Q2UBP1
Gene name |
hulA (AO090012000923) |
Protein name |
Probable E3 ubiquitin-protein ligase hulA |
Names |
HECT ubiquitin ligase A, HECT-type E3 ubiquitin transferase hulA |
Species |
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) |
KEGG Pathway |
aor:AO090012000923 |
EC number |
2.3.2.26: Aminoacyltransferases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q2UBP1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q2UBP1-F1 | Predicted | AlphaFoldDB |
No variants for Q2UBP1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q2UBP1 | |||||
No associated diseases with Q2UBP1
5 regional properties for Q2UBP1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | C2 domain | 1 - 112 | IPR000008 |
| domain | HECT domain | 461 - 816 | IPR000569 |
| domain | WW domain | 229 - 262 | IPR001202-1 |
| domain | WW domain | 333 - 366 | IPR001202-2 |
| domain | WW domain | 393 - 426 | IPR001202-3 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.2.26 | Aminoacyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
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: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| 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 |
| MGSNLPAQPN | LRVTIIAADG | LYKRDVFRFP | DPFAVATVGG | EQTHTTSVIK | KTLNPYWNEM |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FDLRVNEDSI | LAIQIFDQKK | FKKKDQGFLG | VINVRIGDVI | DLQMGGDEML | TRDLKKSNDN |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LVVHGKLIIN | LSTNLSTPNT | NQANGLHRSH | MQPSTSSGLV | PQVSASTPQP | SPGPSQADPT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ASNPSLHPQR | VPSTTRPSST | IVPANGPPAP | PNGQQGSRTN | LSSFEDSQGR | LPAGWERRED |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NLGRTYYVDH | NTRTTTWTRP | SNNYNEQTSR | TQREASMQLE | RRAHQSRMLP | EDRTGASSPN |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LQENQQQAQT | PPAGGSASAV | SMMATGATTA | GTGELPPGWE | QRTTPEGRPY | FVDHNTRTTT |
| 370 | 380 | 390 | 400 | 410 | 420 |
| WVDPRRQQYI | RMYGQNANGT | NTTIQQQPVS | QLGPLPSGWE | MRLTNTARVY | FVDHNTKTTT |
| 430 | 440 | 450 | 460 | 470 | 480 |
| WDDPRLPSSL | DQGVPQYKRD | FRRKLIYFRS | QPALRIMSGQ | CHVKVRRNNI | FEDSYAEIMR |
| 490 | 500 | 510 | 520 | 530 | 540 |
| QSASDLKKRL | MIKFDGEDGL | DYGGLSRREF | FFLLSHEMFN | PFYCLFEYSA | HDNYTLQINP |
| 550 | 560 | 570 | 580 | 590 | 600 |
| HSGVNPEHLN | YFKFIGRVVG | LAIFHRRFLD | SFFIGAFYKM | MLRKKVSLQD | MEGVDEDLHR |
| 610 | 620 | 630 | 640 | 650 | 660 |
| NLTWTLDNDI | EGIIELTFAV | DDEKFGERRT | IDLKPGGRDI | PVTNENKGEY | VELVTEWKIV |
| 670 | 680 | 690 | 700 | 710 | 720 |
| KRVEEQFNAF | MSGFNELIPA | DLVNVFDERE | LELLIGGIAD | IDVDDWKKHT | DYRGYQESDE |
| 730 | 740 | 750 | 760 | 770 | 780 |
| VIQNFWKIVR | TWDAEQKSRL | LQFTTGTSRI | PVNGFKDLQG | SDGPRRFTIE | KSGDPGALPK |
| 790 | 800 | 810 | |||
| SHTCFNRLDL | PPYKTNDVLE | HKLSIAVEET | LGFGQE |