FOG18134
EOG83TX9K

sce:UFD2

Genes: 34

SGD Description
Ubiquitin chain assembly factor (E4); cooperates with a ubiquitin-activating enzyme (E1), a ubiquitin-conjugating enzyme (E2), and a ubiquitin protein ligase (E3) to conjugate ubiquitin to substrates; also functions as an E3


PomBase Description
ubiquitin-protein ligase E4 Ufd2 (predicted)


AspGD Description
Ortholog(s) have cytoplasm, nucleus localization


References

Johnson ES, et al. (1995 Jul 21). A proteolytic pathway that recognizes ubiquitin as a degradation signal.

Koegl M, et al. (1999 Mar 5). A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly.

Kim I, et al. (2004 Jul). Multiple interactions of rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis.

Saeki Y, et al. (2004 Jul 30). Definitive evidence for Ufd2-catalyzed elongation of the ubiquitin chain through Lys48 linkage.

Richly H, et al. (2005 Jan 14). A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting.

Rumpf S, et al. (2006 Jan 20). Functional division of substrate processing cofactors of the ubiquitin-selective Cdc48 chaperone.

Tu D, et al. (2007 Oct 2). Structure and function of the yeast U-box-containing ubiquitin ligase Ufd2p.

Nakatsukasa K, et al. (2008 Jan 11). Dissecting the ER-associated degradation of a misfolded polytopic membrane protein.

Liu C, et al. (2010 Apr 2). Ubiquitin chain elongation enzyme Ufd2 regulates a subset of Doa10 substrates.

Hänzelmann P, et al. (2010 Jun 25). The yeast E4 ubiquitin ligase Ufd2 interacts with the ubiquitin-like domains of Rad23 and Dsk2 via a novel and distinct ubiquitin-like binding domain.

Van Damme P, et al. (2012 Jul 31). N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

Mitochondrial localization predictions
Predotar	TargetP	MitoProt
Raw data
Phobius transmembrane predictions 15 genes with posterior transmembrane prediction > 50%