ESYT2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ESYT2_MOUSE
• UniProt AC: Q3TZZ7
• Protein Name: Extended synaptotagmin-2
• Gene Name: Esyt2
• Organism: Mus musculus (Mouse).
• Sequence Length: 845
• 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 (By similarity)..
• Protein Sequence: MSSAGGEGPEAGPGRAGGRSEPEAPGSALSVDLPGLLGQLARSFALLLPVYALGYLGLSFSWVLLALGLLAWCRRSRGLKASRLCRALALLEDEEQAVRLGVRACDLPAWVHFPDTERAEWLNKTVKHMWPFICQFIEKLFRETIEPAVRGANAHLSTFSFTKVDVGQQPLRVNGVKVYTENVDKRQIILDLQISFVGNCEIDLEIKRYFCRAGVKSIQIHGTMRVILEPLIGDMPLVGALSIFFLRKPLLEINWTGLTNLLDIPGLNGLSDTIILDIISNYLVLPNRITVPLVSEVQIAQLRFPIPKGVLRIHFIEAQDLQGKDTYLKGLVKGKSDPYGIIRVGNQIFQSKVIKENLSPKWNEVYEALVYEHPGQELEIELFDEDPDKDDFLGSLMIDLIEVEKERLLDEWFTLDEVPKGKLHLKLEWLTLMPDAANLDKVLADIRADKDQASDGLSSALLILYLDSARNLPSGKKINSNPNPLVQMSVGHKAQESKIRYKTSEPVWEENFTFFIHNPRRQDLEVEVKDEQHQCSLGSLRIPLSQLLTSDNMTINQRFQLSNSGPNSTLKMKIALRVLHLEKQERPPDYQHSAQVKRPSVSKEGRKMPIKSQMSASPGTGGANTAPSTPVMGVDDKPAMEEKPQPPEASPLGHRDLGRSSSSLLASPSHIAAKEPTPSIASDISLPIATQELRQRLRQLENGTTLGQSPLGQIQLTIRHSSQRNKLIVVVHSCRNLIAFSEDGSDPYVRMYLLPDKRRSGRRKTHVSKKTLNPVFDQSFDFSVSLPEVQRRTLDVAVKNSGGFLSKDKGLLGKVLVVLASEELAKGWTQWYDLTEDGTRPQVIT

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
2	Phosphorylation	------MSSAGGEGP ------CCCCCCCCC	28.97	29472430
3	Phosphorylation	-----MSSAGGEGPE -----CCCCCCCCCC	29.63	26824392
105	Glutathionylation	VRLGVRACDLPAWVH HHHCCCCCCCCEEEC	3.75	24333276
186	Ubiquitination	YTENVDKRQIILDLQ ECCCCCCCEEEEEEE	28.59	27667366
329	Ubiquitination	QGKDTYLKGLVKGKS CCCCCCHHHHCCCCC	39.52	22790023
352	Ubiquitination	GNQIFQSKVIKENLS CHHHHHCHHHHHCCC	36.88	27667366
359	Phosphorylation	KVIKENLSPKWNEVY HHHHHCCCHHHHHHH	35.70	29176673
529	Ubiquitination	QDLEVEVKDEQHQCS CCCEEEEECCCCCCC	41.88	22790023
545	Phosphorylation	GSLRIPLSQLLTSDN CCCEEEHHHHHCCCC	17.27	29899451
549	Phosphorylation	IPLSQLLTSDNMTIN EEHHHHHCCCCCEEC	42.50	29899451
564	Phosphorylation	QRFQLSNSGPNSTLK HHEECCCCCCCCHHH	52.86	29899451
590	Phosphorylation	KQERPPDYQHSAQVK CCCCCCCCCCCCCCC	17.56	29514104
600	Phosphorylation	SAQVKRPSVSKEGRK CCCCCCCCCCCCCCC	42.95	27087446
602	Phosphorylation	QVKRPSVSKEGRKMP CCCCCCCCCCCCCCC	29.35	23737553
603	Ubiquitination	VKRPSVSKEGRKMPI CCCCCCCCCCCCCCC	63.13	-
607	Ubiquitination	SVSKEGRKMPIKSQM CCCCCCCCCCCCCCC	60.94	-
607	Acetylation	SVSKEGRKMPIKSQM CCCCCCCCCCCCCCC	60.94	19851687
611	Acetylation	EGRKMPIKSQMSASP CCCCCCCCCCCCCCC	28.85	19852039
612	Phosphorylation	GRKMPIKSQMSASPG CCCCCCCCCCCCCCC	31.66	29550500
615	Phosphorylation	MPIKSQMSASPGTGG CCCCCCCCCCCCCCC	20.25	29550500
617	Phosphorylation	IKSQMSASPGTGGAN CCCCCCCCCCCCCCC	19.29	29550500
625	Phosphorylation	PGTGGANTAPSTPVM CCCCCCCCCCCCCCC	39.14	29514104
629	Phosphorylation	GANTAPSTPVMGVDD CCCCCCCCCCCCCCC	20.88	29514104
650	Phosphorylation	KPQPPEASPLGHRDL CCCCCCCCCCCCCCC	20.99	26824392
660	Phosphorylation	GHRDLGRSSSSLLAS CCCCCCCCCHHCCCC	32.54	25521595
661	Phosphorylation	HRDLGRSSSSLLASP CCCCCCCCHHCCCCH	23.68	25521595
662	Phosphorylation	RDLGRSSSSLLASPS CCCCCCCHHCCCCHH	26.67	27087446
663	Phosphorylation	DLGRSSSSLLASPSH CCCCCCHHCCCCHHH	29.38	25521595
667	Phosphorylation	SSSSLLASPSHIAAK CCHHCCCCHHHHHCC	27.23	27742792
669	Phosphorylation	SSLLASPSHIAAKEP HHCCCCHHHHHCCCC	25.65	21082442
677	Phosphorylation	HIAAKEPTPSIASDI HHHCCCCCCCHHHCC	30.66	27087446
679	Phosphorylation	AAKEPTPSIASDISL HCCCCCCCHHHCCCC	33.01	27087446
682	Phosphorylation	EPTPSIASDISLPIA CCCCCHHHCCCCCHH	33.53	27087446
685	Phosphorylation	PSIASDISLPIATQE CCHHHCCCCCHHHHH	32.84	27087446
690	Phosphorylation	DISLPIATQELRQRL CCCCCHHHHHHHHHH	24.24	28833060
748	Phosphorylation	SEDGSDPYVRMYLLP CCCCCCCEEEEEECC	12.99	22817900
771	Phosphorylation	KTHVSKKTLNPVFDQ CCCCCHHHCCHHHCC	35.19	24759943

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ESYT2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ESYT2_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ESYT2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of ESYT2_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-685, AND MASSSPECTROMETRY.
PubMed: 19144319

"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-682 AND SER-685, ANDMASS SPECTROMETRY.
PubMed: 19367708

"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662 AND SER-685, ANDMASS SPECTROMETRY.
PubMed: 17242355