Q1PSW8
PR
Gene name |
Trim71 (Gm1127, Lin41) |
Protein name |
E3 ubiquitin-protein ligase TRIM71 |
Names |
Protein lin-41 homolog, mLin41, RING-type E3 ubiquitin transferase TRIM71, Tripartite motif-containing protein 71 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:636931 |
EC number |
2.3.2.27: 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 Q1PSW8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q1PSW8-F1 | Predicted | AlphaFoldDB |
33 variants for Q1PSW8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389090340 | 280 | C>* | No | EVA | |
| rs3389076878 | 285 | C>R | No | EVA | |
| rs3389090320 | 286 | R>I | No | EVA | |
| rs3389074113 | 302 | Q>H | No | EVA | |
| rs3389026441 | 306 | Q>H | No | EVA | |
| rs3389089749 | 373 | V>E | No | EVA | |
| rs3389083505 | 393 | Q>H | No | EVA | |
| rs1134267491 | 400 | S>N | No | EVA | |
| rs3389067383 | 420 | A>T | No | EVA | |
| rs3389074078 | 428 | V>E | No | EVA | |
| rs3400161214 | 466 | S>I | No | EVA | |
| rs3389083447 | 467 | S>R | No | EVA | |
| rs3389058644 | 486 | Q>H | No | EVA | |
| rs3389083484 | 494 | V>I | No | EVA | |
| rs3389047023 | 518 | P>L | No | EVA | |
| rs3389046979 | 524 | G>D | No | EVA | |
| rs3389090383 | 586 | E>* | No | EVA | |
| rs3389047036 | 590 | E>G | No | EVA | |
| rs3389089803 | 590 | E>K | No | EVA | |
| rs3389026483 | 637 | P>S | No | EVA | |
| rs3389085650 | 658 | D>G | No | EVA | |
| rs3389076869 | 675 | L>H | No | EVA | |
| rs3389081979 | 694 | A>T | No | EVA | |
| rs3389080003 | 713 | L>F | No | EVA | |
| rs3389047032 | 713 | L>M | No | EVA | |
| rs3389080152 | 731 | W>L | No | EVA | |
| rs3389056024 | 751 | T>P | No | EVA | |
| rs3389085712 | 773 | S>* | No | EVA | |
| rs3389090392 | 799 | D>E | No | EVA | |
| rs3389079958 | 805 | V>M | No | EVA | |
| rs3389082042 | 828 | M>T | No | EVA | |
| rs3389026491 | 837 | T>I | No | EVA | |
| rs3389089719 | 849 | N>I | No | EVA |
No associated diseases with Q1PSW8
12 regional properties for Q1PSW8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | B-box-type zinc finger | 181 - 230 | IPR000315-1 |
| domain | B-box-type zinc finger | 260 - 301 | IPR000315-2 |
| repeat | NHL repeat | 580 - 623 | IPR001258-1 |
| repeat | NHL repeat | 627 - 670 | IPR001258-2 |
| repeat | NHL repeat | 674 - 717 | IPR001258-3 |
| repeat | NHL repeat | 721 - 764 | IPR001258-4 |
| repeat | NHL repeat | 768 - 811 | IPR001258-5 |
| repeat | NHL repeat | 815 - 855 | IPR001258-6 |
| repeat | Filamin/ABP280 repeat | 470 - 570 | IPR001298 |
| domain | Zinc finger, RING-type | 12 - 94 | IPR001841 |
| repeat | Filamin/ABP280 repeat-like | 466 - 567 | IPR017868 |
| conserved_site | Zinc finger, RING-type, conserved site | 60 - 69 | IPR017907 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.2.27 | 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 |
|---|---|
| P-body | A focus in the cytoplasm where mRNAs may become inactivated by decapping or some other mechanism. Protein and RNA localized to these foci are involved in mRNA degradation, nonsense-mediated mRNA decay (NMD), translational repression, and RNA-mediated gene silencing. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| miRNA binding | Binding to a microRNA, a 21-23 nucleotide RNA that is processed from a stem-loop RNA precursor (pre-miRNA) that is encoded within plant and animal genomes. |
| translation repressor activity | Antagonizes ribosome-mediated translation of mRNA into a polypeptide. |
| 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 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). |
19 GO annotations of biological process
| Name | Definition |
|---|---|
| 3'-UTR-mediated mRNA destabilization | An mRNA destabilization process in which one or more RNA-binding proteins associate with the 3'-untranslated region (UTR) of an mRNA. |
| cellular response to organic substance | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an organic substance stimulus. |
| fibroblast growth factor receptor signaling pathway | The series of molecular signals generated as a consequence of a fibroblast growth factor receptor binding to one of its physiological ligands. |
| G1/S transition of mitotic cell cycle | The mitotic cell cycle transition by which a cell in G1 commits to S phase. The process begins with the build up of G1 cyclin-dependent kinase (G1 CDK), resulting in the activation of transcription of G1 cyclins. The process ends with the positive feedback of the G1 cyclins on the G1 CDK which commits the cell to S phase, in which DNA replication is initiated. |
| miRNA metabolic process | The chemical reactions and pathways involving miRNA, microRNA, a class of single-stranded RNA molecules of about 21-23 nucleotides in length, which regulates gene expression. |
| miRNA processing | A process leading to the generation of a functional miRNA. Includes the cleavage of stem-loop RNA precursors into microRNAs (miRNAs). miRNAs are a class of small RNAs that primarily silence genes by blocking the translation of mRNA transcripts into protein, or by increasing the degradation of non-protein-coding RNA transcripts. |
| miRNA-mediated gene silencing by inhibition of translation | An RNA interference pathway in which microRNAs (miRNAs) block the translation of target mRNAs into proteins. Once incorporated into a RNA-induced silencing complex (RISC), a miRNA will typically mediate repression of translation if the miRNA imperfectly base-pairs with the 3' untranslated regions of target mRNAs. |
| negative regulation of translation | Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA. |
| neural tube closure | The last step in the formation of the neural tube, where the paired neural folds are brought together and fuse at the dorsal midline. |
| neural tube development | The process whose specific outcome is the progression of the neural tube over time, from its formation to the mature structure. The mature structure of the neural tube exists when the tube has been segmented into the forebrain, midbrain, hindbrain and spinal cord regions. In addition neural crest has budded away from the epithelium. |
| positive regulation of miRNA-mediated gene silencing | A process that activates or increases the frequency, rate or extent of gene silencing by a microRNA (miRNA). |
| post-transcriptional regulation of gene expression | Any process that modulates the frequency, rate or extent of gene expression after the production of an RNA transcript. |
| proteasome-mediated 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 ubiquitin, and mediated by the proteasome. |
| protein autoubiquitination | The ubiquitination by a protein of one or more of its own amino acid residues, or residues on an identical protein. Ubiquitination occurs on the lysine residue by formation of an isopeptide crosslink. |
| protein polyubiquitination | Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain. |
| regulation of miRNA-mediated gene silencing | A process that modulates the rate, frequency, or extent of the downregulation of gene expression through the action of microRNAs (miRNAs). |
| regulation of neural precursor cell proliferation | Any process that modulates the frequency, rate or extent of neural precursor cell proliferation. |
| regulation of protein metabolic process | Any process that modulates the frequency, rate or extent of the chemical reactions and pathways involving a protein. |
| stem cell proliferation | The multiplication or reproduction of stem cells, resulting in the expansion of a stem cell population. A stem cell is a cell that retains the ability to divide and proliferate throughout life to provide progenitor cells that can differentiate into specialized cells. |
46 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q5E9G4 | TRIM10 | Tripartite motif-containing protein 10 | Bos taurus (Bovine) | PR |
| Q2T9Z0 | TRIM17 | E3 ubiquitin-protein ligase TRIM17 | Bos taurus (Bovine) | PR |
| Q7YRV4 | TRIM21 | E3 ubiquitin-protein ligase TRIM21 | Bos taurus (Bovine) | PR |
| E1BJS7 | TRIM71 | E3 ubiquitin-protein ligase TRIM71 | Bos taurus (Bovine) | PR |
| Q1PRL4 | TRIM71 | E3 ubiquitin-protein ligase TRIM71 | Gallus gallus (Chicken) | PR |
| Q7YR32 | TRIM10 | Tripartite motif-containing protein 10 | Pan troglodytes (Chimpanzee) | PR |
| O15553 | MEFV | Pyrin | Homo sapiens (Human) | SS |
| Q9BTV5 | FSD1 | Fibronectin type III and SPRY domain-containing protein 1 | Homo sapiens (Human) | PR |
| Q9H2S5 | RNF39 | RING finger protein 39 | Homo sapiens (Human) | PR |
| P19474 | TRIM21 | E3 ubiquitin-protein ligase TRIM21 | Homo sapiens (Human) | PR |
| Q9UJV3 | MID2 | Probable E3 ubiquitin-protein ligase MID2 | Homo sapiens (Human) | PR |
| P29590 | PML | Protein PML | Homo sapiens (Human) | PR |
| Q9C029 | TRIM7 | E3 ubiquitin-protein ligase TRIM7 | Homo sapiens (Human) | PR |
| Q9NQ86 | TRIM36 | E3 ubiquitin-protein ligase TRIM36 | Homo sapiens (Human) | PR |
| Q86UV6 | TRIM74 | Tripartite motif-containing protein 74 | Homo sapiens (Human) | PR |
| Q9UPQ4 | TRIM35 | E3 ubiquitin-protein ligase TRIM35 | Homo sapiens (Human) | PR |
| Q6ZMU5 | TRIM72 | Tripartite motif-containing protein 72 | Homo sapiens (Human) | PR |
| Q86UV7 | TRIM73 | Tripartite motif-containing protein 73 | Homo sapiens (Human) | PR |
| Q8N9V2 | TRIML1 | Probable E3 ubiquitin-protein ligase TRIML1 | Homo sapiens (Human) | PR |
| Q86XT4 | TRIM50 | E3 ubiquitin-protein ligase TRIM50 | Homo sapiens (Human) | PR |
| Q5EBN2 | TRIM61 | Putative tripartite motif-containing protein 61 | Homo sapiens (Human) | PR |
| Q9BZY9 | TRIM31 | E3 ubiquitin-protein ligase TRIM31 | Homo sapiens (Human) | PR |
| Q9BXM9 | FSD1L | FSD1-like protein | Homo sapiens (Human) | PR |
| Q2Q1W2 | TRIM71 | E3 ubiquitin-protein ligase TRIM71 | Homo sapiens (Human) | PR |
| Q9WUH5 | Trim10 | Tripartite motif-containing protein 10 | Mus musculus (Mouse) | PR |
| Q8BZT2 | Sh3rf2 | E3 ubiquitin-protein ligase SH3RF2 | Mus musculus (Mouse) | PR |
| Q7TPM3 | Trim17 | E3 ubiquitin-protein ligase TRIM17 | Mus musculus (Mouse) | PR |
| Q1XH17 | Trim72 | Tripartite motif-containing protein 72 | Mus musculus (Mouse) | PR |
| Q60953 | Pml | Protein PML | Mus musculus (Mouse) | PR |
| Q9JJ26 | Mefv | Pyrin | Mus musculus (Mouse) | SS |
| Q99PQ1 | Trim12a | Tripartite motif-containing protein 12A | Mus musculus (Mouse) | PR |
| Q61510 | Trim25 | E3 ubiquitin/ISG15 ligase TRIM25 | Mus musculus (Mouse) | PR |
| Q810I2 | Trim50 | E3 ubiquitin-protein ligase TRIM50 | Mus musculus (Mouse) | PR |
| Q3TL54 | Trim43a | Tripartite motif-containing protein 43A | Mus musculus (Mouse) | PR |
| P86449 | Trim43c | Tripartite motif-containing protein 43C | Mus musculus (Mouse) | PR |
| O77666 | TRIM26 | Tripartite motif-containing protein 26 | Sus scrofa (Pig) | PR |
| O19085 | TRIM10 | Tripartite motif-containing protein 10 | Sus scrofa (Pig) | PR |
| Q865W2 | TRIM50 | E3 ubiquitin-protein ligase TRIM50 | Sus scrofa (Pig) | PR |
| Q920M2 | Rnf39 | RING finger protein 39 | Rattus norvegicus (Rat) | PR |
| Q9JJ25 | Mefv | Pyrin | Rattus norvegicus (Rat) | SS |
| A0JPQ4 | Trim72 | Tripartite motif-containing protein 72 | Rattus norvegicus (Rat) | PR |
| Q810I1 | Trim50 | E3 ubiquitin-protein ligase TRIM50 | Rattus norvegicus (Rat) | PR |
| D3ZVM4 | Trim71 | E3 ubiquitin-protein ligase TRIM71 | Rattus norvegicus (Rat) | PR |
| Q640S6 | trim72 | Tripartite motif-containing protein 72 | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | PR |
| F6QEU4 | trim71 | E3 ubiquitin-protein ligase TRIM71 | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | PR |
| E7FAM5 | trim71 | E3 ubiquitin-protein ligase TRIM71 | Danio rerio (Zebrafish) (Brachydanio rerio) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MASFPETDFQ | ICLLCKEMCG | SPAPLSSNSS | ASSSSSQTST | SSAGGGGPGA | AARRLHVLPC |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LHAFCRPCLE | AHRLPAPGGA | GPAEALKLRC | PVCDQKVVLA | EAAGMDALPS | SAFLLSNLLD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AVVATAEEPP | PKNGRAGGGP | GGAGGHSNHR | HHAHHPAQRA | AAPAPQPPPG | PAASPGSLLM |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RRPHGCSSCD | EGNAASSRCL | DCQEHLCDNC | VRAHQRVRLT | KDHYIERGPP | GPAAASAAQQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LGLGPPFAGA | PFSILSVFPE | RLGFCQHHDD | EVLHLYCDTC | SVPICRECTL | GRHGGHSFAY |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LQDALQDSRA | LTIQLLADAQ | QGRQALQLSI | EQAQTVAEQV | EMKAKVVQSE | VKAVTARHKK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ALEDRECELL | WKVEKIRQVK | AKSLFLQVEK | LRQSLSKLES | TISAVQQVLE | EGRALDILLA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| RDRMLAQVQE | LKTIRGLLQP | QEDDRIMFTP | PDQALYLALK | SIGFVSSGAF | APLTKATGDG |
| 490 | 500 | 510 | 520 | 530 | 540 |
| IKRALQGKVA | SFTVMGYDHD | GEPRHSGGDL | MSVVVLGPDG | NLFGAEVSDQ | QNGTYIVSYR |
| 550 | 560 | 570 | 580 | 590 | 600 |
| PQLEGEHLVS | VTLYNQHIEN | SPFKVVVKSG | RSYVGIGLPG | LSFGSEGDGE | GKLCRPWGVS |
| 610 | 620 | 630 | 640 | 650 | 660 |
| VDKEGFIIVA | DRSNNRIQVF | KPCGSFHHKF | GTLGSRPGQF | DRPAGVACDA | SRRIIVADKD |
| 670 | 680 | 690 | 700 | 710 | 720 |
| NHRIQIFTFE | GQFLLKFGEK | GTKNGQFNYP | WDVAVNSEGK | ILVSDTRNHR | IQLFGPDGVF |
| 730 | 740 | 750 | 760 | 770 | 780 |
| LNKYGFEGSL | WKHFDSPRGV | AFNNEGHLVV | TDFNNHRLLV | IHPDCQSARF | LGSEGSGNGQ |
| 790 | 800 | 810 | 820 | 830 | 840 |
| FLRPQGVAVD | QEGRIIVADS | RNHRVQMFEA | NGSFLCKFGA | QGSGFGQMDR | PSGIAVTPDG |
| 850 | |||||
| LIVVVDFGNN | RILIF |