CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019426
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E1A-binding protein p400 
Protein Synonyms/Alias
 CAG repeat protein 32; Domino homolog; hDomino; Trinucleotide repeat-containing gene 12 protein; p400 kDa SWI2/SNF2-related protein 
Gene Name
 EP400 
Gene Synonyms/Alias
 CAGH32; KIAA1498; KIAA1818; TNRC12 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
346VGNTGMKKVPKKLEEubiquitination[1]
899LRVELEEKRKKALNLubiquitination[1]
908KKALNLQKVSRRGKEubiquitination[1]
1070VAEAILPKGSARVTTubiquitination[1]
1096GALRDYQKIGLDWLAubiquitination[2, 3]
1291ESQDYYHKVVIRLHRubiquitination[1, 2, 3, 4]
1314RTKRDVEKQLTKKYEubiquitination[1]
1319VEKQLTKKYEHVLKCubiquitination[1]
1333CRLSNRQKALYEDVIubiquitination[1]
1398PSASLILKALERDFWubiquitination[1, 4]
1421DLIGLENKITRHEAEubiquitination[1, 4]
1457AARPAAAKLKASRLFacetylation[5]
1472QPVQYGQKPEGRTVAacetylation[6]
1472QPVQYGQKPEGRTVAubiquitination[1]
1553ASPAHPAKLRAQTTAacetylation[6, 7]
1605LPSGEVVKIAQLASIubiquitination[1, 7]
1634TLQFQGSKFTLSHSQacetylation[6]
1634TLQFQGSKFTLSHSQubiquitination[1, 2, 3]
1693VHGALGSKPPAGGPSubiquitination[4]
1729GEPGTASKPASPIGGubiquitination[1]
1795SLDGRRGKEAGPAHSubiquitination[1]
2014CDRIGRCKDIHIYRLubiquitination[1]
2030SGNSIEEKLLKNGTKubiquitination[1, 7]
2037KLLKNGTKDLIREVAubiquitination[1]
2108RPFIEALKSIEYLEEubiquitination[1, 8, 9]
2181HTSIEQEKERNSEDAubiquitination[1, 7]
2202AWEFWNLKTLQEREAubiquitination[1, 2, 3, 7, 8, 9]
2342QKKNILLKQQVPFAKubiquitination[10]
2349KQQVPFAKPLPTFAKacetylation[6, 7, 11, 12]
2356KPLPTFAKPTAEPGQacetylation[6, 11]
2480GKRSPPIKPLLGMNPacetylation[7, 11, 12]
3155VRLKTPTKPPCQ***acetylation[7]
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] 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]
 [3] 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]
 [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] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] 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]
 [12] 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
Functional Description
 Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. May be required for transcriptional activation of E2F1 and MYC target genes during cellular proliferation. The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400. May regulate ZNF42 transcription activity. 
Sequence Annotation
 DOMAIN 799 871 HSA.
 DOMAIN 1103 1268 Helicase ATP-binding.
 DOMAIN 1899 2056 Helicase C-terminal.
 DOMAIN 2360 2429 Myb-like.
 NP_BIND 1116 1123 ATP (Potential).
 REGION 951 1365 Interactions with RUVBL1 and RUVBL2.
 REGION 2524 2789 Interaction with ZNF42 (By similarity).
 MOTIF 1219 1222 DEAH box-like.
 MOD_RES 736 736 Phosphoserine.
 MOD_RES 755 755 Phosphoserine (By similarity).
 MOD_RES 941 941 Phosphoserine.
 MOD_RES 945 945 Phosphothreonine.
 MOD_RES 1472 1472 N6-acetyllysine.
 MOD_RES 1728 1728 Phosphoserine.
 MOD_RES 1732 1732 Phosphoserine.
 MOD_RES 2349 2349 N6-acetyllysine.
 MOD_RES 2356 2356 N6-acetyllysine.
 MOD_RES 2813 2813 Phosphothreonine.  
Keyword
 Acetylation; Alternative splicing; ATP-binding; Chromatin regulator; Complete proteome; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3159 AA 
Protein Sequence
MHHGTGPQNV QHQLQRSRAC PGSEGEEQPA HPNPPPSPAA PFAPSASPSA PQSPSYQIQQ 60
LMNRSPATGQ NVNITLQSVG PVVGGNQQIT LAPLPLPSPT SPGFQFSAQP RRFEHGSPSY 120
IQVTSPLSQQ VQTQSPTQPS PGPGQALQNV RAGAPGPGLG LCSSSPTGGF VDASVLVRQI 180
SLSPSSGGHF VFQDGSGLTQ IAQGAQVQLQ HPGTPITVRE RRPSQPHTQS GGTIHHLGPQ 240
SPAAAGGAGL QPLASPSHIT TANLPPQISS IIQGQLVQQQ QVLQGPPLPR PLGFERTPGV 300
LLPGAGGAAG FGMTSPPPPT SPSRTAVPPG LSSLPLTSVG NTGMKKVPKK LEEIPPASPE 360
MAQMRKQCLD YHYQEMQALK EVFKEYLIEL FFLQHFQGNM MDFLAFKKKH YAPLQAYLRQ 420
NDLDIEEEEE EEEEEEEKSE VINDEVKVVT GKDGQTGTPV AIATQLPPKV SAAFSSQQQP 480
FQQALAGSLV AGAGSTVETD LFKRQQAMPS TGMAEQSKRP RLEVGHQGVV FQHPGADAGV 540
PLQQLMPTAQ GGMPPTPQAA QLAGQRQSQQ QYDPSTGPPV QNAASLHTPL PQLPGRLPPA 600
GVPTAALSSA LQFAQQPQVV EAQTQLQIPV KTQQPNVPIP APPSSQLPIP PSQPAQLALH 660
VPTPGKVQVQ ASQLSSLPQM VASTRLPVDP APPCPRPLPT SSTSSLAPVS GSGPGPSPAR 720
SSPVNRPSSA TNKALSPVTS RTPGVVASAP TKPQSPAQNA TSSQDSSQDT LTEQITLENQ 780
VHQRIAELRK AGLWSQRRLP KLQEAPRPKS HWDYLLEEMQ WMATDFAQER RWKVAAAKKL 840
VRTVVRHHEE KQLREERGKK EEQSRLRRIA ASTAREIECF WSNIEQVVEI KLRVELEEKR 900
KKALNLQKVS RRGKELRPKG FDALQESSLD SGMSGRKRKA SISLTDDEVD DEEETIEEEE 960
ANEGVVDHQT ELSNLAKEAE LPLLDLMKLY EGAFLPSSQW PRPKPDGEDT SGEEDADDCP 1020
GDRESRKDLV LIDSLFIMDQ FKAAERMNIG KPNAKDIADV TAVAEAILPK GSARVTTSVK 1080
FNAPSLLYGA LRDYQKIGLD WLAKLYRKNL NGILADEAGL GKTVQIIAFF AHLACNEGNW 1140
GPHLVVVRSC NILKWELELK RWCPGLKILS YIGSHRELKA KRQEWAEPNS FHVCITSYTQ 1200
FFRGLTAFTR VRWKCLVIDE MQRVKGMTER HWEAVFTLQS QQRLLLIDSP LHNTFLELWT 1260
MVHFLVPGIS RPYLSSPLRA PSEESQDYYH KVVIRLHRVT QPFILRRTKR DVEKQLTKKY 1320
EHVLKCRLSN RQKALYEDVI LQPGTQEALK SGHFVNVLSI LVRLQRICNH PGLVEPRHPG 1380
SSYVAGPLEY PSASLILKAL ERDFWKEADL SMFDLIGLEN KITRHEAELL SKKKIPRKLM 1440
EEISTSAAPA ARPAAAKLKA SRLFQPVQYG QKPEGRTVAF PSTHPPRTAA PTTASAAPQG 1500
PLRGRPPIAT FSANPEAKAA AAPFQTSQAS ASAPRHQPAS ASSTAASPAH PAKLRAQTTA 1560
QASTPGQPPP QPQAPSHAAG QSALPQRLVL PSQAQARLPS GEVVKIAQLA SITGPQSRVA 1620
QPETPVTLQF QGSKFTLSHS QLRQLTAGQP LQLQGSVLQI VSAPGQPYLR APGPVVMQTV 1680
SQAGAVHGAL GSKPPAGGPS PAPLTPQVGV PGRVAVNALA VGEPGTASKP ASPIGGPTQE 1740
EKTRLLKERL DQIYLVNERR CSQAPVYGRD LLRICALPSH GRVQWRGSLD GRRGKEAGPA 1800
HSYTSSSESP SELMLTLCRC GESLQDVIDR VAFVIPPVVA APPSLRVPRP PPLYSHRMRI 1860
LRQGLREHAA PYFQQLRQTT APRLLQFPEL RLVQFDSGKL EALAILLQKL KSEGRRVLIL 1920
SQMILMLDIL EMFLNFHYLT YVRIDENASS EQRQELMRSF NRDRRIFCAI LSTHSRTTGI 1980
NLVEADTVVF YDNDLNPVMD AKAQEWCDRI GRCKDIHIYR LVSGNSIEEK LLKNGTKDLI 2040
REVAAQGNDY SMAFLTQRTI QELFEVYSPM DDAGFPVKAE EFVVLSQEPS VTETIAPKIA 2100
RPFIEALKSI EYLEEDAQKS AQEGVLGPHT DALSSDSENM PCDEEPSQLE ELADFMEQLT 2160
PIEKYALNYL ELFHTSIEQE KERNSEDAVM TAVRAWEFWN LKTLQEREAR LRLEQEEAEL 2220
LTYTREDAYS MEYVYEDVDG QTEVMPLWTP PTPPQDDSDI YLDSVMCLMY EATPIPEAKL 2280
PPVYVRKERK RHKTDPSAAG RKKKQRHGEA VVPPRSLFDR ATPGLLKIRR EGKEQKKNIL 2340
LKQQVPFAKP LPTFAKPTAE PGQDNPEWLI SEDWALLQAV KQLLELPLNL TIVSPAHTPN 2400
WDLVSDVVNS CSRIYRSSKQ CRNRYENVII PREEGKSKNN RPLRTSQIYA QDENATHTQL 2460
YTSHFDLMKM TAGKRSPPIK PLLGMNPFQK NPKHASVLAE SGINYDKPLP PIQVASLRAE 2520
RIAKEKKALA DQQKAQQPAV AQPPPPQPQP PPPPQQPPPP LPQPQAAGSQ PPAGPPAVQP 2580
QPQPQPQTQP QPVQAPAKAQ PAITTGGSAA VLAGTIKTSV TGTSMPTGAV SGNVIVNTIA 2640
GVPAATFQSI NKRLASPVAP GALTTPGGSA PAQVVHTQPP PRAVGSPATA TPDLVSMATT 2700
QGVRAVTSVT ASAVVTTNLT PVQTPARSLV PQVSQATGVQ LPGKTITPAH FQLLRQQQQQ 2760
QQQQQQQQQQ QQQQQQQQQQ QQQQTTTTSQ VQVPQIQGQA QSPAQIKAVG KLTPEHLIKM 2820
QKQKLQMPPQ PPPPQAQSAP PQPTAQVQVQ TSQPPQQQSP QLTTVTAPRP GALLTGTTVA 2880
NLQVARLTRV PTSQLQAQGQ MQTQAPQPAQ VALAKPPVVS VPAAVVSSPG VTTLPMNVAG 2940
ISVAIGQPQK AAGQTVVAQP VHMQQLLKLK QQAVQQQKAI QPQAAQGPAA VQQKITAQQI 3000
TTPGAQQKVA YAAQPALKTQ FLTTPISQAQ KLAGAQQVQT QIQVAKLPQV VQQQTPVASI 3060
QQVASASQQA SPQTVALTQA TAAGQQVQMI PAVTATAQVV QQKLIQQQVV TTASAPLQTP 3120
GAPNPAQVPA SSDSPSQQPK LQMRVPAVRL KTPTKPPCQ 3159 
Gene Ontology
 GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
 GO:0016607; C:nuclear speck; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003682; F:chromatin binding; IEA:InterPro.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
 GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
 GO:0043967; P:histone H4 acetylation; IDA:UniProtKB. 
Interpro
 IPR013999; HAS_subgr.
 IPR014012; Helicase/SANT-assoc_DNA-bd.
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR009057; Homeodomain-like.
 IPR006562; HSA.
 IPR017877; Myb-like_dom.
 IPR027417; P-loop_NTPase.
 IPR001005; SANT/Myb.
 IPR000330; SNF2_N. 
Pfam
 PF00271; Helicase_C
 PF07529; HSA
 PF00176; SNF2_N 
SMART
 SM00487; DEXDc
 SM00573; HSA
 SM00717; SANT 
PROSITE
 PS00690; DEAH_ATP_HELICASE
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER
 PS51204; HSA
 PS50090; MYB_LIKE 
PRINTS