APRR5_ARATH - dbPTM
APRR5_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID APRR5_ARATH
UniProt AC Q6LA42
Protein Name Two-component response regulator-like APRR5
Gene Name APRR5
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 558
Subcellular Localization Nucleus .
Protein Description Transcriptional repressor of CCA1 and LHY, thereby controlling photoperiodic flowering response. Involved in the positive and negative feedback loops of the circadian clock. Expression of several members of the ARR-like family is controlled by circadian rhythm. Proteolytic substrate of the E3 ubiquitin ligase SCF(ADO1) complex. APRR9, APRR7, and APRR5 coordinately act on the upstream region of the target genes to repress their expression from noon until midnight. The particular coordinated sequential expression of APRR9, APRR7, APRR5, APRR3 and APPR1 result to circadian waves that may be at the basis of the endogenous circadian clock. Negative regulator of shade avoidance response. Involved in the inhibition of leaf expansion in shade avoidance response..
Protein Sequence MTSSEEVVEVTVVKAPEAGGGKLSRRKIRKKDAGVDGLVKWERFLPKIALRVLLVEADDSTRQIIAALLRKCSYRVAAVPDGLKAWEMLKGKPESVDLILTEVDLPSISGYALLTLIMEHDICKNIPVIMMSTQDSVNTVYKCMLKGAADYLVKPLRRNELRNLWQHVWRRQTSLAPDSFPWNESVGQQKAEGASANNSNGKRDDHVVSGNGGDAQSSCTRPEMEGESADVEVSARDAVQMECAKSQFNETRLLANELQSKQAEAIDFMGASFRRTGRRNREESVAQYESRIELDLSLRRPNASENQSSGDRPSLHPSSASAFTRYVHRPLQTQCSASPVVTDQRKNVAASQDDNIVLMNQYNTSEPPPNAPRRNDTSFYTGADSPGPPFSNQLNSWPGQSSYPTPTPINNIQFRDPNTAYTSAMAPASLSPSPSSVSPHEYSSMFHPFNSKPEGLQDRDCSMDVDERRYVSSATEHSAIGNHIDQLIEKKNEDGYSLSVGKIQQSLQREAALTKFRMKRKDRCYEKKVRYESRKKLAEQRPRIKGQFVRQVQSTQAP
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
185PhosphorylationDSFPWNESVGQQKAE
CCCCCCCCCCCHHHH
28.4730291188
195PhosphorylationQQKAEGASANNSNGK
CHHHHCCCCCCCCCC
42.2425561503
199PhosphorylationEGASANNSNGKRDDH
HCCCCCCCCCCCCCC
46.9325561503
499PhosphorylationNEDGYSLSVGKIQQS
CCCCCCCCHHHHHHH
23.9217586839

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 APRR5_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of APRR5_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 APRR5_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ADO1_ARATHZTLphysical
15310821
ADO2_ARATHLKP2physical
15310821
ADO3_ARATHFKF1physical
15310821
WNK1_ARATHWNK1physical
12506983
WNK4_ARATHWNK4physical
12506983
WNK1_ARATHWNK1physical
12091722
APRR9_ARATHPRR9genetic
15767265
APRR7_ARATHPRR7genetic
15767265
APRR1_ARATHTOC1genetic
18178585
APRR7_ARATHPRR7genetic
17519251
LHY_ARATHLHYgenetic
17519251
CCA1_ARATHCCA1genetic
17519251
APRR7_ARATHPRR7genetic
17504813
LHY_ARATHLHYgenetic
17504813
CCA1_ARATHCCA1genetic
17504813
ADO1_ARATHZTLphysical
17693530
APRR7_ARATHPRR7genetic
15695441
APRR9_ARATHPRR9genetic
12955513
ADO1_ARATHZTLphysical
18562312
APRR1_ARATHTOC1physical
20407420
TPL_ARATHTPLphysical
23267111

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of APRR5_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Temporal analysis of sucrose-induced phosphorylation changes inplasma membrane proteins of Arabidopsis.";
Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B.,Schulze W.X.;
Mol. Cell. Proteomics 6:1711-1726(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, AND MASSSPECTROMETRY.

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