DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Insights into eukaryotic DNA priming from the structure and functional interactions of the 4Fe-4S cluster domain of human DNA primase. Insights into eukaryotic DNA priming from the structure and functional interactions of the 4Fe-4S cluster domain of human DNA primase. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Vaithiyalingam S., Warren EM., Eichman BF., Chazin WJ. Only protein-protein interactions in vitro In vitro pull down pull down weight by staining molecular weight estimation by staining weight by staining Vaithiyalingam S., Warren EM., Eichman BF., Chazin WJ. DIP original experiment: DIP-219912X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Insights into eukaryotic DNA priming from the structure and functional interactions of the 4Fe-4S cluster domain of human DNA primase. Insights into eukaryotic DNA priming from the structure and functional interactions of the 4Fe-4S cluster domain of human DNA primase. Insights into eukaryotic DNA priming from the structure and functional interactions of the 4Fe-4S cluster domain of human DNA primase. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Vaithiyalingam S., Warren EM., Eichman BF., Chazin WJ. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Vaithiyalingam S., Warren EM., Eichman BF., Chazin WJ. DIP original experiment: DIP-219913X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Insights into eukaryotic DNA priming from the structure and functional interactions of the 4Fe-4S cluster domain of human DNA primase. Insights into eukaryotic DNA priming from the structure and functional interactions of the 4Fe-4S cluster domain of human DNA primase. Insights into eukaryotic DNA priming from the structure and functional interactions of the 4Fe-4S cluster domain of human DNA primase. Proceedings of the National Academy of Sciences of the United States of America 2010 imex curation Vaithiyalingam S., Warren EM., Eichman BF., Chazin WJ. Only protein-protein interactions in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Vaithiyalingam S., Warren EM., Eichman BF., Chazin WJ. DIP original experiment: DIP-219914X Proceedings of the National Academy of Sciences of the United States of America 2010 IMEx Insights into eukaryotic DNA priming from the structure and functional interactions of the 4Fe-4S cluster domain of human DNA primase. p49643-1 DNA primase large subunit PRIM2 PRIM2A DNA primase 58 kDa subunit protein protein human Homo sapiens Human MEFSGRKWRKLRLAGDQRNASYPHCLQFYLQPPSENISLIEFENLAIDRVKLLKSVENLGVSYVKGTEQYQSKLESELRKLKFSYRENLEDEYEPRRRDHISHFILRLAYCQSEELRRWFIQQEMDLLRFRFSILPKDKIQDFLKDSQLQFEAISDEEKTLREQEIVASSPSLSGLKLGFESIYKIPFADALDLFRGRKVYLEDGFAYVPLKDIVAIILNEFRAKLSKALALTARSLPAVQSDERLQPLLNHLSHSYTGQDYSTQGNVGKISLDQIDLLSTKSFPPCMRQLHKALRENHHLRHGGRMQYGLFLKGIGLTLEQALQFWKQEFIKGKMDPDKFDKGYSYNIRHSFGKEGKRTDYTPFSCLKIILSNPPSQGDYHGCPFRHSDPELLKQKLQSYKISPGGISQILDLVKGTHYQVACQKYFEMIHNVDDCGFSLNHPNQFFCESQRILNGGKDIKKEPIQPETPQPKPSVQKTKDASSALASLNSSLEMDMEGLEDYFSEDS DIP protein P49643-1 original sequence version: 92 rfa2_human Replication protein A 32 kDa subunit RPA34 Replication protein A 34 kDa subunit Replication factor A protein 2 RPA2 REPA2 RPA32 protein protein human Homo sapiens Human MWNSGFESYGSSSYGGAGGYTQSPGGFGSPAPSQAEKKSRARAQHIVPCTISQLLSATLVDEVFRIGNVEISQVTIVGIIRHAEKAPTNIVYKIDDMTAAPMDVRQWVDTDDTSSENTVVPPETYVKVAGHLRSFQNKKSLVAFKIMPLEDMNEFTTHILEVINAHMVLSKANSQPSAGRAPISNPGMSEAGNFGGNSFMPANGLTVAQNQVLNLIKACPRPEGLNFQDLKNQLKHMSVSSIKQAVDFLSNEGHIYSTVDDDHFKSTDAE DIP protein P15927 original sequence version: 119 DIP protein P15927-1 original sequence version: 125 DIP protein P15927 original sequence version: 114 61A563EA7B34A9B1 prim2-rpa2-1 1 5 unspecified role unspecified role prey prey C-terminal domain Region 172-270 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 4 unspecified role unspecified role bait bait C-terminal domain Region 272-464 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecolx Escherichia coli physical association physical association prim2-rpa2-2 3 5 unspecified role unspecified role unspecified role unspecified role C-terminal domain Region 172-270 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 4 unspecified role unspecified role unspecified role unspecified role C-terminal domain Region 272-464 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain P49643-1:p.His299Asp H299D mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain H D This feature has been corrected as a result of our quality control procedures. The original label was 'H299D'. Wed May 02 19:26:18 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'his299asp' Tue Jun 30 17:34:12 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.His299Asp' P49643-1:p.Arg296Glu R296E mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R E This feature has been corrected as a result of our quality control procedures. The original label was 'R296E'. Wed May 02 17:08:50 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg296glu' Tue Jun 30 18:32:12 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg296Glu' P49643-1:p.Arg302Glu R302E mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R E This feature has been corrected as a result of our quality control procedures. The original label was 'R302E'. Wed May 02 16:06:09 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg302glu' Tue Jun 30 16:44:31 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg302Glu' ecolx Escherichia coli direct interaction direct interaction prim2-rpa2-3 2 5 unspecified role unspecified role unspecified role unspecified role C-terminal domain Region 172-270 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 4 unspecified role unspecified role unspecified role unspecified role C-terminal domain Region 272-464 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain P49643-1:p.Arg302Glu R302E mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R E This feature has been corrected as a result of our quality control procedures. The original label was 'R302E'. Wed May 02 16:18:58 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg302glu' Tue Jun 30 19:11:56 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg302Glu' P49643-1:p.His299Asp H299D mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain H D This feature has been corrected as a result of our quality control procedures. The original label was 'H299D'. Wed May 02 16:28:20 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'his299asp' Tue Jun 30 17:53:25 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.His299Asp' ecolx Escherichia coli direct interaction direct interaction