dbPTM

SYN3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SYN3_MOUSE
UniProt AC	Q8JZP2
Protein Name	Synapsin-3
Gene Name	Syn3
Organism	Mus musculus (Mouse).
Sequence Length	579
Subcellular Localization	Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane Peripheral membrane protein Cytoplasmic side. Peripheral membrane protein localized to the cytoplasmic surface of synaptic vesicles..
Protein Description	May be involved in the regulation of neurotransmitter release and synaptogenesis. Binds ATP with high affinity and ADP with a lower affinity. This is consistent with a catalytic role of the C-domain in which ADP would be dissociated by cellular ATP after bound ATP was hydrolyzed (By similarity)..
Protein Sequence	MNFLRRRLSDSSFVANLPNGYMPDLQRPESSSSSPASPATERRHPQPLAASFSSPGSSLFSSFSGAMKQTPQAPSGLMEPPTPVTPVVQRPRILLVIDDAHTDWSKYFHGKKVNGDIEIRVEQAEFSELNLAAYVTGGCMVDMQVVRNGTKIVRSFKPDFILVRQHAYSMALAEDYRSLVIGLQYGGLPAVNSLYSVYNFCSKPWVFSQLIKIFHSLGPEKFPLVEQTFFPNHKPMLTAPNFPVVIKLGHAHAGMGKIKVENQHDYQDITSVVAMAKTYATTEAFIDSKYDIRIQKIGSNYKAYMRTSISGNWKANTGSAMLEQVAMTERYRLWVDSCSEMFGGLDICAVKAVHSKDGRDYIIEVMDSSMPLIGEHVEEDKQLMADLVVSKMSQLLVPGATVPSPLRPWGPQTKPAKSPGQGQLGPLLGQPQPRPPPQGGPRQAQSPQPPRSRSPSQQRLSPQGQQPVSPQSGSPQQQRSPGSPQLSRASGGSSPNQASKPSASLSSHNRPPVQGRSTSQQGEEPQKSASPHPHLNKSQSLTNSLSTSDTSHRGTPSEDEAKAETIRNLRKSFASLFSD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	NFLRRRLSDSSFVAN CCCHHHCCCCCHHCC	33.37	19060867
11	Phosphorylation	LRRRLSDSSFVANLP CHHHCCCCCHHCCCC	23.46	19060867
12	Phosphorylation	RRRLSDSSFVANLPN HHHCCCCCHHCCCCC	28.82	29899451
21	Phosphorylation	VANLPNGYMPDLQRP HCCCCCCCCCCCCCC	16.47	21183079
30	Phosphorylation	PDLQRPESSSSSPAS CCCCCCCCCCCCCCC	37.90	22807455
31	Phosphorylation	DLQRPESSSSSPASP CCCCCCCCCCCCCCC	32.36	21082442
33	Phosphorylation	QRPESSSSSPASPAT CCCCCCCCCCCCCCC	42.14	21183079
34	Phosphorylation	RPESSSSSPASPATE CCCCCCCCCCCCCCC	26.83	21183079
37	Phosphorylation	SSSSSPASPATERRH CCCCCCCCCCCCCCC	20.60	21183079
40	Phosphorylation	SSPASPATERRHPQP CCCCCCCCCCCCCCC	33.15	21183079
51	Phosphorylation	HPQPLAASFSSPGSS CCCCCHHHCCCCCHH	21.76	25521595
53	Phosphorylation	QPLAASFSSPGSSLF CCCHHHCCCCCHHHH	32.88	25521595
54	Phosphorylation	PLAASFSSPGSSLFS CCHHHCCCCCHHHHH	31.13	29899451
57	Phosphorylation	ASFSSPGSSLFSSFS HHCCCCCHHHHHHHC	27.53	29899451
58	Phosphorylation	SFSSPGSSLFSSFSG HCCCCCHHHHHHHCC	39.07	29899451
61	Phosphorylation	SPGSSLFSSFSGAMK CCCHHHHHHHCCCCC	35.45	29899451
62	Phosphorylation	PGSSLFSSFSGAMKQ CCHHHHHHHCCCCCC	18.98	29899451
64	Phosphorylation	SSLFSSFSGAMKQTP HHHHHHHCCCCCCCC	27.82	29899451
102	Phosphorylation	LVIDDAHTDWSKYFH EEEECCCCCHHHHHC	40.67	23140645
107	Phosphorylation	AHTDWSKYFHGKKVN CCCCHHHHHCCCCCC	8.69	22807455
308	Phosphorylation	YKAYMRTSISGNWKA CEEEEEECCCCCCCC	12.37	29899451
310	Phosphorylation	AYMRTSISGNWKANT EEEEECCCCCCCCCC	26.33	29899451
404	Phosphorylation	VPGATVPSPLRPWGP CCCCCCCCCCCCCCC	32.03	19060867
413	Phosphorylation	LRPWGPQTKPAKSPG CCCCCCCCCCCCCCC	41.97	20415495
418	Phosphorylation	PQTKPAKSPGQGQLG CCCCCCCCCCCCCCH	36.05	16944949
446	Phosphorylation	GGPRQAQSPQPPRSR CCCCCCCCCCCCCCC	28.63	29899451
452	Phosphorylation	QSPQPPRSRSPSQQR CCCCCCCCCCHHHCC	42.77	19060867
454	Phosphorylation	PQPPRSRSPSQQRLS CCCCCCCCHHHCCCC	30.10	21183079
456	Phosphorylation	PPRSRSPSQQRLSPQ CCCCCCHHHCCCCCC	39.94	25521595
461	Phosphorylation	SPSQQRLSPQGQQPV CHHHCCCCCCCCCCC	19.84	25521595
469	Phosphorylation	PQGQQPVSPQSGSPQ CCCCCCCCCCCCCCC	24.73	25521595
472	Phosphorylation	QQPVSPQSGSPQQQR CCCCCCCCCCCCHHC	44.62	25521595
474	Phosphorylation	PVSPQSGSPQQQRSP CCCCCCCCCCHHCCC	25.45	25521595
480	Phosphorylation	GSPQQQRSPGSPQLS CCCCHHCCCCCCCHH	29.31	27180971
483	Phosphorylation	QQQRSPGSPQLSRAS CHHCCCCCCCHHHCC	16.92	25521595
487	Phosphorylation	SPGSPQLSRASGGSS CCCCCCHHHCCCCCC	22.13	29899451
490	Phosphorylation	SPQLSRASGGSSPNQ CCCHHHCCCCCCCCC	42.44	29899451
493	Phosphorylation	LSRASGGSSPNQASK HHHCCCCCCCCCCCC	46.26	29899451
494	Phosphorylation	SRASGGSSPNQASKP HHCCCCCCCCCCCCC	31.01	29899451
499	Phosphorylation	GSSPNQASKPSASLS CCCCCCCCCCCCCCC	35.02	21454597
517	Phosphorylation	RPPVQGRSTSQQGEE CCCCCCCCCCCCCCC	38.95	25521595
518	Phosphorylation	PPVQGRSTSQQGEEP CCCCCCCCCCCCCCC	29.24	25521595
519	Phosphorylation	PVQGRSTSQQGEEPQ CCCCCCCCCCCCCCC	23.04	25521595
530	Phosphorylation	EEPQKSASPHPHLNK CCCCCCCCCCCCCCH	30.72	25338131
538	Phosphorylation	PHPHLNKSQSLTNSL CCCCCCHHHHHCCCC	24.75	19060867
540	Phosphorylation	PHLNKSQSLTNSLST CCCCHHHHHCCCCCC	44.23	25177544
542	Phosphorylation	LNKSQSLTNSLSTSD CCHHHHHCCCCCCCC	28.19	30372032
544	Phosphorylation	KSQSLTNSLSTSDTS HHHHHCCCCCCCCCC	20.61	19060867
546	Phosphorylation	QSLTNSLSTSDTSHR HHHCCCCCCCCCCCC	26.20	29899451
547	Phosphorylation	SLTNSLSTSDTSHRG HHCCCCCCCCCCCCC	35.60	29899451
557	Phosphorylation	TSHRGTPSEDEAKAE CCCCCCCCHHHHHHH	58.48	29899451
572	Phosphorylation	TIRNLRKSFASLFSD HHHHHHHHHHHHHCC	21.44	25521595
575	Phosphorylation	NLRKSFASLFSD--- HHHHHHHHHHCC---	28.12	25521595
578	Phosphorylation	KSFASLFSD------ HHHHHHHCC------	47.94	22324799

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
404	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
404	S	Phosphorylation	Kinase	CDK5	Q03114	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
9	S	Phosphorylation		21183079
Phosphorylation at Ser-9 dissociates synapsins from synaptic vesicles.

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 SYN3_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of SYN3_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of SYN3_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461 AND SER-469, ANDMASS SPECTROMETRY.	17114649 [Abstract]
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, AND MASSSPECTROMETRY.	16452087 [Abstract]

show