14335_ARATH - dbPTM
14335_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 14335_ARATH
UniProt AC P42645
Protein Name 14-3-3-like protein GF14 upsilon
Gene Name GRF5
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 268
Subcellular Localization Cytoplasm . Nucleus . Not associated with microtubules (PubMed:21558460). Translocates from the cytosol to the nucleus when phosphorylated (By similarity).
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. May be involved in cell cycle regulation by binding to soluble EDE1 and sequestering it in an inactive form during the early stages of mitosis..
Protein Sequence MSSDSSREENVYLAKLAEQAERYEEMVEFMEKVAKTVETEELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEDSRGNSDHVSIIKDYRGKIETELSKICDGILNLLEAHLIPAASLAESKVFYLKMKGDYHRYLAEFKTGAERKEAAESTLVAYKSAQDIALADLAPTHPIRLGLALNFSVFYYEILNSSDRACSLAKQAFDEAISELDTLGEESYKDSTLIMQLLRDNLTLWTSDLNDEAGDDIKEAPKEVQKVDEQAQPPPSQ
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
238PhosphoserineDNLTLWTSDLNDEAG
CCCEEEECCCCCCCC
28.6323572148
23111157
20466843
24243849
19880383
267PhosphoserineEQAQPPPSQ------
HHCCCCCCC------
55.0519376835

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 14335_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GCL1_ARATHGCL1physical
22737156
CDPK1_ARATHCPK1physical
22737156
EDE1_ARATHEDE1physical
21558460

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
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-267, AND MASSSPECTROMETRY.

TOP