Reviewed,
UniProtKB/Swiss-Prot Q96L91 (EP400_HUMAN)
Last modified
June 16, 2009.
Version 80.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: E1A-binding protein p400 EC=3.6.1.- Alternative name(s): p400 kDa SWI2/SNF2-related protein Domino homolog Short name=hDomino CAG repeat protein 32 Trinucleotide repeat-containing gene 12 protein | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 3160 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| Subunit structure | Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit HTATIP/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 EAF6. May also participate in the formation of NuA4 related complexes which lack the HTATIP/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 By similarity. |
| 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: Miscellaneous discrepancy. Intron retention. The sequence AAH64554.1 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence. |
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 | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | NuA4 histone acetyltransferase complex Ref.10 Inferred from direct assay. Source: UniProtKB |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA bindingInferred from electronic annotation. Source: UniProtKB-KW helicase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Alternative products
| This entry describes 4 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. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 3160 | 3160 | 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 – 2785 | 30 | Poly-Gln | ||||||
| Compositional bias | 2829 – 2835 | 7 | Poly-Pro | ||||||
Amino acid modifications | |||||||||
| Modified residue | 314 | 1 | Phosphothreonine Ref.13 | ||||||
| Modified residue | 315 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 320 | 1 | Phosphothreonine Ref.13 | ||||||
| Modified residue | 736 | 1 | Phosphoserine Ref.11 | ||||||
| Modified residue | 755 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 941 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 943 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 945 | 1 | Phosphothreonine Ref.13 | ||||||
| Modified residue | 1547 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 1728 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 1732 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 2814 | 1 | Phosphothreonine Ref.13 | ||||||
Natural variations | |||||||||
| Alternative sequence | 446 – 481 | 36 | Missing in isoform 2, isoform 3 and isoform 4. | VSP_011992 | |||||
| Alternative sequence | 482 | 1 | Missing in isoform 3. | 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: dbSNP rs13377636. | 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 AA sequence Ref.1 | ||||||
| Sequence conflict | 1645 | 1 | L → F AA sequence Ref.1 | ||||||
| Sequence conflict | 2756 | 1 | Missing in AC137590. Ref.2 | ||||||
| Sequence conflict | 2756 | 1 | Missing in AC137632. Ref.2 | ||||||
| Sequence conflict | 2845 | 1 | T → A in AAK97789. Ref.1 | ||||||
| Sequence conflict | 2845 | 1 | T → A in AAB91441. Ref.7 | ||||||
| Sequence conflict | 2898 | 1 | A → S in AAK97789. Ref.1 | ||||||
| Sequence conflict | 2898 | 1 | A → S in AAB91441. Ref.7 | ||||||
| Sequence conflict | 2913 – 2915 | 3 | ALA → PLP in AAK97789. Ref.1 | ||||||
| Sequence conflict | 2913 – 2915 | 3 | ALA → PLP in AAB91441. Ref.7 | ||||||
| Sequence conflict | 2991 | 1 | A → T in AAK97789. Ref.1 | ||||||
Sequences
| ||||||||||||||||||||||||||||||||||||
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: 11509179] [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: 16541075] [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: 10819331] [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: 14702039] [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: 15489334] [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: 11347906] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2004-3160. 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: 9225980] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2463-3160. 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: 12963728] [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: 15196461] [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: 14966270] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION IN SRCAP-CONTAINING COMPLEX. |
| [11] | "Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-736, MASS SPECTROMETRY. Tissue: Epithelium. |
| [12] | "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1547, MASS SPECTROMETRY. Tissue: Epithelium. |
| [13] | "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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-314; SER-315; THR-320; SER-941; SER-943; THR-945; SER-1728; SER-1732 AND THR-2814, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| 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. |
| RefSeq | NP_056224.2. |
| UniGene | Hs.699245 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q96L91. 5 interactions. |
PTM databases | |
| PhosphoSite | Q96L91. |
Proteomic databases | |
| PRIDE | Q96L91. |
Genome annotation databases | |
| Ensembl | ENSG00000183495. Homo sapiens. [Contig view] |
| GeneID | 57634. |
| KEGG | hsa:57634. |
Organism-specific databases | |
| GeneCards | GC12P131000. |
| H-InvDB | HIX0021564. HIX0023235. |
| HGNC | HGNC:11958. EP400. |
| HPA | HPA016704. |
| MIM | 606265. gene. |
| PharmGKB | PA27808. |
| HUGE | Search... Search... |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOVERGEN | Q96L91. |
Gene expression databases | |
| ArrayExpress | Q96L91. |
| Bgee | Q96L91. |
| CleanEx | HS_EP400. |
| GermOnline | ENSG00000183495. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR014001. DEAD-like_N. IPR001650. DNA/RNA_helicase_C. IPR002464. DNA/RNA_helicase_DEAH_CS. IPR013999. HAS_subgroup. IPR014012. Helicase/SANT-assoc_DNA_bd. IPR014021. Helicase_SF1/SF2_ATP-bd. IPR006562. HSA. IPR017877. MYB-like. IPR001005. SANT_DNA-bd. 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] |
| 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 Resources | |
| 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 project | HPI (Human Proteome Initiative) | ||||||||
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


