CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013471
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 TATA box-binding protein-associated factor RNA polymerase I subunit B 
Protein Synonyms/Alias
 RNA polymerase I-specific TBP-associated factor 63 kDa; TAFI63; TATA box-binding protein-associated factor 1B; TBP-associated factor 1B; Transcription initiation factor SL1/TIF-IB subunit B 
Gene Name
 TAF1B 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
56LIPNTQIKALNRGLKubiquitination[1, 2, 3, 4]
431KYLWKSEKPLYYSFVubiquitination[1, 4]
440LYYSFVDKPVAYKKRacetylation[5, 6, 7, 8]
440LYYSFVDKPVAYKKRubiquitination[9]
508KGQSLLTKNSLYWLSubiquitination[1, 4]
Reference
 [1] 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]
 [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] 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] 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]
 [5] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [6] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [7] 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]
 [8] 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]
 [9] 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
Functional Description
 Component of RNA polymerase I core factor complex that acts as a GTF2B/TFIIB-like factor and plays a key role in multiple steps during trancription initiation such as preinitiation complex (PIC) assembly and postpolymerase recruitment events in polymerase I (Pol I) transcription. Binds rDNA promoters and plays a role in Pol I recruitment as a component of the SL1/TIF-IB complex and, possibly, directly through its interaction with RRN3. 
Sequence Annotation
 ZN_FING 4 39 RRN7-type.
 REGION 40 68 B-reader.
 REGION 69 73 B-linker.
 REGION 74 261 N-terminal cyclin fold.
 REGION 262 372 C-terminal cyclin fold.
 METAL 13 13 Zinc (Probable).
 METAL 16 16 Zinc (Probable).
 METAL 31 31 Zinc (Probable).
 METAL 34 34 Zinc (Probable).
 MOD_RES 440 440 N6-acetyllysine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; DNA-binding; Metal-binding; Nucleus; Polymorphism; Reference proteome; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 588 AA 
Protein Sequence
MDLEEAEEFK ERCTQCAAVS WGLTDEGKYY CTSCHNVTER YQEVTNTDLI PNTQIKALNR 60
GLKKKNNTEK GWDWYVCEGF QYILYQQAEA LKNLGVGPEL KNDVLHNFWK RYLQKSKQAY 120
CKNPVYTTGR KPTVLEDNLS HSDWASEPEL LSDVSCPPFL ESGAESQSDI HTRKPFPVSK 180
ASQSETSVCS GSLDGVEYSQ RKEKGIVKMT MPQTLAFCYL SLLWQREAIT LSDLLRFVEE 240
DHIPYINAFQ HFPEQMKLYG RDRGIFGIES WPDYEDIYKK TVEVGTFLDL PRFPDITEDC 300
YLHPNILCMK YLMEVNLPDE MHSLTCHVVK MTGMGEVDFL TFDPIAKMAK TVKYDVQAVA 360
IIVVVLKLLF LLDDSFEWSL SNLAEKHNEK NKKDKPWFDF RKWYQIMKKA FDEKKQKWEE 420
ARAKYLWKSE KPLYYSFVDK PVAYKKREMV VNLQKQFSTL VESTATAGKK SPSSFQFNWT 480
EEDTDRTCFH GHSLQGVLKE KGQSLLTKNS LYWLSTQKFC RCYCTHVTTY EESNYSLSYQ 540
FILNLFSFLL RIKTSLLHEE VSLVEKKLFE KKYSVKRKKS RSKKVRRH 588 
Gene Ontology
 GO:0070860; C:RNA polymerase I core factor complex; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0001164; F:RNA polymerase I CORE element sequence-specific DNA binding; IDA:UniProtKB.
 GO:0001187; F:RNA polymerase I CORE element sequence-specific DNA binding transcription factor recruiting transcription factor activity; IDA:UniProtKB.
 GO:0017025; F:TBP-class protein binding; TAS:UniProtKB.
 GO:0006363; P:termination of RNA polymerase I transcription; TAS:Reactome.
 GO:0006362; P:transcription elongation from RNA polymerase I promoter; TAS:Reactome. 
Interpro
 IPR021752; TF_Rrn7. 
Pfam
 PF11781; RRN7 
SMART
  
PROSITE
  
PRINTS