CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023817
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transformation/transcription domain-associated protein 
Protein Synonyms/Alias
 350/400 kDa PCAF-associated factor; PAF350/400; STAF40; Tra1 homolog 
Gene Name
 TRRAP 
Gene Synonyms/Alias
 PAF400 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
19VDQTTLMKKYLQFVAubiquitination[1]
20DQTTLMKKYLQFVAAubiquitination[1]
84EVQFLQEKPAQQLRKubiquitination[2]
470QLSAIFKKCKPQSELubiquitination[1]
551TDCRSLVKTLVCGVKubiquitination[1]
568TWGITSCKAPGEAQFubiquitination[1]
579EAQFIPNKQLQPKETubiquitination[1, 2]
897VAYRVLGKFGGSNRKubiquitination[1, 3, 4]
941SLQLPMEKAIETALDubiquitination[1]
951ETALDCLKSANTEPYubiquitination[1]
1016AQDTPARKTFEQALTubiquitination[1]
1357LTKLPCYKSLPSLVPubiquitination[1]
1385YLPQSREKIIAALFKubiquitination[1]
1769PNFGDELKAKVLQHIubiquitination[1, 2]
1771FGDELKAKVLQHILNubiquitination[1]
2022KWELQRIKDQQPDSDubiquitination[1, 2]
2047NSVSSSIKRGLSVDSubiquitination[2]
2059VDSAQEVKRFRTATGubiquitination[1]
2087GADSLLAKPIDKQHTubiquitination[1]
2091LLAKPIDKQHTDTVVubiquitination[1]
2207CMTCGNTKVLRAVHSubiquitination[1]
2362IEKSPDAKILRAVVKubiquitination[2, 5]
2405KMMTYIEKRFPEDLEubiquitination[2]
2438SGSELTAKLEPAFLSubiquitination[2]
2457AQPLIRAKFFEVFDNubiquitination[1]
2543FAMVTHVKQEPREREacetylation[6]
2543FAMVTHVKQEPREREubiquitination[1]
2597MLTNRHDKFLDTLREubiquitination[3, 4]
2638QLFPRLWKILSDRQQubiquitination[3, 4]
2724KGLSLQIKPKQTTEFubiquitination[1]
2829DHWIRCSKELNQWEAubiquitination[1]
2968NNSLHDMKTVVKTWRubiquitination[1]
2972HDMKTVVKTWRNRLPubiquitination[1, 3, 4]
3050QYGKIARKQGLVNVAubiquitination[1, 2, 3, 4]
3078PIVDCFQKIRQQVKCacetylation[6]
3078PIVDCFQKIRQQVKCubiquitination[1]
3346QLQQGLAKCYSVAFEubiquitination[1]
3354CYSVAFEKSGAVSDAubiquitination[1]
3362SGAVSDAKITPHTLNubiquitination[1]
3372PHTLNFVKKLVSTFGubiquitination[2]
3373HTLNFVKKLVSTFGVubiquitination[1]
3415AQDPVFQKLKGQFTTubiquitination[2]
3417DPVFQKLKGQFTTDFubiquitination[1]
3464KFFLIEEKCRFLSNFubiquitination[1]
3508PRVEIVQKHNTAARRubiquitination[1]
3558LLNPCLEKRKETTKRubiquitination[1]
3598LSLVEIYKQRCAKKGubiquitination[1, 2]
3604YKQRCAKKGIEHDNPubiquitination[1]
3639QVLRDILKEVQSNMVubiquitination[1, 2]
3765CFAQPNFKVDGILKTubiquitination[1]
3834QFEGGESKVNTLVAAubiquitination[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] 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] 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]
 [6] 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
Functional Description
 Adapter protein, which is found in various multiprotein chromatin complexes with histone acetyltransferase activity (HAT), which gives a specific tag for epigenetic transcription activation. Component of the NuA4 histone acetyltransferase complex which is responsible for acetylation of nucleosomal histones H4 and H2A. Plays a central role in MYC transcription activation, and also participates in cell transformation by MYC. Required for p53/TP53-, E2F1- and E2F4-mediated transcription activation. Also involved in transcription activation mediated by the adenovirus E1A, a viral oncoprotein that deregulates transcription of key genes. Probably acts by linking transcription factors such as E1A, MYC or E2F1 to HAT complexes such as STAGA thereby allowing transcription activation. Probably not required in the steps following histone acetylation in processes of transcription activation. May be required for the mitotic checkpoint and normal cell cycle progression. 
Sequence Annotation
 DOMAIN 2704 3275 FAT.
 DOMAIN 3528 3826 PI3K/PI4K.
 DOMAIN 3827 3859 FATC.
 REGION 2010 2388 Interaction with TP53.
 MOTIF 2047 2062 Bipartite nuclear localization signal
 MOD_RES 2051 2051 Phosphoserine.
 MOD_RES 2077 2077 Phosphoserine.
 MOD_RES 3078 3078 N6-acetyllysine.  
Keyword
 Acetylation; Activator; Alternative splicing; Chromatin regulator; Complete proteome; Direct protein sequencing; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3859 AA 
Protein Sequence
MAFVATQGAT VVDQTTLMKK YLQFVAALTD VNTPDETKLK MMQEVSENFE NVTSSPQYST 60
FLEHIIPRFL TFLQDGEVQF LQEKPAQQLR KLVLEIIHRI PTNEHLRPHT KNVLSVMFRF 120
LETENEENVL ICLRIIIELH KQFRPPITQE IHHFLDFVKQ IYKELPKVVN RYFENPQVIP 180
ENTVPPPEMV GMITTIAVKV NPEREDSETR THSIIPRGSL SLKVLAELPI IVVLMYQLYK 240
LNIHNVVAEF VPLIMNTIAI QVSAQARQHK LYNKELYADF IAAQIKTLSF LAYIIRIYQE 300
LVTKYSQQMV KGMLQLLSNC PAETAHLRKE LLIAAKHILT TELRNQFIPC MDKLFDESIL 360
IGSGYTARET LRPLAYSTLA DLVHHVRQHL PLSDLSLAVQ LFAKNIDDES LPSSIQTMSC 420
KLLLNLVDCI RSKSEQESGN GRDVLMRMLE VFVLKFHTIA RYQLSAIFKK CKPQSELGAV 480
EAALPGVPTA PAAPGPAPSP APVPAPPPPP PPPPPATPVT PAPVPPFEKQ GEKDKEDKQT 540
FQVTDCRSLV KTLVCGVKTI TWGITSCKAP GEAQFIPNKQ LQPKETQIYI KLVKYAMQAL 600
DIYQVQIAGN GQTYIRVANC QTVRMKEEKE VLEHFAGVFT MMNPLTFKEI FQTTVPYMVE 660
RISKNYALQI VANSFLANPT TSALFATILV EYLLDRLPEM GSNVELSNLY LKLFKLVFGS 720
VSLFAAENEQ MLKPHLHKIV NSSMELAQTA KEPYNYFLLL RALFRSIGGG SHDLLYQEFL 780
PLLPNLLQGL NMLQSGLHKQ HMKDLFVELC LTVPVRLSSL LPYLPMLMDP LVSALNGSQT 840
LVSQGLRTLE LCVDNLQPDF LYDHIQPVRA ELMQALWRTL RNPADSISHV AYRVLGKFGG 900
SNRKMLKESQ KLHYVVTEVQ GPSITVEFSD CKASLQLPME KAIETALDCL KSANTEPYYR 960
RQAWEVIKCF LVAMMSLEDN KHALYQLLAH PNFTEKTIPN VIISHRYKAQ DTPARKTFEQ 1020
ALTGAFMSAV IKDLRPSALP FVASLIRHYT MVAVAQQCGP FLLPCYQVGS QPSTAMFHSE 1080
ENGSKGMDPL VLIDAIAICM AYEEKELCKI GEVALAVIFD VASIILGSKE RACQLPLFSY 1140
IVERLCACCY EQAWYAKLGG VVSIKFLMER LPLTWVLQNQ QTFLKALLFV MMDLTGEVSN 1200
GAVAMAKTTL EQLLMRCATP LKDEERAEEI VAAQEKSFHH VTHDLVREVT SPNSTVRKQA 1260
MHSLQVLAQV TGKSVTVIME PHKEVLQDMV PPKKHLLRHQ PANAQIGLME GNTFCTTLQP 1320
RLFTMDLNVV EHKVFYTELL NLCEAEDSAL TKLPCYKSLP SLVPLRIAAL NALAACNYLP 1380
QSREKIIAAL FKALNSTNSE LQEAGEACMR KFLEGATIEV DQIHTHMRPL LMMLGDYRSL 1440
TLNVVNRLTS VTRLFPNSFN DKFCDQMMQH LRKWMEVVVI THKGGQRSDG NESISECGRC 1500
PLSPFCQFEE MKICSAIINL FHLIPAAPQT LVKPLLEVVM KTERAMLIEA GSPFREPLIK 1560
FLTRHPSQTV ELFMMEATLN DPQWSRMFMS FLKHKDARPL RDVLAANPNR FITLLLPGGA 1620
QTAVRPGSPS TSTMRLDLQF QAIKIISIIV KNDDSWLASQ HSLVSQLRRV WVSENFQERH 1680
RKENMAATNW KEPKLLAYCL LNYCKRNYGD IELLFQLLRA FTGRFLCNMT FLKEYMEEEI 1740
PKNYSIAQKR ALFFRFVDFN DPNFGDELKA KVLQHILNPA FLYSFEKGEG EQLLGPPNPE 1800
GDNPESITSV FITKVLDPEK QADMLDSLRI YLLQYATLLV EHAPHHIHDN NKNRNSKLRR 1860
LMTFAWPCLL SKACVDPACK YSGHLLLAHI IAKFAIHKKI VLQVFHSLLK AHAMEARAIV 1920
RQAMAILTPA VPARMEDGHQ MLTHWTRKII VEEGHTVPQL VHILHLIVQH FKVYYPVRHH 1980
LVQHMVSAMQ RLGFTPSVTI EQRRLAVDLS EVVIKWELQR IKDQQPDSDM DPNSSGEGVN 2040
SVSSSIKRGL SVDSAQEVKR FRTATGAISA VFGRSQSLPG ADSLLAKPID KQHTDTVVNF 2100
LIRVACQVND NTNTAGSPGE VLSRRCVNLL KTALRPDMWP KSELKLQWFD KLLMTVEQPN 2160
QVNYGNICTG LEVLSFLLTV LQSPAILSSF KPLQRGIAAC MTCGNTKVLR AVHSLLSRLM 2220
SIFPTEPSTS SVASKYEELE CLYAAVGKVI YEGLTNYEKA TNANPSQLFG TLMILKSACS 2280
NNPSYIDRLI SVFMRSLQKM VREHLNPQAA SGSTEATSGT SELVMLSLEL VKTRLAVMSM 2340
EMRKNFIQAI LTSLIEKSPD AKILRAVVKI VEEWVKNNSP MAANQTPTLR EKSILLVKMM 2400
TYIEKRFPED LELNAQFLDL VNYVYRDETL SGSELTAKLE PAFLSGLRCA QPLIRAKFFE 2460
VFDNSMKRRV YERLLYVTCS QNWEAMGNHF WIKQCIELLL AVCEKSTPIG TSCQGAMLPS 2520
ITNVINLADS HDRAAFAMVT HVKQEPRERE NSESKEEDVE IDIELAPGDQ TSTPKTKELS 2580
EKDIGNQLHM LTNRHDKFLD TLREVKTGAL LSAFVQLCHI STTLAEKTWV QLFPRLWKIL 2640
SDRQQHALAG EISPFLCSGS HQVQRDCQPS ALNCFVEAMS QCVPPIPIRP CVLKYLGKTH 2700
NLWFRSTLML EHQAFEKGLS LQIKPKQTTE FYEQESITPP QQEILDSLAE LYSLLQEEDM 2760
WAGLWQKRCK YSETATAIAY EQHGFFEQAQ ESYEKAMDKA KKEHERSNAS PAIFPEYQLW 2820
EDHWIRCSKE LNQWEALTEY GQSKGHINPY LVLECAWRVS NWTAMKEALV QVEVSCPKEM 2880
AWKVNMYRGY LAICHPEEQQ LSFIERLVEM ASSLAIREWR RLPHVVSHVH TPLLQAAQQI 2940
IELQEAAQIN AGLQPTNLGR NNSLHDMKTV VKTWRNRLPI VSDDLSHWSS IFMWRQHHYQ 3000
GKPTWSGMHS SSIVTAYENS SQHDPSSNNA MLGVHASASA IIQYGKIARK QGLVNVALDI 3060
LSRIHTIPTV PIVDCFQKIR QQVKCYLQLA GVMGKNECMQ GLEVIESTNL KYFTKEMTAE 3120
FYALKGMFLA QINKSEEANK AFSAAVQMHD VLVKAWAMWG DYLENIFVKE RQLHLGVSAI 3180
TCYLHACRHQ NESKSRKYLA KVLWLLSFDD DKNTLADAVD KYCIGVPPIQ WLAWIPQLLT 3240
CLVGSEGKLL LNLISQVGRV YPQAVYFPIR TLYLTLKIEQ RERYKSDPGP IRATAPMWRC 3300
SRIMHMQREL HPTLLSSLEG IVDQMVWFRE NWHEEVLRQL QQGLAKCYSV AFEKSGAVSD 3360
AKITPHTLNF VKKLVSTFGV GLENVSNVST MFSSAASESL ARRAQATAQD PVFQKLKGQF 3420
TTDFDFSVPG SMKLHNLISK LKKWIKILEA KTKQLPKFFL IEEKCRFLSN FSAQTAEVEI 3480
PGEFLMPKPT HYYIKIARFM PRVEIVQKHN TAARRLYIRG HNGKIYPYLV MNDACLTESR 3540
REERVLQLLR LLNPCLEKRK ETTKRHLFFT VPRVVAVSPQ MRLVEDNPSS LSLVEIYKQR 3600
CAKKGIEHDN PISRYYDRLA TVQARGTQAS HQVLRDILKE VQSNMVPRSM LKEWALHTFP 3660
NATDYWTFRK MFTIQLALIG FAEFVLHLNR LNPEMLQIAQ DTGKLNVAYF RFDINDATGD 3720
LDANRPVPFR LTPNISEFLT TIGVSGPLTA SMIAVARCFA QPNFKVDGIL KTVLRDEIIA 3780
WHKKTQEDTS SPLSAAGQPE NMDSQQLVSL VQKAVTAIMT RLHNLAQFEG GESKVNTLVA 3840
AANSLDNLCR MDPAWHPWL 3859 
Gene Ontology
 GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
 GO:0000125; C:PCAF complex; NAS:UniProtKB.
 GO:0030914; C:STAGA complex; IDA:UniProtKB.
 GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB.
 GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
 GO:0003713; F:transcription coactivator activity; IEA:Compara.
 GO:0003712; F:transcription cofactor activity; IDA:UniProtKB.
 GO:0016578; P:histone deubiquitination; IDA:UniProtKB.
 GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
 GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
 GO:0007093; P:mitotic cell cycle checkpoint; IEA:Compara.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR003152; FATC.
 IPR011009; Kinase-like_dom.
 IPR000403; PI3/4_kinase_cat_dom.
 IPR003151; PIK-rel_kinase_FAT.
 IPR014009; PIK_FAT.
 IPR011990; TPR-like_helical. 
Pfam
 PF02259; FAT
 PF00454; PI3_PI4_kinase 
SMART
 SM00146; PI3Kc 
PROSITE
 PS51189; FAT
 PS51190; FATC
 PS00915; PI3_4_KINASE_1
 PS00916; PI3_4_KINASE_2
 PS50290; PI3_4_KINASE_3 
PRINTS