ELOA1_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ELOA1_DROME
• UniProt AC: Q9VCP0
• Protein Name: Transcription elongation factor B polypeptide 3
• Gene Name: EloA
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 643
• Subcellular Localization: Nucleus .
• Protein Description: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex). May play an important role in metamorphosis..
• Protein Sequence: MASTSNLLDVVRHYQRSIEKHGEDEQRLLHCITKLFNLPIKFEHLQETGIGKTVNALRKISGEVGVAAKTLVTKWKAMVAKEDPSIASTPTAIHNEEDSGKTKSSDEDPDQENKGGNSSSGEDLNTSKHKSKHAKSTKHERSSSSRSHSKSRSDSDKKHKSSRHDKSKDRDKDREGQKEAKEHKEKKSNGEHKSKDSSKSSSSHKSSKSESHKSEHTKSKHEKDKTSHSELKEVKDKSSKHKSSSSKSSKRSHSPPRHEEESQKAKIPKVKSKSEEDSADGFDSSMGANFDDVLGLLNIPISSKKSSSNSKSKFVAKPTAAPSSSALSAPTTAGSSKEALSTSSRPTSKKPELLASTAKLEPLDPNIALELPTISNNYKPMPLNQTVMDVVFNQGGSHKAQASRYFNESEALAQGISSKTMRTKIYSGVRTGQILQVPSLFDLCTRVLQKNIDALEYTGGVPFEVLRPVLERATPQQLLNFEEYNPYLMDDSDVLWQQHVQRHCRSQRREEMETWREMFLRCQEEKDRKLSILAESIKASQKISEAPVRKTQLAFVDSMVKPPRSVQRKQEQYGTKGKLIATPAARVAALSSVTPNAAKVGDARLRVLAAARDTAQVGAGPARSKKAPLMAKTLQFMRGRLKR

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
102	Phosphorylation	NEEDSGKTKSSDEDP CCCCCCCCCCCCCCC	39.42	19429919
104	Phosphorylation	EDSGKTKSSDEDPDQ CCCCCCCCCCCCCCC	48.53	19429919
105	Phosphorylation	DSGKTKSSDEDPDQE CCCCCCCCCCCCCCC	46.72	19429919
118	Phosphorylation	QENKGGNSSSGEDLN CCCCCCCCCCCCCCC	29.20	22817900
119	Phosphorylation	ENKGGNSSSGEDLNT CCCCCCCCCCCCCCH	46.49	22817900
120	Phosphorylation	NKGGNSSSGEDLNTS CCCCCCCCCCCCCHH	46.12	10731132
254	Phosphorylation	KSSKRSHSPPRHEEE CCCCCCCCCCCCHHH	37.53	22817900
262	Phosphorylation	PPRHEEESQKAKIPK CCCCHHHHHHCCCCC	40.02	22817900
531	Phosphorylation	EEKDRKLSILAESIK HHHHHHHHHHHHHHH	20.70	19429919

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

Oops, there are no upstream regulatory protein records of ELOA1_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ELOA1_DROME !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ELOA1_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SRC64_DROME	Src64B	physical	14605208
CORTO_DROME	corto	physical	24204884

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND MASSSPECTROMETRY.
PubMed: 18327897