REMO_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: REMO_ARATH
• UniProt AC: O80837
• Protein Name: Remorin
• Gene Name: DBP
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 190
• Protein Description: Exhibits a non sequence-specific DNA-binding activity..
• Protein Sequence: MAEEQKTSKVDVESPAVLAPAKEPTPAPVEVADEKIHNPPPVESKALAVVEKPIEEHTPKKASSGSADRDVILADLEKEKKTSFIKAWEESEKSKAENRAQKKISDVHAWENSKKAAVEAQLRKIEEKLEKKKAQYGEKMKNKVAAIHKLAEEKRAMVEAKKGEELLKAEEMGAKYRATGVVPKATCGCF

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
7	Phosphorylation	-MAEEQKTSKVDVES -CCCCCCCCCCCCCC	33.21	23111157
14	Phosphorylation	TSKVDVESPAVLAPA CCCCCCCCCCEECCC	20.29	30291188
58	Phosphorylation	EKPIEEHTPKKASSG ECCHHHCCCCCCCCC	39.83	30291188
63	Phosphorylation	EHTPKKASSGSADRD HCCCCCCCCCCCCCC	44.08	15308754
64	Phosphorylation	HTPKKASSGSADRDV CCCCCCCCCCCCCCE	41.44	19880383
66	Phosphorylation	PKKASSGSADRDVIL CCCCCCCCCCCCEEH	29.01	30291188

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of REMO_ARATH !!

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of REMO_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ARR4_ARATH	ARR4	physical	9771897
IMPA3_ARATH	MOS6	physical	21798944
IMPA1_ARATH	IMPA-1	physical	23027878
IMPA3_ARATH	MOS6	physical	23027878
REMO_ARATH	AT2G45820	physical	23027878
REMO_ARATH	AT2G45820	physical	15604702

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-14 AND THR-58, AND MASSSPECTROMETRY.
PubMed: 19376835

"Quantitative phosphoproteomics of early elicitor signaling inArabidopsis.";
Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M.,Menke F.L.H.;
Mol. Cell. Proteomics 6:1198-1214(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND THR-58, AND MASSSPECTROMETRY.
PubMed: 17317660

"Phosphoproteomics of the Arabidopsis plasma membrane and a newphosphorylation site database.";
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
Plant Cell 16:2394-2405(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASSSPECTROMETRY.
PubMed: 15308754

"Large-scale analysis of in vivo phosphorylated membrane proteins byimmobilized metal ion affinity chromatography and mass spectrometry.";
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
Mol. Cell. Proteomics 2:1234-1243(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND MASSSPECTROMETRY.
PubMed: 14506206

"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 THR-58, AND MASSSPECTROMETRY.
PubMed: 17586839