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 yu_jen-2013-2 Localization of SERBP1 in stress granules and nucleoli human-hela Homo sapiens epitheloid cervix carcinoma cells Human hela Human epitheloid cervix carcinoma HeLa cells derivation: cervix; epithelial; adenocarcinoma ATCC no:CCL-2 fluorescence imaging fluorescence microscopy fluorescence imaging immunostaining immunostaining Yu-Jen Lee1, Hung-Ming Wei2, Ling-Yun Chen1 and Chuan Li2,3 cli@csmu.edu.tw 2013 Only protein-protein interactions imex curation yu_jen-2013-1 Localization of SERBP1 in stress granules and nucleoli human-hela Homo sapiens epitheloid cervix carcinoma cells Human hela Human epitheloid cervix carcinoma HeLa cells derivation: cervix; epithelial; adenocarcinoma ATCC no:CCL-2 anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Yu-Jen Lee1, Hung-Ming Wei2, Ling-Yun Chen1 and Chuan Li2,3 cli@csmu.edu.tw 2013 Only protein-protein interactions imex curation tia1_human Nucleolysin TIA-1 isoform p40 TIA1 p40-TIA-1 RNA-binding protein TIA-1 T-cell-restricted intracellular antigen-1 protein protein human Homo sapiens Human MEDEMPKTLYVGNLSRDVTEALILQLFSQIGPCKNCKMIMDTAGNDPYCFVEFHEHRHAAAALAAMNGRKIMGKEVKVNWATTPSSQKKDTSSSTVVSTQRSQDHFHVFVGDLSPEITTEDIKAAFAPFGRISDARVVKDMATGKSKGYGFVSFFNKWDAENAIQQMGGQWLGGRQIRTNWATRKPPAPKSTYESNTKQLSYDEVVNQSSPSNCTVYCGGVTSGLTEQLMRQTFSPFGQIMEIRVFPDKGYSFVRFNSHESAAHAIVSVNGTTIEGHVVKCYWGKETLDMINPVQQQNQIGYPQPYGQWGQWYGNAQQIGQYMPNGWQVPAYGMYGQAWNQQGFNQTQSSAPWMGPNYGVQPPQGQNGSMLPNQPSGYRVAGYETQ pairb_human Plasminogen activator inhibitor 1 RNA-binding protein PAI1 RNA-binding protein 1 SERPINE1 mRNA-binding protein 1 CGI-55 SERBP1 PAIRBP1 protein protein human Homo sapiens Human MPGHLQEGFGCVVTNRFDQLFDDESDPFEVLKAAENKKKEAGGGGVGGPGAKSAAQAAAQTNSNAAGKQLRKESQKDRKNPLPPSVGVVDKKEETQPPVALKKEGIRRVGRRPDQQLQGEGKIIDRRPERRPPRERRFEKPLEEKGEGGEFSVDRPIIDRPIRGRGGLGRGRGGRGRGMGRGDGFDSRGKREFDRHSGSDRSSFSHYSGLKHEDKRGGSGSHNWGTVKDELTESPKYIQKQISYNYSDLDQSNVTEETPEGEEHHPVADTENKENEVEEVKEEGPKEMTLDEWKAIQNKDRAKVEFNIRKPNEGADGQWKKGFVLHKSKSEEAHAEDSVMDHHFRKPANDITSQLEINFGDLGRPGRGGRGGRGGRGRGGRPNRGSRTDKSSASAPDVDDPEAFPALA roa1_human Heterogeneous nuclear ribonucleoprotein A1 HNRNPA1 HNRPA1 Helix-destabilizing protein Single-strand RNA-binding protein hnRNP core protein A1 protein protein human Homo sapiens Human MSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGGYGGGGPGYSGGSRGYGSGGQGYGNQGSGYGGSGSYDSYNNGGGGGFGGGSGSNFGGGGSYNDFGNYNNQSSNFGPMKGGNFGGRSSGPYGGGGQYFAKPRNQGGYGGSSSSSSYGSGRRF nucl_human Nucleolin NCL Protein C23 protein protein human Homo sapiens Human MVKLAKAGKNQGDPKKMAPPPKEVEEDSEDEEMSEDEEDDSSGEEVVIPQKKGKKAAATSAKKVVVSPTKKVAVATPAKKAAVTPGKKAAATPAKKTVTPAKAVTTPGKKGATPGKALVATPGKKGAAIPAKGAKNGKNAKKEDSDEEEDDDSEEDEEDDEDEDEDEDEIEPAAMKAAAAAPASEDEDDEDDEDDEDDDDDEEDDSEEEAMETTPAKGKKAAKVVPVKAKNVAEDEDEEEDDEDEDDDDDEDDEDDDDEDDEEEEEEEEEEPVKEAPGKRKKEMAKQKAAPEAKKQKVEGTEPTTAFNLFVGNLNFNKSAPELKTGISDVFAKNDLAVVDVRIGMTRKFGYVDFESAEDLEKALELTGLKVFGNEIKLEKPKGKDSKKERDARTLLAKNLPYKVTQDELKEVFEDAAEIRLVSKDGKSKGIAYIEFKTEADAEKTFEEKQGTEIDGRSISLYYTGEKGQNQDYRGGKNSTWSGESKTLVLSNLSYSATEETLQEVFEKATFIKVPQNQNGKSKGYAFIEFASFEDAKEALNSCNKREIEGRAIRLELQGPRGSPNARSQPSKTLFVKGLSEDTTEETLKESFDGSVRARIVTDRETGSSKGFGFVDFNSEEDAKAAKEAMEDGEIDGNKVTLDWAKPKGEGGFGGRGGGRGGFGGRGGGRGGRGGFGGRGRGGFGGRGGFRGGRGGGGDHKPQGKKTKFE anm1_human Protein arginine N-methyltransferase 1 PRMT1 Interferon receptor 1-bound protein 4 Histone-arginine N-methyltransferase PRMT1 HMT2 HRMT1L2 IR1B4 protein protein human Homo sapiens Human MAAAEAANCIMENFVATLANGMSLQPPLEEVSCGQAESSEKPNAEDMTSKDYYFDSYAHFGIHEEMLKDEVRTLTYRNSMFHNRHLFKDKVVLDVGSGTGILCMFAAKAGARKVIGIECSSISDYAVKIVKANKLDHVVTIIKGKVEEVELPVEKVDIIISEWMGYCLFYESMLNTVLYARDKWLAPDGLIFPDRATLYVTAIEDRQYKDYKIHWWENVYGFDMSCIKDVAIKEPLVDVVDPKQLVTNACLIKEVDIYTVKVEDLTFTSPFCLQVKRNDYVHALVAYFNIEFTRCHKRTGFSTSPESPYTHWKQTVFYMEDYLTVKTGEEIFGTIGMRPNAKNNRDLDFTIDLDFKGQLCELSCSTDYRMR fmr1_human Synaptic functional regulator FMR1 FMR1 Fragile X mental retardation protein 1 protein protein human Homo sapiens Human MEELVVEVRGSNGAFYKAFVKDVHEDSITVAFENNWQPDRQIPFHDVRFPPPVGYNKDINESDEVEVYSRANEKEPCCWWLAKVRMIKGEFYVIEYAACDATYNEIVTIERLRSVNPNKPATKDTFHKIKLDVPEDLRQMCAKEAAHKDFKKAVGAFSVTYDPENYQLVILSINEVTSKRAHMLIDMHFRSLRTKLSLIMRNEEASKQLESSRQLASRFHEQFIVREDLMGLAIGTHGANIQQARKVPGVTAIDLDEDTCTFHIYGEDQDAVKKARSFLEFAEDVIQVPRNLVGKVIGKNGKLIQEIVDKSGVVRVRIEAENEKNVPQEEEIMPPNSLPSNNSRVGPNAPEEKKHLDIKENSTHFSQPNSTKVQRVLVASSVVAGESQKPELKAWQGMVPFVFVGTKDSIANATVLLDYHLNYLKEVDQLRLERLQIDEQLRQIGASSRPPPNRTDKEKSYVTDDGQGMGRGSRPYRNRGHGRRGPGYTSGTNSEASNASETESDHRDELSDWSLAPTEEERESFLRRGDGRRRGGGGRGQGGRGRGGGFKGNDDHSRTDNRPRNPREAKGRTTDGSLQIRVDCNNERSVHTKTLQNTSSEGSRLRTGKDRNQKKEKPDSVDGQQPLVNGVP ews_human RNA-binding protein EWS EWSR1 EWS EWS oncogene Ewing sarcoma breakpoint region 1 protein protein protein human Homo sapiens Human MASTDYSTYSQAAAQQGYSAYTAQPTQGYAQTTQAYGQQSYGTYGQPTDVSYTQAQTTATYGQTAYATSYGQPPTGYTTPTAPQAYSQPVQGYGTGAYDTTTATVTTTQASYAAQSAYGTQPAYPAYGQQPAATAPTRPQDGNKPTETSQPQSSTGGYNQPSLGYGQSNYSYPQVPGSYPMQPVTAPPSYPPTSYSSTQPTSYDQSSYSQQNTYGQPSSYGQQSSYGQQSSYGQQPPTSYPPQTGSYSQAPSQYSQQSSSYGQQSSFRQDHPSSMGVYGQESGGFSGPGENRSMSGPDNRGRGRGGFDRGGMSRGGRGGGRGGMGSAGERGGFNKPGGPMDEGPDLDLGPPVDPDEDSDNSAIYVQGLNDSVTLDDLADFFKQCGVVKMNKRTGQPMIHIYLDKETGKPKGDATVSYEDPPTAKAAVEWFDGKDFQGSKLKVSLARKKPPMNSMRGGLPPREGRGMPPPLRGGPGGPGGPGGPMGRMGGRGGDRGGFPPRGPRGSRGNPSGGGNVQHRAGDWQCPNPGCGNQNFAWRTECNQCKAPKPEGFLPPPFPPPGGDRGRGGPGGMRGGRGGLMDRGGPGGMFRGGRGGDRGGFRGGRGMDRGGFGGGRRGGPGGPPGPLMEQMGGRRGGRGGPGKMDKGEHRQERRDRPY fxr2_human Fragile X mental retardation syndrome-related protein 2 FXR2 FMR1L2 protein protein human Homo sapiens Human MGGLASGGDVEPGLPVEVRGSNGAFYKGFVKDVHEDSVTIFFENNWQSERQIPFGDVRLPPPADYNKEITEGDEVEVYSRANEQEPCGWWLARVRMMKGDFYVIEYAACDATYNEIVTLERLRPVNPNPLATKGSFFKVTMAVPEDLREACSNENVHKEFKKALGANCIFLNITNSELFILSTTEAPVKRASLLGDMHFRSLRTKLLLMSRNEEATKHLETSKQLAAAFQEEFTVREDLMGLAIGTHGANIQQARKVPGVTAIELGEETCTFRIYGETPEACRQARSYLEFSEDSVQVPRNLVGKVIGKNGKVIQEIVDKSGVVRVRVEGDNDKKNPREEGMVPFIFVGTRENISNAQALLEYHLSYLQEVEQLRLERLQIDEQLRQIGLGFRPPGSGRGSGGSDKAGYSTDESSSSSLHATRTYGGSYGGRGRGRRTGGPAYGPSSDVSTASETESEKREEPNRAGPGDRDPPTRGEESRRRPTGGRGRGPPPAPRPTSRYNSSSISSVLKDPDSNPYSLLDTSEPEPPVDSEPGEPPPASARRRRSRRRRTDEDRTVMDGGLESDGPNMTENGLEDESRPQRRNRSRRRRNRGNRTDGSISGDRQPVTVADYISRAESQSRQRPPLERTKPSEDSLSGQKGDSVSKLPKGPSENGELSAPLELGSMVNGVS serbp1-tia1 1456445 n/a TIA-1 1456447 immunostaining immunostaining unspecified role unspecified role unspecified role unspecified role physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell n/a SERBP1 1456448 immunostaining immunostaining unspecified role unspecified role unspecified role unspecified role physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization false false false F2A serbp1-tia1-1 1456445 n/a TIA-1 1456447 immunostaining immunostaining unspecified role unspecified role unspecified role unspecified role physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell n/a SERBP1 1456448 tag fluorescence tag visualisation by fluorescence tag fluorescence unspecified role unspecified role unspecified role unspecified role over-expressed over expressed level over-expressed fixed cell fixed cell egfp tag egfp tag enhanced green fluorescent protein tag enhanced green fluorescent protein EGFP enhanced green fluorescent protein EGFP egfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false colocalization colocalization false false false F2B F3 T1 SF2 ST1 The SERBP1 and TIA1 double positive SGs reduced from 70% for the full-length to about 50% for the truncated ones. Furthermore, the number of SERBP1-positive SGs per cell and SERBP1-positive area in SGs also reduced in the deletions (Table S1). The results show that less SERBP1 deletion proteins can be recruited to the SGs. We then analyzed the single domain constructs (1-150, 151-270, 271-387). All of the three single domains of SERBP1 could relocalize to cytoplasmic SGs, however, with even fewer cells containing the SERBP1-positive SGs (~40%) and fewer SGs as SERBP1 positive (~35%) (Fig. S2 and Table 1). The results indicate that any segment of SERBP1 is sufficient for the SG localization but complete SG distribution requires the cooperation of more than one domain. hnrnpa1-serbp1 1456445 n/a hnRNPA1 1456449 immunostaining immunostaining unspecified role unspecified role unspecified role unspecified role physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell n/a SERBP1 1456448 tag fluorescence tag visualisation by fluorescence tag fluorescence unspecified role unspecified role unspecified role unspecified role over-expressed over expressed level over-expressed fixed cell fixed cell egfp tag egfp tag enhanced green fluorescent protein tag enhanced green fluorescent protein EGFP enhanced green fluorescent protein EGFP egfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false colocalization colocalization false false false F2C serbp1-tia1-2 1456445 n/a SERBP1 1456448 immunostaining immunostaining unspecified role unspecified role unspecified role unspecified role physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell n/a C23 1456450 immunostaining immunostaining unspecified role unspecified role unspecified role unspecified role physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization false false false F4A t2 serbp1-tia1-3 1456445 n/a C23 1456450 immunostaining immunostaining unspecified role unspecified role unspecified role unspecified role physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell n/a SERBP1 1456448 tag fluorescence tag visualisation by fluorescence tag fluorescence unspecified role unspecified role unspecified role unspecified role over-expressed over expressed level over-expressed fixed cell fixed cell egfp tag egfp tag enhanced green fluorescent protein tag enhanced green fluorescent protein EGFP enhanced green fluorescent protein EGFP egfp tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false colocalization colocalization false false false f4b t2 The SERBP1 and TIA1 double positive SGs reduced from 70% for the full-length to about 50% for the truncated ones. Furthermore, the number of SERBP1-positive SGs per cell and SERBP1-positive area in SGs also reduced in the deletions (Table S1). The results show that less SERBP1 deletion proteins can be recruited to the SGs. We then analyzed the single domain constructs (1-150, 151-270, 271-387). All of the three single domains of SERBP1 could relocalize to cytoplasmic SGs, however, with even fewer cells containing the SERBP1-positive SGs (~40%) and fewer SGs as SERBP1 positive (~35%) (Fig. S2 and Table 1). The results indicate that any segment of SERBP1 is sufficient for the SG localization but complete SG distribution requires the cooperation of more than one domain. serbp1-hnrnpa1-1 1456446 n/a SERBP1 1456448 anti tag western anti tag western blot anti tag western unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell flag tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false n/a PRMT1 1456451 western blot western blot Immuno blot Immuno blot unspecified role unspecified role prey prey living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level n/a hnRNPA1 1456449 western blot western blot Immuno blot Immuno blot unspecified role unspecified role prey prey living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level association association false false false f1a We first showed that hnRNPA1 co-immunoprecipitated with FLAG-tagged SERBP1 (Fig. 1A). The interaction requires RNA because addition of RNase to the HeLa cell extract before the immunoprecipitation totally blocked the interaction. On the other hand, interaction of PRMT1 that can directly interact with SERBP1 [17] was not influenced by RNase treatment. serbp1-fmr1 1456446 n/a FMRP 1456452 western blot western blot Immuno blot Immuno blot unspecified role unspecified role prey prey living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level n/a hnRNPA1 1456449 western blot western blot Immuno blot Immuno blot unspecified role unspecified role prey prey living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level n/a SERBP1 1456448 anti tag western anti tag western blot anti tag western unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell flag tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false binding region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain false association association false false false SF1 We first showed that hnRNPA1 co-immunoprecipitated with FLAG-tagged SERBP1 (Fig. 1A). The interaction requires RNA because addition of RNase to the HeLa cell extract before the immunoprecipitation totally blocked the interaction. On the other hand, interaction of PRMT1 that can directly interact with SERBP1 [17] was not influenced by RNase treatment. The middle RG segment that is important for SERBP1 nuclear localization [2] is not required nor sufficient for the interaction, because RG-deletion interacts with hnRNPA1 or FMRP, while only very weak interaction can be detected for the middle segment (151-270) containing the RG sequences (Fig.S1). In comparison, SERBP1 constructs with N-terminal deletions (151-387) or the N-terminal domain alone (1-150) showed hnRNPA1 or FMRP interaction, indicating that this segment is not required but sufficient for the interaction (Fig. S1). ewsr1-fmr1 1456446 n/a SERBP1 1456448 anti tag western anti tag western blot anti tag western unspecified role unspecified role bait bait over-expressed over expressed level over-expressed living cell living cell flag tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined false n/a EWS 1456453 western blot western blot Immuno blot Immuno blot unspecified role unspecified role prey prey living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level n/a FMRP 1456452 western blot western blot Immuno blot Immuno blot unspecified role unspecified role prey prey living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level n/a FRX2 1456454 western blot western blot Immuno blot Immuno blot unspecified role unspecified role prey prey living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level association association false false false f1b