ELF4_ARATH - dbPTM
ELF4_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ELF4_ARATH
UniProt AC O04211
Protein Name Protein EARLY FLOWERING 4
Gene Name ELF4
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 111
Subcellular Localization Nucleus . Diffuse distribution. Targeted to nuclear bodies after interaction with ELF3 (PubMed:22327739).
Protein Description Component of the central CCA1/LHY-TOC1 feedback loop in the circadian clock that promotes clock accuracy and is required for sustained rhythms in the absence of daily light/dark cycles. Part of a corepressor complex consisting of ELF4, ELF3, and LUX involved in the transcriptional regulation of APRR9. Increases ELF3 nuclear distribution and localization in nuclear bodies. Required for responsiveness to continuous red, by regulating phytochrome B (phyB) signaling (including during seedling de-etiolation) and gene expression. Mediates both entrainment to an environmental cycle and circadian rhythm sustainability under constant conditions. Controls flowering time. Necessary for light-induced expression of both CCA1 and LHY..
Protein Sequence MKRNGETKRRRNVAEEAEQGEDPAMWENLDRNFRQVQSVLDRNRSLIQQVNDNHQSRMADNMSKNVALIQELNGNISKVVNMYSDLNTSFSSGFHGGKNGHDGGGAAGTRA
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
25SulfoxidationEQGEDPAMWENLDRN
HCCCCHHHHHHHHHH
5.8523289948
45PhosphorylationSVLDRNRSLIQQVND
HHHHHCHHHHHHHHH
33.1130291188
56PhosphorylationQVNDNHQSRMADNMS
HHHHHHHHHHHHHHH
19.2422438062

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 ELF4_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ELF4_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 ELF4_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TIC_ARATHTICgenetic
17496120
HUA2_ARATHHUA2genetic
15659097
ELF3_ARATHELF3physical
21753751
PCL1_ARATHPCL1physical
21753751
ELF3_ARATHELF3physical
26545401
PCL1_ARATHPCL1physical
26545401
LWD1_ARATHATAN11physical
26545401
TIC_ARATHTICphysical
26545401
APRR1_ARATHTOC1physical
26545401
PHYB_ARATHPHYBphysical
26545401
PHYC_ARATHPHYCphysical
26545401
PHYE_ARATHPHYEphysical
26545401
PHYD_ARATHPHYDphysical
26545401
PHYA_ARATHPHYAphysical
26545401
COP1_ARATHCOP1physical
26545401
SPA1_ARATHSPA1physical
26545401
FB348_ARATHAT2G16365physical
26545401
14336_ARATHGRF6physical
26545401

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ELF4_ARATH

loading...

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-45, AND MASSSPECTROMETRY.

TOP