CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001214
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L 
Protein Synonyms/Alias
 PCAF-associated factor 65 beta; PAF65-beta 
Gene Name
 TAF5L 
Gene Synonyms/Alias
 PAF65B 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
30VDSDGPLKQGLRLSQubiquitination[1]
247EVLQESIKRVKDGPPubiquitination[2]
481LAFSPNGKYLASAGEubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9, 10]
504LASGTLYKELRGHTDubiquitination[1]
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] 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]
 [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] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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
 Functions as a component of the PCAF complex. The PCAF complex is capable of efficiently acetylating histones in a nucleosomal context. The PCAF complex could be considered as the human version of the yeast SAGA complex. 
Sequence Annotation
 REPEAT 266 305 WD 1.
 REPEAT 340 379 WD 2.
 REPEAT 382 421 WD 3.
 REPEAT 424 463 WD 4.
 REPEAT 466 505 WD 5.
 REPEAT 508 547 WD 6.  
Keyword
 Alternative splicing; Complete proteome; Direct protein sequencing; Nucleus; Reference proteome; Repeat; Transcription; Transcription regulation; WD repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 589 AA 
Protein Sequence
MKRVRTEQIQ MAVSCYLKRR QYVDSDGPLK QGLRLSQTAE EMAANLTVQS ESGCANIVSA 60
APCQAEPQQY EVQFGRLRNF LTDSDSQHSH EVMPLLYPLF VYLHLNLVQN SPKSTVESFY 120
SRFHGMFLQN ASQKDVIEQL QTTQTIQDIL SNFKLRAFLD NKYVVRLQED SYNYLIRYLQ 180
SDNNTALCKV LTLHIHLDVQ PAKRTDYQLY ASGSSSRSEN NGLEPPDMPS PILQNEAALE 240
VLQESIKRVK DGPPSLTTIC FYAFYNTEQL LNTAEISPDS KLLAAGFDNS CIKLWSLRSK 300
KLKSEPHQVD VSRIHLACDI LEEEDDEDDN AGTEMKILRG HCGPVYSTRF LADSSGLLSC 360
SEDMSIRYWD LGSFTNTVLY QGHAYPVWDL DISPYSLYFA SGSHDRTARL WSFDRTYPLR 420
IYAGHLADVD CVKFHPNSNY LATGSTDKTV RLWSAQQGNS VRLFTGHRGP VLSLAFSPNG 480
KYLASAGEDQ RLKLWDLASG TLYKELRGHT DNITSLTFSP DSGLIASASM DNSVRVWDIR 540
NTYCSAPADG SSSELVGVYT GQMSNVLSVQ FMACNLLLVT GITQENQEH 589 
Gene Ontology
 GO:0030914; C:STAGA complex; IDA:UniProtKB.
 GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
 GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
 GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
 GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc. 
Interpro
 IPR020472; G-protein_beta_WD-40_rep.
 IPR007582; TFIID-su_WD40-assoc_reg.
 IPR015943; WD40/YVTN_repeat-like_dom.
 IPR001680; WD40_repeat.
 IPR019775; WD40_repeat_CS.
 IPR017986; WD40_repeat_dom. 
Pfam
 PF04494; TFIID_90kDa
 PF00400; WD40 
SMART
 SM00320; WD40 
PROSITE
 PS00678; WD_REPEATS_1
 PS50082; WD_REPEATS_2
 PS50294; WD_REPEATS_REGION 
PRINTS
 PR00320; GPROTEINBRPT.