TF3C1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TF3C1_MOUSE
• UniProt AC: Q8K284
• Protein Name: General transcription factor 3C polypeptide 1
• Gene Name: Gtf3c1
• Organism: Mus musculus (Mouse).
• Sequence Length: 2101
• 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. Binds to the box B promoter element (By similarity)..
• Protein Sequence: MDALESLLDEVALEGLDGLCLPALWSRLESRSPAFPLPLEPYTQEFLWRALATHPGISFYEEPRERPDLQLQDRYEEIDLETGILESRRDPVTLEDVYPIHMILENKDGIQGSCRYFKERKDITSSIRSKCLQPRCTMVEAFSRWGKKLIIVASQDMRYRALIGLEGDPDLKLPDFSYCILERLGRSRWQGELQRDLHTTAFKVDAGKLHYHRKILNKNGLITMQSHVIRLPTGAQQHSILLLLNRFHVDRRSKYDILMEKLSMMLSTRSNQIETLGKLREELGLCERTFKRLYQYMLNAGLAKVVSLPLQEIHPECGPCKTKKGTDVMVRCLKLLKEFKRKMEDDHDDDDDEEVISKGVPPVDIVFERDMLTQTYELIERRGTKGISQAEIRVAMNVGKLEARMLCRLLQRFKVVKGFMEDEGRQRTTKYISCVFAEESDLSRQYAREKARGELLTTVSLASVQDESLMPEGEEAFLSDSESEEESSCSGGKRRGRGSRGHARASGDAGSGSRPHHSTPAKGGWKVLNLHPLKKPKAAAEERSRRSSACRDGLDTSSSSELNAPFDPHSMDSHSGDIAVIEEVRLDNPKEGGGSQKGGRHGSSQDKPHKTYRLLKRRNLIIEAVTNLRLIESLFTIQKMIMDQEKQEGVSTKCCKKSIIRLVRNLSEEGLLRLYRTTVIQDGIKKKVDLVVHPSMDQNDPLVRSAIEQVRFRISNSSTANRVKVPPAPAPQEEAEEENQEPEVPSRSANSDPNTSSKPESTRVKKTDEKMGITPLKNYKPVIVPGLGRSIGFLPKMPRLKAMHLFLWYLVYGHPAGHTGEQPALHSERKTGKQESSRPGAQPSSGDDWDTSEAKNNTESSSWESEMELSTEIVYVDEISWMRYVPPIPIHRDFGFGWALVSDILLCLPLSIFVQLVQVSYKVDNLEDFLNDPLKKHTLIRFLPRHIRQQLLYKRRYIFSVVENLQRLCYMGLLQFGPTEKFQDKDQVFVFLKKNAVIVDTTICDPHYNLAHSSRPFERRLYVLDSMQDVECYWFDLQCICLNTPLGVVRCPCAQKICPDPGSDPEGSLRKEQESAMDKHNLERKCAMLEYTTGSREVVDEGLVPGDGLGAAGLDSSFYAHLKRNWVWTSYIINKARKNNTSENGLTGRLQTFLSKRPMPLGSGGSGRLPLWSEGRADAELCADKEEQFELDREPTPGRNRKVRGGKSQKRKRLKKEPIRKTKRRRRGEHPEAKSKKLRYQDEADQNALRMMTRLRVSWSMQEDGLLMLCRIASNVLNTKVKGPFVTWQVVRDILHATFEESLDKTSHSVGRRARYIVKNPQAFMNYKVCLAEVYQDKALVGDFMSRKGNYEDPKVCAKEFKEFVEKLKEKFSSGLRNPNLEIPNTLQELFAKYRVLAIGDEKDRVRKEDELNSVEDIHFLVLQNLIQSTLSLSNSQSNSCQSFQIFRLYREFREPVLVRAFMECQKRSLVNRRRVSHSQGPKKNRAVPFVPMSYQLSQSYYKLFTWRFPTTICTESFQFYDRLRTNGMLDQPDHFSFKDLDSSDPSNDLVAFSLDSPGGHCVTALALFSLGLLSVDVRIPEQIVVVDSSMVESEVMKSLGKDGGLDDDEEEEDLDEGSGTKRQGVEVKAHQASHTKYLLMRGYYTVPGMVSTRNLNPNDSIVVNSCQVKFRLRNTPASTQLGPTGFTATPLEELQAGLSCLPASFTSLVDPQLRTHCPEEFAHQMAQSGYSPEDVAASLEILQAVAAADCFGIDKEKLSRQFSALEKIADRRTRTFLDYIQDLLEQEQVMEVGGNTVRLVTMASAQPWLLHSMRLRDMEVDTKASGDDSQSRLPEGPSIEDHTSEGAAVPPVSSHSTKKRPHCPETDAEEATRLPAKKPTLQDVRVAASPRPGAEEQAEAQAPAQLAAPEDADAGGPRQENQENVGVSGLEQLGCEFQLPEGSEDPRGLTESNMAQAAWESGCERVCFVGRPWRGVDGHLNMPVCKGMLEAVLYHIMSRPGVPESCLLQYYQGVLQPVAVLELLRGLESLGCIQKRTLRKPASVSLFSRPVVEGLGQASEAEALSCHESTVTFYEPTLDCTIRLGRVFPHDINWNKWIHL

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
218	Ubiquitination	YHRKILNKNGLITMQ HHHHHCCCCCCEEEE	49.28	-
323	Acetylation	ECGPCKTKKGTDVMV CCCCCCCCCCHHHHH	34.40	7613329
506	Phosphorylation	SRGHARASGDAGSGS CCCCCCCCCCCCCCC	31.49	27717184
519	Phosphorylation	GSRPHHSTPAKGGWK CCCCCCCCCCCCCCE	23.94	25266776
667	Phosphorylation	IRLVRNLSEEGLLRL HHHHHCCCHHHHHHH	36.83	22817900
685	Ubiquitination	TVIQDGIKKKVDLVV HEECCCHHHEECEEE	52.66	27667366
724	Ubiquitination	SSTANRVKVPPAPAP CCCCCCCCCCCCCCC	45.87	-
774	Phosphorylation	TDEKMGITPLKNYKP CCCCCCCCCCCCCCC	19.48	22006019
779	Phosphorylation	GITPLKNYKPVIVPG CCCCCCCCCCEEECC	18.32	24759943
827	Phosphorylation	GEQPALHSERKTGKQ CCCCCCCCCCCCCCC	39.69	23737553
833	Sumoylation	HSERKTGKQESSRPG CCCCCCCCCCCCCCC	57.00	28289178
836	Phosphorylation	RKTGKQESSRPGAQP CCCCCCCCCCCCCCC	29.20	30635358
837	Phosphorylation	KTGKQESSRPGAQPS CCCCCCCCCCCCCCC	41.56	30635358
844	Phosphorylation	SRPGAQPSSGDDWDT CCCCCCCCCCCCCCC	34.57	26643407
845	Phosphorylation	RPGAQPSSGDDWDTS CCCCCCCCCCCCCCH	53.58	26643407
851	Phosphorylation	SSGDDWDTSEAKNNT CCCCCCCCHHHCCCC	24.98	26643407
852	Phosphorylation	SGDDWDTSEAKNNTE CCCCCCCHHHCCCCC	32.84	30635358
1063	Phosphorylation	KICPDPGSDPEGSLR HHCCCCCCCCCCCCH	56.21	30352176
1068	Phosphorylation	PGSDPEGSLRKEQES CCCCCCCCCHHHHHH	24.28	28066266
1123	Ubiquitination	SSFYAHLKRNWVWTS HHHHHHHHHHHHHHH	33.54	-
1142	Phosphorylation	KARKNNTSENGLTGR HHHHCCCCCCCCCHH	31.05	20495213
1155	Phosphorylation	GRLQTFLSKRPMPLG HHHHHHHHCCCCCCC	23.56	-
1163	Phosphorylation	KRPMPLGSGGSGRLP CCCCCCCCCCCCCCC	47.89	24759943
1173	Phosphorylation	SGRLPLWSEGRADAE CCCCCCCCCCCCCHH	37.54	28066266
1196	Phosphorylation	FELDREPTPGRNRKV CCCCCCCCCCCCCCC	33.35	26824392
1307	Phosphorylation	EESLDKTSHSVGRRA HHHHHCCCCCHHHHH	21.36	-
1316	Phosphorylation	SVGRRARYIVKNPQA CHHHHHHHHHCCHHH	14.74	-
1327	Phosphorylation	NPQAFMNYKVCLAEV CHHHHHCHHHHHHHH	7.94	-
1335	Phosphorylation	KVCLAEVYQDKALVG HHHHHHHHCCHHHHH	11.51	-
1393	Ubiquitination	TLQELFAKYRVLAIG HHHHHHHHHCCEECC	26.67	-
1477	Phosphorylation	LVNRRRVSHSQGPKK HHHCCCCCCCCCCCC	18.66	24719451
1638	Phosphorylation	HQASHTKYLLMRGYY EHHHCCCEEECCCCE	13.26	28576409
1670	Ubiquitination	VVNSCQVKFRLRNTP EEECEEEEEEECCCC	10.01	-
1802	Phosphorylation	GNTVRLVTMASAQPW CCEEEEEEHHHCCHH	16.18	25338131
1805	Phosphorylation	VRLVTMASAQPWLLH EEEEEHHHCCHHHHH	19.33	25338131
1830	Phosphorylation	TKASGDDSQSRLPEG CCCCCCCHHHCCCCC	34.49	25338131
1832	Phosphorylation	ASGDDSQSRLPEGPS CCCCCHHHCCCCCCC	39.47	25338131
1854	Phosphorylation	GAAVPPVSSHSTKKR CCCCCCCCCCCCCCC	28.27	-
1890	Phosphorylation	QDVRVAASPRPGAEE HHCCHHCCCCCCHHH	16.23	27087446

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of TF3C1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TF3C1_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of TF3C1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TOX3_MOUSE	Tox3	physical	20211142

Drug and Disease Associations

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