CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004995
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transcription initiation factor TFIID subunit 1 
Protein Synonyms/Alias
 Cell cycle gene 1 protein; TBP-associated factor 250 kDa; p250; Transcription initiation factor TFIID 250 kDa subunit; TAF(II)250; TAFII-250; TAFII250 
Gene Name
 TAF1 
Gene Synonyms/Alias
 BA2R; CCG1; CCGS; TAF2A 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
237FPEFRPGKVLRFLRLubiquitination[1]
249LRLFGPGKNVPSVWRubiquitination[1, 2]
330QSTGDIDKVTDTKPRubiquitination[1]
335IDKVTDTKPRVAEWRubiquitination[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] 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
 Largest component and core scaffold of the TFIID basal transcription factor complex. Contains novel N- and C-terminal Ser/Thr kinase domains which can autophosphorylate or transphosphorylate other transcription factors. Phosphorylates TP53 on 'Thr-55' which leads to MDM2-mediated degradation of TP53. Phosphorylates GTF2A1 and GTF2F1 on Ser residues. Possesses DNA- binding activity. Essential for progression of the G1 phase of the cell cycle. 
Sequence Annotation
 DOMAIN 1 414 Protein kinase 1.
 DOMAIN 1397 1467 Bromo 1.
 DOMAIN 1425 1872 Protein kinase 2.
 DOMAIN 1520 1590 Bromo 2.
 DNA_BIND 1195 1273 HMG box.
 REGION 1342 1629 Interaction with ASF1A and ASF1B.
 MOTIF 1351 1358 Nuclear localization signal (Potential).
 MOD_RES 137 137 Phosphoserine; by autocatalysis.
 MOD_RES 307 307 Phosphoserine; by autocatalysis.
 MOD_RES 1826 1826 Phosphoserine.
 DISULFID 1364 1619  
Keyword
 3D-structure; Alternative splicing; ATP-binding; Bromodomain; Cell cycle; Complete proteome; Disulfide bond; DNA-binding; Dystonia; Host-virus interaction; Kinase; Nucleotide-binding; Nucleus; Parkinsonism; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Serine/threonine-protein kinase; Transcription; Transcription regulation; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1872 AA 
Protein Sequence
MGPGCDLLLR TAATITAAAI MSDTDSDEDS AGGGPFSLAG FLFGNINGAG QLEGESVLDD 60
ECKKHLAGLG ALGLGSLITE LTANEELTGT DGALVNDEGW VRSTEDAVDY SDINEVAEDE 120
SRRYQQTMGS LQPLCHSDYD EDDYDADCED IDCKLMPPPP PPPGPMKKDK DQDSITGEKV 180
DFSSSSDSES EMGPQEATQA ESEDGKLTLP LAGIMQHDAT KLLPSVTELF PEFRPGKVLR 240
FLRLFGPGKN VPSVWRSARR KRKKKHRELI QEEQIQEVEC SVESEVSQKS LWNYDYAPPP 300
PPEQCLSDDE ITMMAPVESK FSQSTGDIDK VTDTKPRVAE WRYGPARLWY DMLGVPEDGS 360
GFDYGFKLRK TEHEPVIKSR MIEEFRKLEE NNGTDLLADE NFLMVTQLHW EDDIIWDGED 420
VKHKGTKPQR ASLAGWLPSS MTRNAMAYNV QQGFAATLDD DKPWYSIFPI DNEDLVYGRW 480
EDNIIWDAQA MPRLLEPPVL TLDPNDENLI LEIPDEKEEA TSNSPSKESK KESSLKKSRI 540
LLGKTGVIKE EPQQNMSQPE VKDPWNLSND EYYYPKQQGL RGTFGGNIIQ HSIPAVELRQ 600
PFFPTHMGPI KLRQFHRPPL KKYSFGALSQ PGPHSVQPLL KHIKKKAKMR EQERQASGGG 660
EMFFMRTPQD LTGKDGDLIL AEYSEENGPL MMQVGMATKI KNYYKRKPGK DPGAPDCKYG 720
ETVYCHTSPF LGSLHPGQLL QAFENNLFRA PIYLHKMPET DFLIIRTRQG YYIRELVDIF 780
VVGQQCPLFE VPGPNSKRAN THIRDFLQVF IYRLFWKSKD RPRRIRMEDI KKAFPSHSES 840
SIRKRLKLCA DFKRTGMDSN WWVLKSDFRL PTEEEIRAMV SPEQCCAYYS MIAAEQRLKD 900
AGYGEKSFFA PEEENEEDFQ MKIDDEVRTA PWNTTRAFIA AMKGKCLLEV TGVADPTGCG 960
EGFSYVKIPN KPTQQKDDKE PQPVKKTVTG TDADLRRLSL KNAKQLLRKF GVPEEEIKKL 1020
SRWEVIDVVR TMSTEQARSG EGPMSKFARG SRFSVAEHQE RYKEECQRIF DLQNKVLSST 1080
EVLSTDTDSS SAEDSDFEEM GKNIENMLQN KKTSSQLSRE REEQERKELQ RMLLAAGSAA 1140
SGNNHRDDDT ASVTSLNSSA TGRCLKIYRT FRDEEGKEYV RCETVRKPAV IDAYVRIRTT 1200
KDEEFIRKFA LFDEQHREEM RKERRRIQEQ LRRLKRNQEK EKLKGPPEKK PKKMKERPDL 1260
KLKCGACGAI GHMRTNKFCP LYYQTNAPPS NPVAMTEEQE EELEKTVIHN DNEELIKVEG 1320
TKIVLGKQLI ESADEVRRKS LVLKFPKQQL PPKKKRRVGT TVHCDYLNRP HKSIHRRRTD 1380
PMVTLSSILE SIINDMRDLP NTYPFHTPVN AKVVKDYYKI ITRPMDLQTL RENVRKRLYP 1440
SREEFREHLE LIVKNSATYN GPKHSLTQIS QSMLDLCDEK LKEKEDKLAR LEKAINPLLD 1500
DDDQVAFSFI LDNIVTQKMM AVPDSWPFHH PVNKKFVPDY YKVIVNPMDL ETIRKNISKH 1560
KYQSRESFLD DVNLILANSV KYNGPESQYT KTAQEIVNVC YQTLTEYDEH LTQLEKDICT 1620
AKEAALEEAE LESLDPMTPG PYTPQPPDLY DTNTSLSMSR DASVFQDESN MSVLDIPSAT 1680
PEKQVTQMRQ GRGRLGEEDS DVDIEGYDDE EEDGKPKTPA PEGEDGDGDL ADEEEGTVQQ 1740
PQASVLYEDL LMSEGEDDEE DAGSDEEGDN PFSAIQLSES GSDSDVGSGG IRPKQPRMLQ 1800
ENTRMDMENE ESMMSYEGDG GEASHGLEDS NISYGSYEEP DPKSNTQDTS FSSIGGYEVS 1860
EEEEDEEEEE QRSGPSVLSQ VHLSEDEEDS EDFHSIAGDS DLDSDE 1906 
Gene Ontology
 GO:0071339; C:MLL1 complex; IDA:UniProtKB.
 GO:0005669; C:transcription factor TFIID complex; IDA:BHF-UCL.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0070577; F:histone acetyl-lysine binding; IDA:BHF-UCL.
 GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
 GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
 GO:0043565; F:sequence-specific DNA binding; ISS:BHF-UCL.
 GO:0003713; F:transcription coactivator activity; IDA:BHF-UCL.
 GO:0000080; P:G1 phase of mitotic cell cycle; IGI:BHF-UCL.
 GO:0018105; P:peptidyl-serine phosphorylation; IDA:BHF-UCL.
 GO:0018107; P:peptidyl-threonine phosphorylation; IDA:BHF-UCL.
 GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
 GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; ISS:BHF-UCL.
 GO:0046777; P:protein autophosphorylation; TAS:UniProtKB.
 GO:0000117; P:regulation of transcription involved in G2/M-phase of mitotic cell cycle; ISS:BHF-UCL.
 GO:0006974; P:response to DNA damage stimulus; IC:BHF-UCL.
 GO:0051123; P:RNA polymerase II transcriptional preinitiation complex assembly; ISS:BHF-UCL.
 GO:0006368; P:transcription elongation 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
 IPR001487; Bromodomain.
 IPR018359; Bromodomain_CS.
 IPR011177; TAF1_animal.
 IPR009067; TAF_II_230-bd.
 IPR022591; TFIID_sub1_DUF3591. 
Pfam
 PF00439; Bromodomain
 PF12157; DUF3591
 PF09247; TBP-binding 
SMART
 SM00297; BROMO 
PROSITE
 PS00633; BROMODOMAIN_1
 PS50014; BROMODOMAIN_2
 PS50118; HMG_BOX_2
 PS50011; PROTEIN_KINASE_DOM 
PRINTS
 PR00503; BROMODOMAIN.