MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it http://mint.bio.uniroma2.it/mint wei-2013a-1 The Aberrant Expression and Localization of Prohibitin During Apoptosis of Human Cholangiocarcinoma Mz-ChA-1 Cells human-liver Homo sapiens liver liver liver fluorescence imaging fluorescence microscopy fluorescence imaging immunostaining immunostaining Wei Song1,2 #, Ling Tian1,#, Shan-Shan Li1, Dong-Yan Shen3,*, Qing-Xi Chen1,* chenqx@xmu.edu.cn 2013 imex curation Song W., Tian L., Li S.S., Shen D.Y., Chen Q.X. FEBS Lett. (0014-5793) Only protein-protein interactions phb_human Prohibitin PHB PHB1 protein protein human Homo sapiens Human MAAKVFESIGKFGLALAVAGGVVNSALYNVDAGHRAVIFDRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVASQLPRIFTSIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAKQVAQQEAERARFVVEKAEQQKKAAIISAEGDSKAAELIANSLATAGDGLIELRKLEAAEDIAYQLSRSRNITYLPAGQSVLLQLPQ aif1_human Allograft inflammatory factor 1 AIF1 G1 IBA1 Ionized calcium-binding adapter molecule 1 Protein G1 protein protein human Homo sapiens Human MSQTRDLQGGKAFGLLKAQQEERLDEINKQFLDDPKYSSDEDLPSKLEGFKEKYMEFDLNGNGDIDIMSLKRMLEKLGVPKTHLELKKLIGEVSSGSGETFSYPDFLRMMLGKRSAILKMILMYEEKAREKEKPTGPPAKKAISELP p53_human Cellular tumor antigen p53 TP53 P53 Tumor suppressor p53 Phosphoprotein p53 Antigen NY-CO-13 protein protein human Homo sapiens Human MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD rb_human Retinoblastoma-associated protein pRb pp110 p105-Rb RB1 p110-RB1 protein protein human Homo sapiens Human MPPKTPRKTAATAAAAAAEPPAPPPPPPPEEDPEQDSGPEDLPLVRLEFEETEEPDFTALCQKLKIPDHVRERAWLTWEKVSSVDGVLGGYIQKKKELWGICIFIAAVDLDEMSFTFTELQKNIEISVHKFFNLLKEIDTSTKVDNAMSRLLKKYDVLFALFSKLERTCELIYLTQPSSSISTEINSALVLKVSWITFLLAKGEVLQMEDDLVISFQLMLCVLDYFIKLSPPMLLKEPYKTAVIPINGSPRTPRRGQNRSARIAKQLENDTRIIEVLCKEHECNIDEVKNVYFKNFIPFMNSLGLVTSNGLPEVENLSKRYEEIYLKNKDLDARLFLDHDKTLQTDSIDSFETQRTPRKSNLDEEVNVIPPHTPVRTVMNTIQQLMMILNSASDQPSENLISYFNNCTVNPKESILKRVKDIGYIFKEKFAKAVGQGCVEIGSQRYKLGVRLYYRVMESMLKSEEERLSIQNFSKLLNDNIFHMSLLACALEVVMATYSRSTSQNLDSGTDLSFPWILNVLNLKAFDFYKVIESFIKAEGNLTREMIKHLERCEHRIMESLAWLSDSPLFDLIKQSKDREGPTDHLESACPLNLPLQNNHTAADMYLSPVRSPKKKGSTTRVNSTANAETQATSAFQTQKPLKSTSLSLFYKKVYRLAYLRLNTLCERLLSEHPELEHIIWTLFQHTLQNEYELMRDRHLDQIMMCSMYGICKVKNIDLKFKIIVTAYKDLPHAVQETFKRVLIKEEEYDSIIVFYNSVFMQRLKTNILQYASTRPPTLSPIPHIPRSPYKFPSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFGTSEKFQKINQMVCNSDRVLKRSAEGSNPPKPLKKLRFDIEGSDEADGSKHLPGESKFQQKLAEMTSTRTRMQKQKMNDSMDTSNKEEK fos_human Proto-oncogene c-Fos Cellular oncogene fos G0/G1 switch regulatory protein 7 FOS G0S7 protein protein human Homo sapiens Human MMFSGFNADYEASSSRCSSASPAGDSLSYYHSPADSFSSMGSPVNAQDFCTDLAVSSANFIPTVTAISTSPDLQWLVQPALVSSVAPSQTRAPHPFGVPAPSAGAYSRAGVVKTMTGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPDDLGFPEEMSVASLDLTGGLPEVATPESEEAFTLPLLNDPEPKPSVEPVKSISSMELKTEPFDDFLFPASSRPSGSETARSVPDMDLSGSFYAADWEPLHSGSLGMGPMATELEPLCTPVVTCTPSCTAYTSSFVFTYPEADSFPSCAAAHRKGSSSNEPSSDSLSSPTLLAL aif1-phb 1468803 n/a PHB 1468804 immunostaining immunostaining unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell n/a AIF 1468805 immunostaining immunostaining unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization false false false f3a f3b f3c f3d f3e f3f The results of merged fluorescence revealed that PHB co-localized with AIF near the nuclear membrane (Figure 3 A–C). After treatment, the green fluorescence of AIF was greatly enhanced and uniformly distributed in the nucleus. The merged fluorescence revealed that the co-localization of PHB with AIF was clearly present in the nucleus but not in the cytoplasm, suggesting that the co-localization between PHB and AIF disappeared from the cytoplasm adjacent to the nuclear membrane (Figure 3 D–F). p53-phb-1 1468803 n/a p53 1468806 immunostaining immunostaining unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell n/a PHB 1468804 immunostaining immunostaining unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization false false false f3g f3h f3i f3j f3k f3l The yellow merged fluorescence indicated that PHB clearly co-localized with p53 in the nuclear membrane region (Figure 3 G–I). After ESC-3 treatment, the green color was enhanced and was scattered in the nucleus. The merged fluorescence suggested that the region of co-localization between PHB and p53 was clearly in the nucleus and was moderately decreased in the cytoplasm near the nuclear membrane (Figure 3 J–L). phb-tp53-5 1468803 n/a PHB 1468804 immunostaining immunostaining unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell n/a Rb 1468807 immunostaining immunostaining unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization false false false f3m f3n f3o f3p f3q f3r In the control cells, the FITC-labeled Rb emitting green fluorescence was primarily distributed in the cytoplasm. The density of the fluorescence at the periphery of the nucleus was relatively stronger, while the fluorescence within the nucleus was weaker. The merged yellow fluorescence revealed that PHB co-localized with Rb in the cytoplasmic compartment, especially near the nucleus (Figure 3 M–O). After ESC-3 treatment, the green Rb fluorescence was enhanced and primarily distributed in the nucleus but had weakened in the cytoplasm. The orange fluorescence appeared in the nucleus, suggesting that the co-localization of PHB with Rb shifted from the cytoplasm to the nucleus (Figure 3 P–R). phb-c-1 1468803 n/a PHB 1468804 immunostaining immunostaining unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell n/a c-Fos 1468808 immunostaining immunostaining unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization false false false f3s f3t f3u f3v f3w f3x The result of merged fluorescence revealed that PHB co-localized with c-Fos in the cytoplasm, especially near the nuclear membrane (Figure 3 S–U). After treatment with ESC-3, the green c-Fos fluorescence was greatly decreased in the cytoplasm and was primarily localized to the nucleus. The merged yellow fluorescence suggested that the co-localization of PHB with c-Fos decreased in the cytoplasm and increased 9 in the nucleus, indicating that the co-localization of PHB with c-Fos shifted from the cytoplasm to the nucleus (Figure 3 V–X).