dbPTM

TAF12_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TAF12_SCHPO
UniProt AC	O13722
Protein Name	Transcription initiation factor TFIID subunit 12
Gene Name	taf12 {ECO:0000312\|EMBL:CAB10099.1}
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	450
Subcellular Localization	Nucleus .
Protein Description	Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II-dependent transcriptional regulation. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction and promoter selectivity, interaction with transcription activators, and chromatin modification through histone acetylation (gcn5) and deubiquitination (ubp8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3 (By similarity)..
Protein Sequence	MNGQHSSPGTPVQRPSAGPVNQAQFSQQRTNQLTSLLHTMTMYQQLAQNVGLNTPQGQVYLLQAQTIRRQLQGHAQSGQLPNQQLLQQLQSNGALQQGTPEPSNTRPRPQLNAQEQTMLLVRHRQLQTAQNYLTEMKEALGRIKNELSTNERLDTSAREALVKQESELTVKIAQFTAAISNGIRSIQQLQNRQASSANGNNTGTSTPVNASTDTRKSTASTPQLQQTQAQANAPQQRINPETSSVPETPVGVSAANVSNESTELATSATQQSGLANNVEKSQTPSYMSANHLPKVDSKSPIPFSVPPSRATLTGGYASGSIGLSTPGLSRAPHYELDNGNRLLSKRKLHDLLQQIDSEEKIEPEVEELLLEIADEFVESVTNFACRLAKHRKSDTLDVRDVQLHLERNWNIRLPGFASDDIVKSARKTGPTPSYQQKQNAIGTAKSLNKD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MNGQHSSPGTPVQ --CCCCCCCCCCCCC	30.27	29996109
7	Phosphorylation	-MNGQHSSPGTPVQR -CCCCCCCCCCCCCC	25.81	29996109
10	Phosphorylation	GQHSSPGTPVQRPSA CCCCCCCCCCCCCCC	24.54	29996109
196	Phosphorylation	LQNRQASSANGNNTG HHHHCCCCCCCCCCC	28.86	25720772
202	Phosphorylation	SSANGNNTGTSTPVN CCCCCCCCCCCCCCC	45.92	25720772
204	Phosphorylation	ANGNNTGTSTPVNAS CCCCCCCCCCCCCCC	27.65	25720772
205	Phosphorylation	NGNNTGTSTPVNAST CCCCCCCCCCCCCCC	31.87	25720772
206	Phosphorylation	GNNTGTSTPVNASTD CCCCCCCCCCCCCCC	30.97	25720772
217	Phosphorylation	ASTDTRKSTASTPQL CCCCCCCCCCCCHHH	26.39	29996109
221	Phosphorylation	TRKSTASTPQLQQTQ CCCCCCCCHHHHHHH	16.76	29996109
281	Phosphorylation	LANNVEKSQTPSYMS CCCCCCHHCCCCCCC	26.27	29996109
283	Phosphorylation	NNVEKSQTPSYMSAN CCCCHHCCCCCCCCC	22.69	24763107
297	Phosphorylation	NHLPKVDSKSPIPFS CCCCCCCCCCCCCCC	37.71	28889911
299	Phosphorylation	LPKVDSKSPIPFSVP CCCCCCCCCCCCCCC	31.82	25720772

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 TAF12_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TAF12_SCHPO !!

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 TAF12_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
PAT1_SCHPO	SPBC19G7.10c	physical	26771498

Drug and Disease Associations

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

Regulatory Network of TAF12_SCHPO

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteome analysis of fission yeast."; Wilson-Grady J.T., Villen J., Gygi S.P.; J. Proteome Res. 7:1088-1097(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297, AND MASSSPECTROMETRY.	18257517 [Abstract]