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 RCC1 chromatin factor bound to the nucleosome core particle. Structure of RCC1 chromatin factor bound to the nucleosome core particle. Nature 2010 imex curation Makde RD., England JR., Yennawar HP., Tan S. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Makde RD., England JR., Yennawar HP., Tan S. DIP original experiment: DIP-219349X Nature 2010 IMEx Structure of RCC1 chromatin factor bound to the nucleosome core particle. Structure of RCC1 chromatin factor bound to the nucleosome core particle. Structure of RCC1 chromatin factor bound to the nucleosome core particle. Nature 2010 imex curation Makde RD., England JR., Yennawar HP., Tan S. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Makde RD., England JR., Yennawar HP., Tan S. DIP original experiment: DIP-219346X Nature 2010 IMEx Structure of RCC1 chromatin factor bound to the nucleosome core particle. Structure of RCC1 chromatin factor bound to the nucleosome core particle. Structure of RCC1 chromatin factor bound to the nucleosome core particle. Nature 2010 imex curation Makde RD., England JR., Yennawar HP., Tan S. Only protein-protein interactions in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Makde RD., England JR., Yennawar HP., Tan S. DIP original experiment: DIP-219348X Nature 2010 IMEx Structure of RCC1 chromatin factor bound to the nucleosome core particle. Structure of RCC1 chromatin factor bound to the nucleosome core particle. Structure of RCC1 chromatin factor bound to the nucleosome core particle. Nature 2010 imex curation Makde RD., England JR., Yennawar HP., Tan S. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Makde RD., England JR., Yennawar HP., Tan S. DIP original experiment: DIP-219350X Nature 2010 IMEx Structure of RCC1 chromatin factor bound to the nucleosome core particle. Structure of RCC1 chromatin factor bound to the nucleosome core particle. Structure of RCC1 chromatin factor bound to the nucleosome core particle. Nature 2010 imex curation Makde RD., England JR., Yennawar HP., Tan S. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Makde RD., England JR., Yennawar HP., Tan S. DIP original experiment: DIP-219351X Nature 2010 IMEx Structure of RCC1 chromatin factor bound to the nucleosome core particle. Structure of RCC1 chromatin factor bound to the nucleosome core particle. Structure of RCC1 chromatin factor bound to the nucleosome core particle. Nature 2010 imex curation Makde RD., England JR., Yennawar HP., Tan S. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Makde RD., England JR., Yennawar HP., Tan S. DIP original experiment: DIP-219347X Nature 2010 IMEx Structure of RCC1 chromatin factor bound to the nucleosome core particle. rcc1_human Regulator of chromosome condensation Chromosome condensation protein 1 Cell cycle regulatory protein RCC1 CHC1 protein protein human Homo sapiens Human MSPKRIAKRRSPPADAIPKSKKVKVSHRSHSTEPGLVLTLGQGDVGQLGLGENVMERKKPALVSIPEDVVQAEAGGMHTVCLSKSGQVYSFGCNDEGALGRDTSVEGSEMVPGKVELQEKVVQVSAGDSHTAALTDDGRVFLWGSFRDNNGVIGLLEPMKKSMVPVQVQLDVPVVKVASGNDHLVMLTADGDLYTLGCGEQGQLGRVPELFANRGGRQGLERLLVPKCVMLKSRGSRGHVRFQDAFCGAYFTFAISHEGHVYGFGLSNYHQLGTPGTESCFIPQNLTSFKNSTKSWVGFSGGQHHTVCMDSEGKAYSLGRAEYGRLGLGEGAEEKSIPTLISRLPAVSSVACGASVGYAVTKDGRVFAWGMGTNYQLGTGQDEDAWSPVEMMGKQLENRVVLSVSSGGQHTVLLVKDKEQS DIP protein P18754 original sequence version: 117 F6D225AF81928305 h2b11_xenla Histone H2B 1.1 protein protein xenla Xenopus laevis (African clawed frog) African clawed frog MPEPAKSAPAPKKGSKKAVTKTQKKDGKKRRKSRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK DIP protein P02281 original sequence version: 91 DIP protein P02281 original sequence version: 111 DIP protein P02281 original sequence version: 126 DA6C122EC8359FD9 q6azj8_xenla Histone H2A h2ac14.L LOC494591 h2ac14 hist1h2aj XELAEV_18003602mg protein protein xenla Xenopus laevis (African clawed frog) African clawed frog MSGRGKQGGKTRAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGRVTIAQGGVLPNIQSVLLPKKTESSKSAKSK DIP protein Q6AZJ8 original sequence version: 49 DIP protein Q6AZJ8 original sequence version: 73 62E46ABF27FA5E98 h4_xenla Histone H4 protein protein xenla Xenopus laevis (African clawed frog) African clawed frog MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG DIP protein P62799 original sequence version: 90 DIP protein P62799 original sequence version: 50 DIP protein P62799 original sequence version: 53 DIP protein P62799 original sequence version: 68 DIP protein P62799 original sequence version: 91 DIP protein P62799 original sequence version: 109 A9E5DFD3F8B97598 h32_xenla Histone H3.2 protein protein xenla Xenopus laevis (African clawed frog) African clawed frog MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA DIP protein P84233 original sequence version: 76 DIP protein P84233 original sequence version: 53 DIP protein P84233 original sequence version: 77 DIP protein P84233 original sequence version: 95 6FD8508EA50A0EEC rcc1_drome Regulator of chromosome condensation Rcc1 Bj1 Chromatin-binding protein Bj1 Regulator of chromosome condensation 1 ortholog CG10480 protein protein drome Drosophila melanogaster (Fruit fly) Fruit fly MPRRKALTNNNNAGEAEQQPPKAKRARIAFHLELPKRRTVLGNVLVCGNGDVGQLGLGEDILERKRLSPVAGIPDAVDISAGGMHNLVLTKSGDIYSFGCNDEGALGRDTSEDGSESKPDLIDLPGKALCISAGDSHSACLLEDGRVFAWGSFRDSHGNMGLTIDGNKRTPIDLMEGTVCCSIASGADHLVILTTAGKVFTVGCAEQGQLGRLSERSISGEGRRGKRDLLRPTQLIITRAKPFEAIWATNYCTFMRESQTQVIWATGLNNFKQLAHETKGKEFALTPIKTELKDIRHIAGGQHHTVILTTDLKCSVVGRPEYGRLGLGDVKDVVEKPTIVKKLTEKIVSVGCGEVCSYAVTIDGKLYSWGSGVNNQLGVGDGDDELEPIVVVSKNTQGKHMLLASGGGQHAIFLVKADKQDQKENVPVKVSGSSSISKKDKTPPQDNVDKEAENVDKQEQKENLPAKASTSSKKNKTPPQDNADKEAENVDKQEQKENLPAKASTSSKKIKTPPQDDAAEEVEEESAQEPTPKKAKKPAAKRGGKKT DIP protein P25171 original sequence version: 98 77D9744EBAF4597A h2b11_xenla-h32_xenla-1 2 8 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 10 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 11 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 12 unspecified role unspecified role unspecified role unspecified role Region 2-422 Region 2-422 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association h2b11_xenla-h32_xenla-2 4 7 unspecified role unspecified role prey prey Region 21-421 Region 21-421 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 8 unspecified role unspecified role bait bait His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 9 unspecified role unspecified role prey prey ecolx Escherichia coli 10 unspecified role unspecified role prey prey ecolx Escherichia coli 11 unspecified role unspecified role prey prey ecolx Escherichia coli association association h2b11_xenla-h32_xenla-3 1 8 unspecified role unspecified role bait bait His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 9 unspecified role unspecified role prey prey ecolx Escherichia coli 10 unspecified role unspecified role prey prey ecolx Escherichia coli 11 unspecified role unspecified role prey prey ecolx Escherichia coli association association h2b11_xenla-h32_xenla-4 3 8 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 10 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 11 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association h2b11_xenla-rcc1-1 5 7 unspecified role unspecified role prey prey Region 21-421 Region 21-421 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain P18754:p.[Lys232Ala;Arg234Ala;Arg237Ala] K232A/R234A/R237A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R A certain certain sequence position certain certain certain sequence position certain R A certain certain sequence position certain certain certain sequence position certain K A This feature has been corrected as a result of our quality control procedures. The original label was 'K232A/R234A/R237A'. Wed May 02 16:31:32 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys232ala,arg234ala,arg237ala' Tue Jun 30 19:48:29 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.[Lys232Ala;Arg234Ala;Arg237Ala]' P18754:p.Lys232Ala K232A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain K A This feature has been corrected as a result of our quality control procedures. The original label was 'K232A'. Wed May 02 19:15:02 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'lys232ala' Tue Jun 30 18:38:00 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Lys232Ala' P18754:p.Arg237Ala R237A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R A This feature has been corrected as a result of our quality control procedures. The original label was 'R237A'. Wed May 02 17:17:20 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg237ala' Tue Jun 30 17:57:09 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg237Ala' P18754:p.Arg234Ala R234A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain R A This feature has been corrected as a result of our quality control procedures. The original label was 'R234A'. Wed May 02 19:25:55 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'arg234ala' Tue Jun 30 17:31:50 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Arg234Ala' ecolx Escherichia coli 8 unspecified role unspecified role bait bait His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli physical association physical association h2b11_xenla-h32_xenla-5 6 8 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 10 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 11 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 12 unspecified role unspecified role unspecified role unspecified role Region 2-422 Region 2-422 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli physical association physical association