PME7_ARATH - dbPTM
PME7_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PME7_ARATH
UniProt AC Q9SRX4
Protein Name Probable pectinesterase/pectinesterase inhibitor 7
Gene Name PME7
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 579
Subcellular Localization Secreted, cell wall.
Protein Description Acts in the modification of cell walls via demethylesterification of cell wall pectin..
Protein Sequence MESPIFILITLSFFLQSVLASSQTLSNSSTICKTTPDPKYCKSVFPHSQGNVQQYGCFSIRKSLSQSRKFIRTVDRYIKRNAHLSQPAVIRALQDCRFLAGLTMDYLLTSFETVNDTSAKTSFKPLSFPKADDIQTLLSAALTNEQTCLEGLTTAASYSATWTVRTGVALPLVNDTKLLGVSLALFTKGWVPKKKKRAGFAWAQPRSGSSTHTKPFRLFRNGALPLKMTEKTKAVYESLSRRKLADGDSNGDGDDGSMVLISDIVTVSQDGTGNFTNITAAVAAAPNNTDGSAGFFLIYVTAGIYEEYISIAKNKRYMMMIGDGINQTVVTGNRSVVDGWTTFNSATFAVTAPNFVAVNITFRNTAGPEKHQAVALRSGADFSIFYSCSFEAYQDTLYTHSLRQFYRECDVYGTVDFIFGNAAVVFQNCNLYPRKPMPNQFNAITAQGRSDPNQNTGTSIQNCTIKPADDLVSSNYTVKTYLGRPWKEYSRTVYMQSYIDGFVEPVGWREWNGDFALSTLYYAEYNNTGPGSNTTNRVTWPGYHVINSTDAANFTVTGLFIEADWIWKTGVPYTSGLIS
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
27N-linked_GlycosylationASSQTLSNSSTICKT
HCCCCCCCCCCCCCC
42.99-
115N-linked_GlycosylationLTSFETVNDTSAKTS
HHCEEECCCCCCCCC
55.02-
174N-linked_GlycosylationGVALPLVNDTKLLGV
CCEECCCCCCCCCCE
59.94-
274N-linked_GlycosylationVSQDGTGNFTNITAA
EECCCCCCCCEEEEE
40.17-
277N-linked_GlycosylationDGTGNFTNITAAVAA
CCCCCCCEEEEEEEE
26.02-
287N-linked_GlycosylationAAVAAAPNNTDGSAG
EEEEECCCCCCCCCC
60.34-
326N-linked_GlycosylationMMIGDGINQTVVTGN
EEECCCCCCEEEECC
36.68-
333N-linked_GlycosylationNQTVVTGNRSVVDGW
CCEEEECCCCEEECC
24.56-
359N-linked_GlycosylationAPNFVAVNITFRNTA
CCCEEEEEEEEECCC
20.18-
462N-linked_GlycosylationNTGTSIQNCTIKPAD
CCCCCEECCEECCHH
24.19-
475N-linked_GlycosylationADDLVSSNYTVKTYL
HHHHHHCCCEEEEEC
29.05-
526N-linked_GlycosylationTLYYAEYNNTGPGSN
EEEEEECCCCCCCCC
30.96-
533N-linked_GlycosylationNNTGPGSNTTNRVTW
CCCCCCCCCCCCEEC
57.76-
547N-linked_GlycosylationWPGYHVINSTDAANF
CCEEEEECCCCCCCC
37.46-
553N-linked_GlycosylationINSTDAANFTVTGLF
ECCCCCCCCEEEEEE
34.54-

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 PME7_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PME7_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 PME7_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PME3_ARATHPME3physical
26183897

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PME7_ARATH

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Related Literatures of Post-Translational Modification

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