| UniProt ID | RB22A_HUMAN | |
|---|---|---|
| UniProt AC | Q9UL26 | |
| Protein Name | Ras-related protein Rab-22A | |
| Gene Name | RAB22A | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 194 | |
| Subcellular Localization |
Endosome membrane Lipid-anchor . Cell membrane Lipid-anchor . Early endosome . Late endosome . Cell projection, ruffle . Cytoplasmic vesicle . Cytoplasmic vesicle, phagosome . Cytoplasmic vesicle, phagosome membrane Lipid-anchor Cytoplasmic side . |
|
| Protein Description | Plays a role in endocytosis and intracellular protein transport. Mediates trafficking of TF from early endosomes to recycling endosomes. [PubMed: 16537905 Required for NGF-mediated endocytosis of NTRK1, and subsequent neurite outgrowth] | |
| Protein Sequence | MALRELKVCLLGDTGVGKSSIVWRFVEDSFDPNINPTIGASFMTKTVQYQNELHKFLIWDTAGQERFRALAPMYYRGSAAAIIVYDITKEETFSTLKNWVKELRQHGPPNIVVAIAGNKCDLIDVREVMERDAKDYADSIHAIFVETSAKNAININELFIEISRRIPSTDANLPSGGKGFKLRRQPSEPKRSCC | |
| 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 |
|---|---|---|---|---|---|
| 7 | Ubiquitination | -MALRELKVCLLGDT -CCCCCEEEEEECCC | 26.58 | - | |
| 14 | Phosphorylation | KVCLLGDTGVGKSSI EEEEECCCCCCCHHH | 31.78 | - | |
| 19 | Phosphorylation | GDTGVGKSSIVWRFV CCCCCCCHHHHHHHH | 21.26 | - | |
| 20 | Phosphorylation | DTGVGKSSIVWRFVE CCCCCCHHHHHHHHC | 25.33 | - | |
| 94 | Phosphorylation | ITKEETFSTLKNWVK CCCHHHHHHHHHHHH | 40.00 | 22210691 | |
| 95 | Phosphorylation | TKEETFSTLKNWVKE CCHHHHHHHHHHHHH | 37.24 | 22210691 | |
| 101 | Acetylation | STLKNWVKELRQHGP HHHHHHHHHHHHHCC | 42.52 | - | |
| 101 | Ubiquitination | STLKNWVKELRQHGP HHHHHHHHHHHHHCC | 42.52 | - | |
| 147 | Phosphorylation | IHAIFVETSAKNAIN EEEEEEECCCCCCCC | 28.78 | 27251275 | |
| 148 | Phosphorylation | HAIFVETSAKNAINI EEEEEECCCCCCCCH | 24.60 | 27251275 | |
| 163 | Phosphorylation | NELFIEISRRIPSTD HHHHHHHHCCCCCCC | 11.61 | 27251275 | |
| 175 | Phosphorylation | STDANLPSGGKGFKL CCCCCCCCCCCCCCC | 64.44 | 21815630 | |
| 178 | Ubiquitination | ANLPSGGKGFKLRRQ CCCCCCCCCCCCCCC | 65.78 | 33845483 | |
| 181 | Ubiquitination | PSGGKGFKLRRQPSE CCCCCCCCCCCCCCC | 50.15 | - | |
| 187 | Phosphorylation | FKLRRQPSEPKRSCC CCCCCCCCCCCCCCC | 59.18 | 29691806 | |
| 190 | Ubiquitination | RRQPSEPKRSCC--- CCCCCCCCCCCC--- | 53.55 | 24816145 | |
| 193 | Geranylgeranylation | PSEPKRSCC------ CCCCCCCCC------ | 3.56 | - | |
| 194 | Geranylgeranylation | SEPKRSCC------- CCCCCCCC------- | 7.05 | - |
| 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 RB22A_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RB22A_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 RB22A_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| EEA1_HUMAN | EEA1 | physical | 11870209 | |
| RABX5_HUMAN | RABGEF1 | physical | 19759177 | |
| RAB5A_HUMAN | RAB5A | physical | 19759177 |
| 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...
| Acetylation | |
| Reference | PubMed |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-101, AND MASS SPECTROMETRY. | |