| UniProt ID | VP26B_HUMAN | |
|---|---|---|
| UniProt AC | Q4G0F5 | |
| Protein Name | Vacuolar protein sorting-associated protein 26B | |
| Gene Name | VPS26B | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 336 | |
| Subcellular Localization |
Cytoplasm . Membrane Peripheral membrane protein . Early endosome . Late endosome . Localizes to early and late endosomal structures (By similarity). |
|
| Protein Description | Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5. May be involved in retrograde transport of SORT1 but not of IGF2R. Acts redundantly with VSP26A in SNX-27 mediated endocytic recycling of SLC2A1/GLUT1 (By similarity).. | |
| Protein Sequence | MSFFGFGQSVEVEILLNDAESRKRAEHKTEDGKKEKYFLFYDGETVSGKVSLALKNPNKRLEHQGIKIEFIGQIELYYDRGNHHEFVSLVKDLARPGEITQSQAFDFEFTHVEKPYESYTGQNVKLRYFLRATISRRLNDVVKEMDIVVHTLSTYPELNSSIKMEVGIEDCLHIEFEYNKSKYHLKDVIVGKIYFLLVRIKIKHMEIDIIKRETTGTGPNVYHENDTIAKYEIMDGAPVRGESIPIRLFLAGYELTPTMRDINKKFSVRYYLNLVLIDEEERRYFKQQEVVLWRKGDIVRKSMSHQAAIASQRFEGTTSLGEVRTPSQLSDNNCRQ | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSFFGFGQS ------CCCCCCCCE | 29.32 | 24043423 | |
| 9 | Phosphorylation | SFFGFGQSVEVEILL CCCCCCCEEEEEEEE | 22.18 | 24043423 | |
| 21 | Phosphorylation | ILLNDAESRKRAEHK EEECCHHHHHHHCCC | 44.84 | 24043423 | |
| 55 | Ubiquitination | GKVSLALKNPNKRLE EEEEEEECCCCCCCE | 65.83 | - | |
| 186 | 2-Hydroxyisobutyrylation | NKSKYHLKDVIVGKI CCCCCCHHHHHHHHH | 36.32 | - | |
| 186 | Ubiquitination | NKSKYHLKDVIVGKI CCCCCCHHHHHHHHH | 36.32 | - | |
| 203 | Acetylation | LLVRIKIKHMEIDII HHHHHCCCCCEEEEE | 31.71 | 11925337 | |
| 211 | Ubiquitination | HMEIDIIKRETTGTG CCEEEEEEEECCCCC | 44.51 | - | |
| 231 | Phosphorylation | ENDTIAKYEIMDGAP CCCCEEEEEEECCCC | 11.15 | 25954137 | |
| 243 | Phosphorylation | GAPVRGESIPIRLFL CCCCCCCCCCEEEEE | 36.17 | 24719451 | |
| 258 | Phosphorylation | AGYELTPTMRDINKK CCEECCCCHHHHHHH | 21.43 | - | |
| 301 | Ubiquitination | RKGDIVRKSMSHQAA ECCHHHHHHHCHHHH | 39.35 | - | |
| 302 | Phosphorylation | KGDIVRKSMSHQAAI CCHHHHHHHCHHHHH | 18.23 | 30266825 | |
| 303 | Sulfoxidation | GDIVRKSMSHQAAIA CHHHHHHHCHHHHHH | 4.68 | 30846556 | |
| 304 | Phosphorylation | DIVRKSMSHQAAIAS HHHHHHHCHHHHHHH | 21.38 | 23927012 | |
| 311 | Phosphorylation | SHQAAIASQRFEGTT CHHHHHHHHCCCCCC | 18.77 | 17525332 | |
| 317 | Phosphorylation | ASQRFEGTTSLGEVR HHHCCCCCCCCCEEC | 13.15 | 29255136 | |
| 318 | Phosphorylation | SQRFEGTTSLGEVRT HHCCCCCCCCCEECC | 32.58 | 29255136 | |
| 319 | Phosphorylation | QRFEGTTSLGEVRTP HCCCCCCCCCEECCH | 33.93 | 23401153 | |
| 325 | Phosphorylation | TSLGEVRTPSQLSDN CCCCEECCHHHCCCC | 32.25 | 29255136 | |
| 327 | Phosphorylation | LGEVRTPSQLSDNNC CCEECCHHHCCCCCC | 43.04 | 29255136 | |
| 330 | Phosphorylation | VRTPSQLSDNNCRQ- ECCHHHCCCCCCCC- | 30.56 | 19413330 |
| 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 VP26B_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of VP26B_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 VP26B_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 |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-319, ANDMASS SPECTROMETRY. | |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND SER-330, ANDMASS SPECTROMETRY. | |
| "ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311, AND MASSSPECTROMETRY. | |
