DRL36_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DRL36_ARATH
• UniProt AC: Q8VZC7
• Protein Name: Probable disease resistance protein At5g45510
• Gene Name: At5g45510
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 1222
• Protein Description: Probable disease resistance protein..
• Protein Sequence: MSDPLKMAAETEEIKPVPAAMGEKKDVVLCKKIVETLGGGGDQRVLLVGEAGIGKTRMAQMVDKEASKDVLCYQTLWLHLNRKFKVNDNYIKEKKFEDEWSLYENIASQLSLYSDFEETEVGERDEDEEEEKKVEDLLKDLKPKIEKYLLEKKEAVVKKLEDDKKKKEKEAAEKLEAEKKLVDPAAKKAKDHGNKNPTDAAKEKTTQVVAGGEDKAQTSSERKPYLLLILDDEGMTSEYEVMVHLGLEDFLKDHTPRKILITRRQETEEATKSGEHAEGEANDSQSGEKKEDTDGEDEIRSADKEEPESQARVKTEEKHEKVVPPTIDDLWGSTNTYGEITFQTTNESQDLLESFNLKEAEALFTSSMFFKDMPNFFFDPVPGTDEKLLNHMLKKSKSLPAAINVLAKSLEYTVKSKSYKLNKDEEERLLKEKIEMVLSAERGNPSDQESSSESPKKASGENPILLLAYKLFKTDGPLKDTILDCFWHSLDFFEHCGCVYYRDLITQWILEGYFDPVRSVEKAYQDGHSIFMELIDRGMLKIQENNVVVPEMAMRNVIDPRRGGHLGKSRLGFSRVYGGNKRKGIGKITQLDDMIKTVQAKKGDKITTILVSGDRLRRVTPKKFFKNLKELEVLGLFEPTVKPFVPSFSDQLKLLRVLIIRDCDLLKSIEELKALTKLNTLEVSGASSLSKISEKFFESFPELRSLHLSGLKIESSPPSISGLKELHCLIIKDCPLLQDLPNIQELVNLEVVDVSGASGLRTCFDNADGAKKNKSKNKNFYLLTKLQHLDFSGSQIERLPIFQDSAVAAKLHSLTRLLLRNCSKLRRLPSLKPLSGLQILDLSGTTSLVEMLEVCFEDKLELKTLNLSGTNLSELATTIEDLSSLNELLLRDCINLDAIPNIEKLENLEVIDVSGSAKLAKIEGSFEKMFYLRVVDLSGTQVETPELPADTKIHCLKRFTRADGKCFERDTWREIKEDIERDRSENASSSDAVVISQEITEKKPVEIREVESNAPRASDCTEKVDVNKERLLKVPIDRALYQKALTSLVDSKIPQEEVLEINETNKLDEEALASAEFVSFVDCTPERVKSIFEKAKLVKGCWLRMCFDIKDPFDGVDEENLKSLETLSITNLLSLETISFIAKLENLKNLSLDCCPKIKTIFPEMPASLPVLNLKHCENLEKVVVGVEVSTHTNLDLKVENCPKFGDYVMVDHSDVPPPHEC

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
73	Phosphorylation	ASKDVLCYQTLWLHL HHHHHHHHHHHHHHH	10.60	19880383
75	Phosphorylation	KDVLCYQTLWLHLNR HHHHHHHHHHHHHCC	8.07	23820729
206	Phosphorylation	DAAKEKTTQVVAGGE HHHHHHCCEEECCCC	30.36	19880383
273	Phosphorylation	ETEEATKSGEHAEGE HHHHHHHCCCCCCCC	45.09	23776212
284	Phosphorylation	AEGEANDSQSGEKKE CCCCCCCCCCCCCCC	26.50	23776212
286	Phosphorylation	GEANDSQSGEKKEDT CCCCCCCCCCCCCCC	53.52	23776212
293	Phosphorylation	SGEKKEDTDGEDEIR CCCCCCCCCCCHHHH	47.17	27532006
301	Phosphorylation	DGEDEIRSADKEEPE CCCHHHHHCCCCCCH	46.62	30407730
398	Phosphorylation	HMLKKSKSLPAAINV HHHHHCCCHHHHHHH	46.83	23111157
450	Phosphorylation	GNPSDQESSSESPKK CCCCCCCCCCCCCCC	33.27	30407730
451	Phosphorylation	NPSDQESSSESPKKA CCCCCCCCCCCCCCC	37.05	30407730
452	Phosphorylation	PSDQESSSESPKKAS CCCCCCCCCCCCCCC	51.91	23776212
454	Phosphorylation	DQESSSESPKKASGE CCCCCCCCCCCCCCC	43.92	23776212
524	Phosphorylation	VRSVEKAYQDGHSIF HHHHHHHHHCCCHHH	20.43	19880383
529	Phosphorylation	KAYQDGHSIFMELID HHHHCCCHHHHHHHH	24.05	19880383
574	Phosphorylation	GKSRLGFSRVYGGNK CCCCCCCCEECCCCC	21.02	19880383

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

Oops, there are no upstream regulatory protein records of DRL36_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DRL36_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 DRL36_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SUMO3_ARATH	SUMO3	physical	20855607

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 THR-293, AND MASSSPECTROMETRY.
PubMed: 19376835

"Site-specific phosphorylation profiling of Arabidopsis proteins bymass spectrometry and peptide chip analysis.";
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,Hirt H.;
J. Proteome Res. 7:2458-2470(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-293, AND MASSSPECTROMETRY.
PubMed: 18433157

"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-293, AND MASSSPECTROMETRY.
PubMed: 17586839