dbPTM

TAF7_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TAF7_MOUSE
UniProt AC	Q9R1C0
Protein Name	Transcription initiation factor TFIID subunit 7
Gene Name	Taf7
Organism	Mus musculus (Mouse).
Sequence Length	341
Subcellular Localization	Nucleus .
Protein Description	Functions as a component of the DNA-binding general transcription factor complex TFIID, a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Present in both of the previously described TFIID species which either lack or contain TAFII30 (TFIID alpha and TFIID beta respectively)..
Protein Sequence	MSKNKDDAPHELESQFILRLPPEYAATVRRAVQSGHVNLKDKLSIELHPDGRHGIVRVDRVPLAAKLVDLPCVTESLKTIDKKTFYKTADISQMLVATVDGDLYPPVEEAAATADPKANKKKDKDKEKKFVWNHGITLPLKNVRKRRFRKTAKKKYIESPDVEKEVKRLLSTDAEAVSTRWEIIAEDETKETENQGLDISSPGMSGHRQGHDSLEHDELREIFNDLSSSSEDEEDVNILDTEEDLERQLQDKLNESDEQHQENEGTNQLVMGIQKQIDNMKGKLQETQDRAKRQEDLIMKVENLALKNRFQAVLDELKQKEDREKEQLSSLQEELESLLEK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
44	Phosphorylation	VNLKDKLSIELHPDG CCCCCCEEEEECCCC	21.54	27600695
66	Ubiquitination	DRVPLAAKLVDLPCV CCCCCCHHHCCCCHH	43.36	-
74	Phosphorylation	LVDLPCVTESLKTID HCCCCHHCCCCCCCC	26.94	22871156
76	Phosphorylation	DLPCVTESLKTIDKK CCCHHCCCCCCCCCH	26.29	22871156
159	Phosphorylation	AKKKYIESPDVEKEV HHHHHCCCCCHHHHH	19.49	28833060
171	Phosphorylation	KEVKRLLSTDAEAVS HHHHHHHHCCHHHHH	28.91	28833060
172	Phosphorylation	EVKRLLSTDAEAVST HHHHHHHCCHHHHHH	38.92	28833060
192	Phosphorylation	AEDETKETENQGLDI EECCCHHHHCCCCCC	41.62	25619855
200	Phosphorylation	ENQGLDISSPGMSGH HCCCCCCCCCCCCCC	30.10	25619855
201	Phosphorylation	NQGLDISSPGMSGHR CCCCCCCCCCCCCCC	26.30	27087446
205	Phosphorylation	DISSPGMSGHRQGHD CCCCCCCCCCCCCCC	37.04	25619855
213	Phosphorylation	GHRQGHDSLEHDELR CCCCCCCCCCHHHHH	29.95	25159016
227	Phosphorylation	REIFNDLSSSSEDEE HHHHHHHCCCCCCHH	30.91	24224561
228	Phosphorylation	EIFNDLSSSSEDEED HHHHHHCCCCCCHHH	45.22	24224561
229	Phosphorylation	IFNDLSSSSEDEEDV HHHHHCCCCCCHHHC	34.08	24224561
230	Phosphorylation	FNDLSSSSEDEEDVN HHHHCCCCCCHHHCC	51.52	24224561
256	Phosphorylation	LQDKLNESDEQHQEN HHHHCHHHHHHHHHC	45.43	25521595
266	Phosphorylation	QHQENEGTNQLVMGI HHHHCCHHHHHHHHH	17.39	25619855
329	Phosphorylation	DREKEQLSSLQEELE HHHHHHHHHHHHHHH	28.79	20469934
330	Phosphorylation	REKEQLSSLQEELES HHHHHHHHHHHHHHH	42.54	20469934
337	Phosphorylation	SLQEELESLLEK--- HHHHHHHHHHHC---	51.37	21183079

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 TAF7_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
256	S	Phosphorylation		17242355
Phosphorylation at Ser-256 by TAF1 in early G1 phase disrupts binding to TAF1 (By similarity).

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 TAF7_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of TAF7_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of TAF7_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND MASSSPECTROMETRY.	19367708 [Abstract]