WRKY1_ARATH - dbPTM
WRKY1_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WRKY1_ARATH
UniProt AC Q9SI37
Protein Name WRKY transcription factor 1
Gene Name WRKY1
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 487
Subcellular Localization Nucleus .
Protein Description Transcription factor. Binds to a 5'-CGTTGACCGAG-3' consensus core sequence which contains a W box, a frequently occurring elicitor-responsive cis-acting element..
Protein Sequence MAEVGKVLASDMELDHSNETKAVDDVVATTDKAEVIPVAVTRTETVVESLESTDCKELEKLVPHTVASQSEVDVASPVSEKAPKVSESSGALSLQSGSEGNSPFIREKVMEDGYNWRKYGQKLVKGNEFVRSYYRCTHPNCKAKKQLERSAGGQVVDTVYFGEHDHPKPLAGAVPINQDKRSDVFTAVSKGEQRIDIVSLIYKLCIVSYDIMFVEKTSGSSVQTLRQTEPPKIHGGLHVSVIPPADDVKTDISQSSRITGDNTHKDYNSPTAKRRKKGGNIELSPVERSTNDSRIVVHTQTLFDIVNDGYRWRKYGQKSVKGSPYPRSYYRCSSPGCPVKKHVERSSHDTKLLITTYEGKHDHDMPPGRVVTHNNMLDSEVDDKEGDANKTPQSSTLQSITKDQHVEDHLRKKTKTNGFEKSLDQGPVLDEKLKEEIKERSDANKDHAANHAKPEAKSDDKTTVCQEKAVGTLESEEQKPKTEPAQS
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
10PhosphorylationEVGKVLASDMELDHS
CHHHHHHHCCCCCCC		33.0719376835
17PhosphorylationSDMELDHSNETKAVD
HCCCCCCCCCCCCCC		35.7130291188
20PhosphorylationELDHSNETKAVDDVV
CCCCCCCCCCCCCEE		28.6719376835
65PhosphorylationLEKLVPHTVASQSEV
HHHHCCCCCCCCCCC		16.2323776212
68PhosphorylationLVPHTVASQSEVDVA
HCCCCCCCCCCCEEC		29.8723776212
70PhosphorylationPHTVASQSEVDVASP
CCCCCCCCCCEECCC		36.7723776212
76PhosphorylationQSEVDVASPVSEKAP
CCCCEECCCCCCCCC		26.1930291188
79PhosphorylationVDVASPVSEKAPKVS
CEECCCCCCCCCCCC		36.4424601666
88PhosphorylationKAPKVSESSGALSLQ
CCCCCCCCCCCEECC		26.9430407730
89PhosphorylationAPKVSESSGALSLQS
CCCCCCCCCCEECCC		24.8430407730
93PhosphorylationSESSGALSLQSGSEG
CCCCCCEECCCCCCC		24.6730407730
96PhosphorylationSGALSLQSGSEGNSP
CCCEECCCCCCCCCC		49.9730589143
98PhosphorylationALSLQSGSEGNSPFI
CEECCCCCCCCCCCH		47.8030407730
102PhosphorylationQSGSEGNSPFIREKV
CCCCCCCCCCHHHHH		31.8530407730
186 (in isoform 2)Phosphorylation-26.4625561503
189 (in isoform 2)Phosphorylation-32.2625561503
267PhosphorylationGDNTHKDYNSPTAKR
CCCCCCCCCCCCHHC		23.4925561503
269PhosphorylationNTHKDYNSPTAKRRK
CCCCCCCCCCHHCCC		19.8727545962
271PhosphorylationHKDYNSPTAKRRKKG
CCCCCCCCHHCCCCC		44.6325561503
284PhosphorylationKGGNIELSPVERSTN
CCCCCCCCCCCCCCC		17.7030291188
394PhosphorylationDANKTPQSSTLQSIT
CCCCCCCHHHHHHHH		26.8828295753
395PhosphorylationANKTPQSSTLQSITK
CCCCCCHHHHHHHHC		28.0828295753
396PhosphorylationNKTPQSSTLQSITKD
CCCCCHHHHHHHHCC		33.7828295753
399PhosphorylationPQSSTLQSITKDQHV
CCHHHHHHHHCCHHH		35.0228295753
472PhosphorylationCQEKAVGTLESEEQK
EEHHHHCCCCCCCCC		22.2825561503
475PhosphorylationKAVGTLESEEQKPKT
HHHCCCCCCCCCCCC		49.9325561503
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 WRKY1_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WRKY1_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 WRKY1_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of WRKY1_ARATH !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of WRKY1_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 SER-76, AND MASSSPECTROMETRY.

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