Q9CQ37
Gene name |
Ube2t |
Protein name |
Ubiquitin-conjugating enzyme E2 T |
Names |
E2 ubiquitin-conjugating enzyme T, Ubiquitin carrier protein T, Ubiquitin-protein ligase T |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:67196 |
EC number |
2.3.2.23: 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 Q9CQ37
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
AF-Q9CQ37-F1 | Predicted | AlphaFoldDB |
21 variants for Q9CQ37
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
rs3388499808 | 16 | I>L | No | EVA | |
rs3388502705 | 16 | I>T | No | EVA | |
rs3388502120 | 17 | E>K | No | EVA | |
rs229797029 | 22 | I>V | No | EVA | |
rs3388503056 | 29 | D>N | No | EVA | |
rs3388498683 | 50 | V>I | No | EVA | |
rs260292046 | 102 | L>I | No | EVA | |
rs3388499766 | 111 | I>V | No | EVA | |
rs3388499786 | 115 | M>V | No | EVA | |
rs3388500191 | 119 | N>K | No | EVA | |
rs3410463644 | 133 | K>E | No | EVA | |
rs3388502517 | 134 | Y>* | No | EVA | |
rs240130430 | 137 | I>M | No | EVA | |
rs46095918 | 149 | A>V | No | EVA | |
rs3388501471 | 158 | D>E | No | EVA | |
rs220512779 | 161 | E>K | No | EVA | |
rs264000216 | 183 | R>G | No | EVA | |
rs3388500015 | 190 | K>N | No | EVA | |
rs3388499995 | 194 | P>S | No | EVA | |
rs234990646 | 196 | V>I | No | EVA | |
rs252146410 | 198 | R>K | No | EVA |
No associated diseases with Q9CQ37
Functions
Description | ||
---|---|---|
EC Number | 2.3.2.23 | Aminoacyltransferases |
Subcellular Localization |
|
|
PANTHER Family | ||
PANTHER Subfamily | ||
PANTHER Protein Class | ||
PANTHER Pathway Category | No pathway information available |
3 GO annotations of cellular component
Name | Definition |
---|---|
nucleolus | A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome. |
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. |
5 GO annotations of molecular function
Name | Definition |
---|---|
ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
chromatin binding | Binding to chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase. |
ubiquitin conjugating enzyme activity | Isoenergetic transfer of ubiquitin from one protein to another via the reaction X-ubiquitin + Y -> Y-ubiquitin + X, where both the X-ubiquitin and Y-ubiquitin linkages are thioester bonds between the C-terminal glycine of ubiquitin and a sulfhydryl side group of a cysteine residue. |
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. |
11 GO annotations of biological process
Name | Definition |
---|---|
cellular response to DNA damage stimulus | 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 stimulus indicating damage to its DNA from environmental insults or errors during metabolism. |
DNA repair | The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. |
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 K11-linked ubiquitination | A protein ubiquitination process in which ubiquitin monomers are attached to a protein, and then ubiquitin polymers are formed by linkages between lysine residues at position 11 of the ubiquitin monomers. K11-linked polyubiquitination targets the substrate protein for degradation. The anaphase-promoting complex promotes the degradation of mitotic regulators by assembling K11-linked polyubiquitin chains. |
protein K27-linked ubiquitination | A protein ubiquitination process in which a polymer of ubiquitin, formed by linkages between lysine residues at position 27 of the ubiquitin monomers, is added to a protein. |
protein K29-linked ubiquitination | A protein ubiquitination process in which a polymer of ubiquitin, formed by linkages between lysine residues at position 29 of the ubiquitin monomers, is added to a protein. K29-linked ubiquitination targets the substrate protein for degradation. |
protein K48-linked ubiquitination | A protein ubiquitination process in which a polymer of ubiquitin, formed by linkages between lysine residues at position 48 of the ubiquitin monomers, is added to a protein. K48-linked ubiquitination targets the substrate protein for degradation. |
protein K6-linked ubiquitination | A protein ubiquitination process in which a polymer of ubiquitin, formed by linkages between lysine residues at position 6 of the ubiquitin monomers, is added to a protein. K6-linked ubiquitination is involved in DNA repair. |
protein K63-linked ubiquitination | A protein ubiquitination process in which a polymer of ubiquitin, formed by linkages between lysine residues at position 63 of the ubiquitin monomers, is added to a protein. K63-linked ubiquitination does not target the substrate protein for degradation, but is involved in several pathways, notably as a signal to promote error-free DNA postreplication repair. |
protein monoubiquitination | Addition of a single ubiquitin group to a protein. |
protein polyubiquitination | Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain. |
19 homologous proteins in AiPD
UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
---|---|---|---|---|
Q32LD2 | UBE2T | Ubiquitin-conjugating enzyme E2 T | Bos taurus (Bovine) | PR |
P35128 | ben | Ubiquitin-conjugating enzyme E2 N | Drosophila melanogaster (Fruit fly) | PR |
P25867 | eff | Ubiquitin-conjugating enzyme E2-17 kDa | Drosophila melanogaster (Fruit fly) | PR |
Q96LR5 | UBE2E2 | Ubiquitin-conjugating enzyme E2 E2 | Homo sapiens (Human) | PR |
Q969T4 | UBE2E3 | Ubiquitin-conjugating enzyme E2 E3 | Homo sapiens (Human) | PR |
Q9NPD8 | UBE2T | Ubiquitin-conjugating enzyme E2 T | Homo sapiens (Human) | PR |
P52483 | Ube2e3 | Ubiquitin-conjugating enzyme E2 E3 | Mus musculus (Mouse) | PR |
P61079 | Ube2d3 | Ubiquitin-conjugating enzyme E2 D3 | Mus musculus (Mouse) | PR |
Q921J4 | Ube2s | Ubiquitin-conjugating enzyme E2 S | Mus musculus (Mouse) | SS |
Q9D1C1 | Ube2c | Ubiquitin-conjugating enzyme E2 C | Mus musculus (Mouse) | PR |
Q9JJZ4 | Ube2j1 | Ubiquitin-conjugating enzyme E2 J1 | Mus musculus (Mouse) | PR |
P61087 | Ube2k | Ubiquitin-conjugating enzyme E2 K | Mus musculus (Mouse) | PR |
Q64362 | Aktip | AKT-interacting protein | Mus musculus (Mouse) | PR |
Q7TSS2 | Ube2q1 | Ubiquitin-conjugating enzyme E2 Q1 | Mus musculus (Mouse) | PR |
A0PJN4 | Ube2ql1 | Ubiquitin-conjugating enzyme E2Q-like protein 1 | Mus musculus (Mouse) | PR |
P35129 | let-70 | Ubiquitin-conjugating enzyme E2 2 | Caenorhabditis elegans | PR |
Q9C8X7 | UBC31 | Probable ubiquitin-conjugating enzyme E2 31 | Arabidopsis thaliana (Mouse-ear cress) | PR |
Q9SLE4 | UBC29 | Ubiquitin-conjugating enzyme E2 29 | Arabidopsis thaliana (Mouse-ear cress) | PR |
Q9LJD7 | COP10 | Constitutive photomorphogenesis protein 10 | Arabidopsis thaliana (Mouse-ear cress) | PR |
10 | 20 | 30 | 40 | 50 | 60 |
MQRASRLKKE | LHMLAIEPPP | GITCWQEKDQ | VADLRAQILG | GANTPYEKGV | FTLEVIIPER |
70 | 80 | 90 | 100 | 110 | 120 |
YPFEPPQVRF | LTPIYHPNID | SSGRICLDIL | KLPPKGAWRP | SLNIATVLTS | IQLLMAEPNP |
130 | 140 | 150 | 160 | 170 | 180 |
DDPLMADISS | EFKYNKIAFL | KKAKQWTEAH | ARQKQKADEE | ELGTSSEVGD | SEESHSTQKR |
190 | 200 | ||||
KARPLGGMEK | KFSPDVQRVY | PGPS |