DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structure of the heterodimeric core primase. Structure of the heterodimeric core primase. Nature structural & molecular biology 2005 imex curation Lao-Sirieix SH., Nookala RK., Roversi P., Bell SD., Pellegrini L. Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Lao-Sirieix SH., Nookala RK., Roversi P., Bell SD., Pellegrini L. DIP original experiment: DIP-254814X Nature structural & molecular biology 2005 IMEx Structure of the heterodimeric core primase. Structure of the heterodimeric core primase. Structure of the heterodimeric core primase. Nature structural & molecular biology 2005 imex curation Lao-Sirieix SH., Nookala RK., Roversi P., Bell SD., Pellegrini L. Only protein-protein interactions yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 2 hybrid two hybrid 2H 2h Gal4 transcription regeneration two-hybrid yeast two hybrid 2-hybrid classical two hybrid classical two hybrid 2H two-hybrid 2-hybrid Gal4 transcription regeneration 2h yeast two hybrid Y2H Y-2H 2 hybrid predetermined predetermined participant predetermined Lao-Sirieix SH., Nookala RK., Roversi P., Bell SD., Pellegrini L. DIP original experiment: DIP-254813X Nature structural & molecular biology 2005 IMEx Structure of the heterodimeric core primase. Structure of the heterodimeric core primase. Structure of the heterodimeric core primase. Nature structural & molecular biology 2005 imex curation Lao-Sirieix SH., Nookala RK., Roversi P., Bell SD., Pellegrini L. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Lao-Sirieix SH., Nookala RK., Roversi P., Bell SD., Pellegrini L. DIP original experiment: DIP-254812X Nature structural & molecular biology 2005 IMEx Structure of the heterodimeric core primase. pris_sacs2 DNA primase small subunit PriS priS priA SSO1048 protein protein sulso Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) MGTFTLHQGQTNLIKSFFRNYYLNAELELPKDMELREFALQPFGSDTYVRHLSFSSSEELRDYLVNRNLPLHLFYSSARYQLPSARNMEEKAWMGSDLLFDIDADHLCKLRSIRFCPVCGNAVVSEKCERDNVETLEYVEMTSECIKRGLEQTRNLVEILEDDFGLKPKVYFSGNRGFHVQVDCYGNCALLDSDERKEIAEYVMGIGVPGYPGGSENAPGWVGRKNRGINGVTIDEQVTIDVKRLIRIPNSLHGKSGLIVKRVPNLDDFEFNETLSPFTGYTIFLPYITIETEVLGSIIKLNRGIPIKIKSSIGIYLHLRNLGEVKAYVR DIP protein Q97Z83 original sequence version: 66 mint DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments on both template strands at replication forks during chromosomal DNA synthesis E9B3C556E619B66E pril_sacs2 DNA primase large subunit PriL priL priB C21_042 SSO0557 protein protein sulso Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) MALDVKKYPFIKSLDDELKKYGGGITLTDLLLNSTTLIDQAKDRIQKTKSGDELPHYVSYNEPVLVFYTTLLSLAILNDVKLIRRYAYAEAKQFRSLLHTENEENLLEISKLLDLKINRCDPIKFYLEKKRRIIQKEFCVHFIDYLKYTKDLKEDWKLSGQILHKGYVYLDKNQLIGLIAESIKSKIVEMIRPLNLKEIPEKLKSLIERRGIIPPCIENILAKEKLNEEEIRTLITFYIDIGKGLSGIVSIMKKYNVSNVEDLYRKYRGDKGTRYIVYSCAKMKQLGLCVSSCNVKNPLQLYFLSNE DIP protein Q9UWW1 original sequence version: 71 mint DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments on both template strands at replication forks during chromosomal DNA synthesis 5EF09A913B4ABAC3 pril-pris-1 1 5 unspecified role unspecified role bait bait Q9UWW1:p.[Phe142Glu;Leu163Glu] F142E/L163E mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain L E certain certain sequence position certain certain certain sequence position certain F E This feature has been corrected as a result of our quality control procedures. The original label was 'F142E/L163E'. Wed May 02 19:52:52 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe142glu,leu163glu' Tue Jun 30 16:47:12 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Phe142Glu;Leu163Glu]' yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 4 unspecified role unspecified role prey prey yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast physical association physical association pril-pris-2 3 5 unspecified role unspecified role unspecified role unspecified role Region 1-212 Region 1-212 sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 4 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction pril-pris-3 2 5 unspecified role unspecified role bait bait yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast 4 unspecified role unspecified role prey prey Q97Z83:p.Gly165Ile G165I mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain G I This feature has been corrected as a result of our quality control procedures. The original label was 'G165I'. Wed May 02 16:31:31 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly165ile' Tue Jun 30 15:56:35 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly165Ile' Q97Z83:p.Phe164Glu F164E mutation decreasing strength mutation decreasing interaction strength mutation decreasing strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain F E This feature has been corrected as a result of our quality control procedures. The original label was 'F164E'. Wed May 02 20:28:03 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe164glu' Tue Jun 30 17:35:24 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Phe164Glu' Q97Z83:p.[Phe164Gly;Ile199Lys] F164G/I199K mutation disrupting strength mutation disrupting interaction strength mutation disrupting strength substitut analysis substitution analysis substitut analysis certain certain sequence position certain certain certain sequence position certain I K certain certain sequence position certain certain certain sequence position certain F G This feature has been corrected as a result of our quality control procedures. The original label was 'F164G/I199K'. Wed May 02 17:54:22 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'phe164gly,ile199lys' Tue Jun 30 19:11:34 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Phe164Gly;Ile199Lys]' yeasx Saccharomyces cerevisiae (Baker's yeast) Baker's yeast physical association physical association