B7YZY9
Gene name |
Su(dx) (AIP4, anon-WO0073329.1, anon-WO0073329.2, anon-WO0073329.4, Dmel\CG4244, ITCH, Itch, Su, (Dx), Su(deltex), Su(DX), Su(Dx), su(dx), CG4244, Dmel_CG4244) |
Protein name |
E3 ubiquitin-protein ligase |
Names |
EC 2.3.2.26 |
Species |
Drosophila melanogaster (Fruit fly) |
KEGG Pathway |
dme:Dmel_CG4244 |
EC number |
2.3.2.-: Aminoacyltransferases |
Protein Class |
HECT DOMAIN UBIQUITIN-PROTEIN LIGASE (PTHR11254) |
Descriptions
The E3 ubiquitin-protein ligase Itch (Su(dx), also known as Itch) is a protein that accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates The Su(dx) exhibited enhanced ligase activity when either the WW2 or L domain was removed. The domains in WW domains, except for the L domain, robustly inhibit the ligase activity of the Su(dx) HECT domain in a dose-dependent manner. This indicates that the L domain is essential but not sufficient for its autoinhibition. Furthermore, the WW domains are involved in its ligase regulation. The recruitment of the adaptor protein dNdfip, which contains multiple-PY motifs, via WW domains results in the release of the inhibitory state of Su(dx), leading to substrate ubiquitination.
Autoinhibitory domains (AIDs)
Target domain |
585-949 (HECT domain) |
Relief mechanism |
Partner binding |
Assay |
Structural analysis, Deletion assay, Mutagenesis experiment |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for B7YZY9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B7YZY9-F1 | Predicted | AlphaFoldDB |
No variants for B7YZY9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B7YZY9 | |||||
No associated diseases with B7YZY9
6 regional properties for B7YZY9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | C2 domain | 30 - 146 | IPR000008 |
| domain | HECT domain | 594 - 949 | IPR000569 |
| domain | WW domain | 363 - 396 | IPR001202-1 |
| domain | WW domain | 395 - 428 | IPR001202-2 |
| domain | WW domain | 477 - 510 | IPR001202-3 |
| domain | WW domain | 521 - 554 | IPR001202-4 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.2.- | Aminoacyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | PTHR11254 | HECT DOMAIN UBIQUITIN-PROTEIN LIGASE |
| PANTHER Subfamily | PTHR11254:SF429 | E3 UBIQUITIN-PROTEIN LIGASE SU(DX) |
| PANTHER Protein Class | ubiquitin-protein ligase | |
| PANTHER Pathway Category |
Ubiquitin proteasome pathway E3 |
|
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| ubiquitin protein ligase activity | Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| protein ubiquitination | The process in which one or more ubiquitin groups are added to a protein. |
| regulation of signal transduction | Any process that modulates the frequency, rate or extent of signal transduction. |
| ubiquitin-dependent protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MADGNGLPAG | AASGGMEAGQ | TVNGAGSASP | TPTSSSGAGA | SGSANQGYHQ | LSVTIEEASL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RNNGFLKPNP | YVELLIDSKS | KRKTDLVKNS | YLPKWNEEFT | VLITPNSTLH | FKVLDHSSFR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KDAMLGERII | NLAHILQHYN | GRCEFLELTI | DLFVTSKSDN | RQTKSGELVA | ILNGLKLDMS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KLQIQPVAGQ | QNGNPPVQAV | NPSVVSDAAA | GRSCMIYGGV | RARMRLRSSS | GNSNGGETRS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PLPNGGGDHR | RSTQAPPVWE | QQQQQSQNQQ | QPLRMVNGSG | AAVPQTAPYP | QQPPAPALAR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PLTQVYGALP | ENTQPAAVYL | PAGGGAAVGP | PGVAGPPIEQ | PGVGLPVSQS | TDPQLQTQPA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DDEPLPAGWE | IRLDQYGRRY | YVDHNTRSTY | WEKPTPLPPG | WEIRKDGRGR | VYYVDHNTRK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TTWQRPNSER | LMHFQHWQGQ | RAHVVSQGNQ | RYLYSQQQQQ | PTAVTAQVTQ | DDEDALGPLP |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DGWEKKIQSD | NRVYFVNHKN | RTTQWEDPRT | QGQEVSLINE | GPLPPGWEIR | YTAAGERFFV |
| 550 | 560 | 570 | 580 | 590 | 600 |
| DHNTRRTTFE | DPRPGAPKGA | KGVYGVPRAY | ERSFRWKLSQ | FRYLCQSNAL | PSHIKITVTR |
| 610 | 620 | 630 | 640 | 650 | 660 |
| QTLFEDSYHQ | IMRLPAYELR | RRLYIIFRGE | EGLDYGGVSR | EWFFLLSHEV | LNPMYCLFEY |
| 670 | 680 | 690 | 700 | 710 | 720 |
| ANKNNYSLQI | NPASYVNPDH | LQYFKFIGRF | IAMALYHGRF | IYSGFTMPFY | KRMLNKKLTI |
| 730 | 740 | 750 | 760 | 770 | 780 |
| KDIETIDPEF | YNSLIWVKDN | NIDECGLELW | FSVDFEVLGQ | IIHHELKENG | EKERVTEENK |
| 790 | 800 | 810 | 820 | 830 | 840 |
| EEYITLMTEW | RMTRGIEQQT | KTFLEGFNEV | VPLEWLKYFD | ERELELILCG | MQDVDVEDWQ |
| 850 | 860 | 870 | 880 | 890 | 900 |
| RNTIYRHYNR | NSKQVVWFWQ | FVRETDNEKR | ARLLQFVTGT | CRVPVGGFAE | LMGSNGPQRF |
| 910 | 920 | 930 | 940 | ||
| CIEKVGKETW | LPRSHTCFNR | LDLPPYKSYD | QLVEKLTFAI | EETEGFCQE |