I2D I2D SUMO modification of E1B-55K oncoprotein regulates isoform-specific binding to the tumour suppressor protein PML. SUMO modification of E1B-55K oncoprotein regulates isoform-specific binding to the tumour suppressor protein PML. Oncogene (0950-9232) 2010 imex curation Wimmer P., Schreiner S., Everett RD., Sirma H., Groitl P., Dobner T. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Baby rat kidney cells were used as a negative control. Two derivatives of this cell line AB120/AB115, stably expressing E1B-55K or mutant E1B-55K-NES were treated with 20nM leptomycin B for 2 hrs before methanol fixation. thomas.dobner@hpi.uni-hamburg.de 06-April-2011: Contacted by JYOTI. orchard Only protein-protein interactions Curated by: I2D - Interologous Interaction Database human-heparg Homo sapiens hepatoma heparg Homo sapiens hepatoma http://www.hpacultures.org.uk/products/celllines/heparg/hepargcells.jsp anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Wimmer P., Schreiner S., Everett RD., Sirma H., Groitl P., Dobner T. Apoptosis - Interactions involving proteins with a function related to apoptosis Baby rat kidney cells were used as a negative control. Two derivatives of this cell line AB120/AB115, stably expressing E1B-55K or mutant E1B-55K-NES were treated with 20nM leptomycin B for 2 hrs before methanol fixation. thomas.dobner@hpi.uni-hamburg.de Accepted 2010-DEC-23 by ORCHARD. 06-April-2011: Contacted by JYOTI. Oncogene (0950-9232) 2010 orchard Only protein-protein interactions imex curation Curated by: I2D - Interologous Interaction Database SUMO modification of E1B-55K oncoprotein regulates isoform-specific binding to the tumour suppressor protein PML. SUMO modification of E1B-55K oncoprotein regulates isoform-specific binding to the tumour suppressor protein PML. Oncogene (0950-9232) 2010 imex curation Wimmer P., Schreiner S., Everett RD., Sirma H., Groitl P., Dobner T. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Baby rat kidney cells were used as a negative control. Two derivatives of this cell line AB120/AB115, stably expressing E1B-55K or mutant E1B-55K-NES were treated with 20nM leptomycin B for 2 hrs before methanol fixation. thomas.dobner@hpi.uni-hamburg.de 06-April-2011: Contacted by JYOTI. orchard Only protein-protein interactions Curated by: I2D - Interologous Interaction Database human-h1299 Homo sapiens lung lymph node carcinoma h1299 Human lung lymph node carcinoma p53 null. These cells have also been reported to secrete the peptide hormone neuromedin B (NMB), but not gastrin releasing peptide (GRP). Also known as NCI H1299 or CRL-5803. http://www.lgcpromochem.com/atcc/ ATCC number: CRL-5803. ATCC number of the cell line is CRL-5803. anti tag coip anti tag coimmunoprecipitation anti tag coip western blot western blot Immuno blot Immuno blot Wimmer P., Schreiner S., Everett RD., Sirma H., Groitl P., Dobner T. Apoptosis - Interactions involving proteins with a function related to apoptosis Baby rat kidney cells were used as a negative control. Two derivatives of this cell line AB120/AB115, stably expressing E1B-55K or mutant E1B-55K-NES were treated with 20nM leptomycin B for 2 hrs before methanol fixation. thomas.dobner@hpi.uni-hamburg.de Accepted 2010-DEC-23 by ORCHARD. 06-April-2011: Contacted by JYOTI. Oncogene (0950-9232) 2010 orchard Only protein-protein interactions imex curation Curated by: I2D - Interologous Interaction Database SUMO modification of E1B-55K oncoprotein regulates isoform-specific binding to the tumour suppressor protein PML. SUMO modification of E1B-55K oncoprotein regulates isoform-specific binding to the tumour suppressor protein PML. Oncogene (0950-9232) 2010 imex curation Wimmer P., Schreiner S., Everett RD., Sirma H., Groitl P., Dobner T. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Baby rat kidney cells were used as a negative control. Two derivatives of this cell line AB120/AB115, stably expressing E1B-55K or mutant E1B-55K-NES were treated with 20nM leptomycin B for 2 hrs before methanol fixation. thomas.dobner@hpi.uni-hamburg.de 06-April-2011: Contacted by JYOTI. orchard Only protein-protein interactions Curated by: I2D - Interologous Interaction Database human-heparg Homo sapiens hepatoma heparg Homo sapiens hepatoma http://www.hpacultures.org.uk/products/celllines/heparg/hepargcells.jsp confocal microscopy confocal microscopy immunostaining immunostaining Wimmer P., Schreiner S., Everett RD., Sirma H., Groitl P., Dobner T. Apoptosis - Interactions involving proteins with a function related to apoptosis Baby rat kidney cells were used as a negative control. Two derivatives of this cell line AB120/AB115, stably expressing E1B-55K or mutant E1B-55K-NES were treated with 20nM leptomycin B for 2 hrs before methanol fixation. thomas.dobner@hpi.uni-hamburg.de Accepted 2010-DEC-23 by ORCHARD. 06-April-2011: Contacted by JYOTI. Oncogene (0950-9232) 2010 orchard Only protein-protein interactions imex curation Curated by: I2D - Interologous Interaction Database SUMO modification of E1B-55K oncoprotein regulates isoform-specific binding to the tumour suppressor protein PML. SUMO modification of E1B-55K oncoprotein regulates isoform-specific binding to the tumour suppressor protein PML. Oncogene (0950-9232) 2010 imex curation Wimmer P., Schreiner S., Everett RD., Sirma H., Groitl P., Dobner T. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Baby rat kidney cells were used as a negative control. Two derivatives of this cell line AB120/AB115, stably expressing E1B-55K or mutant E1B-55K-NES were treated with 20nM leptomycin B for 2 hrs before methanol fixation. thomas.dobner@hpi.uni-hamburg.de 06-April-2011: Contacted by JYOTI. orchard Only protein-protein interactions Curated by: I2D - Interologous Interaction Database human-h1299 Homo sapiens lung lymph node carcinoma h1299 Human lung lymph node carcinoma p53 null. These cells have also been reported to secrete the peptide hormone neuromedin B (NMB), but not gastrin releasing peptide (GRP). Also known as NCI H1299 or CRL-5803. http://www.lgcpromochem.com/atcc/ ATCC number: CRL-5803. ATCC number of the cell line is CRL-5803. anti bait coip anti bait coimmunoprecipitation anti bait coip anti tag western anti tag western blot anti tag western Wimmer P., Schreiner S., Everett RD., Sirma H., Groitl P., Dobner T. Apoptosis - Interactions involving proteins with a function related to apoptosis Baby rat kidney cells were used as a negative control. Two derivatives of this cell line AB120/AB115, stably expressing E1B-55K or mutant E1B-55K-NES were treated with 20nM leptomycin B for 2 hrs before methanol fixation. thomas.dobner@hpi.uni-hamburg.de Accepted 2010-DEC-23 by ORCHARD. 06-April-2011: Contacted by JYOTI. Oncogene (0950-9232) 2010 orchard Only protein-protein interactions imex curation Curated by: I2D - Interologous Interaction Database SUMO modification of E1B-55K oncoprotein regulates isoform-specific binding to the tumour suppressor protein PML. SUMO modification of E1B-55K oncoprotein regulates isoform-specific binding to the tumour suppressor protein PML. Oncogene (0950-9232) 2010 imex curation Wimmer P., Schreiner S., Everett RD., Sirma H., Groitl P., Dobner T. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Baby rat kidney cells were used as a negative control. Two derivatives of this cell line AB120/AB115, stably expressing E1B-55K or mutant E1B-55K-NES were treated with 20nM leptomycin B for 2 hrs before methanol fixation. thomas.dobner@hpi.uni-hamburg.de 06-April-2011: Contacted by JYOTI. orchard Only protein-protein interactions Curated by: I2D - Interologous Interaction Database rat-ab115 Rattus AB115 ab115 ab115-Baby Rat Kidney cell line cell line of polyclonal origin derived from transfection of primary BRK cells with pE1B-NES. fluorescence imaging fluorescence microscopy fluorescence imaging immunostaining immunostaining Wimmer P., Schreiner S., Everett RD., Sirma H., Groitl P., Dobner T. Apoptosis - Interactions involving proteins with a function related to apoptosis Baby rat kidney cells were used as a negative control. Two derivatives of this cell line AB120/AB115, stably expressing E1B-55K or mutant E1B-55K-NES were treated with 20nM leptomycin B for 2 hrs before methanol fixation. thomas.dobner@hpi.uni-hamburg.de Accepted 2010-DEC-23 by ORCHARD. 06-April-2011: Contacted by JYOTI. Oncogene (0950-9232) 2010 orchard Only protein-protein interactions imex curation Curated by: I2D - Interologous Interaction Database SUMO modification of E1B-55K oncoprotein regulates isoform-specific binding to the tumour suppressor protein PML. SUMO modification of E1B-55K oncoprotein regulates isoform-specific binding to the tumour suppressor protein PML. Oncogene (0950-9232) 2010 imex curation Wimmer P., Schreiner S., Everett RD., Sirma H., Groitl P., Dobner T. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Baby rat kidney cells were used as a negative control. Two derivatives of this cell line AB120/AB115, stably expressing E1B-55K or mutant E1B-55K-NES were treated with 20nM leptomycin B for 2 hrs before methanol fixation. thomas.dobner@hpi.uni-hamburg.de 06-April-2011: Contacted by JYOTI. orchard Only protein-protein interactions Curated by: I2D - Interologous Interaction Database rat-ab120 Rat AB120 ab120 AB120 AB120 expresses the Ad5 E1A and wild-type Ad5 E1B-55kDa proteins fluorescence imaging fluorescence microscopy fluorescence imaging immunostaining immunostaining Wimmer P., Schreiner S., Everett RD., Sirma H., Groitl P., Dobner T. Apoptosis - Interactions involving proteins with a function related to apoptosis Baby rat kidney cells were used as a negative control. Two derivatives of this cell line AB120/AB115, stably expressing E1B-55K or mutant E1B-55K-NES were treated with 20nM leptomycin B for 2 hrs before methanol fixation. thomas.dobner@hpi.uni-hamburg.de Accepted 2010-DEC-23 by ORCHARD. 06-April-2011: Contacted by JYOTI. Oncogene (0950-9232) 2010 orchard Only protein-protein interactions imex curation Curated by: I2D - Interologous Interaction Database SUMO modification of E1B-55K oncoprotein regulates isoform-specific binding to the tumour suppressor protein PML. SUMO modification of E1B-55K oncoprotein regulates isoform-specific binding to the tumour suppressor protein PML. Oncogene (0950-9232) 2010 imex curation Wimmer P., Schreiner S., Everett RD., Sirma H., Groitl P., Dobner T. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Baby rat kidney cells were used as a negative control. Two derivatives of this cell line AB120/AB115, stably expressing E1B-55K or mutant E1B-55K-NES were treated with 20nM leptomycin B for 2 hrs before methanol fixation. thomas.dobner@hpi.uni-hamburg.de 06-April-2011: Contacted by JYOTI. orchard Only protein-protein interactions Curated by: I2D - Interologous Interaction Database rat-ab120 Rat AB120 ab120 AB120 AB120 expresses the Ad5 E1A and wild-type Ad5 E1B-55kDa proteins anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Wimmer P., Schreiner S., Everett RD., Sirma H., Groitl P., Dobner T. Apoptosis - Interactions involving proteins with a function related to apoptosis Baby rat kidney cells were used as a negative control. Two derivatives of this cell line AB120/AB115, stably expressing E1B-55K or mutant E1B-55K-NES were treated with 20nM leptomycin B for 2 hrs before methanol fixation. thomas.dobner@hpi.uni-hamburg.de Accepted 2010-DEC-23 by ORCHARD. 06-April-2011: Contacted by JYOTI. Oncogene (0950-9232) 2010 orchard Only protein-protein interactions imex curation Curated by: I2D - Interologous Interaction Database SUMO modification of E1B-55K oncoprotein regulates isoform-specific binding to the tumour suppressor protein PML. SUMO modification of E1B-55K oncoprotein regulates isoform-specific binding to the tumour suppressor protein PML. Oncogene (0950-9232) 2010 imex curation Wimmer P., Schreiner S., Everett RD., Sirma H., Groitl P., Dobner T. Apoptosis - Interactions involving proteins with a function related to apoptosis Cancer - Interactions investigated in the context of cancer Baby rat kidney cells were used as a negative control. Two derivatives of this cell line AB120/AB115, stably expressing E1B-55K or mutant E1B-55K-NES were treated with 20nM leptomycin B for 2 hrs before methanol fixation. thomas.dobner@hpi.uni-hamburg.de 06-April-2011: Contacted by JYOTI. orchard Only protein-protein interactions Curated by: I2D - Interologous Interaction Database rat-ab115 Rattus AB115 ab115 ab115-Baby Rat Kidney cell line cell line of polyclonal origin derived from transfection of primary BRK cells with pE1B-NES. anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Wimmer P., Schreiner S., Everett RD., Sirma H., Groitl P., Dobner T. Apoptosis - Interactions involving proteins with a function related to apoptosis Baby rat kidney cells were used as a negative control. Two derivatives of this cell line AB120/AB115, stably expressing E1B-55K or mutant E1B-55K-NES were treated with 20nM leptomycin B for 2 hrs before methanol fixation. thomas.dobner@hpi.uni-hamburg.de Accepted 2010-DEC-23 by ORCHARD. 06-April-2011: Contacted by JYOTI. Oncogene (0950-9232) 2010 orchard Only protein-protein interactions imex curation Curated by: I2D - Interologous Interaction Database p29590-2 Protein PML PML MYL RNF71 TRIM19 RING finger protein 71 Tripartite motif-containing protein 19 PML-2 PML-V TRIM19beta Promyelocytic leukemia protein PP8675 E3 SUMO-protein ligase PML RING-type E3 SUMO transferase PML protein protein human Homo sapiens Human MEPAPARSPRPQQDPARPQEPTMPPPETPSEGRQPSPSPSPTERAPASEEEFQFLRCQQCQAEAKCPKLLPCLHTLCSGCLEASGMQCPICQAPWPLGADTPALDNVFFESLQRRLSVYRQIVDAQAVCTRCKESADFWCFECEQLLCAKCFEAHQWFLKHEARPLAELRNQSVREFLDGTRKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCCSCALLDSSHSELKCDISAEIQQRQEELDAMTQALQEQDSAFGAVHAQMHAAVGQLGRARAETEELIRERVRQVVAHVRAQERELLEAVDARYQRDYEEMASRLGRLDAVLQRIRTGSALVQRMKCYASDQEVLDMHGFLRQALCRLRQEEPQSLQAAVRTDGFDEFKVRLQDLSSCITQGKDAAVSKKASPEAASTPRDPIDVDLPEEAERVKAQVQALGLAEAQPMAVVQSVPGAHPVPVYAFSIKGPSYGEDVSNTTTAQKRKCSQTQCPRKVIKMESEEGKEARLARSSPEQPRPSTSKAVSPPHLDGPPSPRSPVIGSEVFLPNSNHVASGAGEAEERVVVISSSEDSDAENSVSGPEVQPRTPASPHFRSQGAQPQQVTLRLALRLGNFPVRH Ref.5 (AAG50181) sequence is in conflict in position: 578:P->A. Contains a phosphoserine at position 565. 52E7FB5D57D59233 p29590-1 Protein PML PML MYL RNF71 TRIM19 RING finger protein 71 Tripartite motif-containing protein 19 PML-I TRIM19alpha Promyelocytic leukemia protein PP8675 E3 SUMO-protein ligase PML RING-type E3 SUMO transferase PML protein protein human Homo sapiens Human MEPAPARSPRPQQDPARPQEPTMPPPETPSEGRQPSPSPSPTERAPASEEEFQFLRCQQCQAEAKCPKLLPCLHTLCSGCLEASGMQCPICQAPWPLGADTPALDNVFFESLQRRLSVYRQIVDAQAVCTRCKESADFWCFECEQLLCAKCFEAHQWFLKHEARPLAELRNQSVREFLDGTRKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCCSCALLDSSHSELKCDISAEIQQRQEELDAMTQALQEQDSAFGAVHAQMHAAVGQLGRARAETEELIRERVRQVVAHVRAQERELLEAVDARYQRDYEEMASRLGRLDAVLQRIRTGSALVQRMKCYASDQEVLDMHGFLRQALCRLRQEEPQSLQAAVRTDGFDEFKVRLQDLSSCITQGKDAAVSKKASPEAASTPRDPIDVDLPEEAERVKAQVQALGLAEAQPMAVVQSVPGAHPVPVYAFSIKGPSYGEDVSNTTTAQKRKCSQTQCPRKVIKMESEEGKEARLARSSPEQPRPSTSKAVSPPHLDGPPSPRSPVIGSEVFLPNSNHVASGAGEAEERVVVISSSEDSDAENSSSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAEDRPLVFFDLKIDNETQKISQLAAVNRESKFRVVIQPEAFFSIYSKAVSLEVGLQHFLSFLSSMRRPILACYKLWGPGLPNFFRALEDINRLWEFQEAISGFLAALPLIRERVPGASSFKLKNLAQTYLARNMSERSAMAAVLAMRDLCRLLEVSPGPQLAQHVYPFSSLQCFASLQPLVQAAVLPRAEARLLALHNVSFMELLSAHRRDRQGGLKKYSRYLSLQTTTLPPAQPAFNLQALGTYFEGLLEGPALARAEGVSTPLAGRGLAERASQQS D50968A977E34287 p29590-4 Protein PML PML MYL RNF71 TRIM19 RING finger protein 71 Tripartite motif-containing protein 19 PML-3B PML-VI TRIM19epsilon Promyelocytic leukemia protein PP8675 E3 SUMO-protein ligase PML RING-type E3 SUMO transferase PML protein protein human Homo sapiens Human MEPAPARSPRPQQDPARPQEPTMPPPETPSEGRQPSPSPSPTERAPASEEEFQFLRCQQCQAEAKCPKLLPCLHTLCSGCLEASGMQCPICQAPWPLGADTPALDNVFFESLQRRLSVYRQIVDAQAVCTRCKESADFWCFECEQLLCAKCFEAHQWFLKHEARPLAELRNQSVREFLDGTRKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCCSCALLDSSHSELKCDISAEIQQRQEELDAMTQALQEQDSAFGAVHAQMHAAVGQLGRARAETEELIRERVRQVVAHVRAQERELLEAVDARYQRDYEEMASRLGRLDAVLQRIRTGSALVQRMKCYASDQEVLDMHGFLRQALCRLRQEEPQSLQAAVRTDGFDEFKVRLQDLSSCITQGKDAAVSKKASPEAASTPRDPIDVDLPEEAERVKAQVQALGLAEAQPMAVVQSVPGAHPVPVYAFSIKGPSYGEDVSNTTTAQKRKCSQTQCPRKVIKMESEEGKEARLARSSPEQPRPSTSKAVSPPHLDGPPSPRSPVIGSEVFLPNSNHVASGAGEAGRERNALW Contains a phosphoserine at position 518. Contains a phosphoserine at position 527. Contains a phosphoserine at position 530. 9DC795A6542BA778 pml_human Protein PML PML MYL RNF71 TRIM19 Tripartite motif-containing protein 19 RING finger protein 71 Promyelocytic leukemia protein PP8675 E3 SUMO-protein ligase PML RING-type E3 SUMO transferase PML protein protein human Homo sapiens Human MEPAPARSPRPQQDPARPQEPTMPPPETPSEGRQPSPSPSPTERAPASEEEFQFLRCQQCQAEAKCPKLLPCLHTLCSGCLEASGMQCPICQAPWPLGADTPALDNVFFESLQRRLSVYRQIVDAQAVCTRCKESADFWCFECEQLLCAKCFEAHQWFLKHEARPLAELRNQSVREFLDGTRKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCCSCALLDSSHSELKCDISAEIQQRQEELDAMTQALQEQDSAFGAVHAQMHAAVGQLGRARAETEELIRERVRQVVAHVRAQERELLEAVDARYQRDYEEMASRLGRLDAVLQRIRTGSALVQRMKCYASDQEVLDMHGFLRQALCRLRQEEPQSLQAAVRTDGFDEFKVRLQDLSSCITQGKDAAVSKKASPEAASTPRDPIDVDLPEEAERVKAQVQALGLAEAQPMAVVQSVPGAHPVPVYAFSIKGPSYGEDVSNTTTAQKRKCSQTQCPRKVIKMESEEGKEARLARSSPEQPRPSTSKAVSPPHLDGPPSPRSPVIGSEVFLPNSNHVASGAGEAEERVVVISSSEDSDAENSSSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAEDRPLVFFDLKIDNETQKISQLAAVNRESKFRVVIQPEAFFSIYSKAVSLEVGLQHFLSFLSSMRRPILACYKLWGPGLPNFFRALEDINRLWEFQEAISGFLAALPLIRERVPGASSFKLKNLAQTYLARNMSERSAMAAVLAMRDLCRLLEVSPGPQLAQHVYPFSSLQCFASLQPLVQAAVLPRAEARLLALHNVSFMELLSAHRRDRQGGLKKYSRYLSLQTTTLPPAQPAFNLQALGTYFEGLLEGPALARAEGVSTPLAGRGLAERASQQS DIP protein P29590 original sequence version: 188 DIP protein P29590 original sequence version: 195 DIP protein P29590-1 original sequence version: 187 D50968A977E34287 f1m589_rat Pml protein protein rat Rattus norvegicus (Rat) Rat MPPPEEPSEDHEHSQSPAEQAIKEEFQFLRCPGCQTQAKCPKLLPCLHTLCSGCLEAPGLQCPICQAPGSANANAEALDNVFFESLQRRLAVFRQIVDAQAACTRCKELADFWCFECEQLMCGKCFDAHQWYLKHEARPLAELRDNSVREFLDSTRKSNIFCSNTNHRTPAQTNIYCRGCAKPLCCECALLDRNHSHLQCEIGKEIQQLHEELGTMTQALEEQGRTFDSAHAQMHSAIGQLDDARSDTEKQIRARVRQVIEHVQAQERELLEAVNVRYQRDYQEIAGQLGHLEAVLQRIRTGGALVKRMKLYASEQEVLDMHGFLRKALCRLRQEEPQNHKVQLRTSGFEEFKLCLQDLVSFITQRTDVAVAGRASPEAASTHPEAASAQPEAASTHPEAASAQPEAASAHPESASTPGNSTDLEQPKEVQRAQAQAMELSKTQPVAMVKSVPGAHPVPVYAFSMQGPTYREEASQTVSPMKRKCCHIDCCRKIIKMESTDENEDRLSTSSPEQPRPSTSKAISPPHPDGTSSTESTIPEKETPLPNNNHVASDAGETEERIVVISSSEDSDAENLPSHELDDSSSESSSIQLEGPNSLKALDESLAEPHLEDRTLVFFDLKIDNETQKISQLAAVNRESKFRVLIQPEAFSVYSKAVSLESGLQHFLSFLNSMHRPLLACPRLWGPGLPIFFQALNDINKLWEFQDAISGFLAVLPLIQERIPSASSFKLRNLAKTYLARNMSERSALAAVLAMRDLCCLLEVSPGLQLAQHIYSFSSLQCFASLQPLIQAQVLPQPEARLLALHNVSFLELLTAYRSNRQEGLKKYVHYLSLQTTPSSASTQIAQFLQALSAYMDGQLEGHIPAGAEGTALSLSGRAENKGCLA B62E17B6BA5380B6 p29590-5 Protein PML PML MYL RNF71 TRIM19 RING finger protein 71 Tripartite motif-containing protein 19 PML-IV PML-X TRIM19zeta Promyelocytic leukemia protein PP8675 E3 SUMO-protein ligase PML RING-type E3 SUMO transferase PML protein protein human Homo sapiens Human MEPAPARSPRPQQDPARPQEPTMPPPETPSEGRQPSPSPSPTERAPASEEEFQFLRCQQCQAEAKCPKLLPCLHTLCSGCLEASGMQCPICQAPWPLGADTPALDNVFFESLQRRLSVYRQIVDAQAVCTRCKESADFWCFECEQLLCAKCFEAHQWFLKHEARPLAELRNQSVREFLDGTRKTNNIFCSNPNHRTPTLTSIYCRGCSKPLCCSCALLDSSHSELKCDISAEIQQRQEELDAMTQALQEQDSAFGAVHAQMHAAVGQLGRARAETEELIRERVRQVVAHVRAQERELLEAVDARYQRDYEEMASRLGRLDAVLQRIRTGSALVQRMKCYASDQEVLDMHGFLRQALCRLRQEEPQSLQAAVRTDGFDEFKVRLQDLSSCITQGKDAAVSKKASPEAASTPRDPIDVDLPEEAERVKAQVQALGLAEAQPMAVVQSVPGAHPVPVYAFSIKGPSYGEDVSNTTTAQKRKCSQTQCPRKVIKMESEEGKEARLARSSPEQPRPSTSKAVSPPHLDGPPSPRSPVIGSEVFLPNSNHVASGAGEAEERVVVISSSEDSDAENSSSRELDDSSSESSDLQLEGPSTLRVLDENLADPQAEDRPLVFFDLKIDNESGFSWGYPHPFLI DIP protein P29590-5 original sequence version: 188 DIP protein P29590-5 original sequence version: 195 85FBAEC9F162C8E0 p03243-1 E1B 55 kDa protein E1B protein, large T-antigen E1B-495R E1B-55K protein protein ade05 Human adenovirus C serotype 5 (HAdV-5) HAdV-5 Human adenovirus 5 MERRNPSERGVPAGFSGHASVESGCETQESPATVVFRPPGDNTDGGAAAAAGGSQAAAAGAEPMEPESRPGPSGMNVVQVAELYPELRRILTITEDGQGLKGVKRERGACEATEEARNLAFSLMTRHRPECITFQQIKDNCANELDLLAQKYSIEQLTTYWLQPGDDFEEAIRVYAKVALRPDCKYKISKLVNIRNCCYISGNGAEVEIDTEDRVAFRCSMINMWPGVLGMDGVVIMNVRFTGPNFSGTVFLANTNLILHGVSFYGFNNTCVEAWTDVRVRGCAFYCCWKGVVCRPKSRASIKKCLFERCTLGILSEGNSRVRHNVASDCGCFMLVKSVAVIKHNMVCGNCEDRASQMLTCSDGNCHLLKTIHVASHSRKAWPVFEHNILTRCSLHLGNRRGVFLPYQCNLSHTKILLEPESMSKVNLNGVFDMTMKIWKVLRYDETRTRCRPCECGGKHIRNQPVMLDVTEELRPDHLVLACTRAEFGSSDEDTD DIP protein P03243-1 original sequence version: 63 DIP protein P03243-1 original sequence version: 68 31EE3E4B9762DCE8 pml-e1b-55k 5 15 unspecified role unspecified role neutral component neutral component P03243-1:p.[Leu83Ala;Leu87Ala;Leu91Ala] leu83ala-leu87ala-leu91ala mutation mutation certain certain sequence position certain certain certain sequence position certain L A certain certain sequence position certain certain certain sequence position certain L A certain certain sequence position certain certain certain sequence position certain L A Fri Jul 22 10:59:41 BST 2016 This feature has been corrected as a result of our quality control procedures. The original label was 'leu83ala,leu91ala,leu87ala' Wed May 02 15:14:52 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu83ala,leu87ala,leu91ala' Tue Jun 30 19:31:22 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu83Ala;Leu87Ala;Leu91Ala]' 13 unspecified role unspecified role neutral component neutral component colocalization colocalization Fig. 1a,b Leptomycin B E1B-55K-wt accumulates in several bright stained nuclear aggregates clearly colocalizing with endogenous PML. pml-e1b-55k-1 8 15 unspecified role unspecified role prey prey P03243-1:p.[Leu83Ala;Leu87Ala;Leu91Ala] mutation mutation certain certain sequence position certain certain certain sequence position certain L A certain certain sequence position certain certain certain sequence position certain L A certain certain sequence position certain certain certain sequence position certain L A Wed May 02 14:50:56 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu83ala,leu87ala,leu91ala' Tue Jun 30 16:46:48 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu83Ala;Leu87Ala;Leu91Ala]' 13 unspecified role unspecified role bait bait physical association physical association Fig. 1c pml-e1b-55k-2 8 15 unspecified role unspecified role bait bait P03243-1:p.[Leu83Ala;Leu87Ala;Leu91Ala] mutation mutation certain certain sequence position certain certain certain sequence position certain L A certain certain sequence position certain certain certain sequence position certain L A certain certain sequence position certain certain certain sequence position certain L A Wed May 02 18:58:17 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'leu83ala,leu87ala,leu91ala' Tue Jun 30 15:44:29 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Leu83Ala;Leu87Ala;Leu91Ala]' 13 unspecified role unspecified role prey prey physical association physical association Fig. 1d pml-e1b-55k-3 4 14 unspecified role unspecified role prey prey n-terminal 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 15 unspecified role unspecified role bait bait P03243-1:p.Val103Asp mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain V D Wed May 02 19:58:45 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'val103asp' Tue Jun 30 18:23:24 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Val103Asp' P03243-1:p.Lys104Arg mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain K R Wed May 02 15:46:20 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys104arg' Tue Jun 30 19:17:38 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys104Arg' physical association physical association Fig. 2a, 3a, 5a Binding of E1B-55K is abolished upon superinfection of H1299 cells with 10f.f.u/cell of wild-type virus H5pg4100. pml-e1b-55k-4 4 9 unspecified role unspecified role prey prey n-terminal 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 15 unspecified role unspecified role bait bait physical association physical association Fig. 2a pml-e1b-55k-5 4 10 unspecified role unspecified role prey prey n-terminal 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 15 unspecified role unspecified role bait bait physical association physical association Fig. 3a Specific binding of E1B-55K is observed upon superinfection of H1299 cells with 10f.f.u/cell of wild-type virus H5pg4100. pml-e1b-55k-6 4 11 unspecified role unspecified role prey prey n-terminal 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 15 unspecified role unspecified role bait bait physical association physical association Fig. 3a Specific binding of E1B-55K is observed upon superinfection of H1299 cells with 10f.f.u/cell of wild-type virus H5pg4100. pml-e1b-55k-7 2 14 unspecified role unspecified role bait bait n-terminal 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 15 unspecified role unspecified role prey prey physical association physical association Fig. 2b pml-e1b-55k-8 2 9 unspecified role unspecified role bait bait n-terminal 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 15 unspecified role unspecified role prey prey physical association physical association Fig. 2b pml-e1b-55k-9 3 15 unspecified role unspecified role neutral component neutral component P03243-1:p.Lys104Arg mutation disrupting mutation disrupting interaction mutation disrupting certain certain sequence position certain certain certain sequence position certain K R Wed May 02 16:49:07 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys104arg' Tue Jun 30 18:49:58 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys104Arg' 12 unspecified role unspecified role neutral component neutral component colocalization colocalization Fig. 4a pml-e1b-55k-9-10 1 15 unspecified role unspecified role prey prey 12 unspecified role unspecified role bait bait physical association physical association Fig. 4b pml-e1b-55k 6 15 unspecified role unspecified role neutral component neutral component 13 unspecified role unspecified role neutral component neutral component colocalization colocalization Fig. 1a,b Leptomycin B E1B-55K-wt accumulates in several bright stained nuclear aggregates clearly colocalizing with endogenous PML. pml-e1b-55k-2 7 15 unspecified role unspecified role bait bait 13 unspecified role unspecified role prey prey physical association physical association Fig. 1d pml-e1b-55k-1 7 15 unspecified role unspecified role prey prey 13 unspecified role unspecified role bait bait physical association physical association Fig. 1c