Gene Symbol | UBE2T |
Entrez ID | 29089 |
Uniprot ID | Q9NPD8 |
Description | ubiquitin conjugating enzyme E2T |
Chromosomal Location | chr1: 202,331,657-202,341,980 |
Ontology | GO ID | GO Term | Definition | Evidence |
---|---|---|---|---|
BP |
GO:0006281 |
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. |
IMP |
BP |
GO:0006513 |
protein monoubiquitination |
Addition of a single ubiquitin group to a protein. |
IDA |
BP |
GO:0006974 |
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. |
IMP |
BP |
GO:0035519 |
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. |
IDA |
BP |
GO:0036297 |
interstrand cross-link repair |
Removal of a DNA interstrand crosslink (a covalent attachment of DNA bases on opposite strands of the DNA) and restoration of the DNA. DNA interstrand crosslinks occur when both strands of duplex DNA are covalently tethered together (e.g. by an exogenous or endogenous agent), thus preventing the strand unwinding necessary for essential DNA functions such as transcription and replication. |
TAS |
BP |
GO:0044314 |
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. |
IDA |
BP |
GO:0051865 |
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. |
IDA |
BP |
GO:0070534 |
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. |
IDA |
BP |
GO:0070936 |
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. |
IDA |
BP |
GO:0070979 |
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. |
IDA |
BP |
GO:0085020 |
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. |
IDA |
CC |
GO:0005634 |
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. |
TAS |
CC |
GO:0005654 |
nucleoplasm |
That part of the nuclear content other than the chromosomes or the nucleolus. |
TAS |
CC |
GO:0005737 |
cytoplasm |
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
IBA |
MF |
GO:0003682 |
chromatin binding |
Interacting selectively and non-covalently with chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase. |
IDA |
MF |
GO:0004842 |
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. |
IDA |
MF |
GO:0005524 |
ATP binding |
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
IEA |
MF |
GO:0031625 |
ubiquitin protein ligase binding |
Interacting selectively and non-covalently with a ubiquitin protein ligase enzyme, any of the E3 proteins. |
IPI |
MF |
GO:0061630 |
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 isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate. Note that this may include the extension of ubiquitin chains. |
IBA |
MF |
GO:0061631 |
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. |
IDA |
Domain ID | Description |
---|---|
IPR000608 |
Ubiquitin-conjugating enzyme E2 |
IPR016135 |
Ubiquitin-conjugating enzyme/RWD-like |
IPR023313 |
Ubiquitin-conjugating enzyme, active site |
Pathway ID | Pathway Term | Pathway Source |
---|---|---|
hsa03460 |
Fanconi anemia pathway |
KEGG |
WP2363 |
Gastric Cancer Network 2 |
WikiPathways |
UMLS CUI | UMLS Term |
---|---|
C0015625 |
Fanconi Anemia |
Pubmed ID | Author | Year | Title |
---|---|---|---|
22617121 |
Ouandaogo et al. |
2012 |
Differences in transcriptomic profiles of human cumulus cells isolated from oocytes at GV, MI and MII stages after in vivo andin vitro oocyte maturation |
23824412 |
Piltonen et al. |
2013 |
Mesenchymal Stem/Progenitors and Other Endometrial Cell Types From Women With Polycystic Ovary Syndrome (PCOS) Display Inflammatory and Oncogenic Potential |
Gene Symbol | Entrez ID | Uniprot ID | Score |
---|---|---|---|
PRDX2 |
7001 |
P32119 |
0.49 |
SORBS3 |
10174 |
O60504 |
0.49 |
RACK1 |
10399 |
P63244 |
0.49 |
FANCD2 |
2177 |
Q9BXW9 |
0.52 |
BRCA1 |
672 |
P38398 |
0.56 |
AMFR |
267 |
Q9UKV5 |
0.63 |
TRIM27 |
5987 |
P14373 |
0.63 |
RNF4 |
6047 |
P78317 |
0.63 |
PCGF2 |
7703 |
P35227 |
0.63 |
SNURF |
8926 |
Q9Y675 |
0.63 |
MARCH5 |
54708 |
Q9NX47 |
0.63 |
UBE2T |
29089 |
Q9NPD8 |
0.70 |
FANCL |
55120 |
Q9NW38 |
0.90 |
EWSR1 |
2130 |
Q01844 |
0.49 |
UBE2M |
9040 |
P61081 |
0.49 |
UBE2V1 |
387522 |
Q13404 |
0.49 |
UBA1 |
7317 |
P22314 |
0.56 |
UBA6 |
55236 |
A0AVT1 |
0.56 |
SRA1 |
10011 |
Q9HD15 |
0.59 |
CDK5R1 |
8851 |
Q15078 |
0.63 |
ARIH2 |
10425 |
O95376 |
0.63 |
ZNF277 |
11179 |
Q9NRM2 |
0.63 |
OIP5 |
11339 |
O43482 |
0.63 |
MGRN1 |
23295 |
O60291 |
0.63 |
MBD5 |
55777 |
Q9P267 |
0.63 |
RNF128 |
79589 |
Q8TEB7 |
0.63 |
SLC25A32 |
81034 |
Q9H2D1 |
0.63 |
RDH12 |
145226 |
Q96NR8 |
0.63 |
C11orf65 |
160140 |
Q8NCR3 |
0.63 |
LNX2 |
222484 |
Q8N448 |
0.63 |
RNF144B |
255488 |
Q7Z419 |
0.63 |
SUMO2 |
6613 |
P61956 |
0.73 |