Q61510
Gene name |
Trim25 |
Protein name |
E3 ubiquitin/ISG15 ligase TRIM25 |
Names |
Estrogen-responsive finger protein, RING-type E3 ubiquitin transferase, RING-type E3 ubiquitin transferase TRIM25, Tripartite motif-containing protein 25, Ubiquitin/ISG15-conjugating enzyme TRIM25, Zinc finger protein 147 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:217069 |
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

2 structures for Q61510
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
4B8E | X-ray | 178 A | A/B | 440-634 | PDB |
AF-Q61510-F1 | Predicted | AlphaFoldDB |
38 variants for Q61510
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
rs221897094 | 3 | E>K | No | EVA | |
rs228960245 | 34 | M>T | No | EVA | |
rs3389162262 | 40 | T>A | No | EVA | |
rs3389185970 | 40 | T>K | No | EVA | |
rs3402345555 | 47 | P>S | No | EVA | |
rs3389196024 | 58 | Q>R | No | EVA | |
rs3389206036 | 65 | K>R | No | EVA | |
rs3389202520 | 72 | V>A | No | EVA | |
rs3389165908 | 74 | E>G | No | EVA | |
rs3389186029 | 75 | Q>* | No | EVA | |
rs27099899 | 87 | D>N | No | EVA | |
rs246829048 | 95 | F>S | No | EVA | |
rs3389194865 | 102 | T>A | No | EVA | |
rs3389192764 | 103 | Q>R | No | EVA | |
rs3389191847 | 142 | H>R | No | EVA | |
rs3389206039 | 159 | H>Q | No | EVA | |
rs27099898 | 165 | L>F | No | EVA | |
rs3389205972 | 214 | G>V | No | EVA | |
rs3402678035 | 241 | R>S | No | EVA | |
rs3389191835 | 260 | R>P | No | EVA | |
rs3401935247 | 261 | K>R | No | EVA | |
rs3389191786 | 274 | D>Y | No | EVA | |
rs3389192832 | 314 | Q>P | No | EVA | |
rs3389154348 | 321 | V>I | No | EVA | |
rs3389194886 | 403 | F>L | No | EVA | |
rs3389191815 | 423 | T>I | No | EVA | |
rs3402586342 | 439 | V>I | No | EVA | |
rs3389188197 | 452 | K>M | No | EVA | |
rs3389188247 | 488 | D>H | No | EVA | |
rs3389194825 | 494 | R>L | No | EVA | |
rs3402559967 | 504 | S>* | No | EVA | |
rs3402651161 | 509 | L>* | No | EVA | |
rs3389192821 | 517 | H>R | No | EVA | |
rs3389165845 | 521 | V>M | No | EVA | |
rs3412788203 | 550 | N>D | No | EVA | |
rs3389194874 | 552 | N>D | No | EVA | |
rs3389154357 | 587 | N>I | No | EVA | |
rs3402586374 | 619 | A>S | No | EVA |
No associated diseases with Q61510
12 regional properties for Q61510
Type | Name | Position | InterPro Accession |
---|---|---|---|
domain | Zinc finger, RING-type | 13 - 54 | IPR001841 |
domain | B30.2/SPRY domain | 444 - 634 | IPR001870 |
domain | SPRY domain | 514 - 634 | IPR003877 |
domain | Butyrophylin-like, SPRY domain | 460 - 477 | IPR003879-1 |
domain | Butyrophylin-like, SPRY domain | 499 - 523 | IPR003879-2 |
domain | Butyrophylin-like, SPRY domain | 529 - 542 | IPR003879-3 |
domain | Butyrophylin-like, SPRY domain | 573 - 597 | IPR003879-4 |
domain | Butyrophylin-like, SPRY domain | 604 - 622 | IPR003879-5 |
domain | SPRY-associated | 461 - 513 | IPR006574 |
conserved_site | Zinc finger, RING-type, conserved site | 28 - 37 | IPR017907 |
domain | Zinc finger, RING-type, eukaryotic | 13 - 51 | IPR027370 |
domain | TRIM25, PRY/SPRY domain | 464 - 632 | IPR042753 |
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 |
6 GO annotations of cellular component
Name | Definition |
---|---|
cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
cytoplasmic stress granule | A dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. |
cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
nuclear body | Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins. |
nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
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. |
6 GO annotations of molecular function
Name | Definition |
---|---|
ligase activity | Catalysis of the joining of two molecules, or two groups within a single molecule, using the energy from the hydrolysis of ATP, a similar triphosphate, or a pH gradient. |
metal ion binding | Binding to a metal ion. |
RIG-I binding | Binding to RIG-I, a cytosolic pattern recognition receptor that initiates an antiviral signaling pathway upon binding to viral RNA. |
transcription coactivator activity | A transcription coregulator activity that activates or increases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coactivators modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. A fourth class of coactivator activity is the bridging of a DNA-binding transcription factor to the general (basal) transcription machinery. The Mediator complex, which bridges sequence-specific DNA binding transcription factors and RNA polymerase, is also a transcription coactivator. |
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. |
15 GO annotations of biological process
Name | Definition |
---|---|
cellular response to leukemia inhibitory factor | 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 a leukemia inhibitory factor stimulus. |
innate immune response | Innate immune responses are defense responses mediated by germline encoded components that directly recognize components of potential pathogens. |
negative regulation of viral entry into host cell | Any process that stops, prevents, or reduces the frequency, rate or extent of the entry of viral entry into a host cell. |
positive regulation of DNA-binding transcription factor activity | Any process that activates or increases the frequency, rate or extent of activity of a transcription factor, any factor involved in the initiation or regulation of transcription. |
positive regulation of I-kappaB kinase/NF-kappaB signaling | Any process that activates or increases the frequency, rate or extent of I-kappaB kinase/NF-kappaB signaling. |
positive regulation of NF-kappaB transcription factor activity | Any process that activates or increases the frequency, rate or extent of activity of the transcription factor NF-kappaB. |
protein monoubiquitination | Addition of a single ubiquitin group to a protein. |
regulation of protein localization | Any process that modulates the frequency, rate or extent of any process in which a protein is transported to, or maintained in, a specific location. |
regulation of viral entry into host cell | Any process that modulates the frequency, rate or extent of the viral entry into the host cell. |
response to estrogen | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of stimulus by an estrogen, C18 steroid hormones that can stimulate the development of female sexual characteristics. |
response to vitamin D | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a vitamin D stimulus. |
suppression of viral release by host | A process in which a host organism stops, prevents or reduces the frequency, rate or extent of the release of a virus with which it is infected, from its cells. |
ubiquitin-dependent ERAD pathway | The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome. |
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. |
viral release from host cell | The dissemination of mature viral particles from the host cell, e.g. by cell lysis or the budding of virus particles from the cell membrane. |
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 |
E1BJS7 | TRIM71 | E3 ubiquitin-protein ligase TRIM71 | Bos taurus (Bovine) | PR |
Q7YRV4 | TRIM21 | E3 ubiquitin-protein ligase TRIM21 | 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 |
Q2Q1W2 | TRIM71 | E3 ubiquitin-protein ligase TRIM71 | Homo sapiens (Human) | PR |
Q9BXM9 | FSD1L | FSD1-like protein | 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 |
Q810I2 | Trim50 | E3 ubiquitin-protein ligase TRIM50 | Mus musculus (Mouse) | PR |
Q1PSW8 | Trim71 | E3 ubiquitin-protein ligase TRIM71 | 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 |
F6QEU4 | trim71 | E3 ubiquitin-protein ligase TRIM71 | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | PR |
Q640S6 | trim72 | Tripartite motif-containing protein 72 | 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 |
MAELNPLAEE | LSCSVCLELF | KEPVTTPCGH | NFCMSCLDET | WVVQGPPYRC | PQCRKVYQVR |
70 | 80 | 90 | 100 | 110 | 120 |
PQLQKNTVMC | AVVEQFLQAE | QARTPVDDWT | PPARFSASSA | ATQVACDHCL | TEIAVKTCLV |
130 | 140 | 150 | 160 | 170 | 180 |
CMASFCQEHL | RPHFDSPAFQ | DHPLQSPIRD | LLRRKCTQHN | RLRELFCPEH | GECICHICLV |
190 | 200 | 210 | 220 | 230 | 240 |
EHKTCSPTTL | SQASADLEYK | LRNKLTIMHS | HINGATKALE | DVRSKQQCVQ | DSMKRKMEQL |
250 | 260 | 270 | 280 | 290 | 300 |
RQEYMEMKAV | IDAAETSSLR | KLKEEEKRVY | GKFDTIYQVL | VKKKSEMQKL | KAEVELIMDK |
310 | 320 | 330 | 340 | 350 | 360 |
GDEFEFLEKA | AKLQGESTKP | VYIPKIDLDH | DLIMGIYQGA | ADLKSELKHS | IKKLQKKSEE |
370 | 380 | 390 | 400 | 410 | 420 |
HNGSGNKGDQ | TQSTFKPVQP | SKKTIQEKKT | KKTPVAPGPP | SHFSPNKLPT | FGAPGQSLDS |
430 | 440 | 450 | 460 | 470 | 480 |
KATSPDAAPK | ASAAQPDSVG | VKAKVLENFL | TKSRTELLEY | FVKVIFDYNT | AHNKVSLSNK |
490 | 500 | 510 | 520 | 530 | 540 |
YTTASVSDGL | QHYRSHPQRF | TYCSQVLGLH | CYKNGIHYWE | VELQKNNFCG | VGICYGSMER |
550 | 560 | 570 | 580 | 590 | 600 |
QGPESRLGRN | PNSWCVEWFN | NKISAWHNNV | EKTLPSTKAT | RVGVLLNCDH | GFVIFFAVTE |
610 | 620 | 630 | |||
KVHLMYKFKV | DFTEALYPAF | WVFSAGTTLS | ICSK |