ERF3_SCHPO - dbPTM
ERF3_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERF3_SCHPO
UniProt AC O74718
Protein Name Eukaryotic peptide chain release factor GTP-binding subunit
Gene Name sup35
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 662
Subcellular Localization Cytoplasm .
Protein Description Involved in translation termination. Stimulates the activity of ERF1. Binds guanine nucleotides..
Protein Sequence MASNQPNNGEQDEQLAKQTSKLSMSAKAPTFTPKAAPFIPSFQRPGFVPVNNIAGGYPYAQYTGQGQNSNSPHPTKSYQQYYQKPTGNTVDEDKSRVPDFSKKKSFVPPKPAIPKGKVLSLGGNTSAPKSTKPISISLGGTKAPTTTKPAAPAAQSKTETPAPKVTSESTKKETAAPPPQETPTKSADAELAKTPSAPAAALKKAAEAAEPATVTEDATDLQNEVDQELLKDMYGKEHVNIVFIGHVDAGKSTLGGNILFLTGMVDKRTMEKIEREAKEAGKESWYLSWALDSTSEEREKGKTVEVGRAYFETEHRRFSLLDAPGHKGYVTNMINGASQADIGVLVISARRGEFEAGFERGGQTREHAVLARTQGINHLVVVINKMDEPSVQWSEERYKECVDKLSMFLRRVAGYNSKTDVKYMPVSAYTGQNVKDRVDSSVCPWYQGPSLLEYLDSMTHLERKVNAPFIMPIASKYKDLGTILEGKIEAGSIKKNSNVLVMPINQTLEVTAIYDEADEEISSSICGDQVRLRVRGDDSDVQTGYVLTSTKNPVHATTRFIAQIAILELPSILTTGYSCVMHIHTAVEEVSFAKLLHKLDKTNRKSKKPPMFATKGMKIIAELETQTPVCMERFEDYQYMGRFTLRDQGTTVAVGKVVKILD
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
59PhosphorylationNIAGGYPYAQYTGQG
CCCCCCCCCEECCCC
9.6127738172
71PhosphorylationGQGQNSNSPHPTKSY
CCCCCCCCCCCCCCH
25.1421712547
77PhosphorylationNSPHPTKSYQQYYQK
CCCCCCCCHHHHHCC
30.5624763107
120PhosphorylationIPKGKVLSLGGNTSA
CCCCCEEEECCCCCC
28.1428889911
130PhosphorylationGNTSAPKSTKPISIS
CCCCCCCCCCCEEEE
40.3725720772
174PhosphorylationSESTKKETAAPPPQE
CCCCCCCCCCCCCCC
36.6829996109
182PhosphorylationAAPPPQETPTKSADA
CCCCCCCCCCCCCCH
30.8928889911
184PhosphorylationPPPQETPTKSADAEL
CCCCCCCCCCCCHHH
45.0825720772
194PhosphorylationADAELAKTPSAPAAA
CCHHHHCCCCCHHHH
19.5021712547
196PhosphorylationAELAKTPSAPAAALK
HHHHCCCCCHHHHHH
52.7124763107
319PhosphorylationETEHRRFSLLDAPGH
ECCCCCEEEECCCCC
26.6425720772
539PhosphorylationLRVRGDDSDVQTGYV
EEEECCCCCCCCCEE
44.4128889911

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 ERF3_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERF3_SCHPO !!

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 ERF3_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ERF1_SCHPOsup45physical
9701287
DOM34_SCHPOdom34physical
9701287
DOM34_SCHPOdom34physical
10376874
ERF3_SCHPOsup35physical
26771498

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ERF3_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-182 AND SER-539, ANDMASS SPECTROMETRY.

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