
STXB5_HUMAN	STXBP5	physical	12832401
SNP23_HUMAN	SNAP23	physical	12828989
VATB1_HUMAN	ATP6V1B1	physical	12651853
SNP23_HUMAN	SNAP23	physical	12651853
VAPB_HUMAN	VAPB	physical	12651853
CCSE2_HUMAN	CCSER2	physical	16169070
VIME_HUMAN	VIM	physical	16169070
SNP25_HUMAN	SNAP25	physical	16169070
STXB1_HUMAN	STXBP1	physical	10449403
SNP25_HUMAN	SNAP25	physical	10449403
VAMP2_HUMAN	VAMP2	physical	10449403
CPLX1_HUMAN	CPLX1	physical	10449403
CPLX2_HUMAN	CPLX2	physical	10449403
SNP23_HUMAN	SNAP23	physical	9168999
SNP23_MOUSE	Snap23	physical	9168999
SNP25_RAT	Snap25	physical	9168999
CFTR_HUMAN	CFTR	physical	9384384
SYPH_HUMAN	SYP	physical	7553862
SNP25_HUMAN	SNAP25	physical	7553862
VAMP2_HUMAN	VAMP2	physical	7553862
SNAA_HUMAN	NAPA	physical	7553862
STXB1_HUMAN	STXBP1	physical	7553862
VAMP1_HUMAN	VAMP1	physical	12093152
VAMP2_HUMAN	VAMP2	physical	12093152
SC6A4_HUMAN	SLC6A4	physical	12175857
SC6A1_HUMAN	SLC6A1	physical	9698305
SNP25_HUMAN	SNAP25	physical	10954418
SYTL4_HUMAN	SYTL4	physical	12101244
STXB5_HUMAN	STXBP5	physical	9620695
SYT1_HUMAN	SYT1	physical	10397765
SNP23_HUMAN	SNAP23	physical	8663154
SNP25_HUMAN	SNAP25	physical	8663154
SNP25_HUMAN	SNAP25	physical	7961655
STX1A_HUMAN	STX1A	physical	10100611
VAMP2_HUMAN	VAMP2	physical	9030619
VAMP2_HUMAN	VAMP2	physical	11832227
SNP25_HUMAN	SNAP25	physical	11832227
CPLX1_HUMAN	CPLX1	physical	11832227
VAMP8_HUMAN	VAMP8	physical	11112705
TXLNA_HUMAN	TXLNA	physical	12558796
SNP23_HUMAN	SNAP23	physical	9852078
SNP25_HUMAN	SNAP25	physical	9852078
SNP29_HUMAN	SNAP29	physical	9852078
CDK5_HUMAN	CDK5	physical	9478941
PNUT_DROME	pnut	physical	17456438
SEPT1_DROME	Sep1	physical	17456438
SC6A3_HUMAN	SLC6A3	physical	18617632
KCNB1_HUMAN	KCNB1	physical	22411134
STXB1_HUMAN	STXBP1	physical	12519779
STX1A_HUMAN	STX1A	physical	24722188
SNAB_HUMAN	NAPB	physical	24722188
SNP23_HUMAN	SNAP23	physical	24722188
SNP29_HUMAN	SNAP29	physical	24722188
PSA3_HUMAN	PSMA3	physical	24722188
TXLNA_HUMAN	TXLNA	physical	24722188
TXLNB_HUMAN	TXLNB	physical	24722188
VAMP5_HUMAN	VAMP5	physical	24722188
VAPB_HUMAN	VAPB	physical	24885147
STXB1_HUMAN	STXBP1	physical	15563604
KCNB1_HUMAN	KCNB1	physical	15518587

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.

Regulatory Network of STX1A_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteomic analysis of synaptosomes from human cerebralcortex."; DeGiorgis J.A., Jaffe H., Moreira J.E., Carlotti C.G. Jr., Leite J.P.,Pant H.C., Dosemeci A.; J. Proteome Res. 4:306-315(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASSSPECTROMETRY.	15822905 [Abstract]
"Ca2+-dependent phosphorylation of syntaxin-1A by the death-associatedprotein (DAP) kinase regulates its interaction with Munc18."; Tian J.H., Das S., Sheng Z.H.; J. Biol. Chem. 278:26265-26274(2003). Cited for: PHOSPHORYLATION AT SER-188, AND INTERACTION WITH DAPK1 AND STXBP1.	12730201 [Abstract]

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