DAR4_ARATH - dbPTM
DAR4_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DAR4_ARATH
UniProt AC Q9FKN7
Protein Name Protein DA1-related 4 {ECO:0000303|PubMed:18483219}
Gene Name DAR4 {ECO:0000303|PubMed:18483219}
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 1613
Subcellular Localization
Protein Description NB-LRR receptor-like protein that modulates growth, cell death and freezing tolerance in a temperature-dependent manner. May be involved in defense responses..
Protein Sequence MEPPAARVTPSIKADCSHSVNIICEETVLHSLVSHLSAALRREGISVFVDACGLQETKFFSIKQNQPLTDGARVLVVVISDEVEFYDPWFPKFLKVIQGWQNNGHVVVPVFYGVDSLTRVYGWANSWLEAEKLTSHQSKILSNNVLTDSELVEEIVRDVYGKLYPAERVGIYARLLEIEKLLYKQHRDIRSIGIWGMPGIGKTTLAKAVFNHMSTDYDASCFIENFDEAFHKEGLHRLLKERIGKILKDEFDIESSYIMRPTLHRDKLYDKRILVVLDDVRDSLAAESFLKRLDWFGSGSLIIITSVDKQVFAFCQINQIYTVQGLNVHEALQLFSQSVFGINEPEQNDRKLSMKVIDYVNGNPLALSIYGRELMGKKSEMETAFFELKHCPPLKIQDVLKNAYSALSDNEKNIVLDIAFFFKGETVNYVMQLLEESHYFPRLAIDVLVDKCVLTISENTVQMNNLIQDTCQEIFNGEIETCTRMWEPSRIRYLLEYDELEGSGETKAMPKSGLVAEHIESIFLDTSNVKFDVKHDAFKNMFNLKFLKIYNSCSKYISGLNFPKGLDSLPYELRLLHWENYPLQSLPQDFDFGHLVKLSMPYSQLHKLGTRVKDLVMLKRLILSHSLQLVECDILIYAQNIELIDLQGCTGLQRFPDTSQLQNLRVVNLSGCTEIKCFSGVPPNIEELHLQGTRIREIPIFNATHPPKVKLDRKKLWNLLENFSDVEHIDLECVTNLATVTSNNHVMGKLVCLNMKYCSNLRGLPDMVSLESLKVLYLSGCSELEKIMGFPRNLKKLYVGGTAIRELPQLPNSLEFLNAHGCKHLKSINLDFEQLPRHFIFSNCYRFSSQVIAEFVEKGLVASLARAKQEELIKAPEVIICIPMDTRQRSSFRLQAGRNAMTDLVPWMQKPISGFSMSVVVSFQDDYHNDVGLRIRCVGTWKTWNNQPDRIVERFFQCWAPTEAPKVVADHIFVLYDTKMHPSDSEENHISMWAHEVKFEFHTVSGENNPLGASCKVTECGVEVITAATGDTSVSGIIRESETITIIEKEDTIIDEEDTPLLSRKPEETNRSRSSSELQKLSSTSSKVRSKGNVFWKWLGCFPLQPKNLRSRSRRTTALEEALEEALKEREKLEDTRELQIALIESKKIKKIKQADERDQIKHADEREQRKHSKDHEEEEIESNEKEERRHSKDYVIEELVLKGKGKRKQLDDDKADEKEQIKHSKDHVEEEVNPPLSKCKDCKSAIEDGISINAYGSVWHPQCFCCLRCREPIAMNEISDLRGMYHKPCYKELRHPNCYVCEKKIPRTAEGLKYHEHPFWMETYCPSHDGDGTPKCCSCERLEHCGTQYVMLADFRWLCRECMDSAIMDSDECQPLHFEIREFFEGLHMKIEEEFPVYLVEKNALNKAEKEEKIDKQGDQCLMVVRGICLSEEQIVTSVSQGVRRMLNKQILDTVTESQRVVRKCEVTAILILYGLPRLLTGYILAHEMMHAYLRLNGYRNLNMVLEEGLCQVLGYMWLECQTYVFDTATIASSSSSSRTPLSTTTSKKVDPSDFEKRLVNFCKHQIETDESPFFGDGFRKVNKMMASNNHSLKDTLKEIISISKTPQYSKL
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
379PhosphorylationRELMGKKSEMETAFF
HHHCCCCCHHHHHHH
45.7428295753
383PhosphorylationGKKSEMETAFFELKH
CCCCHHHHHHHHHCC
27.7028295753
757PhosphorylationLVCLNMKYCSNLRGL
EHHHCCHHHHCCCCC
7.1319880383
1309PhosphorylationCEKKIPRTAEGLKYH
ECCCCCCCCCCCCCC
24.5719376835
1539PhosphorylationIASSSSSSRTPLSTT
HCCCCCCCCCCCCCC
41.9624894044

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 DAR4_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DAR4_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 DAR4_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of DAR4_ARATH !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DAR4_ARATH

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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 THR-1309, AND MASSSPECTROMETRY.

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