dbPTM

SV2A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SV2A_HUMAN
UniProt AC	Q7L0J3
Protein Name	Synaptic vesicle glycoprotein 2A
Gene Name	SV2A
Organism	Homo sapiens (Human).
Sequence Length	742
Subcellular Localization	Cell junction, synapse . Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane Multi-pass membrane protein . Enriched in chromaffin granules, not present in adrenal microsomes. Associated with both insulin granules and synaptic-like mic
Protein Description	Plays a role in the control of regulated secretion in neural and endocrine cells, enhancing selectively low-frequency neurotransmission. Positively regulates vesicle fusion by maintaining the readily releasable pool of secretory vesicles (By similarity)..
Protein Sequence	MEEGFRDRAAFIRGAKDIAKEVKKHAAKKVVKGLDRVQDEYSRRSYSRFEEEDDDDDFPAPSDGYYRGEGTQDEEEGGASSDATEGHDEDDEIYEGEYQGIPRAESGGKGERMADGAPLAGVRGGLSDGEGPPGGRGEAQRRKEREELAQQYEAILRECGHGRFQWTLYFVLGLALMADGVEVFVVGFVLPSAEKDMCLSDSNKGMLGLIVYLGMMVGAFLWGGLADRLGRRQCLLISLSVNSVFAFFSSFVQGYGTFLFCRLLSGVGIGGSIPIVFSYFSEFLAQEKRGEHLSWLCMFWMIGGVYAAAMAWAIIPHYGWSFQMGSAYQFHSWRVFVLVCAFPSVFAIGALTTQPESPRFFLENGKHDEAWMVLKQVHDTNMRAKGHPERVFSVTHIKTIHQEDELIEIQSDTGTWYQRWGVRALSLGGQVWGNFLSCFGPEYRRITLMMMGVWFTMSFSYYGLTVWFPDMIRHLQAVDYASRTKVFPGERVEHVTFNFTLENQIHRGGQYFNDKFIGLRLKSVSFEDSLFEECYFEDVTSSNTFFRNCTFINTVFYNTDLFEYKFVNSRLINSTFLHNKEGCPLDVTGTGEGAYMVYFVSFLGTLAVLPGNIVSALLMDKIGRLRMLAGSSVMSCVSCFFLSFGNSESAMIALLCLFGGVSIASWNALDVLTVELYPSDKRTTAFGFLNALCKLAAVLGISIFTSFVGITKAAPILFASAALALGSSLALKLPETRGQVLQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
32	Ubiquitination	HAAKKVVKGLDRVQD HHHHHHHHCHHHHHH	57.66	-
41	Phosphorylation	LDRVQDEYSRRSYSR HHHHHHHHHHHHHHC	18.77	26552605
42	Phosphorylation	DRVQDEYSRRSYSRF HHHHHHHHHHHHHCC	21.12	26552605
45	Phosphorylation	QDEYSRRSYSRFEEE HHHHHHHHHHCCCCC	26.75	30576142
46	Phosphorylation	DEYSRRSYSRFEEED HHHHHHHHHCCCCCC	11.31	24114839
47	Phosphorylation	EYSRRSYSRFEEEDD HHHHHHHHCCCCCCC	31.57	30576142
62	Phosphorylation	DDDFPAPSDGYYRGE CCCCCCCCCCCCCCC	45.86	28796482
65	Phosphorylation	FPAPSDGYYRGEGTQ CCCCCCCCCCCCCCC	8.59	28796482
66	Phosphorylation	PAPSDGYYRGEGTQD CCCCCCCCCCCCCCC	20.05	28796482
71	Phosphorylation	GYYRGEGTQDEEEGG CCCCCCCCCCCCCCC	28.66	28796482
80	Phosphorylation	DEEEGGASSDATEGH CCCCCCCCCCCCCCC	31.83	28348404
81	Phosphorylation	EEEGGASSDATEGHD CCCCCCCCCCCCCCC	30.63	28348404
84	Phosphorylation	GGASSDATEGHDEDD CCCCCCCCCCCCCCC	47.71	28796482
94	Phosphorylation	HDEDDEIYEGEYQGI CCCCCCCCCCCCCCC	18.81	25884760
98	Phosphorylation	DEIYEGEYQGIPRAE CCCCCCCCCCCCCCC	23.93	28796482
113	Sulfoxidation	SGGKGERMADGAPLA CCCCCCCCCCCCCCC	3.29	21406390
123	Methylation	GAPLAGVRGGLSDGE CCCCCCCCCCCCCCC	32.32	115918053
127	Phosphorylation	AGVRGGLSDGEGPPG CCCCCCCCCCCCCCC	47.01	23401153
143	Ubiquitination	RGEAQRRKEREELAQ CCHHHHHHHHHHHHH	64.41	-
212	Phosphorylation	GMLGLIVYLGMMVGA CHHHHHHHHHHHHHH	7.19	-
265	Phosphorylation	FLFCRLLSGVGIGGS HHHHHHHHCCCCCCC	35.70	24043423
272	Phosphorylation	SGVGIGGSIPIVFSY HCCCCCCCHHHHHHH	21.70	24043423
278	Phosphorylation	GSIPIVFSYFSEFLA CCHHHHHHHHHHHHH	17.86	24043423
279	Phosphorylation	SIPIVFSYFSEFLAQ CHHHHHHHHHHHHHH	10.31	24043423
281	Phosphorylation	PIVFSYFSEFLAQEK HHHHHHHHHHHHHHH	21.14	24043423
366 (in isoform 1)	Ubiquitination	-	60.51	21890473
366 (in isoform 2)	Ubiquitination	-	60.51	21890473
366	Ubiquitination	RFFLENGKHDEAWMV CEEECCCCCCCEEEE	60.51	21890473
375	Ubiquitination	DEAWMVLKQVHDTNM CCEEEEEEEHHHHCH	38.57	21890473
375 (in isoform 1)	Ubiquitination	-	38.57	21890473
375 (in isoform 2)	Ubiquitination	-	38.57	21890473
393	Phosphorylation	GHPERVFSVTHIKTI CCHHHEEEEEEEEEE	24.21	29691806
395	Phosphorylation	PERVFSVTHIKTIHQ HHHEEEEEEEEEECC	19.38	20886841
411	Phosphorylation	DELIEIQSDTGTWYQ CCEEEEECCCCCCHH	42.68	-
465	Phosphorylation	SFSYYGLTVWFPDMI HHHHHCEEEECHHHH	16.01	26074081
480	Phosphorylation	RHLQAVDYASRTKVF HHHHHHCHHHCCEEC	10.40	22817900
482	Phosphorylation	LQAVDYASRTKVFPG HHHHCHHHCCEECCC	33.96	25332170
485	Ubiquitination	VDYASRTKVFPGERV HCHHHCCEECCCCCE	40.54	-
498	N-linked_Glycosylation	RVEHVTFNFTLENQI CEEEEEEEEEECCCH	21.45	UniProtKB CARBOHYD
515	Ubiquitination	GGQYFNDKFIGLRLK CCCCCCCCCCEEEEE	39.73	-
548	N-linked_Glycosylation	SSNTFFRNCTFINTV CCCCEECCCEEEEEE	24.83	UniProtKB CARBOHYD
573	N-linked_Glycosylation	FVNSRLINSTFLHNK EECCCCCCCCCCCCC	39.32	UniProtKB CARBOHYD

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
42	S	Phosphorylation	Kinase	TTBK2	Q6IQ55	PSP
45	S	Phosphorylation	Kinase	TTBK2	Q6IQ55	PSP
47	S	Phosphorylation	Kinase	TTBK2	Q6IQ55	PSP
80	S	Phosphorylation	Kinase	TTBK2	Q6IQ55	PSP
81	S	Phosphorylation	Kinase	TTBK2	Q6IQ55	PSP
84	T	Phosphorylation	Kinase	TTBK2	Q6IQ55	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SV2A_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 SV2A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of SV2A_HUMAN !!

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
D00709	Levetiracetam (JAN/USAN/INN); Keppra (TN); E keppra (TN)
D01914	Piracetam (JAN/USAN/INN); Myocalm (TN)
D05817	Seletracetam (USAN/INN)
D08879	Brivaracetam (USAN/INN)
DrugBank
DB01202	Levetiracetam

Regulatory Network of SV2A_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-80; SER-81; THR-84 ANDSER-127, AND MASS SPECTROMETRY.	19690332 [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-127, AND MASSSPECTROMETRY.	15822905 [Abstract]