Synonyms for hjurp or Related words with hjurp

topk              cenpf              stratifin              zwint              baalc              anln              inhbb              calr              cxadr              uqcrh              wdrpuh              parvb              cenpa              nnat              nfyb              nptxr              ptgdr              wwox              troap              zwilch              rybp              gldc              podxl              htpap              uqcrb              fanci              rkip              mlana              tagln              recql              fkbpl              pdgfc              myof              polq              rerg              ncapg              amfr              ncaph              nfkbia              ywhae              tpte              cflar              rfxank              frzb              prosc              aurkb              mtdh              ptprk              procr              pdgfrl             

Examples of "hjurp"
Holliday junction recognition protein is a protein in humans that is encoded by the HJURP gene.
Replenishment of CENPA every cycle, which is important for reestablishing centromere identity, is carried out by HJURP (Holliday Junction Recognition Protein), or Scm3 in fungi and CAL1 in "Drosophila". Tethering HJURP to a non-centromeric locus can give rise to a neocentromere, even after the disassociation of HJURP. Interestingly, there seems to be a co-evolutionary relationship between the "Drosophila" chaperone CAL1 and CENPA which accounts for species incompatibility‚ÄĒthis is discussed more below.
What has been conserved, or appears to have been? Nearly all eukaryotic organisms, apart from budding yeasts ("Saccharomyces cerevisiae") have satellite DNA in their normal centromeres. Yeast, "Drosophila" and mammals all have heterochromatin flanking their centromeres. Interestingly, although the vertebrate chaperone HJURP and the yeast chaperone Scm3 have diverged, their N-terminal domains show striking conservation. On the other hand, frogs and chickens have domains in their chaperones that are not at all shared with that of yeast. Hence, further research into the mechanistic properties of these chaperones may potentially reveal how they help determine where and what type of centromere and neocentromere form.