Ubiquitin protein ligase
From Proteopedia
| Line 1: | Line 1: | ||
| - | {{STRUCTURE_1c4z| PDB=1c4z | SIZE= | + | {{STRUCTURE_1c4z| PDB=1c4z | SIZE=350| SCENE= |right|CAPTION=Human UPL catalytic domain trimer (grey, green, pink) complex with ubiquitin conjugating enzyme E2 (yellow) [[1c4z]] }} |
'''Ubiquitin-protein ligase''' (UPL) ('''E3''') in combination with ubiquitin-conjugating enzyme (E2) causes the attachment of ubiquitin to lysine to a target protein. '''UPL XIAP''' or '''X-linked Inhibitor of Apoptosis Protein''' stops apoptosis induced by viral infection or by overproduction of caspases. UPL XIAP binds caspase-3, -7 and -9. UPL can contain several distinct domains like:<br /> | '''Ubiquitin-protein ligase''' (UPL) ('''E3''') in combination with ubiquitin-conjugating enzyme (E2) causes the attachment of ubiquitin to lysine to a target protein. '''UPL XIAP''' or '''X-linked Inhibitor of Apoptosis Protein''' stops apoptosis induced by viral infection or by overproduction of caspases. UPL XIAP binds caspase-3, -7 and -9. UPL can contain several distinct domains like:<br /> | ||
| Line 233: | Line 233: | ||
**[[2csw]] – hUPL 8 FHA domain - NMR <br /> | **[[2csw]] – hUPL 8 FHA domain - NMR <br /> | ||
**[[4ayc]], [[4gb0]] – hUPL 8 RING domain <br /> | **[[4ayc]], [[4gb0]] – hUPL 8 RING domain <br /> | ||
| - | ** | + | **[[4orh]] – hUPL 8 residues 345-485 + E2 <br /> |
**[[4juy]], [[4oyj]], [[4p09]] – hUPL 31 PUB domain <br /> | **[[4juy]], [[4oyj]], [[4p09]] – hUPL 31 PUB domain <br /> | ||
**[[4ljq]] – hUPL 31 catalytic domain <br /> | **[[4ljq]] – hUPL 31 catalytic domain <br /> | ||
Revision as of 10:17, 27 November 2016
Ubiquitin-protein ligase (UPL) (E3) in combination with ubiquitin-conjugating enzyme (E2) causes the attachment of ubiquitin to lysine to a target protein. UPL XIAP or X-linked Inhibitor of Apoptosis Protein stops apoptosis induced by viral infection or by overproduction of caspases. UPL XIAP binds caspase-3, -7 and -9. UPL can contain several distinct domains like:
- WW domains which contain 2 tryptophans which bind proline-rich peptide;
- UBA – Ubiquitin-Associated Domain;
- TKB – Tyrosine Kinase Binding domain;
- C2 – an 8 β strand domain which coordinates targeting proteins toward cell membrane;
- HECT – Homologous to the E6-AP C-terminus;
- RING – Really Intersting New Gene involved in binding to E2;
- FHA – Forkhead Associated domain recognizing phosphothreonine;
- IBR – involved in binding to E2;
- PHD finger – Plant Homeo Domain is 50-80 amino acid long which contains a CHC motif;
- SRA – SET and RING-Associated domain;
- TUDOR – a ca. 50 amino acids long and recognizes dimethylated arginine;
- CPH – protein-protein interaction domain;
- UBR – a ca. 70 amino acid long zinc finger-like domain;
- CUE – a ubiquitin-binding domain.
UPL XIAP consists of 3 BIR (baculoviral IAP repeat) domains, followed by UBA (ubiquitin-binding) domain and RING (C-terminal RING finger) domain. BIR2 inhibits caspase-3 and -7. BIR3 inhibits caspase-9. Overexpression of UPL XIAP functions as tumor marker. UPL XIAP is inhibited by Smac – a death signaling protein.
For some details see
3D Structures of ubiquitin protein ligase
Updated on 27-November-2016
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Tihitina Y Aytenfisu, Joel L. Sussman
