dbPTM

SYN1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SYN1_HUMAN
UniProt AC	P17600
Protein Name	Synapsin-1
Gene Name	SYN1
Organism	Homo sapiens (Human).
Sequence Length	705
Subcellular Localization	Cell junction, synapse. Golgi apparatus.
Protein Description	Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release. The complex formed with NOS1 and CAPON proteins is necessary for specific nitric-oxid functions at a presynaptic level..
Protein Sequence	MNYLRRRLSDSNFMANLPNGYMTDLQRPQPPPPPPGAHSPGATPGPGTATAERSSGVAPAASPAAPSPGSSGGGGFFSSLSNAVKQTTAAAAATFSEQVGGGSGGAGRGGAASRVLLVIDEPHTDWAKYFKGKKIHGEIDIKVEQAEFSDLNLVAHANGGFSVDMEVLRNGVKVVRSLKPDFVLIRQHAFSMARNGDYRSLVIGLQYAGIPSVNSLHSVYNFCDKPWVFAQMVRLHKKLGTEEFPLIDQTFYPNHKEMLSSTTYPVVVKMGHAHSGMGKVKVDNQHDFQDIASVVALTKTYATAEPFIDAKYDVRVQKIGQNYKAYMRTSVSGNWKTNTGSAMLEQIAMSDRYKLWVDTCSEIFGGLDICAVEALHGKDGRDHIIEVVGSSMPLIGDHQDEDKQLIVELVVNKMAQALPRQRQRDASPGRGSHGQTPSPGALPLGRQTSQQPAGPPAQQRPPPQGGPPQPGPGPQRQGPPLQQRPPPQGQQHLSGLGPPAGSPLPQRLPSPTSAPQQPASQAAPPTQGQGRQSRPVAGGPGAPPAARPPASPSPQRQAGPPQATRQTSVSGPAPPKASGAPPGGQQRQGPPQKPPGPAGPTRQASQAGPVPRTGPPTTQQPRPSGPGPAGRPKPQLAQKPSQDVPPPATAAAGGPPHPQLNKSQSLTNAFNLPEPAPPRPSLSQDEVKAETIRSLRKSFASLFSD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	NYLRRRLSDSNFMAN CHHHHHCCCCCHHHC	36.86	26657352
9 (in isoform 2)	Phosphorylation	-	36.86	-
11	Phosphorylation	LRRRLSDSNFMANLP HHHHCCCCCHHHCCC	28.70	32142685
39	Phosphorylation	PPPPGAHSPGATPGP CCCCCCCCCCCCCCC	25.21	20886841
43	Phosphorylation	GAHSPGATPGPGTAT CCCCCCCCCCCCCCC	34.39	27732954
48	Phosphorylation	GATPGPGTATAERSS CCCCCCCCCCCCCCC	24.78	27732954
50	Phosphorylation	TPGPGTATAERSSGV CCCCCCCCCCCCCCC	28.96	27732954
54	Phosphorylation	GTATAERSSGVAPAA CCCCCCCCCCCCCCC	23.97	30177828
55	O-linked_Glycosylation	TATAERSSGVAPAAS CCCCCCCCCCCCCCC	43.43	UniProtKB CARBOHYD
55	Phosphorylation	TATAERSSGVAPAAS CCCCCCCCCCCCCCC	43.43	30177828
62	Phosphorylation	SGVAPAASPAAPSPG CCCCCCCCCCCCCCC	19.71	26657352
62 (in isoform 2)	Phosphorylation	-	19.71	-
67	Phosphorylation	AASPAAPSPGSSGGG CCCCCCCCCCCCCCC	36.85	26657352
67 (in isoform 2)	Phosphorylation	-	36.85	-
70	Phosphorylation	PAAPSPGSSGGGGFF CCCCCCCCCCCCCHH	29.24	28857561
71	Phosphorylation	AAPSPGSSGGGGFFS CCCCCCCCCCCCHHH	47.58	28857561
78	Phosphorylation	SGGGGFFSSLSNAVK CCCCCHHHHHHHHHH	28.27	27732954
79	Phosphorylation	GGGGFFSSLSNAVKQ CCCCHHHHHHHHHHH	30.57	27732954
81	Phosphorylation	GGFFSSLSNAVKQTT CCHHHHHHHHHHHHH	25.37	27732954
87	O-linked_Glycosylation	LSNAVKQTTAAAAAT HHHHHHHHHHHHHHH	16.82	28657654
87	O-linked_Glycosylation	LSNAVKQTTAAAAAT HHHHHHHHHHHHHHH	16.82	10386995
87 (in isoform 2)	O-linked_Glycosylation	-	16.82	-
94	Phosphorylation	TTAAAAATFSEQVGG HHHHHHHHHHHHCCC	23.98	24076635
96	O-linked_Glycosylation	AAAAATFSEQVGGGS HHHHHHHHHHCCCCC	23.82	UniProtKB CARBOHYD
96	O-linked_Glycosylation	AAAAATFSEQVGGGS HHHHHHHHHHCCCCC	23.82	12438562
96	Phosphorylation	AAAAATFSEQVGGGS HHHHHHHHHHCCCCC	23.82	24076635
96 (in isoform 2)	O-linked_Glycosylation	-	23.82	-
103	O-linked_Glycosylation	SEQVGGGSGGAGRGG HHHCCCCCCCCCCCC	37.01	UniProtKB CARBOHYD
103	O-linked_Glycosylation	SEQVGGGSGGAGRGG HHHCCCCCCCCCCCC	37.01	12438562
103 (in isoform 2)	O-linked_Glycosylation	-	37.01	-
128	Ubiquitination	EPHTDWAKYFKGKKI CCCCCHHHHHCCCEE	47.14	30230243
179	Ubiquitination	VKVVRSLKPDFVLIR EEEHHHCCCCEEEEE	43.73	30230243
238	Ubiquitination	QMVRLHKKLGTEEFP HHHHHHHHHCCCCCC	41.21	30230243
241	Phosphorylation	RLHKKLGTEEFPLID HHHHHHCCCCCCCCC	42.66	24076635
261	O-linked_Glycosylation	NHKEMLSSTTYPVVV CHHHHHHCCCCEEEE	22.32	UniProtKB CARBOHYD
261	O-linked_Glycosylation	NHKEMLSSTTYPVVV CHHHHHHCCCCEEEE	22.32	12438562
261 (in isoform 2)	O-linked_Glycosylation	-	22.32	-
262	O-linked_Glycosylation	HKEMLSSTTYPVVVK HHHHHHCCCCEEEEE	27.29	28657654
262	Phosphorylation	HKEMLSSTTYPVVVK HHHHHHCCCCEEEEE	27.29	28985074
263	O-linked_Glycosylation	KEMLSSTTYPVVVKM HHHHHCCCCEEEEEE	27.98	28657654
263	Phosphorylation	KEMLSSTTYPVVVKM HHHHHCCCCEEEEEE	27.98	28985074
281	Ubiquitination	HSGMGKVKVDNQHDF CCCCCEEEECCCCCH	47.56	30230243
293	Phosphorylation	HDFQDIASVVALTKT CCHHHHHHHHHHCCC	19.91	-
299	Ubiquitination	ASVVALTKTYATAEP HHHHHHCCCCCCCCC	40.15	30230243
300	Phosphorylation	SVVALTKTYATAEPF HHHHHCCCCCCCCCC	17.10	28796482
301	Phosphorylation	VVALTKTYATAEPFI HHHHCCCCCCCCCCC	11.96	28796482
303	Phosphorylation	ALTKTYATAEPFIDA HHCCCCCCCCCCCCC	22.57	24076635
311	Ubiquitination	AEPFIDAKYDVRVQK CCCCCCCCCCEEEEE	37.93	32142685
312	Phosphorylation	EPFIDAKYDVRVQKI CCCCCCCCCEEEEEC	22.76	-
326	Phosphorylation	IGQNYKAYMRTSVSG CCCCEEEEEEECCCC	5.29	21406692
329	Phosphorylation	NYKAYMRTSVSGNWK CEEEEEEECCCCCCC	19.56	21406692
330	Phosphorylation	YKAYMRTSVSGNWKT EEEEEEECCCCCCCC	12.15	21406692
332	Phosphorylation	AYMRTSVSGNWKTNT EEEEECCCCCCCCCC	26.61	21406692
337	Phosphorylation	SVSGNWKTNTGSAML CCCCCCCCCCCHHHH	29.63	27732954
339	Phosphorylation	SGNWKTNTGSAMLEQ CCCCCCCCCHHHHHH	37.43	24076635
341	Phosphorylation	NWKTNTGSAMLEQIA CCCCCCCHHHHHHHH	14.41	24076635
391	Phosphorylation	IIEVVGSSMPLIGDH EEEEECCCCCCCCCC	20.63	25307156
413	Ubiquitination	IVELVVNKMAQALPR HHHHHHHHHHHHCHH	24.81	30230243
427	Phosphorylation	RQRQRDASPGRGSHG HHHHCCCCCCCCCCC	31.98	28674151
430	Methylation	QRDASPGRGSHGQTP HCCCCCCCCCCCCCC	46.99	-
432	O-linked_Glycosylation	DASPGRGSHGQTPSP CCCCCCCCCCCCCCC	24.08	UniProtKB CARBOHYD
432	O-linked_Glycosylation	DASPGRGSHGQTPSP CCCCCCCCCCCCCCC	24.08	12438562
432	Phosphorylation	DASPGRGSHGQTPSP CCCCCCCCCCCCCCC	24.08	30177828
432 (in isoform 2)	O-linked_Glycosylation	-	24.08	-
436	Phosphorylation	GRGSHGQTPSPGALP CCCCCCCCCCCCCCC	30.26	20886841
438	Phosphorylation	GSHGQTPSPGALPLG CCCCCCCCCCCCCCC	39.08	26033855
448	Phosphorylation	ALPLGRQTSQQPAGP CCCCCCCCCCCCCCC	27.43	27251275
449	Phosphorylation	LPLGRQTSQQPAGPP CCCCCCCCCCCCCCC	20.62	27251275
476	Methylation	QPGPGPQRQGPPLQQ CCCCCCCCCCCCHHC	46.70	-
502	Phosphorylation	GLGPPAGSPLPQRLP CCCCCCCCCCCCCCC	25.93	28348404
510	Phosphorylation	PLPQRLPSPTSAPQQ CCCCCCCCCCCCCCC	45.46	15345747
510 (in isoform 2)	Phosphorylation	-	45.46	-
512	Phosphorylation	PQRLPSPTSAPQQPA CCCCCCCCCCCCCCH	41.69	30278072
513	Phosphorylation	QRLPSPTSAPQQPAS CCCCCCCCCCCCCHH	41.14	30278072
520	Phosphorylation	SAPQQPASQAAPPTQ CCCCCCHHHCCCCCC	27.34	25307156
526	O-linked_Glycosylation	ASQAAPPTQGQGRQS HHHCCCCCCCCCCCC	44.25	UniProtKB CARBOHYD
526	O-linked_Glycosylation	ASQAAPPTQGQGRQS HHHCCCCCCCCCCCC	44.25	10386995
526 (in isoform 2)	O-linked_Glycosylation	-	44.25	-
533	Phosphorylation	TQGQGRQSRPVAGGP CCCCCCCCCCCCCCC	36.87	29449344
534	Methylation	QGQGRQSRPVAGGPG CCCCCCCCCCCCCCC	22.75	-
547	Methylation	PGAPPAARPPASPSP CCCCCCCCCCCCCCC	39.58	-
551	Phosphorylation	PAARPPASPSPQRQA CCCCCCCCCCCCCCC	31.52	26503892
551 (in isoform 2)	Phosphorylation	-	31.52	-
553	Phosphorylation	ARPPASPSPQRQAGP CCCCCCCCCCCCCCC	31.04	26503892
553 (in isoform 2)	Phosphorylation	-	31.04	-
556	Methylation	PASPSPQRQAGPPQA CCCCCCCCCCCCCCC	31.53	-
564	O-linked_Glycosylation	QAGPPQATRQTSVSG CCCCCCCCCCCCCCC	20.33	UniProtKB CARBOHYD
564	O-linked_Glycosylation	QAGPPQATRQTSVSG CCCCCCCCCCCCCCC	20.33	10386995
564	Phosphorylation	QAGPPQATRQTSVSG CCCCCCCCCCCCCCC	20.33	23312004
564 (in isoform 2)	O-linked_Glycosylation	-	20.33	-
567	Phosphorylation	PPQATRQTSVSGPAP CCCCCCCCCCCCCCC	28.01	27732954
568	O-linked_Glycosylation	PQATRQTSVSGPAPP CCCCCCCCCCCCCCC	13.12	28657654
568	Phosphorylation	PQATRQTSVSGPAPP CCCCCCCCCCCCCCC	13.12	26657352
568 (in isoform 2)	Phosphorylation	-	13.12	-
570	Phosphorylation	ATRQTSVSGPAPPKA CCCCCCCCCCCCCCC	38.53	27732954
578	O-linked_Glycosylation	GPAPPKASGAPPGGQ CCCCCCCCCCCCCCC	41.43	UniProtKB CARBOHYD
578	O-linked_Glycosylation	GPAPPKASGAPPGGQ CCCCCCCCCCCCCCC	41.43	10386995
578 (in isoform 2)	O-linked_Glycosylation	-	41.43	-
605	Phosphorylation	AGPTRQASQAGPVPR CCCCCCHHHCCCCCC	16.54	17525332
605 (in isoform 2)	Phosphorylation	-	16.54	-
613	Phosphorylation	QAGPVPRTGPPTTQQ HCCCCCCCCCCCCCC	48.23	24719451
618	O-linked_Glycosylation	PRTGPPTTQQPRPSG CCCCCCCCCCCCCCC	30.86	28657654
622	Methylation	PPTTQQPRPSGPGPA CCCCCCCCCCCCCCC	33.41	-
641	Phosphorylation	PQLAQKPSQDVPPPA CCCCCCCCCCCCCCH	46.15	-
641 (in isoform 2)	Phosphorylation	-	46.15	24117733
663	Phosphorylation	PHPQLNKSQSLTNAF CCCCCCCCCCCHHCC	24.75	27732954
665	Phosphorylation	PQLNKSQSLTNAFNL CCCCCCCCCHHCCCC	44.23	27732954
667	Phosphorylation	LNKSQSLTNAFNLPE CCCCCCCHHCCCCCC	29.73	32142685
679	Asymmetric dimethylarginine	LPEPAPPRPSLSQDE CCCCCCCCCCCCHHH	32.17	-
679	Methylation	LPEPAPPRPSLSQDE CCCCCCCCCCCCHHH	32.17	-
681	Phosphorylation	EPAPPRPSLSQDEVK CCCCCCCCCCHHHHH	41.76	27732954
683	Phosphorylation	APPRPSLSQDEVKAE CCCCCCCCHHHHHHH	39.67	25332170
694	Phosphorylation	VKAETIRSLRKSFAS HHHHHHHHHHHHHHH	28.77	24719451
698	Phosphorylation	TIRSLRKSFASLFSD HHHHHHHHHHHHHCC	21.44	29691806
701	Phosphorylation	SLRKSFASLFSD--- HHHHHHHHHHCC---	28.12	29691806

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
9	S	Phosphorylation	Kinase	CAMK1	Q14012	Uniprot
9	S	Phosphorylation	Kinase	CAMK1-FAMILY	-	GPS
9	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
9	S	Phosphorylation	Kinase	PKA	-	Uniprot
438	S	Phosphorylation	Kinase	UHMK1	Q8TAS1	PhosphoELM
551	S	Phosphorylation	Kinase	PDPK1	O15530	Uniprot
551	S	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
551	S	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
568	S	Phosphorylation	Kinase	CAMK2B	Q13554	GPS
568	S	Phosphorylation	Kinase	CAMK2	-	Uniprot
605	S	Phosphorylation	Kinase	CAMK2B	Q13554	GPS
605	S	Phosphorylation	Kinase	PAK-SUBFAMILY	-	GPS
605	S	Phosphorylation	Kinase	CAMK2	-	Uniprot
605	S	Phosphorylation	Kinase	PAK_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
9	S	Phosphorylation		-
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 SYN1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KAT5_HUMAN	KAT5	physical	16169070
SYN1_HUMAN	SYN1	physical	16169070
VIME_HUMAN	VIM	physical	16169070
SYN2_HUMAN	SYN2	physical	10358015
CAPON_HUMAN	NOS1AP	physical	11867766
NOS1_HUMAN	NOS1	physical	11867766
NCF1_HUMAN	NCF1	physical	10899172
BIN1_HUMAN	BIN1	physical	10899172
AMPH_HUMAN	AMPH	physical	10899172
SRC_HUMAN	SRC	physical	10899172
P85A_HUMAN	PIK3R1	physical	10899172
CRK_HUMAN	CRK	physical	10899172
TF3C2_HUMAN	GTF3C2	physical	26496610
PSMD2_HUMAN	PSMD2	physical	26496610
VPS54_HUMAN	VPS54	physical	26496610
LC7L3_HUMAN	LUC7L3	physical	26496610
DGCR8_HUMAN	DGCR8	physical	26496610
ERGI1_HUMAN	ERGIC1	physical	26496610
SP130_HUMAN	SAP130	physical	26496610
ANTR1_HUMAN	ANTXR1	physical	26496610
ERI1_HUMAN	ERI1	physical	26496610
ATG4A_HUMAN	ATG4A	physical	26496610

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300491	Epilepsy X-linked, with variable learning disabilities and behavior disorders (XELBD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SYN1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605, AND MASSSPECTROMETRY.	17525332 [Abstract]
"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-39; SER-427; SER-551;SER-553 AND SER-605, AND MASS SPECTROMETRY.	15822905 [Abstract]

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