BH080_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BH080_ARATH
• UniProt AC: Q9C8P8
• Protein Name: Transcription factor bHLH80
• Gene Name: BHLH80
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 259
• Subcellular Localization: Nucleus .
• Protein Sequence: MQSTHISGGSSGGGGGGGGEVSRSGLSRIRSAPATWIETLLEEDEEEGLKPNLCLTELLTGNNNSGGVITSRDDSFEFLSSVEQGLYNHHQGGGFHRQNSSPADFLSGSGSGTDGYFSNFGIPANYDYLSTNVDISPTKRSRDMETQFSSQLKEEQMSGGISGMMDMNMDKIFEDSVPCRVRAKRGCATHPRSIAERVRRTRISDRIRRLQELVPNMDKQTNTADMLEEAVEYVKALQSQIQELTEQQKRCKCKPKEEQ

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
75	Phosphorylation	VITSRDDSFEFLSSV EEECCCCCCHHHHHH	30.85	27545962
80	Phosphorylation	DDSFEFLSSVEQGLY CCCCHHHHHHHHHCC	37.34	27545962
81	Phosphorylation	DSFEFLSSVEQGLYN CCCHHHHHHHHHCCC	31.64	27545962
87	Phosphorylation	SSVEQGLYNHHQGGG HHHHHHCCCCCCCCC	21.19	27545962
136	Phosphorylation	LSTNVDISPTKRSRD HHCCCCCCCCCCCHH	23.27	19376835
149	Phosphorylation	RDMETQFSSQLKEEQ HHHHHHHHHHHHHHH	13.83	19880383

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

Oops, there are no upstream regulatory protein records of BH080_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BH080_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 BH080_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SUMO3_ARATH	SUMO3	physical	20855607
SUMO1_ARATH	SUMO1	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 SER-136, AND MASSSPECTROMETRY.
PubMed: 19376835