dbPTM

TAF9_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TAF9_HUMAN
UniProt AC	Q16594
Protein Name	Transcription initiation factor TFIID subunit 9
Gene Name	TAF9
Organism	Homo sapiens (Human).
Sequence Length	264
Subcellular Localization	Nucleus .
Protein Description	Essential for cell viability. TAF9 and TAF9B are involved in transcriptional activation as well as repression of distinct but overlapping sets of genes. May have a role in gene regulation associated with apoptosis. TAFs are components of the transcription factor IID (TFIID) complex, the TBP-free TAFII complex (TFTC), the PCAF histone acetylase complex and the STAGA transcription coactivator-HAT complex. TFIID or TFTC are essential for the regulation of RNA polymerase II-mediated transcription..
Protein Sequence	MESGKTASPKSMPKDAQMMAQILKDMGITEYEPRVINQMLEFAFRYVTTILDDAKIYSSHAKKATVDADDVRLAIQCRADQSFTSPPPRDFLLDIARQRNQTPLPLIKPYSGPRLPPDRYCLTAPNYRLKSLQKKASTSAGRITVPRLSVGSVTSRPSTPTLGTPTPQTMSVSTKVGTPMSLTGQRFTVQMPTSQSPAVKASIPATSAVQNVLINPSLIGSKNILITTNMMSSQNTANESSNALKRKREDDDDDDDDDDDYDNL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MESGKTAS -------CCCCCCCC	9.26	-
3	Phosphorylation	-----MESGKTASPK -----CCCCCCCCCC	44.27	26074081
3	O-linked_Glycosylation	-----MESGKTASPK -----CCCCCCCCCC	44.27	30059200
5	Acetylation	---MESGKTASPKSM ---CCCCCCCCCCCC	50.63	19608861
5	Ubiquitination	---MESGKTASPKSM ---CCCCCCCCCCCC	50.63	33845483
6	Phosphorylation	--MESGKTASPKSMP --CCCCCCCCCCCCC	35.57	26074081
8	Phosphorylation	MESGKTASPKSMPKD CCCCCCCCCCCCCHH	37.78	28450419
10	Ubiquitination	SGKTASPKSMPKDAQ CCCCCCCCCCCHHHH	57.82	-
11	Phosphorylation	GKTASPKSMPKDAQM CCCCCCCCCCHHHHH	43.64	25599653
14	Acetylation	ASPKSMPKDAQMMAQ CCCCCCCHHHHHHHH	57.99	7666247
14	Ubiquitination	ASPKSMPKDAQMMAQ CCCCCCCHHHHHHHH	57.99	-
24	Ubiquitination	QMMAQILKDMGITEY HHHHHHHHHCCCCCC	47.50	21963094
46	Phosphorylation	MLEFAFRYVTTILDD HHHHHHHHHHHHHHH	8.83	29083192
48	Phosphorylation	EFAFRYVTTILDDAK HHHHHHHHHHHHHHC	10.13	29083192
49	Phosphorylation	FAFRYVTTILDDAKI HHHHHHHHHHHHHCH	14.97	29083192
55	Acetylation	TTILDDAKIYSSHAK HHHHHHHCHHCCCCC	49.52	25953088
55	Ubiquitination	TTILDDAKIYSSHAK HHHHHHHCHHCCCCC	49.52	-
57	Phosphorylation	ILDDAKIYSSHAKKA HHHHHCHHCCCCCCC	11.92	-
62	Ubiquitination	KIYSSHAKKATVDAD CHHCCCCCCCCCCHH	37.20	29967540
62	Acetylation	KIYSSHAKKATVDAD CHHCCCCCCCCCCHH	37.20	7683671
63	Ubiquitination	IYSSHAKKATVDADD HHCCCCCCCCCCHHH	50.50	-
82	Phosphorylation	IQCRADQSFTSPPPR HEECCCCCCCCCCCC	30.92	29396449
84	Phosphorylation	CRADQSFTSPPPRDF ECCCCCCCCCCCCHH	45.64	21815630
85	Phosphorylation	RADQSFTSPPPRDFL CCCCCCCCCCCCHHH	33.14	25159151
102	Phosphorylation	IARQRNQTPLPLIKP HHHHCCCCCCCCCCC	30.27	25159151
108	Ubiquitination	QTPLPLIKPYSGPRL CCCCCCCCCCCCCCC	45.65	23000965
108	Acetylation	QTPLPLIKPYSGPRL CCCCCCCCCCCCCCC	45.65	19608861
108	Methylation	QTPLPLIKPYSGPRL CCCCCCCCCCCCCCC	45.65	22633535
110	Phosphorylation	PLPLIKPYSGPRLPP CCCCCCCCCCCCCCC	22.66	28634298
111	Phosphorylation	LPLIKPYSGPRLPPD CCCCCCCCCCCCCCC	51.34	26425664
119	Methylation	GPRLPPDRYCLTAPN CCCCCCCCCEECCCC	29.82	-
120	Phosphorylation	PRLPPDRYCLTAPNY CCCCCCCCEECCCCH	10.13	28634298
123	Phosphorylation	PPDRYCLTAPNYRLK CCCCCEECCCCHHHH	36.19	28634298
127	Phosphorylation	YCLTAPNYRLKSLQK CEECCCCHHHHHHHH	19.10	28634298
128	Methylation	CLTAPNYRLKSLQKK EECCCCHHHHHHHHH	42.13	26494163
131	Phosphorylation	APNYRLKSLQKKAST CCCHHHHHHHHHHCC	40.39	-
134	Ubiquitination	YRLKSLQKKASTSAG HHHHHHHHHHCCCCC	56.45	24816145
137	Phosphorylation	KSLQKKASTSAGRIT HHHHHHHCCCCCEEC	31.60	21406692
138	Phosphorylation	SLQKKASTSAGRITV HHHHHHCCCCCEECC	27.70	21406692
139	Phosphorylation	LQKKASTSAGRITVP HHHHHCCCCCEECCC	26.65	21406692
144	Phosphorylation	STSAGRITVPRLSVG CCCCCEECCCEEEEC	24.09	29496963
149	Phosphorylation	RITVPRLSVGSVTSR EECCCEEEECCCCCC	26.22	30278072
152	Phosphorylation	VPRLSVGSVTSRPST CCEEEECCCCCCCCC	21.77	30266825
154	Phosphorylation	RLSVGSVTSRPSTPT EEEECCCCCCCCCCC	22.25	23401153
155	Phosphorylation	LSVGSVTSRPSTPTL EEECCCCCCCCCCCC	39.78	30266825
158	Phosphorylation	GSVTSRPSTPTLGTP CCCCCCCCCCCCCCC	46.00	30266825
159	Phosphorylation	SVTSRPSTPTLGTPT CCCCCCCCCCCCCCC	23.99	23927012
161	Phosphorylation	TSRPSTPTLGTPTPQ CCCCCCCCCCCCCCC	37.60	30266825
164	Phosphorylation	PSTPTLGTPTPQTMS CCCCCCCCCCCCEEE	27.40	30266825
166	Phosphorylation	TPTLGTPTPQTMSVS CCCCCCCCCCEEEEE	28.06	30266825
169	Phosphorylation	LGTPTPQTMSVSTKV CCCCCCCEEEEEEEE	16.77	23927012
171	Phosphorylation	TPTPQTMSVSTKVGT CCCCCEEEEEEEECC	19.12	23927012
173	Phosphorylation	TPQTMSVSTKVGTPM CCCEEEEEEEECCCC	18.40	20068231
174	Phosphorylation	PQTMSVSTKVGTPMS CCEEEEEEEECCCCC	27.82	23927012
178	Phosphorylation	SVSTKVGTPMSLTGQ EEEEEECCCCCCCCC	20.85	25159151
180	Sulfoxidation	STKVGTPMSLTGQRF EEEECCCCCCCCCEE	5.28	21406390
181	Phosphorylation	TKVGTPMSLTGQRFT EEECCCCCCCCCEEE	24.79	25159151
183	Phosphorylation	VGTPMSLTGQRFTVQ ECCCCCCCCCEEEEE	24.78	25159151
186	Methylation	PMSLTGQRFTVQMPT CCCCCCCEEEEECCC	30.46	54559819
188	Phosphorylation	SLTGQRFTVQMPTSQ CCCCCEEEEECCCCC	16.42	20068231
193	Phosphorylation	RFTVQMPTSQSPAVK EEEEECCCCCCCCCC	33.77	26055452
194	Phosphorylation	FTVQMPTSQSPAVKA EEEECCCCCCCCCCC	23.84	25159151
194	O-linked_Glycosylation	FTVQMPTSQSPAVKA EEEECCCCCCCCCCC	23.84	30059200
196	Phosphorylation	VQMPTSQSPAVKASI EECCCCCCCCCCCCC	18.00	25159151
202	O-linked_Glycosylation	QSPAVKASIPATSAV CCCCCCCCCCCCHHH	24.32	30059200
206	O-linked_Glycosylation	VKASIPATSAVQNVL CCCCCCCCHHHHCEE	16.32	30059200
207	O-linked_Glycosylation	KASIPATSAVQNVLI CCCCCCCHHHHCEEC	28.66	30059200
217	O-linked_Glycosylation	QNVLINPSLIGSKNI HCEECCHHHCCCCEE	28.29	30059200
217	Phosphorylation	QNVLINPSLIGSKNI HCEECCHHHCCCCEE	28.29	-
221	O-linked_Glycosylation	INPSLIGSKNILITT CCHHHCCCCEEEEEC	18.61	30059200
221	Phosphorylation	INPSLIGSKNILITT CCHHHCCCCEEEEEC	18.61	-
227	Phosphorylation	GSKNILITTNMMSSQ CCCEEEEECCCCCCC	14.52	24850871
240	Phosphorylation	SQNTANESSNALKRK CCCCCCCCCHHHHHH	28.79	24850871
241	Phosphorylation	QNTANESSNALKRKR CCCCCCCCHHHHHHC	21.68	24850871
245	Ubiquitination	NESSNALKRKREDDD CCCCHHHHHHCCCCC	54.16	-
245	Sumoylation	NESSNALKRKREDDD CCCCHHHHHHCCCCC	54.16	-
245	Acetylation	NESSNALKRKREDDD CCCCHHHHHHCCCCC	54.16	25953088
245	Sumoylation	NESSNALKRKREDDD CCCCHHHHHHCCCCC	54.16	-
261	Phosphorylation	DDDDDDDYDNL---- CCCCCCCCCCC----	17.46	28796482

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 TAF9_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TAF9_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 TAF9_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NC2A_HUMAN	DRAP1	physical	16189514
RBM48_HUMAN	RBM48	physical	16169070
EF1A1_HUMAN	EEF1A1	physical	16169070
TRRAP_HUMAN	TRRAP	physical	11564863
TAF6L_HUMAN	TAF6L	physical	11564863
TAF5L_HUMAN	TAF5L	physical	11564863
TADA3_HUMAN	TADA3	physical	11564863
SUPT3_HUMAN	SUPT3H	physical	11564863
SF3B3_HUMAN	SF3B3	physical	11564863
KAT2A_HUMAN	KAT2A	physical	11564863
ST65G_HUMAN	SUPT7L	physical	11564863
TAF10_HUMAN	TAF10	physical	11564863
TAF12_HUMAN	TAF12	physical	11564863
TAF1_HUMAN	TAF1	physical	11564863
TAF2_HUMAN	TAF2	physical	11564863
TAF4_HUMAN	TAF4	physical	11564863
TAF5_HUMAN	TAF5	physical	11564863
TAF6_HUMAN	TAF6	physical	11564863
TAF7_HUMAN	TAF7	physical	11564863
TBP_HUMAN	TBP	physical	11564863
TADA1_HUMAN	TADA1	physical	11564863
TF65_HUMAN	RELA	physical	15489227
VP16_HHV11	UL48	physical	15081896
NCOR1_HUMAN	NCOR1	physical	9611234
TAF6_HUMAN	TAF6	physical	9611234
TF2B_HUMAN	GTF2B	physical	9611234
KLF6_HUMAN	KLF6	physical	17636026
NUFP1_HUMAN	NUFIP1	physical	17636026
FBRL_HUMAN	FBL	physical	17636026
TAF2_HUMAN	TAF2	physical	7597030
TAF6_HUMAN	TAF6	physical	15601843
NC2A_HUMAN	DRAP1	physical	16713569
IMA5_HUMAN	KPNA1	physical	16713569
IMA7_HUMAN	KPNA6	physical	16713569
RN138_HUMAN	RNF138	physical	16713569
RS14_HUMAN	RPS14	physical	16713569
TAF6L_HUMAN	TAF6L	physical	16713569
UBA1_HUMAN	UBA1	physical	16713569
A4_HUMAN	APP	physical	21832049
TAF6_HUMAN	TAF6	physical	15899866
TBP_HUMAN	TBP	physical	22939629
COIL_HUMAN	COIL	physical	16079131
RS14_HUMAN	RPS14	physical	23246961
FEZ1_HUMAN	FEZ1	physical	20195357
RS24_HUMAN	RPS24	physical	20195357
TBCA_HUMAN	TBCA	physical	20195357
ANK2_HUMAN	ANK2	physical	20195357
NCOA2_HUMAN	NCOA2	physical	20195357
NDRG1_HUMAN	NDRG1	physical	25416956
LTOR5_HUMAN	LAMTOR5	physical	25416956
NC2A_HUMAN	DRAP1	physical	25416956
TAF6L_HUMAN	TAF6L	physical	25416956
CHD2_HUMAN	CHD2	physical	26344197
ELP2_HUMAN	ELP2	physical	26344197
TAF10_HUMAN	TAF10	physical	26344197
TAF4_HUMAN	TAF4	physical	26344197
TAF5_HUMAN	TAF5	physical	26344197
TAF6_HUMAN	TAF6	physical	26344197
TAF7_HUMAN	TAF7	physical	26344197

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 TAF9_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1; LYS-5 AND LYS-108, ANDMASS SPECTROMETRY.	19608861 [Abstract]
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-149; SER-158 ANDTHR-159, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155 AND SER-158, ANDMASS SPECTROMETRY.	19413330 [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-159; THR-161; THR-178AND SER-181, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND MASSSPECTROMETRY.	17081983 [Abstract]