14339_ARATH - dbPTM
14339_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 14339_ARATH
UniProt AC Q96299
Protein Name 14-3-3-like protein GF14 mu
Gene Name GRF9
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 263
Subcellular Localization Nucleus . Cytoplasm . Translocates from the cytosol to the nucleus when phosphorylated.
Protein Description Is associated with a DNA binding complex that binds to the G box, a well-characterized cis-acting DNA regulatory element found in plant genes..
Protein Sequence MGSGKERDTFVYLAKLSEQAERYEEMVESMKSVAKLNVDLTVEERNLLSVGYKNVIGSRRASWRIFSSIEQKEAVKGNDVNVKRIKEYMEKVELELSNICIDIMSVLDEHLIPSASEGESTVFFNKMKGDYYRYLAEFKSGNERKEAADQSLKAYEIATTAAEAKLPPTHPIRLGLALNFSVFYYEIMNAPERACHLAKQAFDEAISELDTLNEESYKDSTLIMQLLRDNLTLWTSDISEEGGDDAHKTNGSAKPGAGGDDAE
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
232PhosphothreonineQLLRDNLTLWTSDIS
HHHHCCCEEEECCCH
26.8919376835
19880383
235PhosphothreonineRDNLTLWTSDISEEG
HCCCEEEECCCHHHC
21.4523572148
20466843
19376835
24243849
19880383
236PhosphoserineDNLTLWTSDISEEGG
CCCEEEECCCHHHCC
22.7423572148
23111157
20466843
19376835
24243849
19880383
21768351
239PhosphoserineTLWTSDISEEGGDDA
EEEECCCHHHCCCCH
34.2919245862
19376835

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 14339_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CNG13_ARATHCNGC13physical
22737156
PUP21_ARATHAT4G18220physical
22737156
FB316_ARATHAT1G61340physical
22920997

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-239, AND MASSSPECTROMETRY.
"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-239, AND MASSSPECTROMETRY.

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