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 Signal-peptide-peptidase-like 2a (SPPL2a) is targeted to lysosomes/late endosomes by a tyrosine motif in its C-terminal tail. Signal-peptide-peptidase-like 2a (SPPL2a) is targeted to lysosomes/late endosomes by a tyrosine motif in its C-terminal tail. FEBS Lett. (0014-5793) 2011 imex curation Behnke J., Schneppenheim J., Koch-Nolte F., Haag F., Saftig P., Schröder B. suggested by lperfetto Only protein-protein interactions 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 predetermined predetermined participant predetermined Behnke J., Schneppenheim J., Koch-Nolte F., Haag F., Saftig P., Schröder B. suggested by lperfetto FEBS Lett. (0014-5793) 2011 Only protein-protein interactions imex curation Signal-peptide-peptidase-like 2a (SPPL2a) is targeted to lysosomes/late endosomes by a tyrosine motif in its C-terminal tail. Signal-peptide-peptidase-like 2a (SPPL2a) is targeted to lysosomes/late endosomes by a tyrosine motif in its C-terminal tail. FEBS Lett. (0014-5793) 2011 imex curation Behnke J., Schneppenheim J., Koch-Nolte F., Haag F., Saftig P., Schröder B. suggested by lperfetto Only protein-protein interactions mouse-embryonic_fibroblast Mus musculus embryonic fibroblasts embryonic_fibroblast Embryonic fibroblast Fibroblasts taken from an embryonic as opposed to a foetal or adult source. Foetus is defined as the stage at which tissue diferentiation is initiated. Tissue taken from an embryonic as opposed to a foetal or adult source. Embryo is defined as the development stage prior to organ formation. fluorescence imaging fluorescence microscopy fluorescence imaging immunostaining immunostaining Behnke J., Schneppenheim J., Koch-Nolte F., Haag F., Saftig P., Schröder B. suggested by lperfetto FEBS Lett. (0014-5793) 2011 Only protein-protein interactions imex curation lamp2_mouse Lysosome-associated membrane glycoprotein 2 Lysosomal membrane glycoprotein type B CD107 antigen-like family member B Lamp2 Lamp-2 protein protein mouse Mus musculus Mouse MCLSPVKGAKLILIFLFLGAVQSNALIVNLTDSKGTCLYAEWEMNFTITYETTNQTNKTITIAVPDKATHDGSSCGDDRNSAKIMIQFGFAVSWAVNFTKEASHYSIHDIVLSYNTSDSTVFPGAVAKGVHTVKNPENFKVPLDVIFKCNSVLTYNLTPVVQKYWGIHLQAFVQNGTVSKNEQVCEEDQTPTTVAPIIHTTAPSTTTTLTPTSTPTPTPTPTPTVGNYSIRNGNTTCLLATMGLQLNITEEKVPFIFNINPATTNFTGSCQPQSAQLRLNNSQIKYLDFIFAVKNEKRFYLKEVNVYMYLANGSAFNISNKNLSFWDAPLGSSYMCNKEQVLSVSRAFQINTFNLKVQPFNVTKGQYSTAQDCSADEDNFLVPIAVGAALGGVLILVLLAYFIGLKRHHTGYEQF 053A874B4DF67C88 lamp2_human Lysosome-associated membrane glycoprotein 2 LAMP2 CD107 antigen-like family member B LGP-96 protein protein human Homo sapiens Human MVCFRLFPVPGSGLVLVCLVLGAVRSYALELNLTDSENATCLYAKWQMNFTVRYETTNKTYKTVTISDHGTVTYNGSICGDDQNGPKIAVQFGPGFSWIANFTKAASTYSIDSVSFSYNTGDNTTFPDAEDKGILTVDELLAIRIPLNDLFRCNSLSTLEKNDVVQHYWDVLVQAFVQNGTVSTNEFLCDKDKTSTVAPTIHTTVPSPTTTPTPKEKPEAGTYSVNNGNDTCLLATMGLQLNITQDKVASVININPNTTHSTGSCRSHTALLRLNSSTIKYLDFVFAVKNENRFYLKEVNISMYLVNGSVFSIANNNLSYWDAPLGSSYMCNKEQTVSVSGAFQINTFDLRVQPFNVTQGKYSTAQDCSADDDNFLVPIAVGAALAGVLILVLLAYFIGLKHHHAGYEQF 9E08E3B62D58F454 spp2a_mouse Signal peptide peptidase-like 2A Sppl2a Psl2 MNCb-3763 Imp3 Intramembrane protease 3 Presenilin-like protein 2 protein protein mouse Mus musculus Mouse MGLLHSLHAPAAALLWSCLLGLAAAQEAILHASTNGVSSLSKDYCMYYNNNWTRLPSSLENATSLSLMNLTGTALCHLSDIPPDGIRNKAVVVHWGPCHFLEKARIAQEGGAAALLIANNSVLIPSSRNKSTFQNVTVLIAVITQKDFKDMKETLGDDITVKMYSPSWPNFDYTLVVIFVIAVFTVALGGYWSGLIELENMKSVEDAEDRETRKKKDDYLTFSPLTVVVFVVICCIMIVLLYFFYRWLVYVMIAIFCIASSMSLYNCLSALIHRMPCGQCTILCCGKNIKVSLIFLSGLCISVAVVWAVFRNEDRWAWILQDILGIAFCLNLIKTMKLPNFMSCVILLGLLLIYDVFFVFITPFITKNGESIMVELAAGPFENAEKLPVVIRVPKLMGYSVMSVCSVPVSVLGFGDIIVPGLLIAYCRRFDVQTGSSIYYISSTIAYAVGMIITFVVLMVMKTGQPALLYLVPCTLITVSVVAWSRKEMKKFWKGSSYQVMDHLDYSTNEENPVTTDEQIVQQ mint May act as intramembrane protease A15109A71FCF25C4 lamp2-sppl2a-3 1 SPPL2a 5 anti tag immunost anti tag immunostaining anti tag immunost predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed fixed cell fixed cell myc tag myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q9JJF9:p.Tyr498Ala mutation disrupting interaction mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Y A Tue Jul 12 10:18:23 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation disrupting' Wed May 02 14:46:16 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr498ala' Tue Jun 30 15:48:43 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr498Ala' LAMP2 4 immunostaining immunostaining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization homomint mint myc-tagged murine SPPL2a in HeLa cells is present in lysosomes/late endosomes as revealed by colocalisation with the lysosomal/late endosomal membrane protein LAMP2 (Fig. 1B, upper panel). f1b f2b f3b We investigated a possible contribution of the two putative tyrosine-based sorting motifs at Y498 and Y506 by site-directed mutagenesis (Fig. 3A) and overexpression of the mutants in HeLa cells (Fig. 3B). Mutation of the proximal tyrosine residue (Y498A) impaired lysosomal/late endosomal targeting of SPPL2a and significant amounts of the mutant protein were detected at the plasma membrane. In contrast, mutation of the distal motif (Y506A) had no influence on the localisation of SPPL2a. Like the single Y498A mutant, a double mutant of both motifs (YY498/506AA) was observed at the plasma membrane to a predominant degree (Fig.3B). lamp2-sppl2a-1 1 SPPL2a 5 anti tag immunost anti tag immunostaining anti tag immunost predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component over-expressed over expressed level over-expressed fixed cell fixed cell myc tag myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Q9JJF9:p.Tyr506Ala mutation disrupting interaction mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Y A Tue Jul 12 10:56:26 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation disrupting' Wed May 02 15:42:31 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr506ala' Tue Jun 30 16:43:39 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr506Ala' Q9JJF9:p.Tyr498Ala mutation disrupting interaction mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain Y A Tue Jul 12 10:56:27 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'mutation disrupting' Wed May 02 17:39:25 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'tyr498ala' Tue Jun 30 16:58:55 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Tyr498Ala' LAMP2 4 immunostaining immunostaining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization homomint mint myc-tagged murine SPPL2a in HeLa cells is present in lysosomes/late endosomes as revealed by colocalisation with the lysosomal/late endosomal membrane protein LAMP2 (Fig. 1B, upper panel). f1b f2b f3b We investigated a possible contribution of the two putative tyrosine-based sorting motifs at Y498 and Y506 by site-directed mutagenesis (Fig. 3A) and overexpression of the mutants in HeLa cells (Fig. 3B). Mutation of the proximal tyrosine residue (Y498A) impaired lysosomal/late endosomal targeting of SPPL2a and significant amounts of the mutant protein were detected at the plasma membrane. In contrast, mutation of the distal motif (Y506A) had no influence on the localisation of SPPL2a. Like the single Y498A mutant, a double mutant of both motifs (YY498/506AA) was observed at the plasma membrane to a predominant degree (Fig.3B). lamp2-sppl2a-2 2 SPPL2a 5 immunostaining immunostaining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell LAMP2 3 immunostaining immunostaining predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component physiological level physiological level endogenous level endogenous endogenous endogenous level fixed cell fixed cell colocalization colocalization f1c homomint mint