CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012692
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transcription initiation factor TFIID subunit 9 
Protein Synonyms/Alias
 RNA polymerase II TBP-associated factor subunit G; STAF31/32; Transcription initiation factor TFIID 31 kDa subunit; TAFII-31; TAFII31; Transcription initiation factor TFIID 32 kDa subunit; TAFII-32; TAFII32 
Gene Name
 TAF9 
Gene Synonyms/Alias
 TAF2G; TAFII31 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MESGKTASPKSMacetylation[1]
5***MESGKTASPKSMubiquitination[2, 3]
10SGKTASPKSMPKDAQubiquitination[3]
14ASPKSMPKDAQMMAQubiquitination[3]
24QMMAQILKDMGITEYubiquitination[3, 4]
55TTILDDAKIYSSHAKubiquitination[3]
63IYSSHAKKATVDADDubiquitination[3]
108QTPLPLIKPYSGPRLacetylation[1]
108QTPLPLIKPYSGPRLubiquitination[2, 3, 5, 6, 7]
245NESSNALKRKREDDDubiquitination[3]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [5] 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]
 [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] 
Functional Description
 Essential for cell viability. TAF9 and TAF9B are involved in transcriptional activation as well as repression of distinct but overlapping sets of genes. May have a role in gene regulation associated with apoptosis. TAFs are components of the transcription factor IID (TFIID) complex, the TBP-free TAFII complex (TFTC), the PCAF histone acetylase complex and the STAGA transcription coactivator-HAT complex. TFIID or TFTC are essential for the regulation of RNA polymerase II-mediated transcription. 
Sequence Annotation
 DNA_BIND 120 137
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 5 5 N6-acetyllysine.
 MOD_RES 149 149 Phosphoserine.
 MOD_RES 158 158 Phosphoserine.
 MOD_RES 159 159 Phosphothreonine.
 MOD_RES 161 161 Phosphothreonine.
 MOD_RES 178 178 Phosphothreonine.
 MOD_RES 181 181 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 264 AA 
Protein Sequence
MESGKTASPK SMPKDAQMMA QILKDMGITE YEPRVINQML EFAFRYVTTI LDDAKIYSSH 60
AKKATVDADD VRLAIQCRAD QSFTSPPPRD FLLDIARQRN QTPLPLIKPY SGPRLPPDRY 120
CLTAPNYRLK SLQKKASTSA GRITVPRLSV GSVTSRPSTP TLGTPTPQTM SVSTKVGTPM 180
SLTGQRFTVQ MPTSQSPAVK ASIPATSAVQ NVLINPSLIG SKNILITTNM MSSQNTANES 240
SNALKRKRED DDDDDDDDDD YDNL 264 
Gene Ontology
 GO:0071339; C:MLL1 complex; IDA:UniProtKB.
 GO:0000125; C:PCAF complex; IDA:UniProtKB.
 GO:0070761; C:pre-snoRNP complex; IDA:BHF-UCL.
 GO:0030914; C:STAGA complex; IDA:UniProtKB.
 GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
 GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB.
 GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
 GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
 GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
 GO:0043066; P:negative regulation of apoptotic process; IMP:BHF-UCL.
 GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
 GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
 GO:0060760; P:positive regulation of response to cytokine stimulus; IMP:BHF-UCL.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
 GO:0006974; P:response to DNA damage stimulus; IC:BHF-UCL.
 GO:0070555; P:response to interleukin-1; IMP:BHF-UCL.
 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. 
Interpro
 IPR009072; Histone-fold.
 IPR003162; TFIID-31. 
Pfam
 PF02291; TFIID-31kDa 
SMART
  
PROSITE
  
PRINTS