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Q96L91

- EP400_HUMAN

UniProt

Q96L91 - EP400_HUMAN

Protein

E1A-binding protein p400

Gene

EP400

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 4 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    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. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1116 – 11238ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. chromatin binding Source: InterPro
    3. DNA binding Source: UniProtKB-KW
    4. helicase activity Source: UniProtKB-KW

    GO - Biological processi

    1. chromatin organization Source: Reactome
    2. histone H2A acetylation Source: UniProtKB
    3. histone H4 acetylation Source: UniProtKB

    Keywords - Molecular functioni

    Chromatin regulator, Helicase, Hydrolase

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
    REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
    REACT_172610. HATs acetylate histones.
    REACT_197820. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E1A-binding protein p400 (EC:3.6.4.-)
    Alternative name(s):
    CAG repeat protein 32
    Domino homolog
    Short name:
    hDomino
    Trinucleotide repeat-containing gene 12 protein
    p400 kDa SWI2/SNF2-related protein
    Gene namesi
    Name:EP400
    Synonyms:CAGH32, KIAA1498, KIAA1818, TNRC12
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:11958. EP400.

    Subcellular locationi

    Nucleus PROSITE-ProRule annotation

    GO - Cellular componenti

    1. NuA4 histone acetyltransferase complex Source: UniProtKB
    2. nuclear speck Source: UniProtKB
    3. nucleoplasm Source: Reactome
    4. Swr1 complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27808.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 31593159E1A-binding protein p400PRO_0000074312Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei736 – 7361Phosphoserine2 Publications
    Modified residuei941 – 9411Phosphoserine1 Publication
    Modified residuei945 – 9451Phosphothreonine1 Publication
    Modified residuei1472 – 14721N6-acetyllysine1 Publication
    Modified residuei1728 – 17281Phosphoserine1 Publication
    Modified residuei1732 – 17321Phosphoserine1 Publication
    Modified residuei2349 – 23491N6-acetyllysine1 Publication
    Modified residuei2356 – 23561N6-acetyllysine1 Publication
    Modified residuei2813 – 28131Phosphothreonine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ96L91.
    PaxDbiQ96L91.
    PRIDEiQ96L91.

    PTM databases

    PhosphoSiteiQ96L91.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ96L91.
    BgeeiQ96L91.
    CleanExiHS_EP400.
    GenevestigatoriQ96L91.

    Organism-specific databases

    HPAiHPA016704.

    Interactioni

    Subunit structurei

    Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. May also participate in the formation of NuA4 related complexes which lack the KAT5/TIP60 catalytic subunit, but which include the SWI/SNF related protein SRCAP. The NuA4 complex interacts with MYC and the adenovirus E1A protein. EP400 interacts with TRRAP, RUVBL1 and RUVBL2. Component of a SWR1-like complex. Interacts with ZNF42. Interacts with PHF5A By similarity.By similarity

    Protein-protein interaction databases

    BioGridi121676. 25 interactions.
    DIPiDIP-29915N.
    IntActiQ96L91. 11 interactions.
    MINTiMINT-1897496.
    STRINGi9606.ENSP00000374213.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96L91.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini799 – 87173HSAPROSITE-ProRule annotationAdd
    BLAST
    Domaini1103 – 1268166Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1899 – 2056158Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini2360 – 242970Myb-likePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni951 – 1365415Interactions with RUVBL1 and RUVBL2Add
    BLAST
    Regioni2524 – 2789266Interaction with ZNF42By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1219 – 12224DEAH box-like

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi278 – 2814Poly-Gln
    Compositional biasi316 – 3194Poly-Pro
    Compositional biasi426 – 43712Poly-GluAdd
    BLAST
    Compositional biasi1517 – 15226Poly-Ala
    Compositional biasi2543 – 255412Poly-ProAdd
    BLAST
    Compositional biasi2557 – 25648Poly-Pro
    Compositional biasi2756 – 278429Poly-GlnAdd
    BLAST
    Compositional biasi2828 – 28347Poly-Pro

    Sequence similaritiesi

    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
    Contains 1 HSA domain.PROSITE-ProRule annotation
    Contains 1 Myb-like domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0553.
    HOVERGENiHBG051488.
    InParanoidiQ96L91.
    KOiK11320.
    OMAiAQVVHTQ.
    OrthoDBiEOG7PVWPN.
    PhylomeDBiQ96L91.
    TreeFamiTF106424.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR013999. HAS_subgr.
    IPR014012. Helicase/SANT-assoc_DNA-bd.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR017877. Myb-like_dom.
    IPR027417. P-loop_NTPase.
    IPR001005. SANT/Myb.
    IPR000330. SNF2_N.
    [Graphical view]
    PfamiPF00271. Helicase_C. 1 hit.
    PF07529. HSA. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00573. HSA. 1 hit.
    SM00717. SANT. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 4 hits.
    PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51204. HSA. 1 hit.
    PS50090. MYB_LIKE. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96L91-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MHHGTGPQNV QHQLQRSRAC PGSEGEEQPA HPNPPPSPAA PFAPSASPSA     50
    PQSPSYQIQQ LMNRSPATGQ NVNITLQSVG PVVGGNQQIT LAPLPLPSPT 100
    SPGFQFSAQP RRFEHGSPSY IQVTSPLSQQ VQTQSPTQPS PGPGQALQNV 150
    RAGAPGPGLG LCSSSPTGGF VDASVLVRQI SLSPSSGGHF VFQDGSGLTQ 200
    IAQGAQVQLQ HPGTPITVRE RRPSQPHTQS GGTIHHLGPQ SPAAAGGAGL 250
    QPLASPSHIT TANLPPQISS IIQGQLVQQQ QVLQGPPLPR PLGFERTPGV 300
    LLPGAGGAAG FGMTSPPPPT SPSRTAVPPG LSSLPLTSVG NTGMKKVPKK 350
    LEEIPPASPE MAQMRKQCLD YHYQEMQALK EVFKEYLIEL FFLQHFQGNM 400
    MDFLAFKKKH YAPLQAYLRQ NDLDIEEEEE EEEEEEEKSE VINDEVKVVT 450
    GKDGQTGTPV AIATQLPPKV SAAFSSQQQP FQQALAGSLV AGAGSTVETD 500
    LFKRQQAMPS TGMAEQSKRP RLEVGHQGVV FQHPGADAGV PLQQLMPTAQ 550
    GGMPPTPQAA QLAGQRQSQQ QYDPSTGPPV QNAASLHTPL PQLPGRLPPA 600
    GVPTAALSSA LQFAQQPQVV EAQTQLQIPV KTQQPNVPIP APPSSQLPIP 650
    PSQPAQLALH VPTPGKVQVQ ASQLSSLPQM VASTRLPVDP APPCPRPLPT 700
    SSTSSLAPVS GSGPGPSPAR SSPVNRPSSA TNKALSPVTS RTPGVVASAP 750
    TKPQSPAQNA TSSQDSSQDT LTEQITLENQ VHQRIAELRK AGLWSQRRLP 800
    KLQEAPRPKS HWDYLLEEMQ WMATDFAQER RWKVAAAKKL VRTVVRHHEE 850
    KQLREERGKK EEQSRLRRIA ASTAREIECF WSNIEQVVEI KLRVELEEKR 900
    KKALNLQKVS RRGKELRPKG FDALQESSLD SGMSGRKRKA SISLTDDEVD 950
    DEEETIEEEE ANEGVVDHQT ELSNLAKEAE LPLLDLMKLY EGAFLPSSQW 1000
    PRPKPDGEDT SGEEDADDCP GDRESRKDLV LIDSLFIMDQ FKAAERMNIG 1050
    KPNAKDIADV TAVAEAILPK GSARVTTSVK FNAPSLLYGA LRDYQKIGLD 1100
    WLAKLYRKNL NGILADEAGL GKTVQIIAFF AHLACNEGNW GPHLVVVRSC 1150
    NILKWELELK RWCPGLKILS YIGSHRELKA KRQEWAEPNS FHVCITSYTQ 1200
    FFRGLTAFTR VRWKCLVIDE MQRVKGMTER HWEAVFTLQS QQRLLLIDSP 1250
    LHNTFLELWT MVHFLVPGIS RPYLSSPLRA PSEESQDYYH KVVIRLHRVT 1300
    QPFILRRTKR DVEKQLTKKY EHVLKCRLSN RQKALYEDVI LQPGTQEALK 1350
    SGHFVNVLSI LVRLQRICNH PGLVEPRHPG SSYVAGPLEY PSASLILKAL 1400
    ERDFWKEADL SMFDLIGLEN KITRHEAELL SKKKIPRKLM EEISTSAAPA 1450
    ARPAAAKLKA SRLFQPVQYG QKPEGRTVAF PSTHPPRTAA PTTASAAPQG 1500
    PLRGRPPIAT FSANPEAKAA AAPFQTSQAS ASAPRHQPAS ASSTAASPAH 1550
    PAKLRAQTTA QASTPGQPPP QPQAPSHAAG QSALPQRLVL PSQAQARLPS 1600
    GEVVKIAQLA SITGPQSRVA QPETPVTLQF QGSKFTLSHS QLRQLTAGQP 1650
    LQLQGSVLQI VSAPGQPYLR APGPVVMQTV SQAGAVHGAL GSKPPAGGPS 1700
    PAPLTPQVGV PGRVAVNALA VGEPGTASKP ASPIGGPTQE EKTRLLKERL 1750
    DQIYLVNERR CSQAPVYGRD LLRICALPSH GRVQWRGSLD GRRGKEAGPA 1800
    HSYTSSSESP SELMLTLCRC GESLQDVIDR VAFVIPPVVA APPSLRVPRP 1850
    PPLYSHRMRI LRQGLREHAA PYFQQLRQTT APRLLQFPEL RLVQFDSGKL 1900
    EALAILLQKL KSEGRRVLIL SQMILMLDIL EMFLNFHYLT YVRIDENASS 1950
    EQRQELMRSF NRDRRIFCAI LSTHSRTTGI NLVEADTVVF YDNDLNPVMD 2000
    AKAQEWCDRI GRCKDIHIYR LVSGNSIEEK LLKNGTKDLI REVAAQGNDY 2050
    SMAFLTQRTI QELFEVYSPM DDAGFPVKAE EFVVLSQEPS VTETIAPKIA 2100
    RPFIEALKSI EYLEEDAQKS AQEGVLGPHT DALSSDSENM PCDEEPSQLE 2150
    ELADFMEQLT PIEKYALNYL ELFHTSIEQE KERNSEDAVM TAVRAWEFWN 2200
    LKTLQEREAR LRLEQEEAEL LTYTREDAYS MEYVYEDVDG QTEVMPLWTP 2250
    PTPPQDDSDI YLDSVMCLMY EATPIPEAKL PPVYVRKERK RHKTDPSAAG 2300
    RKKKQRHGEA VVPPRSLFDR ATPGLLKIRR EGKEQKKNIL LKQQVPFAKP 2350
    LPTFAKPTAE PGQDNPEWLI SEDWALLQAV KQLLELPLNL TIVSPAHTPN 2400
    WDLVSDVVNS CSRIYRSSKQ CRNRYENVII PREEGKSKNN RPLRTSQIYA 2450
    QDENATHTQL YTSHFDLMKM TAGKRSPPIK PLLGMNPFQK NPKHASVLAE 2500
    SGINYDKPLP PIQVASLRAE RIAKEKKALA DQQKAQQPAV AQPPPPQPQP 2550
    PPPPQQPPPP LPQPQAAGSQ PPAGPPAVQP QPQPQPQTQP QPVQAPAKAQ 2600
    PAITTGGSAA VLAGTIKTSV TGTSMPTGAV SGNVIVNTIA GVPAATFQSI 2650
    NKRLASPVAP GALTTPGGSA PAQVVHTQPP PRAVGSPATA TPDLVSMATT 2700
    QGVRAVTSVT ASAVVTTNLT PVQTPARSLV PQVSQATGVQ LPGKTITPAH 2750
    FQLLRQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQTTTTSQ VQVPQIQGQA 2800
    QSPAQIKAVG KLTPEHLIKM QKQKLQMPPQ PPPPQAQSAP PQPTAQVQVQ 2850
    TSQPPQQQSP QLTTVTAPRP GALLTGTTVA NLQVARLTRV PTSQLQAQGQ 2900
    MQTQAPQPAQ VALAKPPVVS VPAAVVSSPG VTTLPMNVAG ISVAIGQPQK 2950
    AAGQTVVAQP VHMQQLLKLK QQAVQQQKAI QPQAAQGPAA VQQKITAQQI 3000
    TTPGAQQKVA YAAQPALKTQ FLTTPISQAQ KLAGAQQVQT QIQVAKLPQV 3050
    VQQQTPVASI QQVASASQQA SPQTVALTQA TAAGQQVQMI PAVTATAQVV 3100
    QQKLIQQQVV TTASAPLQTP GAPNPAQVPA SSDSPSQQPK LQMRVPAVRL 3150
    KTPTKPPCQ 3159
    Length:3,159
    Mass (Da):343,489
    Last modified:January 11, 2011 - v4
    Checksum:i0E502CE1BE9CFAC1
    GO
    Isoform 2 (identifier: Q96L91-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         446-481: Missing.

    Show »
    Length:3,123
    Mass (Da):339,823
    Checksum:i846B71A59CE2B201
    GO
    Isoform 3 (identifier: Q96L91-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         446-481: Missing.
         482-482: Missing.
         515-550: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:3,086
    Mass (Da):335,805
    Checksum:i706B650493BC8580
    GO
    Isoform 4 (identifier: Q96L91-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         446-481: Missing.
         1519-1600: AAAAPFQTSQ...PSQAQARLPS → G

    Note: No experimental confirmation available.

    Show »
    Length:3,042
    Mass (Da):331,778
    Checksum:i6D57F7F463C74FE1
    GO
    Isoform 5 (identifier: Q96L91-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         446-481: Missing.
         482-482: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:3,122
    Mass (Da):339,695
    Checksum:i0F04797ACF402088
    GO

    Sequence cautioni

    The sequence AAH37208.1 differs from that shown. Reason: Intron retention.
    The sequence AAH64554.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAB91441.1 differs from that shown. Reason: Frameshift at positions 2959 and 3020.
    The sequence BAA96022.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti537 – 5371D → G in AAH37208. (PubMed:15489334)Curated
    Sequence conflicti810 – 8101S → P in AAH37208. (PubMed:15489334)Curated
    Sequence conflicti1563 – 15631S → F in AAK97789. (PubMed:11509179)Curated
    Sequence conflicti1642 – 16421L → F in AAK97789. (PubMed:11509179)Curated
    Sequence conflicti1645 – 16451L → F in AAK97789. (PubMed:11509179)Curated
    Sequence conflicti2756 – 27561Q → QQ in AAK97789. (PubMed:11509179)Curated
    Sequence conflicti2756 – 27561Q → QQ in BAB47447. (PubMed:11347906)Curated
    Sequence conflicti2756 – 27561Q → QQ in AAB91441. (PubMed:9225980)Curated
    Sequence conflicti2844 – 28441T → A in AAK97789. (PubMed:11509179)Curated
    Sequence conflicti2844 – 28441T → A in AAB91441. (PubMed:9225980)Curated
    Sequence conflicti2897 – 28971A → S in AAK97789. (PubMed:11509179)Curated
    Sequence conflicti2897 – 28971A → S in AAB91441. (PubMed:9225980)Curated
    Sequence conflicti2912 – 29143ALA → PLP in AAK97789. (PubMed:11509179)Curated
    Sequence conflicti2912 – 29143ALA → PLP in AAB91441. (PubMed:9225980)Curated
    Sequence conflicti2990 – 29901A → T in AAK97789. (PubMed:11509179)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1308 – 13081T → I.
    Corresponds to variant rs13377636 [ dbSNP | Ensembl ].
    VAR_046957

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei446 – 48136Missing in isoform 2, isoform 3, isoform 4 and isoform 5. 4 PublicationsVSP_011992Add
    BLAST
    Alternative sequencei482 – 4821Missing in isoform 3 and isoform 5. 2 PublicationsVSP_011993
    Alternative sequencei515 – 55036Missing in isoform 3. 2 PublicationsVSP_011994Add
    BLAST
    Alternative sequencei1519 – 160082AAAAP…ARLPS → G in isoform 4. 1 PublicationVSP_011995Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY044869 mRNA. Translation: AAK97789.1.
    AC137590 Genomic DNA. No translation available.
    AC137632 Genomic DNA. No translation available.
    AB040931 mRNA. Translation: BAA96022.1. Different initiation.
    AK096311 mRNA. Translation: BAC04759.1.
    BC037208 mRNA. Translation: AAH37208.1. Sequence problems.
    BC064554 mRNA. Translation: AAH64554.1. Sequence problems.
    AB058721 mRNA. Translation: BAB47447.1.
    U80743 mRNA. Translation: AAB91441.1. Frameshift.
    CCDSiCCDS31929.2. [Q96L91-2]
    RefSeqiNP_056224.3. NM_015409.4. [Q96L91-2]
    UniGeneiHs.723478.

    Genome annotation databases

    EnsembliENST00000330386; ENSP00000330620; ENSG00000183495. [Q96L91-4]
    ENST00000332482; ENSP00000331737; ENSG00000183495. [Q96L91-3]
    ENST00000333577; ENSP00000333602; ENSG00000183495. [Q96L91-1]
    ENST00000389561; ENSP00000374212; ENSG00000183495. [Q96L91-2]
    ENST00000389562; ENSP00000374213; ENSG00000183495. [Q96L91-5]
    GeneIDi57634.
    KEGGihsa:57634.
    UCSCiuc001ujm.3. human. [Q96L91-4]
    uc001ujn.3. human. [Q96L91-2]

    Polymorphism databases

    DMDMi317373565.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY044869 mRNA. Translation: AAK97789.1 .
    AC137590 Genomic DNA. No translation available.
    AC137632 Genomic DNA. No translation available.
    AB040931 mRNA. Translation: BAA96022.1 . Different initiation.
    AK096311 mRNA. Translation: BAC04759.1 .
    BC037208 mRNA. Translation: AAH37208.1 . Sequence problems.
    BC064554 mRNA. Translation: AAH64554.1 . Sequence problems.
    AB058721 mRNA. Translation: BAB47447.1 .
    U80743 mRNA. Translation: AAB91441.1 . Frameshift.
    CCDSi CCDS31929.2. [Q96L91-2 ]
    RefSeqi NP_056224.3. NM_015409.4. [Q96L91-2 ]
    UniGenei Hs.723478.

    3D structure databases

    ProteinModelPortali Q96L91.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121676. 25 interactions.
    DIPi DIP-29915N.
    IntActi Q96L91. 11 interactions.
    MINTi MINT-1897496.
    STRINGi 9606.ENSP00000374213.

    PTM databases

    PhosphoSitei Q96L91.

    Polymorphism databases

    DMDMi 317373565.

    Proteomic databases

    MaxQBi Q96L91.
    PaxDbi Q96L91.
    PRIDEi Q96L91.

    Protocols and materials databases

    DNASUi 57634.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000330386 ; ENSP00000330620 ; ENSG00000183495 . [Q96L91-4 ]
    ENST00000332482 ; ENSP00000331737 ; ENSG00000183495 . [Q96L91-3 ]
    ENST00000333577 ; ENSP00000333602 ; ENSG00000183495 . [Q96L91-1 ]
    ENST00000389561 ; ENSP00000374212 ; ENSG00000183495 . [Q96L91-2 ]
    ENST00000389562 ; ENSP00000374213 ; ENSG00000183495 . [Q96L91-5 ]
    GeneIDi 57634.
    KEGGi hsa:57634.
    UCSCi uc001ujm.3. human. [Q96L91-4 ]
    uc001ujn.3. human. [Q96L91-2 ]

    Organism-specific databases

    CTDi 57634.
    GeneCardsi GC12P132434.
    H-InvDB HIX0021564.
    HGNCi HGNC:11958. EP400.
    HPAi HPA016704.
    MIMi 606265. gene.
    neXtProti NX_Q96L91.
    PharmGKBi PA27808.
    HUGEi Search...
    Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0553.
    HOVERGENi HBG051488.
    InParanoidi Q96L91.
    KOi K11320.
    OMAi AQVVHTQ.
    OrthoDBi EOG7PVWPN.
    PhylomeDBi Q96L91.
    TreeFami TF106424.

    Enzyme and pathway databases

    Reactomei REACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
    REACT_169185. DNA Damage/Telomere Stress Induced Senescence.
    REACT_172610. HATs acetylate histones.
    REACT_197820. HATs acetylate histones.

    Miscellaneous databases

    ChiTaRSi EP400. human.
    GeneWikii EP400.
    GenomeRNAii 57634.
    NextBioi 64345.
    PROi Q96L91.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96L91.
    Bgeei Q96L91.
    CleanExi HS_EP400.
    Genevestigatori Q96L91.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR013999. HAS_subgr.
    IPR014012. Helicase/SANT-assoc_DNA-bd.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR017877. Myb-like_dom.
    IPR027417. P-loop_NTPase.
    IPR001005. SANT/Myb.
    IPR000330. SNF2_N.
    [Graphical view ]
    Pfami PF00271. Helicase_C. 1 hit.
    PF07529. HSA. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00573. HSA. 1 hit.
    SM00717. SANT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 4 hits.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51204. HSA. 1 hit.
    PS50090. MYB_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY, ROLE OF EP400-CONTAINING COMPLEXES IN CELLULAR TRANSFORMATION BY ADENOVIRUS E1A PROTEIN, TISSUE SPECIFICITY, INTERACTION WITH TRRAP; RUVBL1 AND RUVBL2.
    2. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1847 (ISOFORM 4).
      Tissue: Brain.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-897 (ISOFORM 3).
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-978 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-895 (ISOFORM 3).
      Tissue: Lymph and Testis.
    6. "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
      DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2004-3159.
      Tissue: Brain.
    7. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2463-3159.
      Tissue: Brain.
    8. "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex."
      Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J., Conaway R.C., Conaway J.W.
      J. Biol. Chem. 278:42733-42736(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN NUA4 COMPLEX.
    9. "The highly conserved and multifunctional NuA4 HAT complex."
      Doyon Y., Cote J.
      Curr. Opin. Genet. Dev. 14:147-154(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON NUA4 COMPLEX.
    10. "Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans."
      Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.
      Mol. Cell. Biol. 24:1884-1896(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION IN SRCAP-CONTAINING COMPLEX.
    11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-941; THR-945; SER-1728 AND SER-1732, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1472; LYS-2349 AND LYS-2356, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-736 AND THR-2813, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-736, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: FUNCTION, IDENTIFICATION IN THE SWR1-LIKE COMPLEX.

    Entry informationi

    Entry nameiEP400_HUMAN
    AccessioniPrimary (citable) accession number: Q96L91
    Secondary accession number(s): O15411
    , Q6P2F5, Q8N8Q7, Q8NE05, Q96JK7, Q9P230
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 23, 2004
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 133 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3