Q9Z1K5
SS
Gene name |
Arih1 |
Protein name |
E3 ubiquitin-protein ligase ARIH1 |
Names |
Protein ariadne-1 homolog, ARI-1, RING-type E3 ubiquitin transferase ARIH1, UbcH7-binding protein, UbcM4-interacting protein 77, Ubiquitin-conjugating enzyme E2-binding protein 1 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:23806 |
EC number |
2.3.2.31: Aminoacyltransferases |
Protein Class |
|
Descriptions
E3 ubiquitin-protein ligase ARIH1 is an E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3, and acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-RING ubiquitin ligase (CRL) complexes and initiating ubiquitination of CRL substrates. ARIH1 is autoinhibited by the ariadne domain, which masks the second RING-type zinc finger that contains the active site and inhibits the E3 activity. The inhibition is relieved upon binding to neddylated cullin-RING ubiquitin ligase complexes, which activate the E3 ligase activity of ARIH1.
Autoinhibitory domains (AIDs)
Target domain |
254-387 (RING2 domain) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
References
- Duda DM et al. (2013) "Structure of HHARI, a RING-IBR-RING ubiquitin ligase: autoinhibition of an Ariadne-family E3 and insights into ligation mechanism", Structure (London, England : 1993), 21, 1030-41
- Kelsall IR et al. (2013) "TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin-RING ligase complexes", The EMBO journal, 32, 2848-60
Autoinhibited structure
Activated structure
1 structures for Q9Z1K5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9Z1K5-F1 | Predicted | AlphaFoldDB |
3 variants for Q9Z1K5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs1134404797 | 129 | T>K | No | Ensembl | |
| rs1134999930 | 130 | R>I | No | Ensembl | |
| rs1132812200 | 131 | I>T | No | Ensembl |
No associated diseases with Q9Z1K5
52 regional properties for Q9Z1K5
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| repeat | Filamin/ABP280 repeat | 253 - 350 | IPR001298-1 |
| repeat | Filamin/ABP280 repeat | 353 - 449 | IPR001298-2 |
| repeat | Filamin/ABP280 repeat | 451 - 546 | IPR001298-3 |
| repeat | Filamin/ABP280 repeat | 548 - 639 | IPR001298-4 |
| repeat | Filamin/ABP280 repeat | 644 - 739 | IPR001298-5 |
| repeat | Filamin/ABP280 repeat | 741 - 842 | IPR001298-6 |
| repeat | Filamin/ABP280 repeat | 844 - 941 | IPR001298-7 |
| repeat | Filamin/ABP280 repeat | 943 - 1037 | IPR001298-8 |
| repeat | Filamin/ABP280 repeat | 1039 - 1130 | IPR001298-9 |
| repeat | Filamin/ABP280 repeat | 1132 - 1225 | IPR001298-10 |
| repeat | Filamin/ABP280 repeat | 1227 - 1325 | IPR001298-11 |
| repeat | Filamin/ABP280 repeat | 1327 - 1418 | IPR001298-12 |
| repeat | Filamin/ABP280 repeat | 1420 - 1514 | IPR001298-13 |
| repeat | Filamin/ABP280 repeat | 1516 - 1611 | IPR001298-14 |
| repeat | Filamin/ABP280 repeat | 1613 - 1707 | IPR001298-15 |
| repeat | Filamin/ABP280 repeat | 1730 - 1819 | IPR001298-16 |
| repeat | Filamin/ABP280 repeat | 1820 - 1911 | IPR001298-17 |
| repeat | Filamin/ABP280 repeat | 1912 - 1997 | IPR001298-18 |
| repeat | Filamin/ABP280 repeat | 2001 - 2092 | IPR001298-19 |
| repeat | Filamin/ABP280 repeat | 2101 - 2188 | IPR001298-20 |
| repeat | Filamin/ABP280 repeat | 2192 - 2283 | IPR001298-21 |
| repeat | Filamin/ABP280 repeat | 2286 - 2378 | IPR001298-22 |
| repeat | Filamin/ABP280 repeat | 2383 - 2474 | IPR001298-23 |
| repeat | Filamin/ABP280 repeat | 2511 - 2602 | IPR001298-24 |
| conserved_site | Actinin-type actin-binding domain, conserved site | 18 - 27 | IPR001589-1 |
| conserved_site | Actinin-type actin-binding domain, conserved site | 94 - 118 | IPR001589-2 |
| domain | Calponin homology domain | 16 - 122 | IPR001715-1 |
| domain | Calponin homology domain | 139 - 242 | IPR001715-2 |
| repeat | Filamin/ABP280 repeat-like | 249 - 347 | IPR017868-1 |
| repeat | Filamin/ABP280 repeat-like | 349 - 446 | IPR017868-2 |
| repeat | Filamin/ABP280 repeat-like | 447 - 543 | IPR017868-3 |
| repeat | Filamin/ABP280 repeat-like | 544 - 636 | IPR017868-4 |
| repeat | Filamin/ABP280 repeat-like | 640 - 736 | IPR017868-5 |
| repeat | Filamin/ABP280 repeat-like | 737 - 839 | IPR017868-6 |
| repeat | Filamin/ABP280 repeat-like | 840 - 938 | IPR017868-7 |
| repeat | Filamin/ABP280 repeat-like | 939 - 1034 | IPR017868-8 |
| repeat | Filamin/ABP280 repeat-like | 1035 - 1127 | IPR017868-9 |
| repeat | Filamin/ABP280 repeat-like | 1128 - 1222 | IPR017868-10 |
| repeat | Filamin/ABP280 repeat-like | 1223 - 1322 | IPR017868-11 |
| repeat | Filamin/ABP280 repeat-like | 1323 - 1415 | IPR017868-12 |
| repeat | Filamin/ABP280 repeat-like | 1416 - 1511 | IPR017868-13 |
| repeat | Filamin/ABP280 repeat-like | 1512 - 1608 | IPR017868-14 |
| repeat | Filamin/ABP280 repeat-like | 1609 - 1704 | IPR017868-15 |
| repeat | Filamin/ABP280 repeat-like | 1709 - 1816 | IPR017868-16 |
| repeat | Filamin/ABP280 repeat-like | 1816 - 1908 | IPR017868-17 |
| repeat | Filamin/ABP280 repeat-like | 1919 - 1994 | IPR017868-18 |
| repeat | Filamin/ABP280 repeat-like | 1997 - 2089 | IPR017868-19 |
| repeat | Filamin/ABP280 repeat-like | 2087 - 2185 | IPR017868-20 |
| repeat | Filamin/ABP280 repeat-like | 2188 - 2280 | IPR017868-21 |
| repeat | Filamin/ABP280 repeat-like | 2282 - 2375 | IPR017868-22 |
| repeat | Filamin/ABP280 repeat-like | 2379 - 2471 | IPR017868-23 |
| repeat | Filamin/ABP280 repeat-like | 2507 - 2601 | IPR017868-24 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.2.31 | Aminoacyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
10 GO annotations of cellular component
| Name | Definition |
|---|---|
| Cajal body | A class of nuclear body, first seen after silver staining by Ramon y Cajal in 1903, enriched in small nuclear ribonucleoproteins, and certain general RNA polymerase II transcription factors; ultrastructurally, they appear as a tangle of coiled, electron-dense threads roughly 0.5 micrometers in diameter; involved in aspects of snRNP biogenesis; the protein coilin serves as a marker for Cajal bodies. Some argue that Cajal bodies are the sites for preassembly of transcriptosomes, unitary particles involved in transcription and processing of RNA. |
| Cul2-RING ubiquitin ligase complex | A ubiquitin ligase complex in which a cullin from the Cul2 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an elongin-BC adaptor and a SOCS/BC box protein. |
| Cul3-RING ubiquitin ligase complex | A ubiquitin ligase complex in which a cullin from the Cul3 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by a BTB-domain-containing protein. |
| Cul4A-RING E3 ubiquitin ligase complex | A ubiquitin ligase complex in which a cullin from the Cul4A subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an adaptor protein. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| Lewy body | Cytoplasmic, spherical inclusion commonly found in damaged neurons, and composed of abnormally phosphorylated, neurofilament proteins aggregated with ubiquitin and alpha-synuclein. |
| nuclear body | Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
| SCF ubiquitin ligase complex | A ubiquitin ligase complex in which a cullin from the Cul1 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by a Skp1 adaptor and an F-box protein. SCF complexes are involved in targeting proteins for degradation by the proteasome. The best characterized complexes are those from yeast and mammals (with core subunits named Cdc53/Cul1, Rbx1/Hrt1/Roc1). |
| ubiquitin ligase complex | A protein complex that includes a ubiquitin-protein ligase and enables ubiquitin protein ligase activity. The complex also contains other proteins that may confer substrate specificity on the complex. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| ubiquitin conjugating enzyme binding | Binding to a ubiquitin conjugating enzyme, any of the E2 proteins. |
| 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. |
| ubiquitin protein ligase binding | Binding to a ubiquitin protein ligase enzyme, any of the E3 proteins. |
| ubiquitin-protein transferase activity | Catalysis of the transfer of ubiquitin from one protein to another via the reaction X-Ub + Y --> Y-Ub + X, where both X-Ub and Y-Ub are covalent linkages. |
| zinc ion binding | Binding to a zinc ion (Zn). |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| positive regulation of proteasomal ubiquitin-dependent protein catabolic process | Any process that activates or increases the frequency, rate or extent of the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome. |
| protein polyubiquitination | Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain. |
| protein ubiquitination | The process in which one or more ubiquitin groups are added to a protein. |
| 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. |
12 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| A2VEA3 | ARIH1 | E3 ubiquitin-protein ligase ARIH1 | Bos taurus (Bovine) | SS |
| Q94981 | ari-1 | E3 ubiquitin-protein ligase ariadne-1 | Drosophila melanogaster (Fruit fly) | SS |
| O76924 | ari-2 | Potential E3 ubiquitin-protein ligase ariadne-2 | Drosophila melanogaster (Fruit fly) | SS |
| Q9Y4X5 | ARIH1 | E3 ubiquitin-protein ligase ARIH1 | Homo sapiens (Human) | EV |
| O95376 | ARIH2 | E3 ubiquitin-protein ligase ARIH2 | Homo sapiens (Human) | EV |
| Q9WVS6 | Prkn | E3 ubiquitin-protein ligase parkin | Mus musculus (Mouse) | EV SS |
| Q9Z1K6 | Arih2 | E3 ubiquitin-protein ligase ARIH2 | Mus musculus (Mouse) | SS |
| O01965 | ari-1.1 | E3 ubiquitin-protein ligase ari-1.1 | Caenorhabditis elegans | SS |
| Q22431 | ari-2 | Potential E3 ubiquitin-protein ligase ariadne-2 | Caenorhabditis elegans | SS |
| B1H1E4 | arih1 | E3 ubiquitin-protein ligase arih1 | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | SS |
| Q6NW85 | arih1l | E3 ubiquitin-protein ligase arih1l | Danio rerio (Zebrafish) (Brachydanio rerio) | SS |
| Q6PFJ9 | arih1 | E3 ubiquitin-protein ligase arih1 | Danio rerio (Zebrafish) (Brachydanio rerio) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDSDEGYNYE | FDEDEECSEE | DSGAEEEEDD | DEDEPDDDNL | DLGEVELVEP | GLGVGGERDG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LLCGETGGGG | GSALGPGGGG | GGGGGGGGPG | HEQEEDYRYE | VLTAEQILQH | MVECIREVNE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VIQNPATITR | ILLSHFNWDK | EKLMERYFDG | NLEKLFAECH | VINPSKKSRT | RQMNTRSSAQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DMPCQICYLN | YPNSYFTGLE | CGHKFCMQCW | SEYLTTKIME | EGMGQTISCP | AHGCDILVDD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NTVMRLITDS | KVKLKYQHLI | TNSFVECNRL | LKWCPAPDCH | HVVKVQYPDA | KPVRCKCGRQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FCFNCGENWH | DPVKCKWLKK | WIKKCDDDSE | TSNWIAANTK | ECPKCHVTIE | KDGGCNHMVC |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RNQNCKAEFC | WVCLGPWEPH | GSAWYNCNRY | NEDDAKAARD | AQERSRAALQ | RYLFYCNRYM |
| 430 | 440 | 450 | 460 | 470 | 480 |
| NHMQSLRFEH | KLYAQVKQKM | EEMQQHNMSW | IEVQFLKKAV | DVLCQCRATL | MYTYVFAFYL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| KKNNQSIIFE | NNQADLENAT | EVLSGYLERD | ISQDSLQDIK | QKVQDKYRYC | ESRRRVLLQH |
| 550 | |||||
| VHEGYEKDLW | EYIED |