ESYT2_HUMAN - dbPTM
ESYT2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ESYT2_HUMAN
UniProt AC A0FGR8
Protein Name Extended synaptotagmin-2
Gene Name ESYT2
Organism Homo sapiens (Human).
Sequence Length 921
Subcellular Localization Cell membrane
Peripheral membrane protein. Endoplasmic reticulum membrane
Multi-pass membrane protein. Detected at sites of contact between the endoplasmic reticulum membrane and the cell membrane. Recruited to the cell membrane via the third C2 do
Protein Description Tethers the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane. Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport. Plays a role in FGF signaling via its role in the rapid internalization of FGFR1 that has been activated by FGF1 binding; this occurs most likely via the AP-2 complex..
Protein Sequence MTANRDAALSSHRHPGCAQRPRTPTFASSSQRRSAFGFDDGNFPGLGERSHAPGSRLGARRRAKTARGLRGHRQRGAGAGLSRPGSARAPSPPRPGGPENPGGVLSVELPGLLAQLARSFALLLPVYALGYLGLSFSWVLLALALLAWCRRSRGLKALRLCRALALLEDEERVVRLGVRACDLPAWVHFPDTERAEWLNKTVKHMWPFICQFIEKLFRETIEPAVRGANTHLSTFSFTKVDVGQQPLRINGVKVYTENVDKRQIILDLQISFVGNCEIDLEIKRYFCRAGVKSIQIHGTMRVILEPLIGDMPLVGALSIFFLRKPLLEINWTGLTNLLDVPGLNGLSDTIILDIISNYLVLPNRITVPLVSEVQIAQLRFPVPKGVLRIHFIEAQDLQGKDTYLKGLVKGKSDPYGIIRVGNQIFQSRVIKENLSPKWNEVYEALVYEHPGQELEIELFDEDPDKDDFLGSLMIDLIEVEKERLLDEWFTLDEVPKGKLHLRLEWLTLMPNASNLDKVLTDIKADKDQANDGLSSALLILYLDSARNLPSGKKISSNPNPVVQMSVGHKAQESKIRYKTNEPVWEENFTFFIHNPKRQDLEVEVRDEQHQCSLGNLKVPLSQLLTSEDMTVSQRFQLSNSGPNSTIKMKIALRVLHLEKRERPPDHQHSAQVKRPSVSKEGRKTSIKSHMSGSPGPGGSNTAPSTPVIGGSDKPGMEEKAQPPEAGPQGLHDLGRSSSSLLASPGHISVKEPTPSIASDISLPIATQELRQRLRQLENGTTLGQSPLGQIQLTIRHSSQRNKLIVVVHACRNLIAFSEDGSDPYVRMYLLPDKRRSGRRKTHVSKKTLNPVFDQSFDFSVSLPEVQRRTLDVAVKNSGGFLSKDKGLLGKVLVALASEELAKGWTQWYDLTEDGTRPQAMT
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
18 (in isoform 2)Phosphorylation-17.84-
35 (in isoform 4)Ubiquitination-13.5321890473
38 (in isoform 2)Phosphorylation-6.6428674419
82PhosphorylationRGAGAGLSRPGSARA
CCCCCCCCCCCCCCC		35.2028464451
91PhosphorylationPGSARAPSPPRPGGP
CCCCCCCCCCCCCCC		46.6917081983
172UbiquitinationALLEDEERVVRLGVR
HHCCCHHHHHHHCCC		30.13-
200UbiquitinationERAEWLNKTVKHMWP
HHHHHHHHHHHHHHH		53.15-
200 (in isoform 6)Ubiquitination-53.15-
201 (in isoform 4)Ubiquitination-33.4421890473
211UbiquitinationHMWPFICQFIEKLFR
HHHHHHHHHHHHHHH		37.2221890473
211 (in isoform 2)Ubiquitination-37.2221890473
225UbiquitinationRETIEPAVRGANTHL
HHCCHHHHCCCCCCC		9.44-
233UbiquitinationRGANTHLSTFSFTKV
CCCCCCCCCCEEEEE		21.57-
236PhosphorylationNTHLSTFSFTKVDVG
CCCCCCCEEEEECCC		31.9024719451
239UbiquitinationLSTFSFTKVDVGQQP
CCCCEEEEECCCCCC		34.1321890473
239 (in isoform 1)Ubiquitination-34.1321890473
239 (in isoform 6)Ubiquitination-34.1321890473
253UbiquitinationPLRINGVKVYTENVD
CEEECCEEEECCCCC		30.81-
255PhosphorylationRINGVKVYTENVDKR
EECCEEEECCCCCCC		11.5628152594
256PhosphorylationINGVKVYTENVDKRQ
ECCEEEECCCCCCCE		24.8728152594
261AcetylationVYTENVDKRQIILDL
EECCCCCCCEEEEEE		41.7527452117
261UbiquitinationVYTENVDKRQIILDL
EECCCCCCCEEEEEE		41.75-
271PhosphorylationIILDLQISFVGNCEI
EEEEEEEEEECCCEE		10.83-
329UbiquitinationLRKPLLEINWTGLTN
HCCCCEECCCCCCCH		5.4133845483
356UbiquitinationTIILDIISNYLVLPN
CHHHHHHHCCEECCC		21.5427667366
372UbiquitinationITVPLVSEVQIAQLR
CEECCCCEEEEEECC		30.84-
377MethylationVSEVQIAQLRFPVPK
CCEEEEEECCCCCCC		34.50-
377UbiquitinationVSEVQIAQLRFPVPK
CCEEEEEECCCCCCC		34.5021890473
377 (in isoform 2)Ubiquitination-34.5021890473
383UbiquitinationAQLRFPVPKGVLRIH
EECCCCCCCCEEEEE		28.1122505724
384UbiquitinationQLRFPVPKGVLRIHF
ECCCCCCCCEEEEEE		62.98-
384 (in isoform 6)Ubiquitination-62.98-
399PhosphorylationIEAQDLQGKDTYLKG
EEEHHCCCCCCCHHH		36.78-
400UbiquitinationEAQDLQGKDTYLKGL
EEHHCCCCCCCHHHH		33.66-
400 (in isoform 6)Ubiquitination-33.66-
403PhosphorylationDLQGKDTYLKGLVKG
HCCCCCCCHHHHCCC		19.29-
403UbiquitinationDLQGKDTYLKGLVKG
HCCCCCCCHHHHCCC		19.29-
405MethylationQGKDTYLKGLVKGKS
CCCCCCHHHHCCCCC		39.52-
405UbiquitinationQGKDTYLKGLVKGKS
CCCCCCHHHHCCCCC		39.522189047
405 (in isoform 1)Ubiquitination-39.5221890473
405 (in isoform 6)Ubiquitination-39.5221890473
407PhosphorylationKDTYLKGLVKGKSDP
CCCCHHHHCCCCCCC		3.26-
411MalonylationLKGLVKGKSDPYGII
HHHHCCCCCCCCCEE		46.0726320211
411UbiquitinationLKGLVKGKSDPYGII
HHHHCCCCCCCCCEE		46.07-
411 (in isoform 6)Ubiquitination-46.07-
427PhosphorylationVGNQIFQSRVIKENL
ECCHHHHHHHHHHCC		20.1220860994
431UbiquitinationIFQSRVIKENLSPKW
HHHHHHHHHCCCHHH		37.38-
431 (in isoform 6)Ubiquitination-37.38-
435PhosphorylationRVIKENLSPKWNEVY
HHHHHCCCHHHHHHH		35.7023312004
447UbiquitinationEVYEALVYEHPGQEL
HHHHHHCCCCCCCEE		14.9033845483
468UbiquitinationEDPDKDDFLGSLMID
CCCCCCCHHHHHHHH		13.76-
484 (in isoform 4)Phosphorylation-8.0822210691
495UbiquitinationWFTLDEVPKGKLHLR
CCCCCCCCCCCEEEE		37.32-
497 (in isoform 4)Phosphorylation-31.5222210691
498UbiquitinationLDEVPKGKLHLRLEW
CCCCCCCCEEEEEEE		38.57-
498 (in isoform 6)Ubiquitination-38.57-
502 (in isoform 4)Phosphorylation-21.5822210691
506 (in isoform 4)Phosphorylation-1.6022210691
513PhosphorylationLTLMPNASNLDKVLT
HHHCCCCHHHHHHHH		44.5628857561
514 (in isoform 4)Phosphorylation-50.2622210691
519 (in isoform 4)Phosphorylation-4.3622210691
525UbiquitinationVLTDIKADKDQANDG
HHHHHHCCHHHCCCC		50.49-
535PhosphorylationQANDGLSSALLILYL
HCCCCHHHHHHHHHH		28.1628270605
541PhosphorylationSSALLILYLDSARNL
HHHHHHHHHHHHCCC		11.0630576142
541UbiquitinationSSALLILYLDSARNL
HHHHHHHHHHHHCCC		11.06-
544PhosphorylationLLILYLDSARNLPSG
HHHHHHHHHCCCCCC		26.9128270605
550PhosphorylationDSARNLPSGKKISSN
HHHCCCCCCCCCCCC		67.4224719451
550UbiquitinationDSARNLPSGKKISSN
HHHCCCCCCCCCCCC		67.42-
552AcetylationARNLPSGKKISSNPN
HCCCCCCCCCCCCCC		51.8025953088
553MalonylationRNLPSGKKISSNPNP
CCCCCCCCCCCCCCC		51.8826320211
553UbiquitinationRNLPSGKKISSNPNP
CCCCCCCCCCCCCCC		51.88-
555PhosphorylationLPSGKKISSNPNPVV
CCCCCCCCCCCCCCE		32.7028450419
556PhosphorylationPSGKKISSNPNPVVQ
CCCCCCCCCCCCCEE		60.8328450419
562 (in isoform 6)Ubiquitination-4.11-
568UbiquitinationVVQMSVGHKAQESKI
CEEEECCCCHHHHCC		21.81-
576 (in isoform 6)Phosphorylation-30.5428842319
578UbiquitinationQESKIRYKTNEPVWE
HHHCCCEECCCCCEE		34.72-
589UbiquitinationPVWEENFTFFIHNPK
CCEECCEEEEECCCC		29.26-
599 (in isoform 6)Ubiquitination-49.15-
619UbiquitinationSLGNLKVPLSQLLTS
CCCCCCCCHHHCCCC		25.38-
625PhosphorylationVPLSQLLTSEDMTVS
CCHHHCCCCCCCCHH		38.3728348404
626PhosphorylationPLSQLLTSEDMTVSQ
CHHHCCCCCCCCHHH		31.4128348404
630PhosphorylationLLTSEDMTVSQRFQL
CCCCCCCCHHHEEEC		29.3628348404
631UbiquitinationLTSEDMTVSQRFQLS
CCCCCCCHHHEEECC		3.54-
632PhosphorylationTSEDMTVSQRFQLSN
CCCCCCHHHEEECCC		13.3828348404
638PhosphorylationVSQRFQLSNSGPNST
HHHEEECCCCCCCCH		20.4033259812
640PhosphorylationQRFQLSNSGPNSTIK
HEEECCCCCCCCHHH		52.8621955146
644PhosphorylationLSNSGPNSTIKMKIA
CCCCCCCCHHHHEHH		34.3421955146
645PhosphorylationSNSGPNSTIKMKIAL
CCCCCCCHHHHEHHH		31.1221955146
647AcetylationSGPNSTIKMKIALRV
CCCCCHHHHEHHHHH		33.9425953088
647UbiquitinationSGPNSTIKMKIALRV
CCCCCHHHHEHHHHH		33.94-
648PhosphorylationGPNSTIKMKIALRVL
CCCCHHHHEHHHHHH		3.1620068231
649UbiquitinationPNSTIKMKIALRVLH
CCCHHHHEHHHHHHH		21.59-
659UbiquitinationLRVLHLEKRERPPDH
HHHHHHHCCCCCCCC		66.95-
660PhosphorylationRVLHLEKRERPPDHQ
HHHHHHCCCCCCCCC		35.4620068231
663PhosphorylationHLEKRERPPDHQHSA
HHHCCCCCCCCCCCC		33.6418452278
665PhosphorylationEKRERPPDHQHSAQV
HCCCCCCCCCCCCCC		57.6819651622
668 (in isoform 6)Ubiquitination-22.98-
669PhosphorylationRPPDHQHSAQVKRPS
CCCCCCCCCCCCCCC		17.5226074081
670 (in isoform 6)Ubiquitination-18.96-
671PhosphorylationPDHQHSAQVKRPSVS
CCCCCCCCCCCCCCC		44.2620068231
673PhosphorylationHQHSAQVKRPSVSKE
CCCCCCCCCCCCCCC		46.6518452278
676PhosphorylationSAQVKRPSVSKEGRK
CCCCCCCCCCCCCCC		42.9528176443
677PhosphorylationAQVKRPSVSKEGRKT
CCCCCCCCCCCCCCC		11.9720068231
678PhosphorylationQVKRPSVSKEGRKTS
CCCCCCCCCCCCCCC		29.3525137130
680 (in isoform 6)Ubiquitination-57.64-
684PhosphorylationVSKEGRKTSIKSHMS
CCCCCCCCCHHHHCC		34.0323927012
685PhosphorylationSKEGRKTSIKSHMSG
CCCCCCCCHHHHCCC		30.9330278072
688PhosphorylationGRKTSIKSHMSGSPG
CCCCCHHHHCCCCCC		23.8129255136
691PhosphorylationTSIKSHMSGSPGPGG
CCHHHHCCCCCCCCC		30.6029255136
693PhosphorylationIKSHMSGSPGPGGSN
HHHHCCCCCCCCCCC		21.2729255136
699PhosphorylationGSPGPGGSNTAPSTP
CCCCCCCCCCCCCCC		36.6025159151
701PhosphorylationPGPGGSNTAPSTPVI
CCCCCCCCCCCCCCC		41.4629255136
703PhosphorylationPGGSNTAPSTPVIGG
CCCCCCCCCCCCCCC		36.3832142685
704PhosphorylationGGSNTAPSTPVIGGS
CCCCCCCCCCCCCCC		42.7723401153
705PhosphorylationGSNTAPSTPVIGGSD
CCCCCCCCCCCCCCC		22.1030278072
706PhosphorylationSNTAPSTPVIGGSDK
CCCCCCCCCCCCCCC		21.7732645325
708PhosphorylationTAPSTPVIGGSDKPG
CCCCCCCCCCCCCCC		5.6420166139
709PhosphorylationAPSTPVIGGSDKPGM
CCCCCCCCCCCCCCC		29.7719651622
710PhosphorylationPSTPVIGGSDKPGME
CCCCCCCCCCCCCCC		22.8820068231
711PhosphorylationSTPVIGGSDKPGMEE
CCCCCCCCCCCCCCH		36.9330278072
715PhosphorylationIGGSDKPGMEEKAQP
CCCCCCCCCCHHCCC		41.7018691976
720PhosphorylationKPGMEEKAQPPEAGP
CCCCCHHCCCCCCCC		30.32-
725PhosphorylationEKAQPPEAGPQGLHD
HHCCCCCCCCCCHHH		40.5120166139
727PhosphorylationAQPPEAGPQGLHDLG
CCCCCCCCCCHHHCC		31.9218691976
730PhosphorylationPEAGPQGLHDLGRSS
CCCCCCCHHHCCCCH		2.0920166139
733PhosphorylationGPQGLHDLGRSSSSL
CCCCHHHCCCCHHHC		4.2320166139
736PhosphorylationGLHDLGRSSSSLLAS
CHHHCCCCHHHCCCC		32.5423927012
737PhosphorylationLHDLGRSSSSLLASP
HHHCCCCHHHCCCCC		23.6823927012
738PhosphorylationHDLGRSSSSLLASPG
HHCCCCHHHCCCCCC		26.6723927012
739PhosphorylationDLGRSSSSLLASPGH
HCCCCHHHCCCCCCC		29.3825159151
743PhosphorylationSSSSLLASPGHISVK
CHHHCCCCCCCEEEC		31.2422167270
748PhosphorylationLASPGHISVKEPTPS
CCCCCCEEECCCCCC		22.8225159151
753PhosphorylationHISVKEPTPSIASDI
CEEECCCCCCHHHCC		30.6629255136
755PhosphorylationSVKEPTPSIASDISL
EECCCCCCHHHCCCC		33.0129255136
758PhosphorylationEPTPSIASDISLPIA
CCCCCHHHCCCCCHH		33.5329255136
761PhosphorylationPSIASDISLPIATQE
CCHHHCCCCCHHHHH		32.8429255136
766PhosphorylationDISLPIATQELRQRL
CCCCCHHHHHHHHHH		24.2430266825
789PhosphorylationLGQSPLGQIQLTIRH
CCCCCCCCCEEEEEE		28.12-
796PhosphorylationQIQLTIRHSSQRNKL
CCEEEEEECCCCCCE		28.13-
797PhosphorylationIQLTIRHSSQRNKLI
CEEEEEECCCCCCEE		20.5120068231
817PhosphorylationCRNLIAFSEDGSDPY
CCCHHHCCCCCCCCC		26.2528152594
820UbiquitinationLIAFSEDGSDPYVRM
HHHCCCCCCCCCEEE		29.8732015554
821PhosphorylationIAFSEDGSDPYVRMY
HHCCCCCCCCCEEEE		47.9728152594
824PhosphorylationSEDGSDPYVRMYLLP
CCCCCCCCEEEEECC		12.9925884760
847UbiquitinationKTHVSKKTLNPVFDQ
CCCCCHHHCCHHHCC		35.19-
854PhosphorylationTLNPVFDQSFDFSVS
HCCHHHCCCCCEECC		34.24-
875UbiquitinationRTLDVAVKNSGGFLS
HCCCEEECCCCCCCC		35.34-
882PhosphorylationKNSGGFLSKDKGLLG
CCCCCCCCCCCCHHH		36.2329214152
893PhosphorylationGLLGKVLVALASEEL
CHHHHHHHHHHHHHH		4.61-
896 (in isoform 6)Ubiquitination-12.73-
915PhosphorylationYDLTEDGTRPQAMT-
ECCCCCCCCCCCCC-		52.0422617229
921PhosphorylationGTRPQAMT-------
CCCCCCCC-------		38.1722199227
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

Oops, there are no upstream regulatory protein records of ESYT2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ESYT2_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 ESYT2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PM34_HUMANSLC25A17physical
22939629
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 ESYT2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-691; SER-738; SER-739;SER-743; SER-748; SER-755; SER-758 AND SER-761, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-758 AND SER-761, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743; SER-755; SER-758AND SER-761, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743; SER-758 ANDSER-761, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743, AND MASSSPECTROMETRY.

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