dbPTM

RPB4_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RPB4_DROME
UniProt AC	Q9VEA5
Protein Name	DNA-directed RNA polymerase II subunit Rpb4 {ECO:0000312\|FlyBase:FBgn0263757}
Gene Name	Rpb4 {ECO:0000312\|FlyBase:FBgn0263757}
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	139
Subcellular Localization	Nucleus .
Protein Description	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Associates with POLR2G..
Protein Sequence	MSFMNPVDMVDEDAADLQFPKEFENAETLLISEVHMLLDHRKRQNESADEEQEFSEVFMKTYAYTDSFRKFKNKETIMSARSLLMQKKLHKFELAALGNLCPEAPEEAKALIPSLEGRFEDEELRQILDDIGTKRSLQY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference	Orthologous Protein Cluster
Oops, there are no PTM records of RPB4_DROME !!

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 RPB4_DROME !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RPB4_DROME !!

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 RPB4_DROME !!

Protein-Protein Interaction

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

Drug and Disease Associations

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

Regulatory Network of RPB4_DROME

Related Literatures of Post-Translational Modification