BioPAX pathway converted from "MSL acetylates histone H4" in the Reactome database.2.3.1.48MSL acetylates histone H4MSL acetylates histone H4This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a>Converted from EntitySet in ReactomeReactome DB_ID: 100321041nucleoplasmGO0005654Homologues of HIST1H4 [nucleoplasm]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityLOC107131556 [nucleoplasm]Histone H4 [nucleoplasm]Reactomehttp://www.reactome.orgBos taurusNCBI Taxonomy9913UniProtA0A3Q1LMV7UniProtP62803Reactome DB_ID: 1135601acetyl-CoA [ChEBI:15351]acetyl-CoAChEBI15351Converted from EntitySet in ReactomeReactome DB_ID: 100646941Homologues of AcK17-HIST1H4 [nucleoplasm]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntityLOC107131556 [nucleoplasm]AcK17-HIST1H4 [nucleoplasm]Reactome DB_ID: 24850021coenzyme A [ChEBI:15346]coenzyme AChEBI15346PHYSIOL-LEFT-TO-RIGHTACTIVATIONReactome DB_ID: 10064712MSL [nucleoplasm]MSLReactome DB_ID: 100646981Ghost homologue of MSL1 [nucleoplasm]Ghost homologue of MSL1Reactome DB_ID: 100647021UniProt:F1MP98KAT8UniProtF1MP98Chain Coordinates1EQUAL458EQUALReactome DB_ID: 100647061UniProt:F1MRF9MSL2UniProtF1MRF91EQUAL577EQUALReactome DB_ID: 100647101UniProt:E1BFW0MSL3UniProtE1BFW01EQUAL521EQUALReactome Database ID Release 7510064712Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10064712ReactomeR-BTA-33218341Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-BTA-3321834.1GO0004402GO molecular functionReactome Database ID Release 7510064713Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10064713Reactome Database ID Release 7510064715Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=10064715ReactomeR-BTA-33218831Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-BTA-3321883.1The MSL complex has histone acetyltransferase (HAT) activity with a high specificity for histone H4 lysine-17 (H4K16) (Smith et al. 2000, 2005, Conrad et al. 2012). The subunit responsible for this activity is KAT8 (Males Absent on the First, MOF) a member of the MYST (named for yeast and human members MOZ, YBF2, SAS2, and Tip60) HAT family. In Drosophilla, the MSL complex associates at hundreds of sites along the X chromosome in somatic cells, resulting in the hyperacetylation of H4K16 (Lavender et al. 1994, Smith et al. 2000). In humans MSL is responsible for the majority of H4 acetylation at lysine-17 in the cell. KAT8 is a component of other complexes (Smith et al. 2005, Mendjan et al. 2006, Cai et al. 2010).7981944Pubmed1994Histone H4 acetylated at lysine 16 and proteins of the Drosophila dosage compensation pathway co-localize on the male X chromosome through mitosisLavender, J SBirley, A JPalmer, M JKuroda, M ITurner, B MChromosome Res. 2:398-40410594033Pubmed2000The drosophila MSL complex acetylates histone H4 at lysine 16, a chromatin modification linked to dosage compensationSmith, E RPannuti, AGu, WSteurnagel, ACook, RGAllis, C DLucchesi, J CMol. Cell. Biol. 20:312-822421046Pubmed2012The MOF chromobarrel domain controls genome-wide H4K16 acetylation and spreading of the MSL complexConrad, ThomasCavalli, Florence M GHolz, HerbertHallacli, ErincKind, JopIlik, IbrahimVaquerizas, Juan MLuscombe, Nicholas MAkhtar, AsifaDev. Cell 22:610-2410786633Pubmed2000A new human member of the MYST family of histone acetyl transferases with high sequence similarity to Drosophila MOFNeal, K CPannuti, ASmith, E RLucchesi, J CBiochim. Biophys. Acta 1490:170-416543150Pubmed2006Nuclear pore components are involved in the transcriptional regulation of dosage compensation in DrosophilaMendjan, SaschaTaipale, MikkoKind, JopHolz, HerbertGebhardt, PhilippSchelder, MalgorzataVermeulen, MichielBuscaino, AlessiaDuncan, KentMueller, JuergWilm, MatthiasStunnenberg, Henk GSaumweber, HaraldAkhtar, AsifaMol. Cell 21:811-2320018852Pubmed2010Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complexCai, YongJin, JingjiSwanson, Selene KCole, Michael DChoi, Seung HyukFlorens, Laurence AWashburn, Michael PConaway, Joan WConaway, Ronald CJ. Biol. Chem. 285:4268-7216227571Pubmed2005A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16Smith, Edwin RCayrou, ChristelleHuang, RongLane, William SCôté, JacquesLucchesi, John CMol. Cell. Biol. 25:9175-88inferred by electronic annotationIEAGOIEA