T2FA_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: T2FA_DROME
• UniProt AC: Q05913
• Protein Name: General transcription factor IIF subunit 1
• Gene Name: TfIIFalpha
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 577
• Subcellular Localization: Nucleus.
• Protein Description: TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation..
• Protein Sequence: MSSASKSTPSAASGSSTSAAAAAAASVASGSASSSANVQEFKIRVPKMPKKHHVMRFNATLNVDFAQWRNVKLERENNMKEFRGMEEDQPKFGAGSEYNRDQREEARRKKFGIIARKYRPEAQPWILKVGGKTGKKFKGIREGGVGENAAFYVFTHAPDGAIEAYPLTEWYNFQPIQRYKSLSAEEAEQEFGRRKKVMNYFSLMLRKRLRGDEEEEQDPEEAKLIKAATKKSKELKITDMDEWIDSEDESDSEDEEDKKKKEQEDSDDGKAKGKGKKGADKKKKKRDVDDEAFEESDDGDEEGREMDYDTSSSEDEPDPEAKVDKDMKGVAEEDALRKLLTSDEEEDDEKKSDESDKEDADGEKKKKDKGKDEVSKDKKKKKPTKDDKKGKSNGSGDSSTDFSSDSTDSEDDLSNGPPKKKVVVKDKDKEKEKEKESAASSKVIASSSNANKSRSATPTLSTDASKRKMNSLPSDLTASDTSNSPTSTPAKRPKNEISTSLPTSFSGGKVEDYGITEEAVRRYLKRKPLTATELLTKFKNKKTPVSSDRLVETMTKILKKINPVKHTIQGKMYLWIK

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
33	Phosphorylation	SVASGSASSSANVQE HHHCCCCCCCCCCCE	26.90	22817900
181	Phosphorylation	QPIQRYKSLSAEEAE CCCHHHHCCCHHHHH	20.72	19429919
183	Phosphorylation	IQRYKSLSAEEAEQE CHHHHCCCHHHHHHH	40.50	22817900
246	Phosphorylation	DMDEWIDSEDESDSE CHHHHHCCCCCCCCC	37.50	19429919
250	Phosphorylation	WIDSEDESDSEDEED HHCCCCCCCCCCHHH	59.77	19429919
252	Phosphorylation	DSEDESDSEDEEDKK CCCCCCCCCCHHHHH	57.11	19429919
266	Phosphorylation	KKKEQEDSDDGKAKG HHHHHHCCCCCCCCC	36.53	19429919
296	Phosphorylation	DDEAFEESDDGDEEG CHHHHHCCCCCCCCC	33.53	19429919
341	Phosphorylation	DALRKLLTSDEEEDD HHHHHHHCCCCCCCH	44.56	19429919
342	Phosphorylation	ALRKLLTSDEEEDDE HHHHHHCCCCCCCHH	42.89	19429919
352	Phosphorylation	EEDDEKKSDESDKED CCCHHHHCCCCCCCC	58.65	19429919
355	Phosphorylation	DEKKSDESDKEDADG HHHHCCCCCCCCCCC	60.00	19429919
446	Phosphorylation	ASSKVIASSSNANKS HHHCCHHCCCCCCCC	24.15	22817900
447	Phosphorylation	SSKVIASSSNANKSR HHCCHHCCCCCCCCC	20.70	22668510
448	Phosphorylation	SKVIASSSNANKSRS HCCHHCCCCCCCCCC	37.15	22668510
453	Phosphorylation	SSSNANKSRSATPTL CCCCCCCCCCCCCCC	31.13	19429919
455	Phosphorylation	SNANKSRSATPTLST CCCCCCCCCCCCCCC	43.52	19429919
457	Phosphorylation	ANKSRSATPTLSTDA CCCCCCCCCCCCCHH	20.32	19429919
459	Phosphorylation	KSRSATPTLSTDASK CCCCCCCCCCCHHHH	29.05	19429919
461	Phosphorylation	RSATPTLSTDASKRK CCCCCCCCCHHHHHH	27.07	19429919
479	Phosphorylation	LPSDLTASDTSNSPT CCCCCCCCCCCCCCC	35.86	22817900
482	Phosphorylation	DLTASDTSNSPTSTP CCCCCCCCCCCCCCC	40.06	22817900
484	Phosphorylation	TASDTSNSPTSTPAK CCCCCCCCCCCCCCC	29.35	22817900
488	Phosphorylation	TSNSPTSTPAKRPKN CCCCCCCCCCCCCCC	29.73	18327897

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

Oops, there are no upstream regulatory protein records of T2FA_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of T2FA_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 T2FA_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NHP2_DROME	NHP2	physical	14605208
RPB4_DROME	Rpb4	physical	25242320
T2FB_DROME	TfIIFbeta	physical	25242320

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-183; SER-246; SER-250;SER-252; THR-341; SER-342; SER-352; SER-355; SER-453; SER-455;THR-457; SER-482; SER-484 AND THR-488, AND MASS SPECTROMETRY.
PubMed: 18327897