DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Crystal structure of the catalytic domain of Haspin, an atypical kinase implicated in chromatin organization. Crystal structure of the catalytic domain of Haspin, an atypical kinase implicated in chromatin organization. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Villa F., Capasso P., Tortorici M., Forneris F., de Marco A., Mattevi A., Musacchio A. Only protein-protein interactions in vitro In vitro spr surface plasmon resonance Optical biosensor BIAcore(r) BIAcore(r) Optical biosensor spr predetermined predetermined participant predetermined Villa F., Capasso P., Tortorici M., Forneris F., de Marco A., Mattevi A., Musacchio A. DIP original experiment: DIP-134787X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Crystal structure of the catalytic domain of Haspin, an atypical kinase implicated in chromatin organization. Crystal structure of the catalytic domain of Haspin, an atypical kinase implicated in chromatin organization. Crystal structure of the catalytic domain of Haspin, an atypical kinase implicated in chromatin organization. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Villa F., Capasso P., Tortorici M., Forneris F., de Marco A., Mattevi A., Musacchio A. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay weight autoradiogra molecular weight estimation by autoradiography weight autoradiogra Villa F., Capasso P., Tortorici M., Forneris F., de Marco A., Mattevi A., Musacchio A. DIP original experiment: DIP-134789X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Crystal structure of the catalytic domain of Haspin, an atypical kinase implicated in chromatin organization. Crystal structure of the catalytic domain of Haspin, an atypical kinase implicated in chromatin organization. Crystal structure of the catalytic domain of Haspin, an atypical kinase implicated in chromatin organization. Proceedings of the National Academy of Sciences of the United States of America 2009 imex curation Villa F., Capasso P., Tortorici M., Forneris F., de Marco A., Mattevi A., Musacchio A. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Villa F., Capasso P., Tortorici M., Forneris F., de Marco A., Mattevi A., Musacchio A. DIP original experiment: DIP-134788X Proceedings of the National Academy of Sciences of the United States of America 2009 IMEx Crystal structure of the catalytic domain of Haspin, an atypical kinase implicated in chromatin organization. h32_mouse Histone H3.2 H3c13 H3c14 H3c15 H3c2 H3c3 H3c4 H3c6 H3c7 H3-143 H3-53 H3-B H3-F H3-clustered histone 13 H3-clustered histone 14 H3-clustered histone 15 H3-clustered histone 2 H3-clustered histone 3 H3-clustered histone 4 H3-clustered histone 6 H3-clustered histone 7 H3.2 H3.2-221 H3.2-614 H3.2-615 H3.2-616 H3b H3f Hist1h3b Hist1h3c Hist1h3d Hist1h3e Hist1h3f Hist2h3b Hist2h3c1 Hist2h3c2 Hist2h3ca1 Hist2h3ca2 protein protein mouse Mus musculus Mouse MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA DIP protein P84228 original sequence version: 65 6FD8508EA50A0EEC q8tf76-1 Serine/threonine-protein kinase haspin HASPIN GSG2 Germ cell-specific gene 2 protein H-haspin Haploid germ cell-specific nuclear protein kinase protein protein human Homo sapiens Human MAASLPGPGSRLFRTYGAADGRRQRRPGREAAQWFPPQDRRRFFNSSGSSDASIGDPSQSDDPDDPDDPDFPGSPVRRRRRRPGGRVPKDRPSLTVTPKRWKLRARPSLTVTPRRLGLRARPPQKCSTPCGPLRLPPFPSRDSGRLSPDLSVCGQPRDGDELGISASLFSSLASPCPGSPTPRDSVISIGTSACLVAASAVPSGLHLPEVSLDRASLPCSQEEATGGAKDTRMVHQTRASLRSVLFGLMNSGTPEDSEFRADGKNMRESCCKRKLVVGNGPEGPGLSSTGKRRATGQDSCQERGLQEAVRREHQEASVPKGRIVPRGIDRLERTRSSRKSKHQEATETSLLHSHRFKKGQKLGKDSFPTQDLTPLQNVCFWTKTRASFSFHKKKIVTDVSEVCSIYTTATSLSGSLLSECSNRPVMNRTSGAPSSWHSSSMYLLSPLNTLSISNKKASDAEKVYGECSQKGPVPFSHCLPTEKLQRCEKIGEGVFGEVFQTIADHTPVAIKIIAIEGPDLVNGSHQKTFEEILPEIIISKELSLLSGEVCNRTEGFIGLNSVHCVQGSYPPLLLKAWDHYNSTKGSANDRPDFFKDDQLFIVLEFEFGGIDLEQMRTKLSSLATAKSILHQLTASLAVAEASLRFEHRDLHWGNVLLKKTSLKKLHYTLNGKSSTIPSCGLQVSIIDYTLSRLERDGIVVFCDVSMDEDLFTGDGDYQFDIYRLMKKENNNRWGEYHPYSNVLWLHYLTDKMLKQMTFKTKCNTPAMKQIKRKIQEFHRTMLNFSSATDLLCQHSLFK DIP protein Q8TF76-1 original sequence version: 87 DIP protein Q8TF76-1 original sequence version: 85 hist1h3b-gsg2-1 1 4 unspecified role unspecified role bait bait Region 1-50 Region 1-50 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 5 unspecified role unspecified role prey prey Kinase domain Region 452-798 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain Q8TF76-1:p.Glu492Ala E492A mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain E A This feature has been corrected as a result of our quality control procedures. The original label was 'E492A'. Wed May 02 15:22:17 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'glu492ala' Tue Jun 30 20:02:00 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Glu492Ala' Q8TF76-1:p.His651Ala H651A mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain H A This feature has been corrected as a result of our quality control procedures. The original label was 'H651A'. Wed May 02 14:47:03 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'his651ala' Tue Jun 30 16:03:42 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.His651Ala' Q8TF76-1:p.Asp707Leu D707L mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain D L This feature has been corrected as a result of our quality control procedures. The original label was 'D707L'. Wed May 02 15:44:09 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp707leu' Tue Jun 30 18:16:22 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp707Leu' Q8TF76-1:p.Asp709Asn D709N mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain D N This feature has been corrected as a result of our quality control procedures. The original label was 'D709N'. Wed May 02 15:22:51 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp709asn' Tue Jun 30 16:01:10 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp709Asn' Q8TF76-1:p.Gly713Phe G713F mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain G F This feature has been corrected as a result of our quality control procedures. The original label was 'G713F'. Wed May 02 20:33:27 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly713phe' Tue Jun 30 18:07:36 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly713Phe' ecolx Escherichia coli direct interaction direct interaction gsg2-hist1h3b-1 2 4 enzyme target enzyme target substrate substrate unspecified role unspecified role Region 1-50 Region 1-50 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain pThr pThr opthr O-phospho-L-threonine (2S,3R)-2-amino-3-(phosphonooxy)butanoic acid 2-amino-3-hydroxybutanoic acid 3-phosphate 2-azanyl-3-(phosphonooxy)butanoic acid MOD_RES Phosphothreonine O-phospho-L-threonine O-phosphorylated L-threonine O3-phosphothreonine threonine phosphate ester OPThr Phospho Phospho Threonyl Phosphorylation phosphorylationt western blot western blot Immuno blot Immuno blot certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli 5 enzyme enzyme unspecified role unspecified role Kinase domain Region 452-798 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain ecolx Escherichia coli phosphorylation phosphorylation reaction phosphorylation hist1h3b-gsg2-2 3 5 unspecified role unspecified role prey prey Kinase domain Region 452-798 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 Region 1-30 Region 1-30 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecolx Escherichia coli direct interaction direct interaction