CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023107
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 General transcription factor 3C polypeptide 4 
Protein Synonyms/Alias
 TF3C-delta; Transcription factor IIIC 90 kDa subunit; TFIIIC 90 kDa subunit; TFIIIC90; Transcription factor IIIC subunit delta 
Gene Name
 GTF3C4 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
33GGGEAGGKEPAADAAubiquitination[1, 2]
59TRREPAVKLQYAVSGubiquitination[2, 3]
119PLNSCLLKVGSKTEVubiquitination[3]
123CLLKVGSKTEVAECKubiquitination[3]
137KEKFAASKDPTVSQTubiquitination[1, 3]
156RVFNPEGKALPPMRGubiquitination[3]
165LPPMRGFKYTSWSPMubiquitination[3]
225ETSYRLSKNEAPEGNubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9]
348KILPVNLKAVKGYFTubiquitination[9, 10, 11]
351PVNLKAVKGYFTLRQubiquitination[3]
364RQPVILWKEMDQLPVubiquitination[3, 10, 11]
446YTCSSDGKVRQLIPIubiquitination[9]
460IFTDVALKFEHQLIKubiquitination[3]
467KFEHQLIKLSDVFGSubiquitination[8, 10, 11]
598TPSEALWKPTHEDSKubiquitination[1]
629QEEGTSSKQVVKQGLubiquitination[1, 2, 3]
633TSSKQVVKQGLQERSubiquitination[3]
641QGLQERSKEGDVEEPubiquitination[3]
760ILPFTDRKQAVCSNGubiquitination[3, 9]
807PEDPDWIKRLLQSPCubiquitination[1, 2, 3, 4, 5, 9]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [7] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] 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
Functional Description
 Essential for RNA polymerase III to make a number of small nuclear and cytoplasmic RNAs, including 5S RNA, tRNA, and adenovirus-associated (VA) RNA of both cellular and viral origin. Has histone acetyltransferase activity (HAT) with unique specificity for free and nucleosomal H3. May cooperate with GTF3C5 in facilitating the recruitment of TFIIIB and RNA polymerase through direct interactions with BRF1, POLR3C and POLR3F. May be localized close to the A box. 
Sequence Annotation
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 611 611 Phosphoserine.  
Keyword
 Acetylation; Acyltransferase; Complete proteome; Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 822 AA 
Protein Sequence
MNTADQARVG PADDGPAPSG EEEGEGGGEA GGKEPAADAA PGPSAAFRLM VTRREPAVKL 60
QYAVSGLEPL AWSEDHRVSV STARSIAVLE LICDVHNPGQ DLVIHRTSVP APLNSCLLKV 120
GSKTEVAECK EKFAASKDPT VSQTFMLDRV FNPEGKALPP MRGFKYTSWS PMGCDANGRC 180
LLAALTMDNR LTIQANLNRL QWVQLVDLTE IYGERLYETS YRLSKNEAPE GNLGDFAEFQ 240
RRHSMQTPVR MEWSGICTTQ QVKHNNECRD VGSVLLAVLF ENGNIAVWQF QLPFVGKESI 300
SSCNTIESGI TSPSVLFWWE YEHNNRKMSG LIVGSAFGPI KILPVNLKAV KGYFTLRQPV 360
ILWKEMDQLP VHSIKCVPLY HPYQKCSCSL VVAARGSYVF WCLLLISKAG LNVHNSHVTG 420
LHSLPIVSMT ADKQNGTVYT CSSDGKVRQL IPIFTDVALK FEHQLIKLSD VFGSVRTHGI 480
AVSPCGAYLA IITTEGMING LHPVNKNYQV QFVTLKTFEE AAAQLLESSV QNLFKQVDLI 540
DLVRWKILKD KHIPQFLQEA LEKKIESSGV TYFWRFKLFL LRILYQSMQK TPSEALWKPT 600
HEDSKILLVD SPGMGNADDE QQEEGTSSKQ VVKQGLQERS KEGDVEEPTD DSLPTTGDAG 660
GREPMEEKLL EIQGKIEAVE MHLTREHMKR VLGEVYLHTW ITENTSIPTR GLCNFLMSDE 720
EYDDRTARVL IGHISKKMNK QTFPEHCSLC KEILPFTDRK QAVCSNGHIW LRCFLTYQSC 780
QSLIYRRCLL HDSIARHPAP EDPDWIKRLL QSPCPFCDSP VF 822 
Gene Ontology
 GO:0000127; C:transcription factor TFIIIC complex; IDA:HGNC.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0008047; F:enzyme activator activity; TAS:ProtInc.
 GO:0004402; F:histone acetyltransferase activity; TAS:ProtInc.
 GO:0042791; P:5S class rRNA transcription from RNA polymerase III type 1 promoter; IC:HGNC.
 GO:0006384; P:transcription initiation from RNA polymerase III promoter; TAS:ProtInc.
 GO:0042797; P:tRNA transcription from RNA polymerase III promoter; IC:HGNC. 
Interpro
 IPR024761; TFIIIC_delta_N.
 IPR024764; TFIIIC_Znf. 
Pfam
 PF12657; TFIIIC_delta
 PF12660; zf-TFIIIC 
SMART
  
PROSITE
  
PRINTS