Q96L91 (EP400_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 119.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | 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 names |
| ||||
| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 3159 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | 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. Ref.10 |
| Subunit structure | 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. Interacts with ZNF42. Interacts with PHF5A By similarity. Ref.1 Ref.8 Ref.10 |
| Subcellular location | Nucleus By similarity. |
| Tissue specificity | Ubiquitously expressed. Ref.1 |
| Sequence similarities | Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain. Contains 1 HSA domain. Contains 1 Myb-like domain. |
| Sequence caution | The sequence AAB91441.1 differs from that shown. Reason: Frameshift at positions 2959 and 3020. 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 BAA96022.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Nucleus |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Ligand | ATP-binding DNA-binding Nucleotide-binding |
| Molecular function | Chromatin regulator Helicase Hydrolase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | histone H2A acetylation Inferred from direct assay Ref.10. Source: UniProtKB histone H4 acetylationInferred from direct assay Ref.10. Source: UniProtKB |
| Cellular_component | NuA4 histone acetyltransferase complex Inferred from direct assay Ref.10. Source: UniProtKB nuclear speckInferred from sequence or structural similarity. Source: UniProtKB |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA bindingInferred from electronic annotation. Source: UniProtKB-KW chromatin bindingInferred from electronic annotation. Source: InterPro helicase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Alternative products
| This entry describes 5 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q96L91-1) 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. | ||||||
| Isoform 2 (identifier: Q96L91-2) The sequence of this isoform differs from the canonical sequence as follows: 446-481: Missing. | ||||||
| Isoform 3 (identifier: Q96L91-3) 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. | ||||||
| Isoform 4 (identifier: Q96L91-4) 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. | ||||||
| Isoform 5 (identifier: Q96L91-5) The sequence of this isoform differs from the canonical sequence as follows: 446-481: Missing. 482-482: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 3159 | 3159 | E1A-binding protein p400 | PRO_0000074312 | |||||
Regions | |||||||||
| Domain | 799 – 871 | 73 | HSA | ||||||
| Domain | 1103 – 1268 | 166 | Helicase ATP-binding | ||||||
| Domain | 1899 – 2056 | 158 | Helicase C-terminal | ||||||
| Domain | 2360 – 2429 | 70 | Myb-like | ||||||
| Nucleotide binding | 1116 – 1123 | 8 | ATP Potential | ||||||
| Region | 951 – 1365 | 415 | Interactions with RUVBL1 and RUVBL2 | ||||||
| Region | 2524 – 2789 | 266 | Interaction with ZNF42 By similarity | ||||||
| Motif | 1219 – 1222 | 4 | DEAH box-like | ||||||
| Compositional bias | 278 – 281 | 4 | Poly-Gln | ||||||
| Compositional bias | 316 – 319 | 4 | Poly-Pro | ||||||
| Compositional bias | 426 – 437 | 12 | Poly-Glu | ||||||
| Compositional bias | 1517 – 1522 | 6 | Poly-Ala | ||||||
| Compositional bias | 2543 – 2554 | 12 | Poly-Pro | ||||||
| Compositional bias | 2557 – 2564 | 8 | Poly-Pro | ||||||
| Compositional bias | 2756 – 2784 | 29 | Poly-Gln | ||||||
| Compositional bias | 2828 – 2834 | 7 | Poly-Pro | ||||||
Amino acid modifications | |||||||||
| Modified residue | 736 | 1 | Phosphoserine Ref.15 Ref.17 | ||||||
| Modified residue | 755 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 941 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 945 | 1 | Phosphothreonine Ref.12 | ||||||
| Modified residue | 1472 | 1 | N6-acetyllysine Ref.14 | ||||||
| Modified residue | 1728 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 1732 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 2349 | 1 | N6-acetyllysine Ref.14 | ||||||
| Modified residue | 2356 | 1 | N6-acetyllysine Ref.14 | ||||||
| Modified residue | 2813 | 1 | Phosphothreonine Ref.15 | ||||||
Natural variations | |||||||||
| Alternative sequence | 446 – 481 | 36 | Missing in isoform 2, isoform 3, isoform 4 and isoform 5. | VSP_011992 | |||||
| Alternative sequence | 482 | 1 | Missing in isoform 3 and isoform 5. | VSP_011993 | |||||
| Alternative sequence | 515 – 550 | 36 | Missing in isoform 3. | VSP_011994 | |||||
| Alternative sequence | 1519 – 1600 | 82 | AAAAP…ARLPS → G in isoform 4. | VSP_011995 | |||||
| Natural variant | 1308 | 1 | T → I. Corresponds to variant rs13377636 [ dbSNP | Ensembl ]. | VAR_046957 | |||||
Experimental info | |||||||||
| Sequence conflict | 537 | 1 | D → G in AAH37208. Ref.5 | ||||||
| Sequence conflict | 810 | 1 | S → P in AAH37208. Ref.5 | ||||||
| Sequence conflict | 1563 | 1 | S → F in AAK97789. Ref.1 | ||||||
| Sequence conflict | 1642 | 1 | L → F in AAK97789. Ref.1 | ||||||
| Sequence conflict | 1645 | 1 | L → F in AAK97789. Ref.1 | ||||||
| Sequence conflict | 2756 | 1 | Q → QQ in AAK97789. Ref.1 | ||||||
| Sequence conflict | 2756 | 1 | Q → QQ in BAB47447. Ref.6 | ||||||
| Sequence conflict | 2756 | 1 | Q → QQ in AAB91441. Ref.7 | ||||||
| Sequence conflict | 2844 | 1 | T → A in AAK97789. Ref.1 | ||||||
| Sequence conflict | 2844 | 1 | T → A in AAB91441. Ref.7 | ||||||
| Sequence conflict | 2897 | 1 | A → S in AAK97789. Ref.1 | ||||||
| Sequence conflict | 2897 | 1 | A → S in AAB91441. Ref.7 | ||||||
| Sequence conflict | 2912 – 2914 | 3 | ALA → PLP in AAK97789. Ref.1 | ||||||
| Sequence conflict | 2912 – 2914 | 3 | ALA → PLP in AAB91441. Ref.7 | ||||||
| Sequence conflict | 2990 | 1 | A → T in AAK97789. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The p400 complex is an essential E1A transformation target." Fuchs M., Gerber J., Drapkin R., Sif S., Ikura T., Ogryzko V., Lane W.S., Nakatani Y., Livingston D.M. Cell 106:297-307(2001) [PubMed] [Europe PMC] [Abstract] 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. 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. 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] | "cDNAs with long CAG trinucleotide repeats from human brain." Margolis R.L., Abraham M.R., Gatchell S.B., Li S.-H., Kidwai A.S., Breschel T.S., Stine O.C., Callahan C., McInnis M.G., Ross C.A. Hum. Genet. 100:114-122(1997) [PubMed] [Europe PMC] [Abstract] 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] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-941; THR-945; SER-1728 AND SER-1732, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [13] | "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. |
| [14] | "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, MASS SPECTROMETRY. |
| [15] | "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, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [16] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| [17] | "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, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | 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. |
| IPI | IPI00064931. IPI00167535. IPI00783692. IPI00798339. IPI00878154. |
| RefSeq | NP_056224.3. NM_015409.4. |
| UniGene | Hs.595201. |
3D structure databases | |
| ProteinModelPortal | Q96L91. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-29915N. |
| IntAct | Q96L91. 7 interactions. |
| MINT | MINT-1897496. |
| STRING | 9606.ENSP00000374213. |
PTM databases | |
| PhosphoSite | Q96L91. |
Polymorphism databases | |
| DMDM | 209572748. |
Proteomic databases | |
| PaxDb | Q96L91. |
| PRIDE | Q96L91. |
Protocols and materials databases | |
| DNASU | 57634. |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000330386; ENSP00000330620; ENSG00000183495. ENST00000332482; ENSP00000331737; ENSG00000183495. ENST00000333577; ENSP00000333602; ENSG00000183495. ENST00000389561; ENSP00000374212; ENSG00000183495. ENST00000389562; ENSP00000374213; ENSG00000183495. ENST00000537902; ENSP00000442702; ENSG00000183495. ENST00000541296; ENSP00000439509; ENSG00000183495. |
| GeneID | 57634. |
| KEGG | hsa:57634. |
| UCSC | uc001ujm.3. human. uc001ujn.3. human. uc021rgq.1. human. |
Organism-specific databases | |
| CTD | 57634. |
| GeneCards | GC12P132434. |
| H-InvDB | HIX0021564. |
| HGNC | HGNC:11958. EP400. |
| HPA | HPA016704. |
| MIM | 606265. gene. |
| neXtProt | NX_Q96L91. |
| PharmGKB | PA27808. |
| HUGE | Search... Search... |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | COG0553. |
| HOVERGEN | HBG051488. |
| InParanoid | Q96L91. |
| KO | K11320. |
| OMA | MQKQKLQ. |
| OrthoDB | EOG4RBQHQ. |
Gene expression databases | |
| ArrayExpress | Q96L91. |
| Bgee | Q96L91. |
| CleanEx | HS_EP400. |
| Genevestigator | Q96L91. |
| GermOnline | ENSG00000183495. Homo sapiens. |
Family and domain databases | |
| 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. [Graphical view] |
| Pfam | PF00271. Helicase_C. 1 hit. PF07529. HSA. 1 hit. PF00176. SNF2_N. 1 hit. [Graphical view] |
| SMART | SM00487. DEXDc. 1 hit. SM00573. HSA. 1 hit. SM00717. SANT. 1 hit. [Graphical view] |
| SUPFAM | SSF46689. Homeodomain_like. 1 hit. SSF52540. SSF52540. 3 hits. |
| PROSITE | PS00690. DEAH_ATP_HELICASE. False negative. PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. PS51204. HSA. 1 hit. PS50090. MYB_LIKE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | EP400. human. |
| GenomeRNAi | 57634. |
| NextBio | 64345. |
| SOURCE | Search... |
Entry information
| Entry name | EP400_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q96L91 Secondary accession number(s): O15411 Q9P230 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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. | ||||||||
Relevant documents
| Human chromosome 12 Human chromosome 12: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
