EPN2_ARATH - dbPTM
EPN2_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EPN2_ARATH
UniProt AC Q67YI9
Protein Name Clathrin interactor EPSIN 2
Gene Name EPSIN2
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 895
Subcellular Localization Golgi apparatus . Cytoplasmic vesicle, clathrin-coated vesicle . Localizes also to a novel cellular compartment, the 'delta compartment', characterized by colocalization of EPSIN2 and DELTA-ADR.
Protein Description May have a role in transport via clathrin-coated vesicles from the trans-Golgi network to endosomes. Stimulates clathrin assembly (By similarity). Binds to membranes enriched in phosphatidylinositol 3-phosphate (PtdIns(3)P). Plays an important role in protein trafficking..
Protein Sequence MKKVFGQTVRDLKREVNKKVLKVPGVEQKVLDATSNEPWGPHGSLLADLAQASRNYHEYQLIMVVIWKRLSDTGKNWRHVYKALTVLEYMVGHGSERVIDEIRERAYQISTLSDFQYIDSGGRDQGSNVRKKSQSLVALVNDKERIAEVRQKAAANRDKYRSSAPGGMYKPSGGYGDKYDYGSRDEERSSYGREREYGYRDDDRNSRDGDRHSRDSEDRYGRDGNRDDDYRGRSRSVDNYGSRGRSSEREREDDGHSSSRGSGARADDNSQDGRGGLQRKFSEQNIGAPPSYEEAVSDSRSPVYSERDGGETPQVTAPGAASPPPPQVAAPEAASPPTGTNTANTTATFVNESPSQKVETFDEFDPRSAFSAGPPAYASTDGVTAPPTVTSMSAPTTSNSVEMDLLGSLADVFSSNALAIVPADSIYVETNGQANAGPAPSFSTSQPSTQSFDDPFGDSPFKAFTSTDTDSTPQQNFGASFQPPPPAFTSEVSHPDTAHNFGFGDSFSAVANPDPASQNVQPPSNSPGFPQEQFATSQSGIDILAGILPPSGPPVQSGPSIPTSQFPPSGNNMYEGFHSQPPVSTAPNLPGQTPFGQAVQPYNMVPHSQNMTGAMPFNSGGFMHQPGSQTPYSTPSGPAGQFMAHQGHGMPPSHGPQRTQSGPVTLQGNNNVMGDMFSQATPNSLTSSSSHPDLTPLTGAIEIVPPPQKKFEPKSSVWADTLSRGLVNFNISGSKTNPLADIGVDFEAINRREKRLEKQTNTPATSTINMGKAMGSGTGLGRSGATAMRPPPNPMTGSGMPMGGGMGVGSYGGMNQNQPMGMGMGAGMNQNQPMGMGMGPGMNMNMNMGGYGQGYPMQPQNPGMVPSPNMPGNNYNPMMGQGGYNPQQSYGGGYR
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
162PhosphorylationANRDKYRSSAPGGMY
HCHHHHHHCCCCCCC		27.9725561503
163PhosphorylationNRDKYRSSAPGGMYK
CHHHHHHCCCCCCCC		29.5025561503
189PhosphorylationGSRDEERSSYGRERE
CCCCHHHHCCCCCCC		31.0625561503
190PhosphorylationSRDEERSSYGREREY
CCCHHHHCCCCCCCC		37.5229654922
191PhosphorylationRDEERSSYGREREYG
CCHHHHCCCCCCCCC		22.8125561503
234PhosphorylationDDDYRGRSRSVDNYG
CCCCCCCCCCCCCCC		31.5623776212
236PhosphorylationDYRGRSRSVDNYGSR
CCCCCCCCCCCCCCC		34.7623776212
240PhosphorylationRSRSVDNYGSRGRSS
CCCCCCCCCCCCCCC		16.4123776212
242PhosphorylationRSVDNYGSRGRSSER
CCCCCCCCCCCCCCC		22.6223776212
257PhosphorylationEREDDGHSSSRGSGA
CCCCCCCCCCCCCCC		35.2225561503
258PhosphorylationREDDGHSSSRGSGAR
CCCCCCCCCCCCCCC		20.5525561503
259PhosphorylationEDDGHSSSRGSGARA
CCCCCCCCCCCCCCC		43.6125561503
262PhosphorylationGHSSSRGSGARADDN
CCCCCCCCCCCCCCC		28.3325561503
270PhosphorylationGARADDNSQDGRGGL
CCCCCCCCCCCCCCH		36.3225368622
282PhosphorylationGGLQRKFSEQNIGAP
CCHHHHHHHCCCCCC		41.1130291188
291PhosphorylationQNIGAPPSYEEAVSD
CCCCCCCCHHHHHCC		44.0823776212
292PhosphorylationNIGAPPSYEEAVSDS
CCCCCCCHHHHHCCC		24.4623776212
297PhosphorylationPSYEEAVSDSRSPVY
CCHHHHHCCCCCCCC		36.6023776212
299PhosphorylationYEEAVSDSRSPVYSE
HHHHHCCCCCCCCCC		27.4423776212
301PhosphorylationEAVSDSRSPVYSERD
HHHCCCCCCCCCCCC		23.7524601666
304PhosphorylationSDSRSPVYSERDGGE
CCCCCCCCCCCCCCC		14.2723776212
305PhosphorylationDSRSPVYSERDGGET
CCCCCCCCCCCCCCC		26.7923776212
312PhosphorylationSERDGGETPQVTAPG
CCCCCCCCCCCCCCC		23.4623776212
316PhosphorylationGGETPQVTAPGAASP
CCCCCCCCCCCCCCC		23.1423776212
322PhosphorylationVTAPGAASPPPPQVA
CCCCCCCCCCCCCCC		37.0923776212
335PhosphorylationVAAPEAASPPTGTNT
CCCCCCCCCCCCCCC		38.1623776212
338PhosphorylationPEAASPPTGTNTANT
CCCCCCCCCCCCCCC		61.0823776212
340PhosphorylationAASPPTGTNTANTTA
CCCCCCCCCCCCCEE		31.6923776212
342PhosphorylationSPPTGTNTANTTATF
CCCCCCCCCCCEEEE		22.5623776212
345PhosphorylationTGTNTANTTATFVNE
CCCCCCCCEEEEECC		18.4923776212
346PhosphorylationGTNTANTTATFVNES
CCCCCCCEEEEECCC		24.4123776212
348PhosphorylationNTANTTATFVNESPS
CCCCCEEEEECCCHH		26.4823776212
353PhosphorylationTATFVNESPSQKVET
EEEEECCCHHCCEEE		25.3423776212
355PhosphorylationTFVNESPSQKVETFD
EEECCCHHCCEEECC		52.4923776212
661PhosphorylationHGPQRTQSGPVTLQG
CCCCCCCCCCEEECC		44.4429654922
736PhosphorylationFNISGSKTNPLADIG
EECCCCCCCCHHHHC		43.7119880383
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_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EPN2_ARATH !!
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_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CLAH2_ARATHAT3G08530physical
17277094
AP2A1_ARATHalpha-ADRphysical
17277094
AP3D_ARATHdelta-ADRphysical
17277094
VTI12_ARATHVTI1Bphysical
17277094
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EPN2_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270 AND SER-282, ANDMASS SPECTROMETRY.
"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana.";
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.;
J. Proteomics 72:439-451(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND MASSSPECTROMETRY.

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