CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023926
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 General transcription factor 3C polypeptide 3 
Protein Synonyms/Alias
 Transcription factor IIIC 102 kDa subunit; TFIIIC 102 kDa subunit; TFIIIC102; Transcription factor IIIC subunit gamma; TF3C-gamma 
Gene Name
 GTF3C3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
41KSLQEKGKLSAEENPacetylation[1]
41KSLQEKGKLSAEENPubiquitination[2, 3, 4, 5]
63SSGINSTKSQDKDVNubiquitination[2]
67NSTKSQDKDVNEGETubiquitination[4, 6]
234SLEQDNIKQAIFCYTubiquitination[4]
242QAIFCYTKALKYEPTubiquitination[4]
245FCYTKALKYEPTNVRubiquitination[2, 3, 4, 6]
268YEQMGDHKMAMDGYRubiquitination[2, 4, 6]
298QLARDMAKSYYEANDubiquitination[2, 4, 5]
344ISNKQYDKALEIITDubiquitination[4]
359FSGIVLEKKTSEEGTubiquitination[2, 4]
360SGIVLEKKTSEEGTSubiquitination[4]
467LRHAECLKALGYMERubiquitination[4]
481RAAESYGKVVDLAPLubiquitination[2, 3, 4, 5, 6]
508QQLGQPEKALEALEPubiquitination[2]
534NAAQQELKLLLHRSTubiquitination[5]
580VCLISSSKSGERHLYubiquitination[4]
590ERHLYLIKVSRDKISubiquitination[4]
595LIKVSRDKISDSNDQubiquitination[2]
699MVMENVNKPQLWNIFubiquitination[5]
728FCLRLMLKNPENHALubiquitination[4, 6]
Reference
 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [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] 
Functional Description
 Involved in RNA polymerase III-mediated transcription. Integral, tightly associated component of the DNA-binding TFIIIC2 subcomplex that directly binds tRNA and virus-associated RNA promoters. 
Sequence Annotation
 REPEAT 149 182 TPR 1.
 REPEAT 183 216 TPR 2.
 REPEAT 217 250 TPR 3.
 REPEAT 252 284 TPR 4.
 REPEAT 290 323 TPR 5.
 REPEAT 326 361 TPR 6.
 REPEAT 421 454 TPR 7.
 REPEAT 456 489 TPR 8.
 REPEAT 491 523 TPR 9.
 REPEAT 733 766 TPR 10.
 REPEAT 811 844 TPR 11.
 MOD_RES 43 43 Phosphoserine.  
Keyword
 Alternative splicing; Complete proteome; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; TPR repeat; Transcription. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 886 AA 
Protein Sequence
MSGFSPELID YLEGKISFEE FERRREERKT REKKSLQEKG KLSAEENPDD SEVPSSSGIN 60
STKSQDKDVN EGETSDGVRK SVHKVFASML GENEDDEEEE EEEEEEEEEE ETPEQPTAGD 120
VFVLEMVLNR ETKKMMKEKR PRSKLPRALR GLMGEANIRF ARGEREEAIL MCMEIIRQAP 180
LAYEPFSTLA MIYEDQGDME KSLQFELIAA HLNPSDTEEW VRLAEMSLEQ DNIKQAIFCY 240
TKALKYEPTN VRYLWERSSL YEQMGDHKMA MDGYRRILNL LSPSDGERFM QLARDMAKSY 300
YEANDVTSAI NIIDEAFSKH QGLVSMEDVN IAAELYISNK QYDKALEIIT DFSGIVLEKK 360
TSEEGTSEEN KAPENVTCTI PDGVPIDITV KLMVCLVHLN ILEPLNPLLT TLVEQNPEDM 420
GDLYLDVAEA FLDVGEYNSA LPLLSALVCS ERYNLAVVWL RHAECLKALG YMERAAESYG 480
KVVDLAPLHL DARISLSTLQ QQLGQPEKAL EALEPMYDPD TLAQDANAAQ QELKLLLHRS 540
TLLFSQGKMY GYVDTLLTML AMLLKVAMNR AQVCLISSSK SGERHLYLIK VSRDKISDSN 600
DQESANCDAK AIFAVLTSVL TKDDWWNLLL KAIYSLCDLS RFQEAELLVD SSLEYYSFYD 660
DRQKRKELEY FGLSAAILDK NFRKAYNYIR IMVMENVNKP QLWNIFNQVT MHSQDVRHHR 720
FCLRLMLKNP ENHALCVLNG HNAFVSGSFK HALGQYVQAF RTHPDEPLYS FCIGLTFIHM 780
ASQKYVLRRH ALIVQGFSFL NRYLSLRGPC QESFYNLGRG LHQLGLIHLA IHYYQKALEL 840
PPLVVEGIEL DQLDLRRDIA YNLSLIYQSS GNTGMAQTLL YTYCSI 886 
Gene Ontology
 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
 IPR001440; TPR-1.
 IPR013026; TPR-contain_dom.
 IPR011990; TPR-like_helical.
 IPR019734; TPR_repeat. 
Pfam
 PF00515; TPR_1
 PF13181; TPR_8 
SMART
 SM00028; TPR 
PROSITE
 PS50005; TPR
 PS50293; TPR_REGION 
PRINTS