As a step forward to achieve the generation of human complex-type N-glycans in the methylotrophic yeast Hansenula polymorpha, we here report the modification of the yeast glycosylation pathway by heterologous expression of the human gene encoding ${eta}$-1,2-N-acetylglucosaminyltransferase I (GnTI). For the optimal expression of human GnTI in the yeast Golgi compartment, the catalytic domain of the GnTI was fused to various N-terminal leader sequences derived from the yeast type II membrane proteins. The vectors containing GnTI fusion constructs were introduced into the H. polymorpha $och1{Delta}$ single and $och1{Delta}alg3{Delta}$ double mutant strains expressing the ER-targeted Aspergillus saitoi ${alpha}$-1,2 mannosidase, respectively. Both of the glycoengineered $Hpoch1{Delta}$ and $Hpoch1{Delta}Hpalg3{Delta}$ strains were shown to produce successfully the hybrid-type glycans with a monoantennary N-acetylglucosamine ($GlcNAc_1Man_5GlcNAc_2$ and $GlcNAc_1Man_3GlcNAc_2$, respectively) by N-glycan profile analysis of cell wall proteins. Furthermore, by comparative analysis of byproduct formation and the glycosylation site occupancy, we propose that the $Hpoch1{Delta}$ strain would be more suitable than the $Hpoch1{Delta}Hpalg3{Delta}$ strain as a host for the production of recombinant proteins with humanized glycans.