| UniProt ID | RILP_HUMAN | |
|---|---|---|
| UniProt AC | Q96NA2 | |
| Protein Name | Rab-interacting lysosomal protein | |
| Gene Name | RILP | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 401 | |
| Subcellular Localization | Late endosome membrane . Lysosome membrane . Cytoplasmic vesicle, phagosome membrane . Associated with late endosomal, lysosomal and phagosomal membranes. The interaction with RAB7A is necessary for its recruitment to phagosomes. | |
| Protein Description | Rab effector playing a role in late endocytic transport to degradative compartments. Involved in the regulation of lysosomal morphology and distribution. Induces recruitment of dynein-dynactin motor complexes to Rab7A-containing late endosome and lysosome compartments. Promotes centripetal migration of phagosomes and the fusion of phagosomes with the late endosomes and lysosomes.. | |
| Protein Sequence | MEPRRAAPGVPGWGSREAAGSASAAELVYHLAGALGTELQDLARRFGPEAAAGLVPLVVRALELLEQAAVGPAPDSLQVSAQPAEQELRRLREENERLRRELRAGPQEERALLRQLKEVTDRQRDELRAHNRDLRQRGQETEALQEQLQRLLLVNAELRHKLAAMQTQLRAAQDRERERQQPGEAATPQAKERARGQAGRPGHQHGQEPEWATAGAGAPGNPEDPAEAAQQLGRPSEAGQCRFSREEFEQILQERNELKAKVFLLKEELAYFQRELLTDHRVPGLLLEAMKVAVRKQRKKIKAKMLGTPEEAESSEDEAGPWILLSDDKGDHPPPPESKIQSFFGLWYRGKAESSEDETSSPAPSKLGGEEEAQPQSPAPDPPCSALHEHLCLGASAAPEA | |
| 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 |
|---|---|---|---|---|---|
| 187 | Phosphorylation | QQPGEAATPQAKERA CCCCCCCCHHHHHHH | 24.00 | 25262027 | |
| 308 | Phosphorylation | IKAKMLGTPEEAESS HHHHHCCCHHHHHCC | 24.46 | 20068231 | |
| 314 | Phosphorylation | GTPEEAESSEDEAGP CCHHHHHCCCCCCCC | 46.18 | 25159151 | |
| 315 | Phosphorylation | TPEEAESSEDEAGPW CHHHHHCCCCCCCCE | 40.34 | 15933719 | |
| 326 | Phosphorylation | AGPWILLSDDKGDHP CCCEEEEECCCCCCC | 40.08 | 20068231 | |
| 338 | Phosphorylation | DHPPPPESKIQSFFG CCCCCCHHHHHHHHH | 40.61 | 20068231 | |
| 354 | Phosphorylation | WYRGKAESSEDETSS HHCCCCCCCCCCCCC | 43.84 | 25159151 | |
| 355 | Phosphorylation | YRGKAESSEDETSSP HCCCCCCCCCCCCCC | 40.34 | 25159151 | |
| 359 | Phosphorylation | AESSEDETSSPAPSK CCCCCCCCCCCCCHH | 46.99 | 29396449 | |
| 360 | Phosphorylation | ESSEDETSSPAPSKL CCCCCCCCCCCCHHC | 32.07 | 29396449 | |
| 361 | Phosphorylation | SSEDETSSPAPSKLG CCCCCCCCCCCHHCC | 32.28 | 25627689 | |
| 365 | Phosphorylation | ETSSPAPSKLGGEEE CCCCCCCHHCCCCCC | 42.49 | - | |
| 377 | Phosphorylation | EEEAQPQSPAPDPPC CCCCCCCCCCCCCCC | 29.70 | 30576142 |
| 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 RILP_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RILP_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 RILP_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| RAB7A_HUMAN | RAB7A | physical | 11448994 | |
| VPS36_HUMAN | VPS36 | physical | 17010938 | |
| SNF8_HUMAN | SNF8 | physical | 17010938 | |
| RAB7A_HUMAN | RAB7A | physical | 18552835 | |
| RAB7B_HUMAN | RAB7B | physical | 18552835 | |
| VPS11_HUMAN | VPS11 | physical | 25445562 | |
| VPS16_HUMAN | VPS16 | physical | 25445562 | |
| VPS18_HUMAN | VPS18 | physical | 25445562 | |
| VPS39_HUMAN | VPS39 | physical | 25445562 | |
| VPS41_HUMAN | VPS41 | physical | 25445562 | |
| RAB7A_HUMAN | RAB7A | physical | 25445562 | |
| RAB7A_HUMAN | RAB7A | physical | 26911690 | |
| RAB7A_HUMAN | RAB7A | physical | 25080504 |
| 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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| Phosphorylation | |
| Reference | PubMed |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314 AND SER-315, ANDMASS SPECTROMETRY. | |