dbPTM

TFC7_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TFC7_YEAST
UniProt AC	Q12415
Protein Name	Transcription factor tau 55 kDa subunit
Gene Name	TFC7
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	435
Subcellular Localization	Nucleus .
Protein Description	TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauA domain of TFIIIC that binds boxA DNA promoter sites of tRNA and similar genes..
Protein Sequence	MVVNTIYIARHGYRSNWLPEGPYPDPLTGIDSDVPLAEHGVQQAKELAHYLLSLDNQPEAAFASPFYRCLETVQPIAKLLEIPVYLERGIGEWYRPDRKPVIPVPAGYEILSKFFPGVISQEWDSTLTPNEKGETEQEMYMRFKKFWPLFIERVEKEYPNVECILLVTHAASKIALGMSLLGYDNPRMSLNENGDKIRSGSCSLDKYEILKKSYDTIDETDDQTSFTYIPFSDRKWVLTMNGNTEFLSSGEEMNWNFDCVAEAGSDADIKKRQMTKKTSSPIPEADDQTEVETVYISVDIPSGNYKERTEIAKSAILQYSGLETDAPLFRIGNRLYEGSWERLVGTELAFPNAAHVHKKTAGLLSPTEENETTNAGQSKGSSTANDPNIQIQEEDVGLPDSTNTSRDHTGDKEEVQSEKIYRIKERIVLSNVRPM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MVVNTIYIARHG ---CCCCEEEEECCC	11.98	30377154
7	Phosphorylation	-MVVNTIYIARHGYR -CCCCEEEEECCCCC	6.11	28132839
201	Phosphorylation	GDKIRSGSCSLDKYE CCCCCCCCCCCCHHH	11.20	21440633
220	Phosphorylation	SYDTIDETDDQTSFT HHCCCCCCCCCCEEE	40.92	22369663
224	Phosphorylation	IDETDDQTSFTYIPF CCCCCCCCEEEEEEC	32.57	25521595
225	Phosphorylation	DETDDQTSFTYIPFS CCCCCCCEEEEEECC	15.23	22369663
227	Phosphorylation	TDDQTSFTYIPFSDR CCCCCEEEEEECCCC	21.95	22369663
228	Phosphorylation	DDQTSFTYIPFSDRK CCCCEEEEEECCCCC	12.46	22369663
279	Phosphorylation	RQMTKKTSSPIPEAD HHCCCCCCCCCCCCC	42.89	28889911
280	Phosphorylation	QMTKKTSSPIPEADD HCCCCCCCCCCCCCC	31.89	27214570
339	Phosphorylation	GNRLYEGSWERLVGT CCCCCCCCHHHHCCC	17.52	22369663
360	Phosphorylation	AAHVHKKTAGLLSPT CCCCCHHCCCCCCCC	30.66	19795423
365	Phosphorylation	KKTAGLLSPTEENET HHCCCCCCCCCCCCC	34.51	25521595
367	Phosphorylation	TAGLLSPTEENETTN CCCCCCCCCCCCCCC	53.18	25752575
372	Phosphorylation	SPTEENETTNAGQSK CCCCCCCCCCCCCCC	36.61	29734811
373	Phosphorylation	PTEENETTNAGQSKG CCCCCCCCCCCCCCC	19.52	26447709
378	Phosphorylation	ETTNAGQSKGSSTAN CCCCCCCCCCCCCCC	37.76	29688323
417	Phosphorylation	GDKEEVQSEKIYRIK CCHHHHCCHHHHEEH	46.14	28889911

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 TFC7_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TFC7_YEAST !!

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 TFC7_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TFC4_YEAST	TFC4	physical	8617241
TFC1_YEAST	TFC1	physical	9584160
TFC1_YEAST	TFC1	physical	16429126
TFC3_YEAST	TFC3	physical	16429126
TFC4_YEAST	TFC4	physical	16429126
TFC6_YEAST	TFC6	physical	16429126
TFC8_YEAST	TFC8	physical	16429126
IDI1_YEAST	IDI1	physical	18467557
HSP71_YEAST	SSA1	physical	19536198
TFC1_YEAST	TFC1	physical	17409385
RPB1_YEAST	RPO21	physical	23569204

Drug and Disease Associations

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

Regulatory Network of TFC7_YEAST

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-224; SER-225; SER-279;SER-280; SER-365 AND THR-367, AND MASS SPECTROMETRY.	18407956 [Abstract]
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND MASSSPECTROMETRY.	17563356 [Abstract]
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND MASSSPECTROMETRY.	17330950 [Abstract]
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND MASSSPECTROMETRY.	15665377 [Abstract]