| Tag | Content |
|---|
| CPLM ID | CPLM-016873 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | E1A-binding protein p400 |
Protein Synonyms/Alias | Domino homolog; mDomino; p400 kDa SWI2/SNF2-related protein |
Gene Name | Ep400 |
Gene Synonyms/Alias | Kiaa1498 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 732 | RPSSATNKALSPITS | acetylation | [1] | | 2265 | KQQTPFAKPLPTYVK | acetylation | [2] | | 2396 | GKRSPPIKPLLGMNP | acetylation | [1] | | 2931 | YAAQPALKTQFLTTP | acetylation | [1] | | 3068 | VRLKTPTKPPCQ*** | acetylation | [1] |
|
Reference | [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways. Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y. Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [ PMID: 22826441] [2] 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 (By similarity). Regulates transcriptional activity of ZNF42. |
Sequence Annotation | DOMAIN 798 870 HSA.
DOMAIN 1102 1267 Helicase ATP-binding.
DOMAIN 1815 1972 Helicase C-terminal.
DOMAIN 2276 2345 Myb-like.
NP_BIND 1115 1122 ATP (Potential).
REGION 950 1364 Interactions with RUVBL1 and RUVBL2 (By
REGION 2440 2699 Interaction with ZNF42.
MOTIF 1218 1221 DEAD box-like.
MOD_RES 735 735 Phosphoserine (By similarity).
MOD_RES 754 754 Phosphoserine.
MOD_RES 940 940 Phosphoserine (By similarity).
MOD_RES 944 944 Phosphothreonine (By similarity).
MOD_RES 1471 1471 N6-acetyllysine (By similarity).
MOD_RES 1646 1646 Phosphoserine (By similarity).
MOD_RES 1650 1650 Phosphoserine (By similarity).
MOD_RES 2265 2265 N6-acetyllysine (By similarity).
MOD_RES 2272 2272 N6-acetyllysine (By similarity). |
Keyword | Acetylation; Alternative splicing; ATP-binding; Chromatin regulator; Complete proteome; Direct protein sequencing; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 3072 AA |
Protein Sequence | MHHGSGPQNV QHQLQRSRSF TGSEEEQPAH PNLPPSPAAP FAPSASPSAP QSPGYQIQQL 60
MSRSPVAGQN VNITLQNVGP VVGGNQQITL APLPLPNPTS PGFQFGAQQR RFEHGSPSYI 120
QVTSPMSQQV QTQSPTQPSP GPGQTLQNVR AGAPGPGLGI CSNSPTGGFV DASVLVRQIS 180
LSPSSGGHFV FQEAPGLTQM AQGAQVQLQH SGAPITVRER RLSQPHAQSG GTIHHLGPQS 240
PAAAGGTGLQ PLASPNHITT ASLPPQISSI IQGQLIQQQQ QVLQGQPMNR SLGFERTPGV 300
LLPGVGGPSA FGMTSPPPPT SPSRTTMPPG LSSVPLTSMG SSGMKKVPKK LEEIPPASQE 360
MAQMRKQCLD YHYKEMEALK EVFKEYLIEL FFLQHLQGNM MDFLAFKKKH YAPLQAYLRQ 420
NDLDIEEEEE EEEEEEGKSE VINDEVKVVT GKDGQTGTPV AIATQLPPNV SAAFSSQQQP 480
FQHQSLTGSL VVGPGSATEA DPFKRQQVMP PTEQSKRPRL EVGHPGVVFQ HPGVNAGVPL 540
QQLMPTVQGG MPPTPQATQL TGQKQSQQQY DPSTGPPVQN AASLHTPPPQ LPARLPPASV 600
PATALPSTLQ FSQQSQMVEA STQLQIPVKT QQLNAPIPAP LPSQLPAPSS QPAQPALHVP 660
MPGKAQMQTS QLSSQTQTVA STRPPLDSAQ PCQRSLPTSS SSSSLVPVSG SGPGPSPARS 720
SPVNRPSSAT NKALSPITSR SPGVAVSAPP KPQSPAQNAA SSQDGSQDKL AEQITLENQI 780
HQRIADLRKE GLWSLRRLPK LQEAPRPKSH WDYLLEEMQW MATDFAQERR WKLAAAKKLV 840
RTVARHHEEK KLREERGKKE EQSRLRRIAA TTAREIEYFW SNIEQVVEIK LQVELEEKRK 900
KALNLQKVSR RGKESRLKGF DTSPEHSLDL GISGRKRKAS TSLTDDEVED EEETIEEEEA 960
HEGLVDHHTE LTNLAKEAEL PLIDLMKLYE GAFLPNFQWP QPEPDHEESS GEEDVEDCPS 1020
DRESRRDSVL IDSLFIMDQF KAAERMSIGK SNTKDITEVT AVAEAILPKG SARVTTAVKF 1080
SAPSLLYGAL RDYQKIGLDW LAKLYRKNLN GILADEAGLG KTVQIIAFFA HLACNEGNWG 1140
PHLVVMRSCN ILKWELELKR WCPGLKTLSY VGSHRELKAK RQEWTEPNNF HICITSYKQF 1200
FRGYTAFSRV HWKCLVVDEM QRVKGMTERH WEAIFKLQSQ QRLLLIDVPL HNTFLELWTM 1260
VHFLIPGISR PYLSFPLKAP NEENQDYYHK MVIRLHRVTQ PFILRRTKRD VEKQLTRKYE 1320
HVLKCRLSSR QKALYEDVIL QPRTQEALKS GHFVSVLSVL TRLQRICNHP GLVEPRVPGS 1380
SFAAGSLQYK SASLILRVLE REFWKETDLS IFDLIGLENK ITRHEAELLC KKKVTRKLME 1440
EVFASPPPSA RPAAVKLKAS RLFQPVQYGQ KPEGRTVAFP STHPPRMANT NTSTATPQGQ 1500
VRGRPPIATF SANPDTKGGE VVKIAQLASI AGPQSRVAQP ETPVTLQFQG NKFTLSHSQL 1560
RQLTAGQPLQ LQGSVLQIVS APGQPYLRAP GPVVMQTVSQ AGAVHSTLGS KPPTSGPSPA 1620
PLTPQVGVPG RVAVSAMAVG EPGLASKPAS PAAGPTQEEK SRLLKERLDQ IHFINERRCS 1680
QAPVYGRDLL RICSLPGRRK RPLCWSLDSN FGKGPKGVNY DMSLSKSEGD LILTLSQESL 1740
QDVLGRVACV IPPVVATPPS LWVARPPSLY SSRLRALRQC LREHTGPYHR QLQQLTALRS 1800
LQFPELRLVQ FDSGKLEALA ILLQKLKSEG RRVLILSQMV LMLDILEMFL NFHYLTYVRI 1860
DENANSEQRQ ELMRSFNRDR RIFCALLSTH SRATGINLVE ADTVVFYDND LNPVMDAKAQ 1920
EWCDRIGRCK DIHIYRLVSG NSIEEKLLKN GTKDLIREVA AQGNDYSMAF LTQRTIQELF 1980
EVYSPMDDTG FPVKAEEFVV LSQEPSVSET IAPKIARPFI EALKSIECLE EDAQRSTEEA 2040
VPGSSSVAVS SDSDGSRYDE EPSQLEELAD FMEQLTPIEK YALNYLELFH TTTEQEKERI 2100
SEDLVMASMK DWETRNARAL QEREARLQLE QEEAELLTYT REDAYTMEYV YEDADGQTEV 2160
MPLWTPPTPP QDDNDIYIDS VMCLMYETTP IPEAKLPPVY VRKERKRHKT DPSAAGRKKK 2220
QRHGEAVVPP RSLFDRATPG MLKIRREGKE QKKNLLLKQQ TPFAKPLPTY VKSSGEPAQD 2280
SPDWLIGEDW ALLQAVKQLL ELPLNLTIVS PAHTPNWDLV SDVVNSCSRI YRSSKQCRNR 2340
YENVIIPREE GKSKNNRPLR TSQIYAQDEN ATHTQLYTSH FELMKMTAGK RSPPIKPLLG 2400
MNPFQKNPKH ASVLAESGIN YDKPLPPIQV ASLRAERIAK EKKALADQQK AQQPPVTQPP 2460
PQQQQQQQQQ QQQQQQQQQP PPPPQQPPPP VPQPQAASSQ TPAGQPAVQP QPQPQVQTQP 2520
QPVQPQSKGQ PTMTTVGSAA VLAGTIKTSV TGTSIPTGTV SGNVIVNTIA GVPAATFQSI 2580
NKRLASPVAP GTLTTSGGSA PAQVVHTQQR AVGSPATATT DLVSMTTTQG VRAVTSVTAS 2640
AVVTTNLTPV QTPTRSLVTQ VSQATGVQLP GKTITPAAHF QLLRQQQQQQ QQQQQQQQTS 2700
QVQVPQLQSQ AQSPAQIKAV SKLGPEHIIK MQKQKMQLPP QPPPPQAQPG PPQQPAQVQV 2760
QTPQPPQQQQ SPQLTTVTAP RPGALLTGTT VTNLQVARLT RVPTSQLQAQ GQMQTQTPQP 2820
AQVALAKPPV VSVPAAVVSS PGVTTLPMNV AGISVAIGQP QKTAGQTVVA QPVNVQQLLK 2880
YKQQTAVQQQ KAIQPQVAQG QAAVQQKLTT QQITTQGPQQ KVAYAAQPAL KTQFLTTPIS 2940
QAQKLAGTQQ VQTQIQVAKL PQVVQQQTPV ASIQQVASAS QQASPQTVTL TQATAAGQQV 3000
QMIPTVTATA QLVQQKLIQQ QVVTTASASL QTPGGPSPAQ LPASSDSPSQ QPKLQMRVPA 3060
VRLKTPTKPP CQ 3072 |
Gene Ontology | GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB. GO:0016607; C:nuclear speck; IDA: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; ISS:UniProtKB. GO:0043967; P:histone H4 acetylation; ISS:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |