{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Tasaki T"],"funding":["NHLBI NIH HHS","CIHR"],"pagination":["3800-5"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3593856"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["110(10)"],"pubmed_abstract":["The N-end rule pathway is a proteolytic system in which destabilizing N-terminal residues of short-lived proteins act as degradation determinants (N-degrons). Substrates carrying N-degrons are recognized by N-recognins that mediate ubiquitylation-dependent selective proteolysis through the proteasome. Our previous studies identified the mammalian N-recognin family consisting of UBR1/E3α, UBR2, UBR4/p600, and UBR5, which recognize destabilizing N-terminal residues through the UBR box. In the current study, we addressed the physiological function of a poorly characterized N-recognin, 570-kDa UBR4, in mammalian development. UBR4-deficient mice die during embryogenesis and exhibit pleiotropic abnormalities, including impaired vascular development in the yolk sac (YS). Vascular development in U"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["UBR box N-recognin-4 (UBR4), an N-recognin of the N-end rule pathway, and its role in yolk sac vascular development and autophagy."],"pmcid":["PMC3593856"],"funding_grant_id":["R01 HL083365","HL083365"],"pubmed_authors":["Kwon YT","Sung KS","Kim ST","Tasaki T","Cha-Molstad HJ","Hwang J","Zakrzewska A","Sun M","Soung NK","Kim SH","Kang MJ","Yi EC","Nguyen MD","Lee BE","Yoo YD","Kim BY"],"additional_accession":[]},"is_claimable":false,"name":"UBR box N-recognin-4 (UBR4), an N-recognin of the N-end rule pathway, and its role in yolk sac vascular development and autophagy.","description":"The N-end rule pathway is a proteolytic system in which destabilizing N-terminal residues of short-lived proteins act as degradation determinants (N-degrons). Substrates carrying N-degrons are recognized by N-recognins that mediate ubiquitylation-dependent selective proteolysis through the proteasome. Our previous studies identified the mammalian N-recognin family consisting of UBR1/E3α, UBR2, UBR4/p600, and UBR5, which recognize destabilizing N-terminal residues through the UBR box. In the current study, we addressed the physiological function of a poorly characterized N-recognin, 570-kDa UBR4, in mammalian development. UBR4-deficient mice die during embryogenesis and exhibit pleiotropic abnormalities, including impaired vascular development in the yolk sac (YS). Vascular development in U","dates":{"release":"2013-01-01T00:00:00Z","publication":"2013 Mar","modification":"2026-05-05T09:56:41.762Z","creation":"2026-04-07T21:45:52.193Z"},"accession":"S-EPMC3593856","cross_references":{"pubmed":["23431188"],"doi":["10.1073/pnas.1217358110"]}}