UBC13 MMS2: Difference between revisions

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== Function ==

Ubc13 functions as a heterodimer with Mms2, a structurally similar protein to Ubc13 that lacks the catalytic cysteine residue in the active site<ref name=mckenna>5. McKenna, S.; Spyracopoulos, L. F.; Moraes, T. F.; Pastushok, L. F.; Ptak, C. F.; Xiao W FAU - Ellison,,M.J.; Ellison, M. J. Noncovalent interaction between ubiquitin and the human DNA repair protein Mms2 is required for Ubc13-mediated polyubiquitination. The Journal of biological chemistry JID - 2985121R 1207.</ref><ref name=Pastushok> 7. Pastushok, L.; FAU, M. T.; FAU, E. M.; Xiao, W. A single Mms2 "key" residue insertion into a Ubc13 pocket determines the interface specificity of a human Lys63 ubiquitin conjugation complex. The Journal of biological chemistry JID - 2985121R 0902.</ref>. The Ubc13-E2 complex with Mms2 functions primarily to enhance DNA repair from double stranded breaks. Mms2 bound to Ubc13 helps orient the ubiquitin molecule for proper ubiquitination of the K63 residue. Mms2 is considered a UEV protein ~~(Ubiquitin-conjugating Enzyme Variant)~~, because it lacks the catalytic cysteine residue necessary for proper thioester formation.

Ubc13 functions as a heterodimer with Mms2, a structurally similar protein to Ubc13 that lacks the catalytic cysteine residue in the active site<ref name=mckenna>5. McKenna, S.; Spyracopoulos, L. F.; Moraes, T. F.; Pastushok, L. F.; Ptak, C. F.; Xiao W FAU - Ellison,,M.J.; Ellison, M. J. Noncovalent interaction between ubiquitin and the human DNA repair protein Mms2 is required for Ubc13-mediated polyubiquitination. The Journal of biological chemistry JID - 2985121R 1207.</ref><ref name=Pastushok> 7. Pastushok, L.; FAU, M. T.; FAU, E. M.; Xiao, W. A single Mms2 "key" residue insertion into a Ubc13 pocket determines the interface specificity of a human Lys63 ubiquitin conjugation complex. The Journal of biological chemistry JID - 2985121R 0902.</ref>. The Ubc13-E2 complex with Mms2 functions primarily to enhance DNA repair from double stranded breaks. Mms2 bound to Ubc13 helps orient the ubiquitin molecule for proper ubiquitination of the K63 residue. Mms2 is considered a Ubiquitin E2 variant (UEV) protein , because it lacks the catalytic cysteine residue necessary for proper thioester formation.

== Regulation ==

UBC13 MMS2: Difference between revisions

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 == Function ==
-Ubc13 functions as a heterodimer with Mms2, a structurally similar protein to Ubc13 that lacks the catalytic cysteine residue in the active site<ref name=mckenna>5. McKenna, S.; Spyracopoulos, L. F.; Moraes, T. F.; Pastushok, L. F.; Ptak, C. F.; Xiao W FAU - Ellison,,M.J.; Ellison, M. J. Noncovalent interaction between ubiquitin and the human DNA repair protein Mms2 is required for Ubc13-mediated polyubiquitination. The Journal of biological chemistry JID - 2985121R 1207.</ref><ref name=Pastushok> 7. Pastushok, L.; FAU, M. T.; FAU, E. M.; Xiao, W. A single Mms2 "key" residue insertion into a Ubc13 pocket determines the interface specificity of a human Lys63 ubiquitin conjugation complex. The Journal of biological chemistry JID - 2985121R 0902.</ref>.  The Ubc13-E2 complex with Mms2 functions primarily to enhance DNA repair from double stranded breaks.  Mms2 bound to Ubc13 helps orient the ubiquitin molecule for proper ubiquitination of the K63 residue.  Mms2 is considered a UEV protein (Ubiquitin-conjugating Enzyme Variant), because it lacks the catalytic cysteine residue necessary for proper thioester formation.
+Ubc13 functions as a heterodimer with Mms2, a structurally similar protein to Ubc13 that lacks the catalytic cysteine residue in the active site<ref name=mckenna>5. McKenna, S.; Spyracopoulos, L. F.; Moraes, T. F.; Pastushok, L. F.; Ptak, C. F.; Xiao W FAU - Ellison,,M.J.; Ellison, M. J. Noncovalent interaction between ubiquitin and the human DNA repair protein Mms2 is required for Ubc13-mediated polyubiquitination. The Journal of biological chemistry JID - 2985121R 1207.</ref><ref name=Pastushok> 7. Pastushok, L.; FAU, M. T.; FAU, E. M.; Xiao, W. A single Mms2 "key" residue insertion into a Ubc13 pocket determines the interface specificity of a human Lys63 ubiquitin conjugation complex. The Journal of biological chemistry JID - 2985121R 0902.</ref>.  The Ubc13-E2 complex with Mms2 functions primarily to enhance DNA repair from double stranded breaks.  Mms2 bound to Ubc13 helps orient the ubiquitin molecule for proper ubiquitination of the K63 residue.  Mms2 is considered a Ubiquitin E2 variant (UEV) protein , because it lacks the catalytic cysteine residue necessary for proper thioester formation.
 == Regulation ==