| UniProt ID | GOLI_HUMAN | |
|---|---|---|
| UniProt AC | Q86XS8 | |
| Protein Name | E3 ubiquitin-protein ligase RNF130 | |
| Gene Name | RNF130 {ECO:0000312|EMBL:AAH17100.2} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 419 | |
| Subcellular Localization |
Membrane Single-pass type I membrane protein . Cytoplasm . |
|
| Protein Description | May have a role during the programmed cell death of hematopoietic cells (By similarity). Acts as an E3 ubiquitin-protein ligase.. | |
| Protein Sequence | MSCAGRAGPARLAALALLTCSLWPARADNASQEYYTALINVTVQEPGRGAPLTFRIDRGRYGLDSPKAEVRGQVLAPLPLHGVADHLGCDPQTRFFVPPNIKQWIALLQRGNCTFKEKISRAAFHNAVAVVIYNNKSKEEPVTMTHPGTGDIIAVMITELRGKDILSYLEKNISVQMTIAVGTRMPPKNFSRGSLVFVSISFIVLMIISSAWLIFYFIQKIRYTNARDRNQRRLGDAAKKAISKLTTRTVKKGDKETDPDFDHCAVCIESYKQNDVVRILPCKHVFHKSCVDPWLSEHCTCPMCKLNILKALGIVPNLPCTDNVAFDMERLTRTQAVNRRSALGDLAGDNSLGLEPLRTSGISPLPQDGELTPRTGEINIAVTKEWFIIASFGLLSALTLCYMIIRATASLNANEVEWF | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 29 | N-linked_Glycosylation | LWPARADNASQEYYT CCCCCCCCCCHHHEE | 40.27 | UniProtKB CARBOHYD | |
| 31 | Phosphorylation | PARADNASQEYYTAL CCCCCCCCHHHEEEE | 29.78 | 22210691 | |
| 34 | Phosphorylation | ADNASQEYYTALINV CCCCCHHHEEEEEEE | 9.85 | 22210691 | |
| 35 | Phosphorylation | DNASQEYYTALINVT CCCCHHHEEEEEEEE | 5.70 | 22210691 | |
| 40 | N-linked_Glycosylation | EYYTALINVTVQEPG HHEEEEEEEEECCCC | 25.02 | 19159218 | |
| 53 | Phosphorylation | PGRGAPLTFRIDRGR CCCCCCEEEEECCCC | 15.14 | 23612710 | |
| 112 | N-linked_Glycosylation | IALLQRGNCTFKEKI HHHHHCCCCCHHHHH | 24.68 | UniProtKB CARBOHYD | |
| 135 | N-linked_Glycosylation | VAVVIYNNKSKEEPV EEEEEECCCCCCCCE | 32.76 | UniProtKB CARBOHYD | |
| 172 | N-linked_Glycosylation | ILSYLEKNISVQMTI HHHHHHHCCEEEEEE | 23.53 | UniProtKB CARBOHYD | |
| 174 | Phosphorylation | SYLEKNISVQMTIAV HHHHHCCEEEEEEEE | 18.72 | 23612710 | |
| 189 | N-linked_Glycosylation | GTRMPPKNFSRGSLV CCCCCCCCCCCCCCE | 45.99 | UniProtKB CARBOHYD | |
| 209 | Phosphorylation | FIVLMIISSAWLIFY HHHHHHHHHHHHHHH | 11.77 | - | |
| 210 | Phosphorylation | IVLMIISSAWLIFYF HHHHHHHHHHHHHHH | 17.04 | - | |
| 216 | Phosphorylation | SSAWLIFYFIQKIRY HHHHHHHHHHHHHCC | 7.87 | - | |
| 243 | Phosphorylation | DAAKKAISKLTTRTV HHHHHHHHHHHHCCC | 26.86 | 29396449 | |
| 244 | Ubiquitination | AAKKAISKLTTRTVK HHHHHHHHHHHCCCC | 43.68 | - | |
| 283 | Ubiquitination | VVRILPCKHVFHKSC EEEEEECCCEECHHH | 40.64 | - | |
| 305 | Ubiquitination | HCTCPMCKLNILKAL HCCCCHHHHHHHHHC | 38.01 | - | |
| 310 | Ubiquitination | MCKLNILKALGIVPN HHHHHHHHHCCCCCC | 37.46 | - | |
| 341 | Phosphorylation | TQAVNRRSALGDLAG HHHHHHHHHHHHHCC | 25.30 | 30266825 | |
| 351 | Phosphorylation | GDLAGDNSLGLEPLR HHHCCCCCCCCCCCC | 28.67 | 26074081 | |
| 359 | Phosphorylation | LGLEPLRTSGISPLP CCCCCCCCCCCCCCC | 38.70 | 19690332 | |
| 360 | Phosphorylation | GLEPLRTSGISPLPQ CCCCCCCCCCCCCCC | 27.91 | 19690332 | |
| 363 | Phosphorylation | PLRTSGISPLPQDGE CCCCCCCCCCCCCCC | 24.74 | - | |
| 372 | Phosphorylation | LPQDGELTPRTGEIN CCCCCCCCCCCCEEE | 13.36 | 23401153 |
| 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 GOLI_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GOLI_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 GOLI_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| UBC_HUMAN | UBC | physical | 16549277 | |
| UB2D1_HUMAN | UBE2D1 | physical | 16549277 | |
| UB2D3_HUMAN | UBE2D3 | physical | 16549277 | |
| UB2D2_HUMAN | UBE2D2 | physical | 16549277 | |
| UB2E1_HUMAN | UBE2E1 | physical | 16549277 |
| 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. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-40, AND MASS SPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, AND MASSSPECTROMETRY. | |
