UniProt ID | UB2G1_HUMAN | |
---|---|---|
UniProt AC | P62253 | |
Protein Name | Ubiquitin-conjugating enzyme E2 G1 | |
Gene Name | UBE2G1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 170 | |
Subcellular Localization | ||
Protein Description | Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. May be involved in degradation of muscle-specific proteins. Mediates polyubiquitination of CYP3A4.. | |
Protein Sequence | MTELQSALLLRRQLAELNKNPVEGFSAGLIDDNDLYRWEVLIIGPPDTLYEGGVFKAHLTFPKDYPLRPPKMKFITEIWHPNVDKNGDVCISILHEPGEDKYGYEKPEERWLPIHTVETIMISVISMLADPNGDSPANVDAAKEWREDRNGEFKRKVARCVRKSQETAFE | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
1 | Acetylation | -------MTELQSAL -------CCHHHHHH | 6.24 | 22814378 | |
2 | Acetylation | ------MTELQSALL ------CCHHHHHHH | 45.46 | 22223895 | |
2 | Phosphorylation | ------MTELQSALL ------CCHHHHHHH | 45.46 | 20068231 | |
6 | Phosphorylation | --MTELQSALLLRRQ --CCHHHHHHHHHHH | 33.24 | 20068231 | |
19 | Ubiquitination | RQLAELNKNPVEGFS HHHHHHCCCCCCCCC | 75.22 | - | |
56 | Ubiquitination | LYEGGVFKAHLTFPK EEECCEEEEEEECCC | 32.27 | 33845483 | |
63 | Ubiquitination | KAHLTFPKDYPLRPP EEEEECCCCCCCCCC | 66.75 | 23000965 | |
65 | Phosphorylation | HLTFPKDYPLRPPKM EEECCCCCCCCCCCC | 15.42 | 17384208 | |
71 | Ubiquitination | DYPLRPPKMKFITEI CCCCCCCCCCEEEEE | 58.36 | 23000965 | |
73 | Ubiquitination | PLRPPKMKFITEIWH CCCCCCCCEEEEECC | 39.48 | 23000965 | |
76 | Phosphorylation | PPKMKFITEIWHPNV CCCCCEEEEECCCCC | 25.26 | - | |
85 | Ubiquitination | IWHPNVDKNGDVCIS ECCCCCCCCCCEEEE | 59.55 | 21963094 | |
101 | Ubiquitination | LHEPGEDKYGYEKPE EECCCCCCCCCCCCH | 35.95 | 21963094 | |
102 | Phosphorylation | HEPGEDKYGYEKPEE ECCCCCCCCCCCCHH | 36.94 | 28796482 | |
104 | Phosphorylation | PGEDKYGYEKPEERW CCCCCCCCCCCHHHC | 20.07 | 28796482 | |
106 | Ubiquitination | EDKYGYEKPEERWLP CCCCCCCCCHHHCCC | 49.60 | 27667366 | |
163 | Ubiquitination | KVARCVRKSQETAFE HHHHHHHHHHHHHCC | 35.77 | 24816145 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UB2G1_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of UB2G1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
HOIL1_HUMAN | RBCK1 | physical | 19549727 | |
AMFR_HUMAN | AMFR | physical | 19560420 | |
A4_HUMAN | APP | physical | 21832049 | |
UBP8_HUMAN | USP8 | physical | 22939629 | |
WWP2_HUMAN | WWP2 | physical | 22939629 | |
UB2G1_HUMAN | UBE2G1 | physical | 20061386 |
Kegg Disease | ||||||
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There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides."; Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.; Nat. Biotechnol. 21:566-569(2003). Cited for: PROTEIN SEQUENCE OF 2-11, AND ACETYLATION AT THR-2. |