| UniProt ID | VAMP4_HUMAN | |
|---|---|---|
| UniProt AC | O75379 | |
| Protein Name | Vesicle-associated membrane protein 4 | |
| Gene Name | VAMP4 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 141 | |
| Subcellular Localization |
Golgi apparatus, trans-Golgi network membrane Single-pass type IV membrane protein . Associated with trans Golgi network (TGN) and newly formed immature secretory granules (ISG). Not found on the mature secretory organelles. |
|
| Protein Description | Involved in the pathway that functions to remove an inhibitor (probably synaptotagmin-4) of calcium-triggered exocytosis during the maturation of secretory granules. May be a marker for this sorting pathway that is critical for remodeling the secretory response of granule.. | |
| Protein Sequence | MPPKFKRHLNDDDVTGSVKSERRNLLEDDSDEEEDFFLRGPSGPRFGPRNDKIKHVQNQVDEVIDVMQENITKVIERGERLDELQDKSESLSDNATAFSNRSKQLRRQMWWRGCKIKAIMALVAAILLLVIIILIVMKYRT | |
| 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 |
|---|---|---|---|---|---|
| 4 (in isoform 2) | Ubiquitination | - | 58.61 | - | |
| 15 | Phosphorylation | HLNDDDVTGSVKSER CCCCCCCCCCHHHHH | 30.63 | 30108239 | |
| 17 | Phosphorylation | NDDDVTGSVKSERRN CCCCCCCCHHHHHHH | 19.60 | 23401153 | |
| 19 | Ubiquitination | DDVTGSVKSERRNLL CCCCCCHHHHHHHCC | 48.58 | - | |
| 19 (in isoform 2) | Ubiquitination | - | 48.58 | - | |
| 20 | Phosphorylation | DVTGSVKSERRNLLE CCCCCHHHHHHHCCC | 33.89 | 29255136 | |
| 30 | Phosphorylation | RNLLEDDSDEEEDFF HHCCCCCCCCCCCCC | 60.28 | 19664994 | |
| 30 (in isoform 2) | Phosphorylation | - | 60.28 | 27732954 | |
| 42 | Phosphorylation | DFFLRGPSGPRFGPR CCCCCCCCCCCCCCC | 65.34 | 23403867 | |
| 73 | Ubiquitination | VMQENITKVIERGER HHHHHHHHHHHHHHH | 37.10 | - | |
| 86 (in isoform 2) | Ubiquitination | - | 69.90 | - | |
| 87 | Ubiquitination | RLDELQDKSESLSDN HHHHHHHHHHHCHHH | 43.07 | - | |
| 88 | Phosphorylation | LDELQDKSESLSDNA HHHHHHHHHHCHHHH | 40.48 | 23401153 | |
| 90 | Phosphorylation | ELQDKSESLSDNATA HHHHHHHHCHHHHHH | 40.02 | 29255136 | |
| 92 | Phosphorylation | QDKSESLSDNATAFS HHHHHHCHHHHHHHH | 37.79 | 25159151 | |
| 96 | Phosphorylation | ESLSDNATAFSNRSK HHCHHHHHHHHHHHH | 34.19 | 27732954 | |
| 99 | Phosphorylation | SDNATAFSNRSKQLR HHHHHHHHHHHHHHH | 28.95 | 27732954 | |
| 114 (in isoform 2) | Ubiquitination | - | 2.86 | - | |
| 115 | Ubiquitination | QMWWRGCKIKAIMAL HHHHHHHHHHHHHHH | 50.49 | - | |
| 116 (in isoform 2) | Ubiquitination | - | 4.19 | - | |
| 117 | Ubiquitination | WWRGCKIKAIMALVA HHHHHHHHHHHHHHH | 19.84 | - | |
| 137 (in isoform 2) | Ubiquitination | - | 2.21 | - | |
| 138 | Ubiquitination | IIILIVMKYRT---- HHHHHHHHHCC---- | 22.23 | - | |
| 139 | Phosphorylation | IILIVMKYRT----- HHHHHHHHCC----- | 11.03 | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 30 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 30 | S | Phosphorylation | Kinase | CK2_GROUP | - | PhosphoELM |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VAMP4_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 VAMP4_HUMAN !! | ||||||
| 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 |
| "Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASSSPECTROMETRY. | |
| "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-30, AND MASSSPECTROMETRY. | |
| "Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASSSPECTROMETRY. | |
| "Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASSSPECTROMETRY. | |
