dbPTM

TAF12_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TAF12_HUMAN
UniProt AC	Q16514
Protein Name	Transcription initiation factor TFIID subunit 12
Gene Name	TAF12
Organism	Homo sapiens (Human).
Sequence Length	161
Subcellular Localization	Nucleus .
Protein Description	TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TAFs components-TIIFD are essential for mediating regulation of RNA polymerase transcription..
Protein Sequence	MNQFGPSALINLSNFSSIKPEPASTPPQGSMANSTAVVKIPGTPGAGGRLSPENNQVLTKKKLQDLVREVDPNEQLDEDVEEMLLQIADDFIESVVTAACQLARHRKSSTLEVKDVQLHLERQWNMWIPGFGSEEIRPYKKACTTEAHKQRMALIRKTTKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13 (in isoform 2)	Phosphorylation	-	31.20	22210691
13	Phosphorylation	PSALINLSNFSSIKP HHHEEECCCCCCCCC	31.20	28122231
16	Phosphorylation	LINLSNFSSIKPEPA EEECCCCCCCCCCCC	35.09	28122231
17	Phosphorylation	INLSNFSSIKPEPAS EECCCCCCCCCCCCC	30.41	28122231
19	Sumoylation	LSNFSSIKPEPASTP CCCCCCCCCCCCCCC	45.32	-
19	Sumoylation	LSNFSSIKPEPASTP CCCCCCCCCCCCCCC	45.32	28112733
21 (in isoform 2)	Phosphorylation	-	48.79	22210691
24	Phosphorylation	SIKPEPASTPPQGSM CCCCCCCCCCCCCCC	52.76	28348404
25	Phosphorylation	IKPEPASTPPQGSMA CCCCCCCCCCCCCCC	40.89	28348404
30	Phosphorylation	ASTPPQGSMANSTAV CCCCCCCCCCCCEEE	14.96	28122231
34	Phosphorylation	PQGSMANSTAVVKIP CCCCCCCCEEEEECC	14.27	26074081
35	Phosphorylation	QGSMANSTAVVKIPG CCCCCCCEEEEECCC	24.23	26074081
43	Phosphorylation	AVVKIPGTPGAGGRL EEEECCCCCCCCCCC	17.13	25159151
51	O-linked_Glycosylation	PGAGGRLSPENNQVL CCCCCCCCCCCCCCC	28.89	30379171
51	Phosphorylation	PGAGGRLSPENNQVL CCCCCCCCCCCCCCC	28.89	19664994
59	O-linked_Glycosylation	PENNQVLTKKKLQDL CCCCCCCCHHHHHHH	41.80	30379171
59	Phosphorylation	PENNQVLTKKKLQDL CCCCCCCCHHHHHHH	41.80	30266825
60	Ubiquitination	ENNQVLTKKKLQDLV CCCCCCCHHHHHHHH	43.69	27667366
61	Ubiquitination	NNQVLTKKKLQDLVR CCCCCCHHHHHHHHH	54.18	-
114	Ubiquitination	KSSTLEVKDVQLHLE CCCCEEEEEHHHHHH	42.69	-
140	Ubiquitination	SEEIRPYKKACTTEA CCCCCCCHHHCCHHH	36.26	27667366
140	Acetylation	SEEIRPYKKACTTEA CCCCCCCHHHCCHHH	36.26	25953088

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_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TAF12_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TBP_HUMAN	TBP	physical	17268553
TAF1A_HUMAN	TAF1A	physical	17268553
TAF1C_HUMAN	TAF1C	physical	17268553
CPSF1_HUMAN	CPSF1	physical	9311784
ERCC1_HUMAN	ERCC1	physical	22323595
TAF4B_HUMAN	TAF4B	physical	15601843
TBP_HUMAN	TBP	physical	8663456

Drug and Disease Associations

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

Regulatory Network of TAF12_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASSSPECTROMETRY.	19369195 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43 AND SER-51, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND THR-59, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASSSPECTROMETRY.	19007248 [Abstract]