UniProt Accession

 TF3C1_HUMAN; Q12789; B2RP21; Q12838; Q6DKN9; Q9Y4W9 

Genbank Protein ID

 U02619; AC002303; AC025275; AC002551; BC044857; BC137229; U06485 

Genbank Nucleotide ID

 AAA17985.1; AAB67637.1; AAC05811.1; AAH44857.1; AAI37230.1; AAA85638.1 

Protein Name

 General transcription factor 3C polypeptide 1 

Protein Synonyms/Alias

 TF3C-alpha; TFIIIC box B-binding subunit; Transcription factor IIIC 220 kDa subunit; TFIIIC 220 kDa subunit; TFIIIC220; Transcription factor IIIC subunit alpha 

Gene Name

 GTF3C1 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
107	IHMILENKDGIQGSC	ubiquitination	[1]
121	CRYFKERKNITNDIR	ubiquitination	[1]
172	QEGDPDLKLPDFSYC	ubiquitination	[2]
203	DLHTTAFKVDAGKLH	ubiquitination	[1]
218	YHRKILNKNGLITMQ	ubiquitination	[1, 3]
254	FHVDRRSKYDILMEK	ubiquitination	[1, 4, 5]
323	ECGPCKTKKGTDVMV	ubiquitination	[1]
337	VRCLKLLKEFKRNDH	ubiquitination	[1]
355	EDEEVISKTVPPVDI	ubiquitination	[1]
382	LIERRGTKGISQAEI	ubiquitination	[1, 6]
397	RVAMNVGKLEARMLC	ubiquitination	[1, 6, 7]
414	LQRFKVVKGFMEDEG	ubiquitination	[1, 7]
427	EGRQRTTKYISCVFA	ubiquitination	[1]
521	TPTKGGWKVVNLHPL	ubiquitination	[4, 5]
530	VNLHPLKKQPPSFPG	ubiquitination	[1, 6]
590	EVRMENPKESSSSLK	ubiquitination	[1]
597	KESSSSLKTGRHSSG	ubiquitination	[1]
607	RHSSGQDKPHETYRL	acetylation	[6]
607	RHSSGQDKPHETYRL	ubiquitination	[8]
639	ESLFTIQKMIMDQEK	ubiquitination	[1]
646	KMIMDQEKQEGVSTK	ubiquitination	[1, 6, 7]
685	TVIQDGIKKKVDLVV	ubiquitination	[1, 6, 7]
686	VIQDGIKKKVDLVVH	ubiquitination	[1]
724	SSTANRVKTSQPPVP	ubiquitination	[1, 6, 7, 8]
770	RMKKSDNKMGITPLR	ubiquitination	[1, 6]
796	RSLGFLPKMPRLRVV	ubiquitination	[1, 6]
1090	DKHNLERKCAMLEYT	ubiquitination	[1]
1128	SSFYGHLKRNWIWTS	ubiquitination	[1, 6, 7]
1143	YIINQAKKENTAAEN	ubiquitination	[1]
1162	RLQTFLSKRPMPLSA	ubiquitination	[1]
1242	EFPGEKSKRLRYHDE	acetylation	[9]
1286	ASNVLNTKVKGPFVT	ubiquitination	[1]
1288	NVLNTKVKGPFVTWQ	ubiquitination	[1]
1325	RRARYIVKNPQAYLN	ubiquitination	[1]
1344	LAEVYQDKALVGDFM	ubiquitination	[1]
1377	FVEKLKEKFSSALRN	ubiquitination	[1]
1409	VLAIGDEKDQTRKED	ubiquitination	[1, 6]
1473	KAFMECQKRSLVNRR	ubiquitination	[1]
1535	DRMRAAGKLDQPDRF	ubiquitination	[1, 6, 7, 8]
1608	EVIKSLGKDGSLEDD	ubiquitination	[1, 6, 7, 8]
1629	LDEGVGGKRRSMEVK	ubiquitination	[7, 8, 10]
1636	KRRSMEVKPAQASHT	ubiquitination	[1, 6]
1676	VVNSCQMKFQLRCTP	ubiquitination	[1, 6]
1771	RRFSALEKAGGGRTR	ubiquitination	[1, 6, 7, 8]
1820	LLHSVRLKDREDADI	ubiquitination	[1, 7]
2105	PHEVNWNKWIHL***	ubiquitination	[1]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [7] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [8] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [9] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [10] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 

Functional 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. 

Sequence Annotation

 MOD_RES 667 667 Phosphoserine.
 MOD_RES 739 739 Phosphoserine.
 MOD_RES 1062 1062 Phosphoserine.
 MOD_RES 1068 1068 Phosphoserine.
 MOD_RES 1632 1632 Phosphoserine.
 MOD_RES 1653 1653 Phosphoserine.
 MOD_RES 1856 1856 Phosphoserine.
 MOD_RES 1865 1865 Phosphoserine.
 MOD_RES 1868 1868 Phosphoserine.
 MOD_RES 1969 1969 Phosphoserine.  

Keyword

 Alternative splicing; Complete proteome; Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 2109 AA 

Protein Sequence

Gene Ontology

 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0030529; C:ribonucleoprotein complex; IEA:Compara.
 GO:0000127; C:transcription factor TFIIIC complex; IDA:HGNC.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0042791; P:5S class rRNA transcription from RNA polymerase III type 1 promoter; IC:HGNC.
 GO:0042797; P:tRNA transcription from RNA polymerase III promoter; IC:HGNC. 

Interpro

 IPR007309; TFIIIC_Bblock-bd. 

Pfam

 PF04182; B-block_TFIIIC 

SMART

  

PROSITE

  

PRINTS