MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Roles of GINS2 in K562 human chronic myelogenous leukemia and NB4 acute promyelocytic leukemia cells. Roles of GINS2 in K562 human chronic myelogenous leukemia and NB4 acute promyelocytic leukemia cells. International journal of molecular medicine 2013 imex curation Gao Y., Wang S., Liu B., Zhong L. Cancer - Interactions investigated in the context of cancer gaoyanjun7610@163.com 27-Mar-2018: Contacted by IntAct-Help. Only protein-protein interactions imex curation human-k_562 Homo sapiens myeloid leukemia cells. k562 Myelogenous leukemia K562 cells anti bait coip anti bait coimmunoprecipitation anti bait coip western blot western blot Immuno blot Immuno blot Gao Y., Wang S., Liu B., Zhong L. Cancer - Interactions investigated in the context of cancer gaoyanjun7610@163.com Accepted 2018-FEB-07 AT 11:44 GMT AT 11:44 GMT by LUANA International journal of molecular medicine 2013 Only protein-protein interactions imex curation imex curation 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 psf2_human DNA replication complex GINS protein PSF2 GINS complex subunit 2 GINS2 CGI-122 DC5 HSPC037 PSF2 protein protein human Homo sapiens Human MDAAEVEFLAEKELVTIIPNFSLDKIYLIGGDLGPFNPGLPVEVPLWLAINLKQRQKCRLLPPEWMDVEKLEKMRDHERKEETFTPMPSPYYMELTKLLLNHASDNIPKADEIRTLVKDMWDTRIAKLRVSADSFVRQQEAHAKLDNLTLMEINTSGTFLTQALNHMYKLRTNLQPLESTQSQDF DIP protein Q9Y248 original sequence version: 41 DIP protein Q9Y248 original sequence version: 58 4F6A18B1ED76F93C gins2-pml-1 1 2 unspecified role unspecified role bait bait living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level 3 unspecified role unspecified role prey prey living cell living cell physiological level physiological level endogenous level endogenous endogenous endogenous level physical association physical association f2d Results from the co-immunoprecipitation indicated an interaction between PML (NLS-) and GINS2 The interaction between endogenous PML and endogenous GINS2 via co-immunoprecipitation has been experienced also in NB4 cells with success