EPN2_MOUSE - dbPTM
EPN2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EPN2_MOUSE
UniProt AC Q8CHU3
Protein Name Epsin-2
Gene Name Epn2
Organism Mus musculus (Mouse).
Sequence Length 595
Subcellular Localization Cytoplasm. In punctate structures throughout the cell and particularly concentrated in the region of the Golgi complex..
Protein Description Plays a role in the formation of clathrin-coated invaginations and endocytosis..
Protein Sequence MTTSSIRRQMKNIVNNYSEAEIKVREATSNDPWGPSSSLMTEIADLTYNVVAFSEIMSMVWKRLNDHGKNWRHVYKALTLLDYLIKTGSERVAQQCRENIFAIQTLKDFQYIDRDGKDQGINVREKSKQLVALLKDEERLKVERVQALKTKERMAQVATGVGSNQITFGRGSSQPNLSTSYSEQEYGKAGGSPASYHGSTSPRVSSELEQARPQTSGEEELQLQLALAMSREVAEQSSESVQTARGSKEERLRRGDDLRLQMALEESRRDTVKVPKKKEAKACCKPGSHSQQTTLLDLMDALPSSGPVTQKTEPWSAGASANQTNPWGGTVAPSNITDPWPSFGTKPAASVDPWGVPTTASTQSVPKNSDPWAASQQPASNAGKTTDAWGAAKPSSASGSFELFSNFNGTVKDDFSEFDNLRTSKKPAESGASVPPQDSRTTSPDLFESQSLTSASSKPSSARKTPESFLGPNAALVNLDSLVTKPAPPAQSLNPFLAPGAAAPAPVNPFQVNQPQPLTLNQLRGSPVLGSSASFGSGPGVETVAPMTSVAPHSSVGASGSSLTPLGPTAMNMVGSVGIPPSAAQSTGTTNPFLL
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
2Phosphorylation------MTTSSIRRQ
------CCHHHHHHH		35.0729472430
3Phosphorylation-----MTTSSIRRQM
-----CCHHHHHHHH		21.1229472430
4Phosphorylation----MTTSSIRRQMK
----CCHHHHHHHHH		18.0129472430
5Phosphorylation---MTTSSIRRQMKN
---CCHHHHHHHHHH		20.3029472430
105PhosphorylationENIFAIQTLKDFQYI
HCCCEEEECCCCCEE		29.66-
107UbiquitinationIFAIQTLKDFQYIDR
CCEEEECCCCCEECC		60.94-
111PhosphorylationQTLKDFQYIDRDGKD
EECCCCCEECCCCCC		12.55-
117UbiquitinationQYIDRDGKDQGINVR
CEECCCCCCCCCCHH		51.68-
128UbiquitinationINVREKSKQLVALLK
CCHHHHHHHHHHHHC		59.73-
135UbiquitinationKQLVALLKDEERLKV
HHHHHHHCCHHHHHH		65.04-
159PhosphorylationERMAQVATGVGSNQI
HHHHHHHHCCCCCEE		33.2829514104
163PhosphorylationQVATGVGSNQITFGR
HHHHCCCCCEEEECC		24.1325338131
170MethylationSNQITFGRGSSQPNL
CCEEEECCCCCCCCC		37.3124129315
172PhosphorylationQITFGRGSSQPNLST
EEEECCCCCCCCCCC		25.1624925903
173PhosphorylationITFGRGSSQPNLSTS
EEECCCCCCCCCCCC		53.1025521595
178PhosphorylationGSSQPNLSTSYSEQE
CCCCCCCCCCCCHHH		23.1925619855
179PhosphorylationSSQPNLSTSYSEQEY
CCCCCCCCCCCHHHH		34.5525619855
180PhosphorylationSQPNLSTSYSEQEYG
CCCCCCCCCCHHHHH		24.2425619855
181PhosphorylationQPNLSTSYSEQEYGK
CCCCCCCCCHHHHHC		19.1325619855
182PhosphorylationPNLSTSYSEQEYGKA
CCCCCCCCHHHHHCC		32.3524925903
186PhosphorylationTSYSEQEYGKAGGSP
CCCCHHHHHCCCCCC		24.5025619855
188UbiquitinationYSEQEYGKAGGSPAS
CCHHHHHCCCCCCCC		42.8522790023
192PhosphorylationEYGKAGGSPASYHGS
HHHCCCCCCCCCCCC		19.1727087446
195PhosphorylationKAGGSPASYHGSTSP
CCCCCCCCCCCCCCC		22.5027087446
196PhosphorylationAGGSPASYHGSTSPR
CCCCCCCCCCCCCCC		16.5925177544
199PhosphorylationSPASYHGSTSPRVSS
CCCCCCCCCCCCCCH		16.6423684622
200PhosphorylationPASYHGSTSPRVSSE
CCCCCCCCCCCCCHH		47.5521082442
201PhosphorylationASYHGSTSPRVSSEL
CCCCCCCCCCCCHHH		16.6527087446
205PhosphorylationGSTSPRVSSELEQAR
CCCCCCCCHHHHHHC		21.2627742792
206PhosphorylationSTSPRVSSELEQARP
CCCCCCCHHHHHHCC		43.2627742792
215PhosphorylationLEQARPQTSGEEELQ
HHHHCCCCCCHHHHH		41.1928464351
240PhosphorylationVAEQSSESVQTARGS
HHHHCHHHHHHHCCC		22.8229899451
243PhosphorylationQSSESVQTARGSKEE
HCHHHHHHHCCCHHH		19.0329899451
247PhosphorylationSVQTARGSKEERLRR
HHHHHCCCHHHHHHH		31.1929899451
267PhosphorylationLQMALEESRRDTVKV
HHHHHHHHHCCCCCC		24.2026060331
271PhosphorylationLEESRRDTVKVPKKK
HHHHHCCCCCCCCHH		22.0323684622
359O-linked_GlycosylationDPWGVPTTASTQSVP
CCCCCCCCCCCCCCC		16.7330059200
369PhosphorylationTQSVPKNSDPWAASQ
CCCCCCCCCCCHHHC		51.6925338131
384UbiquitinationQPASNAGKTTDAWGA
CCCCCCCCCCCCCCC		45.93-
385PhosphorylationPASNAGKTTDAWGAA
CCCCCCCCCCCCCCC		29.0522345495
386PhosphorylationASNAGKTTDAWGAAK
CCCCCCCCCCCCCCC		27.4922345495
395PhosphorylationAWGAAKPSSASGSFE
CCCCCCCCCCCCCEE		37.5222345495
396PhosphorylationWGAAKPSSASGSFEL
CCCCCCCCCCCCEEE		34.6722345495
398PhosphorylationAAKPSSASGSFELFS
CCCCCCCCCCEEECC		36.6022345495
400PhosphorylationKPSSASGSFELFSNF
CCCCCCCCEEECCCC		17.0422345495
405PhosphorylationSGSFELFSNFNGTVK
CCCEEECCCCCCCCC		53.8122345495
410PhosphorylationLFSNFNGTVKDDFSE
ECCCCCCCCCCCHHH		26.0322345495
433PhosphorylationKPAESGASVPPQDSR
CCCCCCCCCCCCCCC		38.3928066266
439PhosphorylationASVPPQDSRTTSPDL
CCCCCCCCCCCCCCH		26.6925521595
441PhosphorylationVPPQDSRTTSPDLFE
CCCCCCCCCCCCHHH		35.2627087446
442PhosphorylationPPQDSRTTSPDLFES
CCCCCCCCCCCHHHC		36.8325521595
443PhosphorylationPQDSRTTSPDLFESQ
CCCCCCCCCCHHHCC		18.7924925903
449PhosphorylationTSPDLFESQSLTSAS
CCCCHHHCCCCCCCC		20.1021149613
451PhosphorylationPDLFESQSLTSASSK
CCHHHCCCCCCCCCC		42.7824925903
453PhosphorylationLFESQSLTSASSKPS
HHHCCCCCCCCCCCC		27.7424925903
454PhosphorylationFESQSLTSASSKPSS
HHCCCCCCCCCCCCH		31.2925777480
456PhosphorylationSQSLTSASSKPSSAR
CCCCCCCCCCCCHHC		38.3725777480
457PhosphorylationQSLTSASSKPSSARK
CCCCCCCCCCCHHCC		48.5825777480
458UbiquitinationSLTSASSKPSSARKT
CCCCCCCCCCHHCCC		46.56-
460PhosphorylationTSASSKPSSARKTPE
CCCCCCCCHHCCCCH		40.1325777480
461PhosphorylationSASSKPSSARKTPES
CCCCCCCHHCCCCHH		40.3925777480
465PhosphorylationKPSSARKTPESFLGP
CCCHHCCCCHHHCCC		27.0826824392
468PhosphorylationSARKTPESFLGPNAA
HHCCCCHHHCCCCCE		27.2921149613
481PhosphorylationAALVNLDSLVTKPAP
CEEEEHHHHCCCCCC		28.0922324799
484PhosphorylationVNLDSLVTKPAPPAQ
EEHHHHCCCCCCCHH		36.2822324799
526PhosphorylationTLNQLRGSPVLGSSA
CHHHCCCCCCCCCCC		12.8523649490
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 EPN2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EPN2_MOUSE !!
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 EPN2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VGFR3_MOUSEFlt4physical
25314967
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EPN2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-192, AND MASSSPECTROMETRY.
"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-192; SER-195 ANDSER-443, AND MASS SPECTROMETRY.
"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 SER-173; THR-442 ANDSER-449, AND MASS SPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-182, ANDMASS SPECTROMETRY.

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