Primary Information
BoMiProt ID	Bomi88
Protein Name	Ubiquitin-conjugating enzyme E2 D3
Organism	Bos taurus
Uniprot ID	Q3ZCF7
Milk Fraction	Exosome
Ref Sequence ID	NP_001068603.1
Aminoacid Length	147
Molecular Weight	16745
FASTA Sequence	Download
Gene Name	UBE2D3
Gene ID	326583
Protein Existence Status	Reviewed: Experimental evidence at transcript level
Secondary Information
Protein Function	Key mediators of chain assembly; able to govern the switch from ubiquitin chain initiation to elongation, regulate the processivity of chain formation and establish the topology of assembled chains, determine the consequences of ubiquitylation for the modified proteins; E2s have an active role in determining the length and topology of ubiquitin chains and the processivity of the chain assembly reaction; E2 strongly influences the selection of the correct modifier, ubiquitin, and a suitable E3
Biochemical Properties	As found in humans, active E2s possess a core ubiquitinconjugating (UBC) domain, which contains the catalytic Cys residue and interacts with E1s; ubiquitinylated E2s engage E3s to catalyse substrate ubiquitylation; a single E2 can interact with several different E3s; interactions between E2s and E3s are usually weak, with dissociation constants in the micromolar range; E2s bind cofactors that influence their localization, activity or specificity; E2s exist mainly as E2~Ub conjugates and are therefore poised to react - E2~Ub conjugates have low rates of Ub transfer in the absence of an E3 ligase
Significance in milk	integral components of the ubiquitin proteasome system in milk
PTMs	Ubiquitylation on lysine residues; sumolylation
Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation
Predicted Disorder Regions	NA
DisProt Annotation
TM Helix Prediction	No TM helices
Significance of PTMs	SUMO can also act as a covalent modulator of E2 activity
Linking IDs
Bibliography	1. VanDemark, A. P., Hofmann, R. M., Tsui, C., Pickart, C. M., & Wolberger, C. (2001). Molecular insights into polyubiquitin chain assembly: Crystal structure of the Mms2/Ubc13 heterodimer. Cell, 105(6), 711–720. https://doi.org/10.1016/S0092-8674(01)00387-7. 2. Yin, Q., Lin, S.-C., Lamothe, B., Lu, M., Lo, Y.-C., Hura, G., … Wu, H. (2009). E2 interaction and dimerization in the crystal structure of TRAF6. Nature Structural & Molecular Biology, 16(6), 658–666. https://doi.org/10.1038/nsmb.1605. 3. Skowyra, D., Craig, K. L., Tyers, M., Elledge, S. J., & Harper, J. W. (1997). F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex. Cell, 91(2), 209–219. https://doi.org/10.1016/S0092-8674(00)80403-1. 4. Ozkan, E., Yu, H., & Deisenhofer, J. (2005). Mechanistic insight into the allosteric activation of a ubiquitin-conjugating enzyme by RING-type ubiquitin ligases. Proceedings of the National Academy of Sciences of the United States of America, 102(52), 18890–18895. https://doi.org/10.1073/pnas.0509418102. 5. Lin, Y., Hwang, W. C., & Basavappa, R. (2002). Structural and functional analysis of the human mitotic-specific ubiquitin-conjugating enzyme, UbcH10. The Journal of Biological Chemistry, 277(24), 21913–21921. https://doi.org/10.1074/jbc.M109398200.