CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010758
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transcription initiation factor IIB 
Protein Synonyms/Alias
 General transcription factor TFIIB; S300-II 
Gene Name
 GTF2B 
Gene Synonyms/Alias
 TF2B; TFIIB 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
59WRTFSNDKATKDPSRubiquitination[1]
86DLSTMIGKGTGAASFubiquitination[2, 3]
100FDEFGNSKYQNRRTMubiquitination[1, 2, 4, 5, 6, 7]
119RAMMNAFKEITTMADubiquitination[1, 2, 3, 5, 6]
143DRTNNLFKQVYEQKSubiquitination[1, 4, 7]
149FKQVYEQKSLKGRANubiquitination[1]
178EGVPRTFKEICAVSRubiquitination[1, 6]
238AATHIARKAVELDLVacetylation[8]
238AATHIARKAVELDLVubiquitination[1]
272SAEKRTQKEIGDIAGubiquitination[1]
305DLFPTDFKFDTPVDKubiquitination[1, 2]
312KFDTPVDKLPQL***ubiquitination[2]
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] 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] 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]
 [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] 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]
 [6] 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]
 [7] 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]
 [8] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional Description
 General factor that plays a major role in the activation of eukaryotic genes transcribed by RNA polymerase II. 
Sequence Annotation
 REPEAT 124 200 1.
 REPEAT 218 294 2.
 ZN_FING 11 42 TFIIB-type.
 METAL 15 15 Zinc.
 METAL 18 18 Zinc.
 METAL 34 34 Zinc.
 METAL 37 37 Zinc.
 MOD_RES 76 76 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; Host-virus interaction; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 316 AA 
Protein Sequence
MASTSRLDAL PRVTCPNHPD AILVEDYRAG DMICPECGLV VGDRVIDVGS EWRTFSNDKA 60
TKDPSRVGDS QNPLLSDGDL STMIGKGTGA ASFDEFGNSK YQNRRTMSSS DRAMMNAFKE 120
ITTMADRINL PRNIVDRTNN LFKQVYEQKS LKGRANDAIA SACLYIACRQ EGVPRTFKEI 180
CAVSRISKKE IGRCFKLILK ALETSVDLIT TGDFMSRFCS NLCLPKQVQM AATHIARKAV 240
ELDLVPGRSP ISVAAAAIYM ASQASAEKRT QKEIGDIAGV ADVTIRQSYR LIYPRAPDLF 300
PTDFKFDTPV DKLPQL 316 
Gene Ontology
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0003677; F:DNA binding; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
 GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
 GO:0022415; P:viral reproductive process; TAS:Reactome.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR013763; Cyclin-like.
 IPR000812; TFIIB.
 IPR023486; TFIIB_CS.
 IPR013150; TFIIB_cyclin.
 IPR013137; Znf_TFIIB. 
Pfam
 PF08271; TF_Zn_Ribbon
 PF00382; TFIIB 
SMART
 SM00385; CYCLIN 
PROSITE
 PS00782; TFIIB
 PS51134; ZF_TFIIB 
PRINTS
 PR00685; TIFACTORIIB.