SYN2_MOUSE - dbPTM
SYN2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYN2_MOUSE
UniProt AC Q64332
Protein Name Synapsin-2
Gene Name Syn2
Organism Mus musculus (Mouse).
Sequence Length 586
Subcellular Localization Cell junction, synapse.
Protein Description Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release. May play a role in noradrenaline secretion by sympathetic neurons..
Protein Sequence MMNFLRRRLSDSSFIANLPNGYMTDLQRPEPQQPPPAPGPGAATASAATSAASPGPERRPPPAQAPAPQPAPQPAPTPSVGSSFFSSLSQAVKQTAASAGLVDAPAPSAASRKAKVLLVVDEPHTDWAKCFRGKKILGDYDIKVEQAEFSELNLVAHADGTYAVDMQVLRNGTKVVRSFRPDFVLIRQHAFGMAENEDFRHLVIGMQYAGLPSINSLESIYNFCDKPWVFAQMVAIFKTLGGEKFPLIEQTYYPNHREMLTLPTFPVVVKIGHAHSGMGKVKVENHYDFQDIASVVALTQTYATAEPFIDAKYDIRVQKIGNNYKAYMRTSISGNWKTNTGSAMLEQIAMSDRYKLWVDACSEMFGGLDICAVKAVHGKDGKDYIFEVMDCSMPLIGEHQVEDRQLITDLVISKMNQLLSRTPALSPQRPLTTQQPQSGTLKEPDSSKTPPQRPPPQGGPGQPQGMQPPGKVLPPRRLPSGPSLPSSSSSSSSSSSSSSAPQRPGGPTTTHGDASSSSNSLAEAQAPQAAPAQKPQPHPQLNKSQSLTNAFSFSESSFFRSSANEDEAKAETIRSLRKSFASLFSD
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
10PhosphorylationNFLRRRLSDSSFIAN
CHHHHHCCCCCHHHC		33.3722817900
12PhosphorylationLRRRLSDSSFIANLP
HHHHCCCCCHHHCCC		24.6329899451
49PhosphorylationAATASAATSAASPGP
CHHCHHHHHCCCCCC		20.7228066266
50PhosphorylationATASAATSAASPGPE
HHCHHHHHCCCCCCC		19.6728066266
53PhosphorylationSAATSAASPGPERRP
HHHHHCCCCCCCCCC		30.0619060867
79O-linked_GlycosylationPQPAPTPSVGSSFFS
CCCCCCCCCCHHHHH		41.4022645316
83PhosphorylationPTPSVGSSFFSSLSQ
CCCCCCHHHHHHHHH		25.1229899451
87PhosphorylationVGSSFFSSLSQAVKQ
CCHHHHHHHHHHHHH		27.2129899451
89PhosphorylationSSFFSSLSQAVKQTA
HHHHHHHHHHHHHHH		20.3129899451
95O-linked_GlycosylationLSQAVKQTAASAGLV
HHHHHHHHHHHCCCC		20.6255414111
95PhosphorylationLSQAVKQTAASAGLV
HHHHHHHHHHHCCCC		20.6229899451
108PhosphorylationLVDAPAPSAASRKAK
CCCCCCCCHHHCCCE		38.2822817900
111PhosphorylationAPAPSAASRKAKVLL
CCCCCHHHCCCEEEE		33.7525521595
129UbiquitinationEPHTDWAKCFRGKKI
CCCCCHHHHHCCCCC		29.6522790023
135UbiquitinationAKCFRGKKILGDYDI
HHHHCCCCCCCCCCE		46.0922790023
140PhosphorylationGKKILGDYDIKVEQA
CCCCCCCCCEEEEEE		20.1222324799
178PhosphorylationNGTKVVRSFRPDFVL
CCCEEEECCCCCEEE		17.6329899451
244UbiquitinationFKTLGGEKFPLIEQT
HHHHCCCCCCCEEEE		56.4022790023
253PhosphorylationPLIEQTYYPNHREML
CCEEEECCCCHHHHC		10.84-
287PhosphorylationKVKVENHYDFQDIAS
EEEEECCCCHHHHHH		29.9929899451
294PhosphorylationYDFQDIASVVALTQT
CCHHHHHHHHHHCCE		19.9129899451
304PhosphorylationALTQTYATAEPFIDA
HHCCEEECCCCCCCC		22.57-
331PhosphorylationYKAYMRTSISGNWKT
CEEEEEEECCCCCCC		12.3729899451
333PhosphorylationAYMRTSISGNWKTNT
EEEEEECCCCCCCCC		26.3329899451
338PhosphorylationSISGNWKTNTGSAML
ECCCCCCCCCCHHHH		29.6325521595
340PhosphorylationSGNWKTNTGSAMLEQ
CCCCCCCCCHHHHHH		37.4325521595
342PhosphorylationNWKTNTGSAMLEQIA
CCCCCCCHHHHHHHH		14.4125521595
351PhosphorylationMLEQIAMSDRYKLWV
HHHHHHCCCHHHHHH		15.2029899451
391S-palmitoylationYIFEVMDCSMPLIGE
EEEEEEECCCCCCCC		1.7128680068
413PhosphorylationLITDLVISKMNQLLS
HHHHHHHHHHHHHHH		20.5522817900
420PhosphorylationSKMNQLLSRTPALSP
HHHHHHHHCCCCCCC		42.5825521595
422PhosphorylationMNQLLSRTPALSPQR
HHHHHHCCCCCCCCC		14.9925521595
426PhosphorylationLSRTPALSPQRPLTT
HHCCCCCCCCCCCCC		22.5425521595
432PhosphorylationLSPQRPLTTQQPQSG
CCCCCCCCCCCCCCC		25.8224925903
433PhosphorylationSPQRPLTTQQPQSGT
CCCCCCCCCCCCCCC		32.6522324799
438PhosphorylationLTTQQPQSGTLKEPD
CCCCCCCCCCCCCCC		40.1924925903
440PhosphorylationTQQPQSGTLKEPDSS
CCCCCCCCCCCCCCC		39.6524925903
442UbiquitinationQPQSGTLKEPDSSKT
CCCCCCCCCCCCCCC		68.0222790023
446PhosphorylationGTLKEPDSSKTPPQR
CCCCCCCCCCCCCCC		44.4423335269
447 (in isoform 2)Phosphorylation-48.1825521595
447PhosphorylationTLKEPDSSKTPPQRP
CCCCCCCCCCCCCCC		48.1823335269
462 (in isoform 2)Phosphorylation-30.2129899451
480PhosphorylationLPPRRLPSGPSLPSS
CCCCCCCCCCCCCCC		68.85-
520PhosphorylationDASSSSNSLAEAQAP
CCCCCCCCHHHHCCC		30.79-
544PhosphorylationPHPQLNKSQSLTNAF
CCCCCCHHHHHHHHH		24.7524925903
546PhosphorylationPQLNKSQSLTNAFSF
CCCCHHHHHHHHHCC		44.2324925903
548PhosphorylationLNKSQSLTNAFSFSE
CCHHHHHHHHHCCCH		29.7324925903
552PhosphorylationQSLTNAFSFSESSFF
HHHHHHHCCCHHHHH		26.0024925903
554PhosphorylationLTNAFSFSESSFFRS
HHHHHCCCHHHHHCC		35.0624925903
556PhosphorylationNAFSFSESSFFRSSA
HHHCCCHHHHHCCCC		31.1129899451
557PhosphorylationAFSFSESSFFRSSAN
HHCCCHHHHHCCCCC		25.0929899451
572PhosphorylationEDEAKAETIRSLRKS
HHHHHHHHHHHHHHH		26.9222324799
575PhosphorylationAKAETIRSLRKSFAS
HHHHHHHHHHHHHHH		28.7729899451
579PhosphorylationTIRSLRKSFASLFSD
HHHHHHHHHHHHHCC		21.4425521595
582PhosphorylationSLRKSFASLFSD---
HHHHHHHHHHCC---		28.1225521595
585PhosphorylationKSFASLFSD------
HHHHHHHCC------		47.9422324799
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
10SPhosphorylationKinaseCAMK1Q91YS8
Uniprot
10SPhosphorylationKinasePKA-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
10SPhosphorylation

22673524
426SPhosphorylation

21183079
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 SYN2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SYN2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SYN2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-422 AND SER-426, ANDMASS SPECTROMETRY.

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