dbPTM

TF2AA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TF2AA_HUMAN
UniProt AC	P52655
Protein Name	Transcription initiation factor IIA subunit 1
Gene Name	GTF2A1
Organism	Homo sapiens (Human).
Sequence Length	376
Subcellular Localization	Nucleus.
Protein Description	TFIIA is a component of the transcription machinery of RNA polymerase II and plays an important role in transcriptional activation. TFIIA in a complex with TBP mediates transcriptional activity..
Protein Sequence	MANSANTNTVPKLYRSVIEDVINDVRDIFLDDGVDEQVLMELKTLWENKLMQSRAVDGFHSEEQQLLLQVQQQHQPQQQQHHHHHHHQQAQPQQTVPQQAQTQQVLIPASQQATAPQVIVPDSKLIQHMNASNMSAAATAATLALPAGVTPVQQILTNSGQLLQVVRAANGAQYIFQPQQSVVLQQQVIPQMQPGGVQAPVIQQVLAPLPGGISPQTGVIIQPQQILFTGNKTQVIPTTVAAPTPAQAQITATGQQQPQAQPAQTQAPLVLQVDGTGDTSSEEDEDEEEDYDDDEEEDKEKDGAEDGQVEEEPLNSEDDVSDEEGQELFDTENVVVCQYDKIHRSKNKWKFHLKDGIMNLNGRDYIFSKAIGDAEW

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MANSANTNT ------CCCCCCCCH	20.77	22814378
4	Phosphorylation	----MANSANTNTVP ----CCCCCCCCHHH	17.23	20068231
9	Phosphorylation	ANSANTNTVPKLYRS CCCCCCCHHHHHHHH	35.83	-
12	Acetylation	ANTNTVPKLYRSVIE CCCCHHHHHHHHHHH	54.54	19608861
12	Ubiquitination	ANTNTVPKLYRSVIE CCCCHHHHHHHHHHH	54.54	24816145
16	Phosphorylation	TVPKLYRSVIEDVIN HHHHHHHHHHHHHHH	17.56	21712546
49	Acetylation	LKTLWENKLMQSRAV HHHHHHCHHHHHCCC	33.55	27452117
49	Ubiquitination	LKTLWENKLMQSRAV HHHHHHCHHHHHCCC	33.55	29967540
167	Methylation	GQLLQVVRAANGAQY CHHHHHHHHHCCCEE	29.17	-
229	O-linked_Glycosylation	QPQQILFTGNKTQVI CCEEEEEECCCCEEE	36.08	23301498
238	O-linked_Glycosylation	NKTQVIPTTVAAPTP CCCEEEEEEECCCCC	23.84	23301498
239	O-linked_Glycosylation	KTQVIPTTVAAPTPA CCEEEEEEECCCCCC	11.64	23301498
244	O-linked_Glycosylation	PTTVAAPTPAQAQIT EEEECCCCCCCCEEE	26.91	23301498
251	O-linked_Glycosylation	TPAQAQITATGQQQP CCCCCEEECCCCCCC	13.19	23301498
253	O-linked_Glycosylation	AQAQITATGQQQPQA CCCEEECCCCCCCCC	27.20	23301498
265	O-linked_Glycosylation	PQAQPAQTQAPLVLQ CCCCCCCCCCCEEEE	28.89	23301498
279	Phosphorylation	QVDGTGDTSSEEDED EECCCCCCCCCCCCC	35.18	25137130
280	Phosphorylation	VDGTGDTSSEEDEDE ECCCCCCCCCCCCCC	40.26	25137130
281	Phosphorylation	DGTGDTSSEEDEDEE CCCCCCCCCCCCCCC	47.28	25137130
296	Ubiquitination	EDYDDDEEEDKEKDG CCCCCCCHHHHHHCC	77.74	30230243
307	Ubiquitination	EKDGAEDGQVEEEPL HHCCCCCCCCCCCCC	25.57	30230243
316	Phosphorylation	VEEEPLNSEDDVSDE CCCCCCCCCCCCCHH	50.51	17081983
321	Phosphorylation	LNSEDDVSDEEGQEL CCCCCCCCHHHHHCC	46.42	17081983
331	Phosphorylation	EGQELFDTENVVVCQ HHHCCCCCCCEEEEE	23.33	29802988
346	Ubiquitination	YDKIHRSKNKWKFHL CCHHCCCCCEEEEEE	63.60	30230243
368	Phosphorylation	NGRDYIFSKAIGDAE CCCEEEEEEHHCCCC	16.18	24719451

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
280	S	Phosphorylation	Kinase	TAF1	P21675	Uniprot
280	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
280	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
281	S	Phosphorylation	Kinase	TAF1	P21675	Uniprot
281	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
281	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
316	S	Phosphorylation	Kinase	TAF1	P21675	Uniprot
316	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
316	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
321	S	Phosphorylation	Kinase	TAF1	P21675	Uniprot
321	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
321	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TF2AA_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 TF2AA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TBP_HUMAN	TBP	physical	7724559
T2EB_HUMAN	GTF2E2	physical	9618479
HMGB1_HUMAN	HMGB1	physical	9880542
GCN1_HUMAN	GCN1L1	physical	17643375
TBPL1_HUMAN	TBPL1	physical	17643375
T2AG_HUMAN	GTF2A2	physical	17643375
TAF4_HUMAN	TAF4	physical	17643375
GRP75_HUMAN	HSPA9	physical	17643375
TAF6_HUMAN	TAF6	physical	17643375
TAF5_HUMAN	TAF5	physical	17643375
DOCK7_HUMAN	DOCK7	physical	17643375
CNOT1_HUMAN	CNOT1	physical	17643375
TBP_HUMAN	TBP	physical	17643375
TBPL2_HUMAN	TBPL2	physical	17643375
ROA1_HUMAN	HNRNPA1	physical	17643375
MYLK2_HUMAN	MYLK2	physical	17643375
ZEB1_HUMAN	ZEB1	physical	22939629
BOP1_HUMAN	BOP1	physical	22863883
GARS_HUMAN	GARS	physical	22863883
GORS2_HUMAN	GORASP2	physical	22863883
MAOX_HUMAN	ME1	physical	22863883
PDIA6_HUMAN	PDIA6	physical	22863883
RADI_HUMAN	RDX	physical	22863883
RUSD2_HUMAN	RPUSD2	physical	22863883
TBCD_HUMAN	TBCD	physical	22863883
UGDH_HUMAN	UGDH	physical	22863883
T2AG_HUMAN	GTF2A2	physical	25416956
NFYA_HUMAN	NFYA	physical	25416956
TBP_HUMAN	TBP	physical	12941701
TBP_MOUSE	Tbp	physical	12941701
CQ062_HUMAN	C17orf62	physical	26186194
SHIP2_HUMAN	INPPL1	physical	26186194
T2AG_HUMAN	GTF2A2	physical	26186194
TBPL1_HUMAN	TBPL1	physical	26186194
PTCD2_HUMAN	PTCD2	physical	26186194
TBP_HUMAN	TBP	physical	26186194
T2AG_HUMAN	GTF2A2	physical	26344197
PTMA_HUMAN	PTMA	physical	26344197
TBPL1_HUMAN	TBPL1	physical	28514442
CQ062_HUMAN	C17orf62	physical	28514442
T2AG_HUMAN	GTF2A2	physical	28514442
SHIP2_HUMAN	INPPL1	physical	28514442
TBP_HUMAN	TBP	physical	28514442
PTCD2_HUMAN	PTCD2	physical	28514442
BCAT1_HUMAN	BCAT1	physical	28514442
TBP_HUMAN	TBP	physical	29111974

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 TF2AA_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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 LYS-12, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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-316 AND SER-321, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"Taf(II) 250 phosphorylates human transcription factor IIA on serineresidues important for TBP binding and transcription activity."; Solow S., Salunek M., Ryan R., Lieberman P.M.; J. Biol. Chem. 276:15886-15892(2001). Cited for: PHOSPHORYLATION AT SER-280; SER-281; SER-316 AND SER-321, ANDMUTAGENESIS OF SER-280; SER-281; SER-316 AND SER-321.	11278496 [Abstract]