| UniProt ID | ARRD4_HUMAN | |
|---|---|---|
| UniProt AC | Q8NCT1 | |
| Protein Name | Arrestin domain-containing protein 4 | |
| Gene Name | ARRDC4 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 418 | |
| Subcellular Localization |
Early endosome . Cell membrane Peripheral membrane protein Cytoplasmic side . Cytoplasmic vesicle . Also found in extracellular vesicles different from exosomes. |
|
| Protein Description | Functions as an adapter recruiting ubiquitin-protein ligases to their specific substrates (By similarity). Plays a role in endocytosis of activated G protein-coupled receptors (GPCRs) (Probable). Through an ubiquitination-dependent mechanism plays also a role in the incorporation of SLC11A2 into extracellular vesicles (By similarity). May play a role in glucose uptake. [PubMed: 19605364] | |
| Protein Sequence | MGGEAGCAAAVGAEGRVKSLGLVFEDERKGCYSSGETVAGHVLLEASEPVALRALRLEAQGRATAAWGPSTCPRASASTAALAVFSEVEYLNVRLSLREPPAGEGIILLQPGKHEFPFRFQLPSEPLVTSFTGKYGSIQYCVRAVLERPKVPDQSVKRELQVVSHVDVNTPALLTPVLKTQEKMVGCWFFTSGPVSLSAKIERKGYCNGEAIPIYAEIENCSSRLIVPKAAIFQTQTYLASGKTKTIRHMVANVRGNHIASGSTDTWNGKTLKIPPVTPSILDCCIIRVDYSLAVYIHIPGAKKLMLELPLVIGTIPYNGFGSRNSSIASQFSMDMSWLTLTLPEQPEAPPNYADVVSEEEFSRHIPPYPQPPNCEGEVCCPVFACIQEFRFQPPPLYSEVDPHPSDVEESQPVSFIL | |
| 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 |
|---|---|---|---|---|---|
| 37 | Phosphorylation | GCYSSGETVAGHVLL CCCCCCCEECCEEEE | 21.12 | 22817900 | |
| 76 | Phosphorylation | PSTCPRASASTAALA CCCCCCCCHHHHHHH | 24.83 | 29116813 | |
| 96 | Phosphorylation | EYLNVRLSLREPPAG EEEEEEEEECCCCCC | 18.15 | 23532336 | |
| 206 | Phosphorylation | AKIERKGYCNGEAIP EEEEECCCCCCCEEC | 5.93 | - | |
| 229 | Ubiquitination | SSRLIVPKAAIFQTQ CCCCEECHHHHEECH | 39.29 | 21890473 | |
| 291 | Phosphorylation | CCIIRVDYSLAVYIH HEEEEECEEEEEEEE | 11.61 | - | |
| 292 | Phosphorylation | CIIRVDYSLAVYIHI EEEEECEEEEEEEEC | 12.85 | - | |
| 296 | Phosphorylation | VDYSLAVYIHIPGAK ECEEEEEEEECCCHH | 4.91 | - | |
| 398 | Phosphorylation | RFQPPPLYSEVDPHP CCCCCCCCCCCCCCC | 14.46 | - |
| 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 ARRD4_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ARRD4_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 ARRD4_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| NED4L_HUMAN | NEDD4L | physical | 23236378 | |
| ITCH_HUMAN | ITCH | physical | 23236378 | |
| WWP2_HUMAN | WWP2 | physical | 23236378 | |
| ARRB1_HUMAN | ARRB1 | physical | 23236378 | |
| ARRB2_HUMAN | ARRB2 | physical | 23236378 | |
| ADRB2_HUMAN | ADRB2 | physical | 21982743 | |
| V2R_HUMAN | AVPR2 | physical | 23236378 |
| 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 |
| "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37, AND MASSSPECTROMETRY. | |