BioPAX pathway converted from "SENP1,2,5 proteolytically process SUMO1" in the Reactome database.SENP1,2,5 proteolytically process SUMO1SENP1,2,5 proteolytically process SUMO1This 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>Reactome DB_ID: 106726461nucleoplasmGO0005654UniProt:Q8N0B4SUMOReactomehttp://www.reactome.orgDictyostelium discoideumNCBI Taxonomy44689UniProtQ8N0B4Chain Coordinates2EQUAL101EQUALReactome DB_ID: 1066159812EQUAL97EQUALPHYSIOL-LEFT-TO-RIGHTACTIVATIONConverted from EntitySet in ReactomeReactome DB_ID: 10672657SENP1,2,5 [nucleoplasm]Converted from EntitySet in Reactome. Each synonym is a name of a PhysicalEntity, and each XREF points to one PhysicalEntitySENP5 [nucleoplasm]SENP1 [nucleoplasm]SENP2 [nucleoplasm]UniProtQ54DG4GO0070139GO molecular functionReactome Database ID Release 7510672658Database 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=10672658Reactome Database ID Release 7510672660Database 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=10672660ReactomeR-DDI-29908401Reactome 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-DDI-2990840.1The SUMO1 precursor has 4 extra residues at the C-terminus which can be removed endoproteolytically by either SENP1, SENP2, or SENP5 (Zheng and Au, 2005, Mikolajczyk et al. 2007). The order of processing activity is: SENP1 greater than SENP2 greater than SENP5 (Mikolajczyk et al. 2007). Both SENP1 and SENP2 shuttle between the nucleus and cytoplasmic and both are predominantly nucleoplasmic (Bailey and O'Hare 2004, Kim et al. 2005, Zhang et al. 2002, Hang and Dasso 2002, Itahana et al. 2006).15487983Pubmed2005Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1Xu, ZhengAu, SWBiochem. J. 386:325-3016738331Pubmed2006Nucleocytoplasmic shuttling modulates activity and ubiquitination-dependent turnover of SUMO-specific protease 2Itahana, YokoYeh, Edward T HZhang, YanpingMol. Cell. Biol. 26:4675-8912192048Pubmed2002Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complexZhang, HSaitoh, HisatoMatunis, Michael JMol. Cell. Biol. 22:6498-50816253240Pubmed2005Desumoylation of homeodomain-interacting protein kinase 2 (HIPK2) through the cytoplasmic-nuclear shuttling of the SUMO-specific protease SENP1Kim, Young HoSung, Ki SaLee, Sook-JeongKim, Yong-OuChoi, Cheol YongKim, YongsokFEBS Lett. 579:6272-811896061Pubmed2002Association of the human SUMO-1 protease SENP2 with the nuclear poreHang, JunDasso, MaryJ. Biol. Chem. 277:19961-617591783Pubmed2007Small ubiquitin-related modifier (SUMO)-specific proteases: profiling the specificities and activities of human SENPsMikolajczyk, JowitaDrag, MBékés, MiklósCao, John TRonai, Ze'evSalvesen, Guy SJ. Biol. Chem. 282:26217-2414563852Pubmed2004Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1Bailey, DanielO'Hare, PeterJ. Biol. Chem. 279:692-703inferred by electronic annotationIEAGOIEA