| UniProt ID | GPS2_HUMAN | |
|---|---|---|
| UniProt AC | Q13227 | |
| Protein Name | G protein pathway suppressor 2 {ECO:0000303|PubMed:19917673, ECO:0000303|PubMed:8943324} | |
| Gene Name | GPS2 {ECO:0000312|HGNC:HGNC:4550} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 327 | |
| Subcellular Localization | Nucleus . Mitochondrion . Cytoplasm, cytosol . Sumoylation regulates the subcellular location (PubMed:24943844). Relocates from the mitochondria to the nucleus following desumoylation, leading to mediate mitochondrial stress response (By similarity). | |
| Protein Description | Key regulator of inflammation, lipid metabolism and mitochondrion homeostasis that acts by inhibiting the activity of the ubiquitin-conjugating enzyme UBE2N/Ubc13, thereby inhibiting 'Lys-63'-linked ubiquitination (By similarity). In the nucleus, can both acts as a corepressor and coactivator of transcription, depending on the context. [PubMed: 24943844 Acts as a transcription coactivator in adipocytes by promoting the recruitment of PPARG to promoters: acts by inhibiting the activity of the ubiquitin-conjugating enzyme UBE2N/Ubc13, leading to stabilization of KDM4A and subsequent histone H3 'Lys-9' (H3K9) demethylation (By similarity Promotes cholesterol efflux by acting as a transcription coactivator] | |
| Protein Sequence | MPALLERPKLSNAMARALHRHIMMERERKRQEEEEVDKMMEQKMKEEQERRKKKEMEERMSLEETKEQILKLEEKLLALQEEKHQLFLQLKKVLHEEEKRRRKEQSDLTTLTSAAYQQSLTVHTGTHLLSMQGSPGGHNRPGTLMAADRAKQMFGPQVLTTRHYVGSAAAFAGTPEHGQFQGSPGGAYGTAQPPPHYGPTQPAYSPSQQLRAPSAFPAVQYLSQPQPQPYAVHGHFQPTQTGFLQPGGALSLQKQMEHANQQTGFSDSSSLRPMHPQALHPAPGLLASPQLPVQMQPAGKSGFAATSQPGPRLPFIQHSQNPRFYHK | |
| 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 |
|---|---|---|---|---|---|
| 45 | Sumoylation | KMMEQKMKEEQERRK HHHHHHHHHHHHHHH | 66.20 | 24943844 | |
| 66 | Ubiquitination | RMSLEETKEQILKLE HHCHHHHHHHHHHHH | 51.40 | 21906983 | |
| 66 | Ubiquitination | RMSLEETKEQILKLE HHCHHHHHHHHHHHH | 51.40 | - | |
| 71 | Ubiquitination | ETKEQILKLEEKLLA HHHHHHHHHHHHHHH | 56.32 | 22817900 | |
| 71 | Sumoylation | ETKEQILKLEEKLLA HHHHHHHHHHHHHHH | 56.32 | 24943844 | |
| 71 | Ubiquitination | ETKEQILKLEEKLLA HHHHHHHHHHHHHHH | 56.32 | - | |
| 75 | 2-Hydroxyisobutyrylation | QILKLEEKLLALQEE HHHHHHHHHHHHHHH | 39.15 | - | |
| 75 | Ubiquitination | QILKLEEKLLALQEE HHHHHHHHHHHHHHH | 39.15 | 29967540 | |
| 75 | Ubiquitination | QILKLEEKLLALQEE HHHHHHHHHHHHHHH | 39.15 | - | |
| 83 | Ubiquitination | LLALQEEKHQLFLQL HHHHHHHHHHHHHHH | 35.58 | 29967540 | |
| 83 | Ubiquitination | LLALQEEKHQLFLQL HHHHHHHHHHHHHHH | 35.58 | - | |
| 83 | 2-Hydroxyisobutyrylation | LLALQEEKHQLFLQL HHHHHHHHHHHHHHH | 35.58 | - | |
| 91 | Ubiquitination | HQLFLQLKKVLHEEE HHHHHHHHHHHHHHH | 28.07 | 29967540 | |
| 91 | 2-Hydroxyisobutyrylation | HQLFLQLKKVLHEEE HHHHHHHHHHHHHHH | 28.07 | - | |
| 92 | Ubiquitination | QLFLQLKKVLHEEEK HHHHHHHHHHHHHHH | 59.63 | - | |
| 92 | Ubiquitination | QLFLQLKKVLHEEEK HHHHHHHHHHHHHHH | 59.63 | - | |
| 119 | Phosphorylation | TSAAYQQSLTVHTGT HHHHHHHCCEEECCC | 15.52 | 28348404 | |
| 121 | Phosphorylation | AAYQQSLTVHTGTHL HHHHHCCEEECCCCE | 18.58 | 28348404 | |
| 124 | Phosphorylation | QQSLTVHTGTHLLSM HHCCEEECCCCEEEE | 39.17 | 28348404 | |
| 126 | Phosphorylation | SLTVHTGTHLLSMQG CCEEECCCCEEEECC | 15.54 | 27251275 | |
| 130 | Phosphorylation | HTGTHLLSMQGSPGG ECCCCEEEECCCCCC | 18.54 | 28348404 | |
| 134 | Phosphorylation | HLLSMQGSPGGHNRP CEEEECCCCCCCCCC | 11.95 | 28348404 | |
| 151 | Ubiquitination | LMAADRAKQMFGPQV CCHHHHHHHHHCCCE | 43.09 | - | |
| 151 | Ubiquitination | LMAADRAKQMFGPQV CCHHHHHHHHHCCCE | 43.09 | 27667366 | |
| 161 | O-linked_Glycosylation | FGPQVLTTRHYVGSA HCCCEEEECCCCCCH | 15.99 | 30379171 | |
| 204 | Phosphorylation | YGPTQPAYSPSQQLR CCCCCCCCCHHHHCC | 28.00 | 26074081 | |
| 205 | Phosphorylation | GPTQPAYSPSQQLRA CCCCCCCCHHHHCCC | 21.85 | 26074081 | |
| 207 | Phosphorylation | TQPAYSPSQQLRAPS CCCCCCHHHHCCCCC | 25.31 | 26074081 | |
| 251 | Phosphorylation | LQPGGALSLQKQMEH CCCCCHHHHHHHHHH | 28.37 | 24719451 | |
| 312 | Asymmetric dimethylarginine | ATSQPGPRLPFIQHS CCCCCCCCCCCCCCC | 61.99 | - | |
| 312 | Methylation | ATSQPGPRLPFIQHS CCCCCCCCCCCCCCC | 61.99 | 24129315 | |
| 323 | Methylation | IQHSQNPRFYHK--- CCCCCCCCCCCC--- | 52.91 | 19917673 | |
| 323 | Asymmetric dimethylarginine | IQHSQNPRFYHK--- CCCCCCCCCCCC--- | 52.91 | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of GPS2_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 GPS2_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| 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. | ||||||
loading...