| UniProt ID | RN170_HUMAN | |
|---|---|---|
| UniProt AC | Q96K19 | |
| Protein Name | E3 ubiquitin-protein ligase RNF170 | |
| Gene Name | RNF170 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 258 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . |
|
| Protein Description | E3 ubiquitin-protein ligase that plays an essential role in stimulus-induced inositol 1,4,5-trisphosphate receptor type 1 (ITPR1) ubiquitination and degradation via the endoplasmic reticulum-associated degradation (ERAD) pathway. Also involved in ITPR1 turnover in resting cells.. | |
| Protein Sequence | MAKYQGEVQSLKLDDDSVIEGVSDQVLVAVVVSFALIATLVYALFRNVHQNIHPENQELVRVLREQLQTEQDAPAATRQQFYTDMYCPICLHQASFPVETNCGHLFCGACIIAYWRYGSWLGAISCPICRQTVTLLLTVFGEDDQSQDVLRLHQDINDYNRRFSGQPRSIMERIMDLPTLLRHAFREMFSVGGLFWMFRIRIILCLMGAFFYLISPLDFVPEALFGILGFLDDFFVIFLLLIYISIMYREVITQRLTR | |
| 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 |
|---|---|---|---|---|---|
| 3 (in isoform 5) | Ubiquitination | - | 36.49 | 21890473 | |
| 3 | Ubiquitination | -----MAKYQGEVQS -----CCCCCCCCEE | 36.49 | 23000965 | |
| 3 (in isoform 1) | Ubiquitination | - | 36.49 | 21890473 | |
| 3 (in isoform 2) | Ubiquitination | - | 36.49 | 21890473 | |
| 3 (in isoform 3) | Ubiquitination | - | 36.49 | 21890473 | |
| 8 (in isoform 4) | Phosphorylation | - | 6.31 | 21060948 | |
| 10 | Phosphorylation | KYQGEVQSLKLDDDS CCCCCCEECCCCCCH | 32.42 | 27251275 | |
| 13 (in isoform 4) | Phosphorylation | - | 12.08 | 21060948 | |
| 15 (in isoform 4) | Phosphorylation | - | 61.59 | 21060948 | |
| 18 (in isoform 4) | Phosphorylation | - | 6.25 | 21060948 | |
| 21 (in isoform 4) | Phosphorylation | - | 17.07 | 21060948 | |
| 25 (in isoform 4) | Phosphorylation | - | 23.96 | 21060948 | |
| 119 | Phosphorylation | IAYWRYGSWLGAISC HHHHHHHCHHHHHCC | 15.36 | 28857561 | |
| 134 (in isoform 3) | Phosphorylation | - | 18.31 | - | |
| 169 | Phosphorylation | RFSGQPRSIMERIMD HHCCCCCHHHHHHHH | 32.73 | 22210691 | |
| 179 | Phosphorylation | ERIMDLPTLLRHAFR HHHHHHHHHHHHHHH | 45.80 | 28555341 | |
| 224 (in isoform 2) | Phosphorylation | - | 3.73 | 28787133 |
| 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 RN170_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RN170_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 RN170_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| RN170_HUMAN | RNF170 | physical | 25882839 | |
| UB2D2_HUMAN | UBE2D2 | physical | 25882839 | |
| RDH14_HUMAN | RDH14 | physical | 28514442 | |
| ERLN1_HUMAN | ERLIN1 | physical | 28514442 | |
| ST7L_HUMAN | ST7L | physical | 28514442 | |
| ERLN2_HUMAN | ERLIN2 | physical | 28514442 | |
| ABCBA_HUMAN | ABCB10 | physical | 28514442 | |
| TYW1_HUMAN | TYW1 | physical | 28514442 | |
| ASPH2_HUMAN | ASPHD2 | physical | 28514442 | |
| AT132_HUMAN | ATP13A2 | physical | 28514442 | |
| PDE3B_HUMAN | PDE3B | physical | 28514442 | |
| BI1_HUMAN | TMBIM6 | physical | 28514442 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 608984 | Ataxia, sensory, 1, autosomal dominant (SNAX1) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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