EPN2_HUMAN - dbPTM
EPN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EPN2_HUMAN
UniProt AC O95208
Protein Name Epsin-2
Gene Name EPN2
Organism Homo sapiens (Human).
Sequence Length 641
Subcellular Localization Cytoplasm . Cytoplasmic vesicle, clathrin-coated vesicle . In punctate structures throughout the cell, associated with clathrin-coated vesicles, 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 MTTSSIRRQMKNIVNNYSEAEIKVREATSNDPWGPSSSLMTEIADLTYNVVAFSEIMSMVWKRLNDHGKNWRHVYKALTLLDYLIKTGSERVAQQCRENIFAIQTLKDFQYIDRDGKDQGINVREKSKQLVALLKDEERLKAERAQALKTKERMAQVATGMGSNQITFGRGSSQPNLSTSHSEQEYGKAGGSPASYHGSPEASLCPQHRTGAPLGQSEELQPLSQRHPFLPHLGLASRPNGDWSQPCLTCDRAARATSPRVSSELEQARPQTSGEEELQLQLALAMSREVAEQEERLRRGDDLRLQMALEESRRDTVKIPKKKEHGSLPQQTTLLDLMDALPSSGPAAQKAEPWGPSASTNQTNPWGGPAAPASTSDPWPSFGTKPAASIDPWGVPTGATVQSVPKNSDPWAASQQPASSAGKRASDAWGAVSTTKPVSVSGSFELFSNLNGTIKDDFSEFDNLRTSKKTAESVTSLPSQNNGTTSPDPFESQPLTVASSKPSSARKTPESFLGPNAALVNLDSLVTRPAPPAQSLNPFLAPGAPATSAPVNPFQVNQPQPLTLNQLRGSPVLGTSTSFGPGPGVESMAVASMTSAAPQPALGATGSSLTPLGPAMMNMVGSVGIPPSAAQATGTTNPFLL
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		35.0720071362
4Phosphorylation----MTTSSIRRQMK
----CCHHHHHHHHH		18.0120071362
5Phosphorylation---MTTSSIRRQMKN
---CCHHHHHHHHHH		20.3028355574
11UbiquitinationSSIRRQMKNIVNNYS
HHHHHHHHHHHHHCH		34.8721890473
11UbiquitinationSSIRRQMKNIVNNYS
HHHHHHHHHHHHHCH		34.8721890473
17PhosphorylationMKNIVNNYSEAEIKV
HHHHHHHCHHHEEEE		11.5925627689
18PhosphorylationKNIVNNYSEAEIKVR
HHHHHHCHHHEEEEE		32.2423403867
33UbiquitinationEATSNDPWGPSSSLM
ECCCCCCCCCCHHHH		33.9027667366
68 (in isoform 3)Ubiquitination-28.0521890473
69UbiquitinationKRLNDHGKNWRHVYK
HHHHHCCCCHHHHHH		50.33-
75PhosphorylationGKNWRHVYKALTLLD
CCCHHHHHHHHHHHH		5.6122817900
78 (in isoform 3)Ubiquitination-2.7921890473
79PhosphorylationRHVYKALTLLDYLIK
HHHHHHHHHHHHHHH		30.0921406692
83PhosphorylationKALTLLDYLIKTGSE
HHHHHHHHHHHHCCH		15.4220068231
96 (in isoform 3)Ubiquitination-3.8121890473
107UbiquitinationIFAIQTLKDFQYIDR
CCEEEECCCCCEECC		60.9423000965
107 (in isoform 1)Ubiquitination-60.9421890473
107 (in isoform 2)Ubiquitination-60.9421890473
107UbiquitinationIFAIQTLKDFQYIDR
CCEEEECCCCCEECC		60.9421890473
111PhosphorylationQTLKDFQYIDRDGKD
EECCCCCEECCCCCC		12.55-
117UbiquitinationQYIDRDGKDQGINVR
CEECCCCCCCCCCHH		51.6821906983
117 (in isoform 1)Ubiquitination-51.6821890473
117 (in isoform 2)Ubiquitination-51.6821890473
128UbiquitinationINVREKSKQLVALLK
CCHHHHHHHHHHHHC		59.7333845483
134 (in isoform 3)Phosphorylation-4.7825921289
135UbiquitinationKQLVALLKDEERLKA
HHHHHHHCCHHHHHH		65.0421906983
135 (in isoform 1)Ubiquitination-65.0421890473
135 (in isoform 2)Ubiquitination-65.0421890473
138UbiquitinationVALLKDEERLKAERA
HHHHCCHHHHHHHHH		73.7332015554
141PhosphorylationLKDEERLKAERAQAL
HCCHHHHHHHHHHHH		55.1932142685
141UbiquitinationLKDEERLKAERAQAL
HCCHHHHHHHHHHHH		55.1923503661
147 (in isoform 3)Phosphorylation-15.2727155012
149UbiquitinationAERAQALKTKERMAQ
HHHHHHHHHHHHHHH		61.6432142685
150PhosphorylationERAQALKTKERMAQV
HHHHHHHHHHHHHHH		38.7029978859
153 (in isoform 3)Phosphorylation-27.5630266825
156 (in isoform 3)Phosphorylation-18.9426846344
157 (in isoform 3)Phosphorylation-3.6030266825
159PhosphorylationERMAQVATGMGSNQI
HHHHHHHHCCCCCCE		28.9229978859
160 (in isoform 3)Phosphorylation-14.5523927012
161 (in isoform 3)Phosphorylation-4.6425159151
162 (in isoform 3)Phosphorylation-25.4523927012
163PhosphorylationQVATGMGSNQITFGR
HHHHCCCCCCEEECC		19.3729978859
163 (in isoform 2)Phosphorylation-19.3724719451
167PhosphorylationGMGSNQITFGRGSSQ
CCCCCCEEECCCCCC		15.4029978859
170MethylationSNQITFGRGSSQPNL
CCCEEECCCCCCCCC		37.31-
172PhosphorylationQITFGRGSSQPNLST
CEEECCCCCCCCCCC		25.1630266825
173PhosphorylationITFGRGSSQPNLSTS
EEECCCCCCCCCCCC		53.1030266825
173 (in isoform 2)Phosphorylation-53.1024719451
178PhosphorylationGSSQPNLSTSHSEQE
CCCCCCCCCCCCHHH		34.2130266825
179PhosphorylationSSQPNLSTSHSEQEY
CCCCCCCCCCCHHHH		33.3630266825
180PhosphorylationSQPNLSTSHSEQEYG
CCCCCCCCCCHHHHH		22.9523927012
182PhosphorylationPNLSTSHSEQEYGKA
CCCCCCCCHHHHHCC		40.5225159151
186PhosphorylationTSHSEQEYGKAGGSP
CCCCHHHHHCCCCCC		24.5023927012
186 (in isoform 2)Phosphorylation-24.5025159151
188UbiquitinationHSEQEYGKAGGSPAS
CCHHHHHCCCCCCHH		42.8527667366
188 (in isoform 2)Ubiquitination-42.8521890473
192PhosphorylationEYGKAGGSPASYHGS
HHHCCCCCCHHHCCC		19.1726055452
192 (in isoform 2)Phosphorylation-19.1726846344
195PhosphorylationKAGGSPASYHGSPEA
CCCCCCHHHCCCCCH		22.5017081983
195 (in isoform 2)Phosphorylation-22.5026846344
196PhosphorylationAGGSPASYHGSPEAS
CCCCCHHHCCCCCHH		16.5921609022
196 (in isoform 2)Phosphorylation-16.5930266825
199PhosphorylationSPASYHGSPEASLCP
CCHHHCCCCCHHCCC		13.2727732954
199 (in isoform 2)Phosphorylation-13.2723927012
200 (in isoform 2)Phosphorylation-45.8525159151
201PhosphorylationASYHGSPEASLCPQH
HHHCCCCCHHCCCCC		53.2232142685
201 (in isoform 2)Phosphorylation-53.2223927012
203PhosphorylationYHGSPEASLCPQHRT
HCCCCCHHCCCCCCC		28.9227732954
223PhosphorylationQSEELQPLSQRHPFL
CCHHCCCHHHCCCCC		4.3732142685
226PhosphorylationELQPLSQRHPFLPHL
HCCCHHHCCCCCCCC		35.7532142685
237PhosphorylationLPHLGLASRPNGDWS
CCCCCCCCCCCCCCC		54.0027251275
249PhosphorylationDWSQPCLTCDRAARA
CCCCCCHHCCHHHHC		21.0527251275
257PhosphorylationCDRAARATSPRVSSE
CCHHHHCCCCCHHHH		33.4424300666
258PhosphorylationDRAARATSPRVSSEL
CHHHHCCCCCHHHHH		15.1024300666
259 (in isoform 2)Phosphorylation-36.0224719451
261UbiquitinationARATSPRVSSELEQA
HHCCCCCHHHHHHHH		9.3027667366
270 (in isoform 2)Phosphorylation-44.8324719451
272PhosphorylationLEQARPQTSGEEELQ
HHHHCCCCCCHHHHH		41.19-
273PhosphorylationEQARPQTSGEEELQL
HHHCCCCCCHHHHHH		38.67-
287PhosphorylationLQLALAMSREVAEQE
HHHHHHHHHHHHHHH		21.49-
312PhosphorylationLQMALEESRRDTVKI
HHHHHHHHHHCCCCC		24.2028555341
316PhosphorylationLEESRRDTVKIPKKK
HHHHHHCCCCCCCCC		23.1430266825
318UbiquitinationESRRDTVKIPKKKEH
HHHHCCCCCCCCCCC		56.2227667366
326 (in isoform 3)Ubiquitination-31.7821890473
327PhosphorylationPKKKEHGSLPQQTTL
CCCCCCCCCCCCCCH		38.4925849741
332PhosphorylationHGSLPQQTTLLDLMD
CCCCCCCCCHHHHHH		17.7328857561
333PhosphorylationGSLPQQTTLLDLMDA
CCCCCCCCHHHHHHH		22.4528857561
343PhosphorylationDLMDALPSSGPAAQK
HHHHHCCCCCCHHHC		49.1022468782
344PhosphorylationLMDALPSSGPAAQKA
HHHHCCCCCCHHHCC		47.0222468782
366UbiquitinationSTNQTNPWGGPAAPA
CCCCCCCCCCCCCCC		26.8432015554
366 (in isoform 2)Ubiquitination-26.8421890473
369PhosphorylationQTNPWGGPAAPASTS
CCCCCCCCCCCCCCC		22.7032142685
408PhosphorylationVQSVPKNSDPWAASQ
EECCCCCCCCCHHHC		51.6927251275
414PhosphorylationNSDPWAASQQPASSA
CCCCCHHHCCCCCHH		22.9228348404
419PhosphorylationAASQQPASSAGKRAS
HHHCCCCCHHCCCHH		27.6625159151
420PhosphorylationASQQPASSAGKRASD
HHCCCCCHHCCCHHH		43.0525159151
423AcetylationQPASSAGKRASDAWG
CCCCHHCCCHHHCCC		44.5026051181
423MethylationQPASSAGKRASDAWG
CCCCHHCCCHHHCCC		44.50-
423UbiquitinationQPASSAGKRASDAWG
CCCCHHCCCHHHCCC		44.5027667366
423 (in isoform 1)Ubiquitination-44.5021890473
426PhosphorylationSSAGKRASDAWGAVS
CHHCCCHHHCCCCCC		31.7125849741
429PhosphorylationGKRASDAWGAVSTTK
CCCHHHCCCCCCCCC		10.5632142685
451PhosphorylationFELFSNLNGTIKDDF
EEEHHCCCCCCCCCC		50.2232142685
454PhosphorylationFSNLNGTIKDDFSEF
HHCCCCCCCCCCHHH		4.9632142685
454 (in isoform 2)Phosphorylation-4.9624719451
466PhosphorylationSEFDNLRTSKKTAES
HHHHCHHCCCCHHHH		48.3328555341
470PhosphorylationNLRTSKKTAESVTSL
CHHCCCCHHHHHHCC		39.1228450419
473PhosphorylationTSKKTAESVTSLPSQ
CCCCHHHHHHCCCCC		28.3828450419
475PhosphorylationKKTAESVTSLPSQNN
CCHHHHHHCCCCCCC		33.5528450419
476PhosphorylationKTAESVTSLPSQNNG
CHHHHHHCCCCCCCC		35.8129496963
479PhosphorylationESVTSLPSQNNGTTS
HHHHCCCCCCCCCCC		51.3228450419
484PhosphorylationLPSQNNGTTSPDPFE
CCCCCCCCCCCCCCC		26.6528450419
485PhosphorylationPSQNNGTTSPDPFES
CCCCCCCCCCCCCCC		39.3928450419
486PhosphorylationSQNNGTTSPDPFESQ
CCCCCCCCCCCCCCC		27.4325159151
492PhosphorylationTSPDPFESQPLTVAS
CCCCCCCCCCCEEEC		37.1625850435
496PhosphorylationPFESQPLTVASSKPS
CCCCCCCEEECCCCC		22.2525002506
499PhosphorylationSQPLTVASSKPSSAR
CCCCEEECCCCCCCC		34.2626074081
500PhosphorylationQPLTVASSKPSSARK
CCCEEECCCCCCCCC		38.5626074081
503PhosphorylationTVASSKPSSARKTPE
EEECCCCCCCCCCCH		40.1326074081
504PhosphorylationVASSKPSSARKTPES
EECCCCCCCCCCCHH		40.3925159151
508PhosphorylationKPSSARKTPESFLGP
CCCCCCCCCHHHCCC		27.0829255136
511PhosphorylationSARKTPESFLGPNAA
CCCCCCHHHCCCCCE		27.2923663014
570PhosphorylationTLNQLRGSPVLGTST
CHHHHCCCCCCCCCC		12.8510470851
578O-linked_GlycosylationPVLGTSTSFGPGPGV
CCCCCCCCCCCCCCC		28.15OGP
622PhosphorylationAMMNMVGSVGIPPSA
HHHHCCCCCCCCHHH		13.03-
628PhosphorylationGSVGIPPSAAQATGT
CCCCCCHHHHHHCCC		30.77-
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EPN2_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 EPN2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBP1_HUMANRALBP1physical
20709745
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 EPN2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192 AND SER-195, ANDMASS SPECTROMETRY.

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