| Tag | Content |
|---|
| CPLM ID | CPLM-019427 |
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 |
|---|
| 1362 | PSASLILKALERDFW | ubiquitination | [1] | | 1402 | SKKKIPRKLMEEIST | ubiquitination | [1] | | 2072 | RPFIEALKSIEYLEE | ubiquitination | [1] | | 2166 | AWEFWNLKTLQEREA | ubiquitination | [1] |
|
Reference | [1] 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] |
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 VINDEQQALA GSLVAGAGST VETDLFKRQQ AMPSTGMAEQ 480
SKRPRLEVGH QGVVFQHPGA DAGVPLQQLM PTAQGGMPPT PQAAQLAGQR QSQQQYDPST 540
GPPVQNAASL HTPLPQLPGR LPPAGVPTAA LSSALQFAQQ PQVVEAQTQL QIPVKTQQPN 600
VPIPAPPSSQ LPIPPSQPAQ LALHVPTPGK VQVQASQLSS LPQMVASTRL PVDPAPPCPR 660
PLPTSSTSSL APVSGSGPGP SPARSSPVNR PSSATNKALS PVTSRTPGVV ASAPTKPQSP 720
AQNATSSQDS SQDTLTEQIT LENQVHQRIA ELRKAGLWSQ RRLPKLQEAP RPKSHWDYLL 780
EEMQWMATDF AQERRWKVAA AKKLVRTVVR HHEEKQLREE RGKKEEQSRL RRIAASTARE 840
IECFWSNIEQ VVEIKLRVEL EEKRKKALNL QKVSRRGKEL RPKGFDALQE SSLDSGMSGR 900
KRKASISLTD DEVDDEEETI EEEEANEGVV DHQTELSNLA KEAELPLLDL MKLYEGAFLP 960
SSQWPRPKPD GEDTSGEEDA DDCPGDRESR KDLVLIDSLF IMDQFKAAER MNIGKPNAKD 1020
IADVTAVAEA ILPKGSARVT TSVKFNAPSL LYGALRDYQK IGLDWLAKLY RKNLNGILAD 1080
EAGLGKTVQI IAFFAHLACN EGNWGPHLVV VRSCNILKWE LELKRWCPGL KILSYIGSHR 1140
ELKAKRQEWA EPNSFHVCIT SYTQFFRGLT AFTRVRWKCL VIDEMQRVKG MTERHWEAVF 1200
TLQSQQRLLL IDSPLHNTFL ELWTMVHFLV PGISRPYLSS PLRAPSEESQ DYYHKVVIRL 1260
HRVTQPFILR RTKRDVEKQL TKKYEHVLKC RLSNRQKALY EDVILQPGTQ EALKSGHFVN 1320
VLSILVRLQR ICNHPGLVEP RHPGSSYVAG PLEYPSASLI LKALERDFWK EADLSMFDLI 1380
GLENKITRHE AELLSKKKIP RKLMEEISTS AAPAARPAAA KLKASRLFQP VQYGQKPEGR 1440
TVAFPSTHPP RTAAPTTASA APQGPLRGRP PIATFSANPE AKAAAAPFQT SQASASAPRH 1500
QPASASSTAA SPAHPAKLRA QTTAQASTPG QPPPQPQAPS HAAGQSALPQ RLVLPSQAQA 1560
RLPSGEVVKI AQLASITGPQ SRVAQPETPV TLQFQGSKFT LSHSQLRQLT AGQPLQLQGS 1620
VLQIVSAPGQ PYLRAPGPVV MQTVSQAGAV HGALGSKPPA GGPSPAPLTP QVGVPGRVAV 1680
NALAVGEPGT ASKPASPIGG PTQEEKTRLL KERLDQIYLV NERRCSQAPV YGRDLLRICA 1740
LPSHGRVQWR GSLDGRRGKE AGPAHSYTSS SESPSELMLT LCRCGESLQD VIDRVAFVIP 1800
PVVAAPPSLR VPRPPPLYSH RMRILRQGLR EHAAPYFQQL RQTTAPRLLQ FPELRLVQFD 1860
SGKLEALAIL LQKLKSEGRR VLILSQMILM LDILEMFLNF HYLTYVRIDE NASSEQRQEL 1920
MRSFNRDRRI FCAILSTHSR TTGINLVEAD TVVFYDNDLN PVMDAKAQEW CDRIGRCKDI 1980
HIYRLVSGNS IEEKLLKNGT KDLIREVAAQ GNDYSMAFLT QRTIQELFEV YSPMDDAGFP 2040
VKAEEFVVLS QEPSVTETIA PKIARPFIEA LKSIEYLEED AQKSAQEGVL GPHTDALSSD 2100
SENMPCDEEP SQLEELADFM EQLTPIEKYA LNYLELFHTS IEQEKERNSE DAVMTAVRAW 2160
EFWNLKTLQE REARLRLEQE EAELLTYTRE DAYSMEYVYE DVDGQTEVMP LWTPPTPPQD 2220
DSDIYLDSVM CLMYEATPIP EAKLPPVYVR KERKRHKTDP SAAGRKKKQR HGEAVVPPRS 2280
LFDRATPGLL KIRREGKEQK KNILLKQQVP FAKPLPTFAK PTAEPGQDNP EWLISEDWAL 2340
LQAVKQLLEL PLNLTIVSPA HTPNWDLVSD VVNSCSRIYR SSKQCRNRYE NVIIPREEGK 2400
SKNNRPLRTS QIYAQDENAT HTQLYTSHFD LMKMTAGKRS PPIKPLLGMN PFQKNPKHAS 2460
VLAESGINYD KPLPPIQVAS LRAERIAKEK KALADQQKAQ QPAVAQPPPP QPQPPPPPQQ 2520
PPPPLPQPQA AGSQPPAGPP AVQPQPQPQP QTQPQPVQAP AKAQPAITTG GSAAVLAGTI 2580
KTSVTGTSMP TGAVSGNVIV NTIAGVPAAT FQSINKRLAS PVAPGALTTP GGSAPAQVVH 2640
TQPPPRAVGS PATATPDLVS MATTQGVRAV TSVTASAVVT TNLTPVQTPA RSLVPQVSQA 2700
TGVQLPGKTI TPAHFQLLRQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQTT TTSQVQVPQI 2760
QGQAQSPAQI KAVGKLTPEH LIKMQKQKLQ MPPQPPPPQA QSAPPQPTAQ VQVQTSQPPQ 2820
QQSPQLTTVT APRPGALLTG TTVANLQVAR LTRVPTSQLQ AQGQMQTQAP QPAQVALAKP 2880
PVVSVPAAVV SSPGVTTLPM NVAGISVAIG QPQKAAGQTV VAQPVHMQQL LKLKQQAVQQ 2940
QKAIQPQAAQ GPAAVQQKIT AQQITTPGAQ QKVAYAAQPA LKTQFLTTPI SQAQKLAGAQ 3000
QVQTQIQVAK LPQVVQQQTP VASIQQVASA SQQASPQTVA LTQATAAGQQ VQMIPAVTAT 3060
AQVVQQKLIQ QQVVTTASAP LQTPGAPNPA QVPASSDSPS QQPKLQMRVP AVRLKTPTKP 3120
PCQ 3123 |
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 | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |