dbPTM

TF3C2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TF3C2_HUMAN
UniProt AC	Q8WUA4
Protein Name	General transcription factor 3C polypeptide 2
Gene Name	GTF3C2
Organism	Homo sapiens (Human).
Sequence Length	911
Subcellular Localization	Nucleus.
Protein Description	Required for RNA polymerase III-mediated transcription. Component of TFIIIC that initiates transcription complex assembly on tRNA and is required for transcription of 5S rRNA and other stable nuclear and cytoplasmic RNAs. May play a direct role in stabilizing interactions of TFIIIC2 with TFIIIC1..
Protein Sequence	MDTCGVGYVALGEAGPVGNMTVVDSPGQEVLNQLDVKTSSEMTSAEASVEMSLPTPLPGFEDSPDQRRLPPEQESLSRLEQPDLSSEMSKVSKPRASKPGRKRGGRTRKGPKRPQQPNPPSAPLVPGLLDQSNPLSTPMPKKRGRKSKAELLLLKLSKDLDRPESQSPKRPPEDFETPSGERPRRRAAQVALLYLQELAEELSTALPAPVSCPEGPKVSSPTKPKKIRQPAACPGGEEVDGAPRDEDFFLQVEAEDVEESEGPSESSSEPEPVVPRSTPRGSTSGKQKPHCRGMAPNGLPNHIMAPVWKCLHLTKDFREQKHSYWEFAEWIPLAWKWHLLSELEAAPYLPQEEKSPLFSVQREGLPEDGTLYRINRFSSITAHPERWDVSFFTGGPLWALDWCPVPEGAGASQYVALFSSPDMNETHPLSQLHSGPGLLQLWGLGTLQQESCPGNRAHFVYGIACDNGCIWDLKFCPSGAWELPGTPRKAPLLPRLGLLALACSDGKVLLFSLPHPEALLAQQPPDAVKPAIYKVQCVATLQVGSMQATDPSECGQCLSLAWMPTRPHQHLAAGYYNGMVVFWNLPTNSPLQRIRLSDGSLKLYPFQCFLAHDQAVRTLQWCKANSHFLVSAGSDRKIKFWDLRRPYEPINSIKRFLSTELAWLLPYNGVTVAQDNCYASYGLCGIHYIDAGYLGFKAYFTAPRKGTVWSLSGSDWLGTIAAGDISGELIAAILPDMALNPINVKRPVERRFPIYKADLIPYQDSPEGPDHSSASSGVPNPPKARTYTETVNHHYLLFQDTDLGSFHDLLRREPMLRMQEGEGHSQLCLDRLQLEAIHKVRFSPNLDSYGWLVSGGQSGLVRIHFVRGLASPLGHRMQLESRAHFNAMFQPSSPTRRPGFSPTSHRLLPTP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MDTCGVGYVA -----CCCCCCCEEE	15.17	20068231
8	Phosphorylation	MDTCGVGYVALGEAG CCCCCCCEEEECCCC	4.71	28348404
21	Phosphorylation	AGPVGNMTVVDSPGQ CCCCCCEEEECCCCH	22.75	26074081
25	Phosphorylation	GNMTVVDSPGQEVLN CCEEEECCCCHHHHH	21.22	20068231
37	Sumoylation	VLNQLDVKTSSEMTS HHHHCCCCCCCCCCC	42.21	-
39	Phosphorylation	NQLDVKTSSEMTSAE HHCCCCCCCCCCCCE	20.70	-
48	Phosphorylation	EMTSAEASVEMSLPT CCCCCEEEEEECCCC	15.32	-
52	Phosphorylation	AEASVEMSLPTPLPG CEEEEEECCCCCCCC	20.07	26074081
55	Phosphorylation	SVEMSLPTPLPGFED EEEECCCCCCCCCCC	42.63	26074081
63	Phosphorylation	PLPGFEDSPDQRRLP CCCCCCCCCCHHCCC	24.15	28985074
75	Phosphorylation	RLPPEQESLSRLEQP CCCHHHHHHHHHCCC	31.19	26074081
85	Phosphorylation	RLEQPDLSSEMSKVS HHCCCCHHHHHHHCC	31.47	21815630
86	Phosphorylation	LEQPDLSSEMSKVSK HCCCCHHHHHHHCCC	44.61	21815630
88	Sulfoxidation	QPDLSSEMSKVSKPR CCCHHHHHHHCCCCC	5.19	21406390
89	Phosphorylation	PDLSSEMSKVSKPRA CCHHHHHHHCCCCCC	26.34	21406692
93	Ubiquitination	SEMSKVSKPRASKPG HHHHHCCCCCCCCCC	41.32	24816145
104	Ubiquitination	SKPGRKRGGRTRKGP CCCCCCCCCCCCCCC	32.73	24816145
121	Phosphorylation	PQQPNPPSAPLVPGL CCCCCCCCCCCCCCC	43.72	24732914
132	Phosphorylation	VPGLLDQSNPLSTPM CCCCCCCCCCCCCCC	39.83	25159151
132	Ubiquitination	VPGLLDQSNPLSTPM CCCCCCCCCCCCCCC	39.83	24816145
136	Phosphorylation	LDQSNPLSTPMPKKR CCCCCCCCCCCCCCC	31.55	25159151
137	Phosphorylation	DQSNPLSTPMPKKRG CCCCCCCCCCCCCCC	31.15	25159151
147	Phosphorylation	PKKRGRKSKAELLLL CCCCCCCCHHHHHHH	35.42	29214152
148	Methylation	KKRGRKSKAELLLLK CCCCCCCHHHHHHHH	49.25	24129315
148	Ubiquitination	KKRGRKSKAELLLLK CCCCCCCHHHHHHHH	49.25	33845483
155	Ubiquitination	KAELLLLKLSKDLDR HHHHHHHHHHHCCCC	51.16	33845483
157	Phosphorylation	ELLLLKLSKDLDRPE HHHHHHHHHCCCCCH	23.65	23927012
159	Ubiquitination	LLLKLSKDLDRPESQ HHHHHHHCCCCCHHC	50.88	33845483
165	Phosphorylation	KDLDRPESQSPKRPP HCCCCCHHCCCCCCC	38.34	29255136
166	Ubiquitination	DLDRPESQSPKRPPE CCCCCHHCCCCCCCH	63.19	33845483
167	Phosphorylation	LDRPESQSPKRPPED CCCCHHCCCCCCCHH	41.49	29255136
177	Phosphorylation	RPPEDFETPSGERPR CCCHHCCCCCCCCHH	23.81	30266825
179	Phosphorylation	PEDFETPSGERPRRR CHHCCCCCCCCHHHH	61.78	30266825
203	Phosphorylation	QELAEELSTALPAPV HHHHHHHHHCCCCCC	18.21	26074081
204	Phosphorylation	ELAEELSTALPAPVS HHHHHHHHCCCCCCC	44.85	26074081
208	Ubiquitination	ELSTALPAPVSCPEG HHHHCCCCCCCCCCC	20.27	24816145
211	Phosphorylation	TALPAPVSCPEGPKV HCCCCCCCCCCCCCC	23.93	27174698
219	Phosphorylation	CPEGPKVSSPTKPKK CCCCCCCCCCCCCCC	36.40	30266825
220	Phosphorylation	PEGPKVSSPTKPKKI CCCCCCCCCCCCCCC	39.31	30266825
222	Phosphorylation	GPKVSSPTKPKKIRQ CCCCCCCCCCCCCCC	63.02	21955146
260	Phosphorylation	EAEDVEESEGPSESS EEECCCCCCCCCCCC	34.06	24275569
264	Phosphorylation	VEESEGPSESSSEPE CCCCCCCCCCCCCCC	62.05	24275569
266	Phosphorylation	ESEGPSESSSEPEPV CCCCCCCCCCCCCCC	43.43	24275569
268	Phosphorylation	EGPSESSSEPEPVVP CCCCCCCCCCCCCCC	67.46	24275569
309	Ubiquitination	HIMAPVWKCLHLTKD CHHHHHHHHHHHCHH	27.44	23000965
315	Ubiquitination	WKCLHLTKDFREQKH HHHHHHCHHHHHHHH	62.32	23000965
320	Ubiquitination	LTKDFREQKHSYWEF HCHHHHHHHHHHHHH	44.50	23000965
321	Ubiquitination	TKDFREQKHSYWEFA CHHHHHHHHHHHHHH	29.75	23000965
326	Ubiquitination	EQKHSYWEFAEWIPL HHHHHHHHHHHHHHH	27.09	23000965
332	Ubiquitination	WEFAEWIPLAWKWHL HHHHHHHHHHHHHHH	19.66	23000965
348	Ubiquitination	SELEAAPYLPQEEKS HHHHHCCCCCHHHCC	26.70	23000965
354	Ubiquitination	PYLPQEEKSPLFSVQ CCCCHHHCCCCCEEE	57.53	23000965
360	Ubiquitination	EKSPLFSVQREGLPE HCCCCCEEEECCCCC	4.95	23000965
370	Phosphorylation	EGLPEDGTLYRINRF CCCCCCCCEEEEECC	32.70	27067055
379	Phosphorylation	YRINRFSSITAHPER EEEECCCCCCCCHHH	22.65	-
424	Ubiquitination	LFSSPDMNETHPLSQ EECCCCCCCCCCHHH	59.40	23000965
430	Ubiquitination	MNETHPLSQLHSGPG CCCCCCHHHCCCCCC	34.84	23000965
436	Ubiquitination	LSQLHSGPGLLQLWG HHHCCCCCCHHHHHC	33.02	23000965
474	Ubiquitination	NGCIWDLKFCPSGAW CCEEEEEECCCCCCC	42.31	21963094
485	Ubiquitination	SGAWELPGTPRKAPL CCCCCCCCCCCCCCC	62.06	21963094
486	Phosphorylation	GAWELPGTPRKAPLL CCCCCCCCCCCCCCC	20.27	28387310
489	Ubiquitination	ELPGTPRKAPLLPRL CCCCCCCCCCCCHHH	56.40	29967540
500	Ubiquitination	LPRLGLLALACSDGK CHHHCHHEEECCCCE	9.73	29967540
504	Phosphorylation	GLLALACSDGKVLLF CHHEEECCCCEEEEE	43.73	-
513	Ubiquitination	GKVLLFSLPHPEALL CEEEEEECCCHHHHH	3.37	21963094
589	Ubiquitination	FWNLPTNSPLQRIRL EEECCCCCCCCEEEC	29.48	21963094
597	Phosphorylation	PLQRIRLSDGSLKLY CCCEEECCCCCEEEE	30.03	30266825
600	Phosphorylation	RIRLSDGSLKLYPFQ EEECCCCCEEEECEE	27.59	30266825
602	Acetylation	RLSDGSLKLYPFQCF ECCCCCEEEECEEHH	47.90	25953088
602	Ubiquitination	RLSDGSLKLYPFQCF ECCCCCEEEECEEHH	47.90	-
623	Methylation	VRTLQWCKANSHFLV HHHHHHHHCCCCEEE	47.87	-
639	Ubiquitination	AGSDRKIKFWDLRRP CCCCCCEEEEECCCC	43.36	29967540
647	Phosphorylation	FWDLRRPYEPINSIK EEECCCCCCCHHHHH	32.31	20068231
650	Ubiquitination	LRRPYEPINSIKRFL CCCCCCCHHHHHHHH	4.16	29967540
652	Phosphorylation	RPYEPINSIKRFLST CCCCCHHHHHHHHHH	30.15	20068231
654	Ubiquitination	YEPINSIKRFLSTEL CCCHHHHHHHHHHHH	36.60	21963094
665	Ubiquitination	STELAWLLPYNGVTV HHHHHHHCCCCCEEE	2.70	21963094
693	Ubiquitination	IHYIDAGYLGFKAYF EEEEECCCCCEEEEE	12.84	21963094
756	Ubiquitination	ERRFPIYKADLIPYQ HHCCCCEECCCCCCC	35.82	21963094
762	Phosphorylation	YKADLIPYQDSPEGP EECCCCCCCCCCCCC	20.26	30278072
765	Phosphorylation	DLIPYQDSPEGPDHS CCCCCCCCCCCCCCC	14.88	23401153
767	Ubiquitination	IPYQDSPEGPDHSSA CCCCCCCCCCCCCCC	83.65	21963094
769	Ubiquitination	YQDSPEGPDHSSASS CCCCCCCCCCCCCCC	34.18	21963094
772	Phosphorylation	SPEGPDHSSASSGVP CCCCCCCCCCCCCCC	34.67	30278072
773	Phosphorylation	PEGPDHSSASSGVPN CCCCCCCCCCCCCCC	28.84	22115753
775	Phosphorylation	GPDHSSASSGVPNPP CCCCCCCCCCCCCCC	29.58	30278072
776	Phosphorylation	PDHSSASSGVPNPPK CCCCCCCCCCCCCCC	43.45	30278072
783	Ubiquitination	SGVPNPPKARTYTET CCCCCCCCCCCEEEE	52.32	29967540
794	Ubiquitination	YTETVNHHYLLFQDT EEEEECCCEEEEECC	15.10	29967540
795	Ubiquitination	TETVNHHYLLFQDTD EEEECCCEEEEECCC	9.50	21963094
831	Methylation	HSQLCLDRLQLEAIH CHHHHHHHHHHHHHH	16.04	-
839	Ubiquitination	LQLEAIHKVRFSPNL HHHHHHHCCCCCCCC	29.06	-
871	Phosphorylation	HFVRGLASPLGHRMQ EEEECCCCCCCHHCH	26.21	30266825
871	Ubiquitination	HFVRGLASPLGHRMQ EEEECCCCCCCHHCH	26.21	21963094
876	Methylation	LASPLGHRMQLESRA CCCCCCHHCHHHHHH	16.85	-
892	Phosphorylation	FNAMFQPSSPTRRPG HHHHCCCCCCCCCCC	37.86	29255136
893	Phosphorylation	NAMFQPSSPTRRPGF HHHCCCCCCCCCCCC	36.65	29255136
895	Phosphorylation	MFQPSSPTRRPGFSP HCCCCCCCCCCCCCC	41.06	22167270
901	Phosphorylation	PTRRPGFSPTSHRLL CCCCCCCCCCHHCCC	32.93	29255136
903	Phosphorylation	RRPGFSPTSHRLLPT CCCCCCCCHHCCCCC	35.65	23927012
904	Phosphorylation	RPGFSPTSHRLLPTP CCCCCCCHHCCCCCC	15.25	23927012
906	Phosphorylation	GFSPTSHRLLPTP-- CCCCCHHCCCCCC--	37.37	32645325
910	Phosphorylation	TSHRLLPTP------ CHHCCCCCC------	41.42	21406692

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 TF3C2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TF3C2_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 TF3C2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TF3C3_HUMAN	GTF3C3	physical	10373544
TF3C5_HUMAN	GTF3C5	physical	10373544
TF3C1_HUMAN	GTF3C1	physical	7729686
TF3C4_HUMAN	GTF3C4	physical	7729686
TF3C3_HUMAN	GTF3C3	physical	7729686
TF3C5_HUMAN	GTF3C5	physical	7729686
TF3C5_HUMAN	GTF3C5	physical	22939629
TF3C3_HUMAN	GTF3C3	physical	22939629
TF3C4_HUMAN	GTF3C4	physical	22939629
TF3C6_HUMAN	GTF3C6	physical	22939629
MIPT3_HUMAN	TRAF3IP1	physical	28514442
ZN496_HUMAN	ZNF496	physical	28514442
ZN638_HUMAN	ZNF638	physical	28514442
C1QBP_HUMAN	C1QBP	physical	28514442
ZN579_HUMAN	ZNF579	physical	28514442
RBM27_HUMAN	RBM27	physical	28514442
BAG1_HUMAN	BAG1	physical	28514442
RBM26_HUMAN	RBM26	physical	28514442
LS14B_HUMAN	LSM14B	physical	28514442
DDX51_HUMAN	DDX51	physical	28514442
DDX50_HUMAN	DDX50	physical	28514442
UBP15_HUMAN	USP15	physical	27173435
JIP4_HUMAN	SPAG9	physical	27173435
MCM2_HUMAN	MCM2	physical	27173435
MCM4_HUMAN	MCM4	physical	27173435

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 TF3C2_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-63 AND THR-895, AND MASSSPECTROMETRY.	19690332 [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 SER-132 AND SER-167, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-893, AND MASSSPECTROMETRY.	18220336 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-167, ANDMASS SPECTROMETRY.	16964243 [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-167 AND SER-220, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-895, AND MASSSPECTROMETRY.	18187866 [Abstract]