Protein Name:
Testis-expressed protein 264
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UniprotKB/SwissProt ID: Q9Y6I9 (Q9Y6I9)
Gene Name:
TEX264
Organism: Homo sapiens (Human)
Function: Major reticulophagy (also called ER-phagy) receptor that acts independently of other candidate reticulophagy receptors to remodel subdomains of the endoplasmic reticulum into autophagosomes upon nutrient stress, which then fuse with lysosomes for endoplasmic reticulum turnover (PubMed:31006537, PubMed:31006538). The ATG8-containing isolation membrane (IM) cradles a tubular segment of TEX264-positive ER near a three-way junction, allowing the formation of a synapse of 2 juxtaposed membranes with trans interaction between the TEX264 and ATG8 proteins (PubMed:31006537). Expansion of the IM would extend the capture of ER, possibly through a 'zipper-like' process involving continued trans TEX264-ATG8 interactions, until poorly understood mechanisms lead to the fission of relevant membranes and, ultimately, autophagosomal membrane closure (PubMed:31006537). Also involved in the repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis: acts by bridging VCP/p97 to covalent DNA-protein cross-links (DPCs) and initiating resolution of DPCs by SPRTN (PubMed:32152270)
Other Modifications: View all modification sites in dbPTM
Protein Subcellular Localization: Endoplasmic reticulum membrane. Cytoplasmic vesicle, autophagosome. Cytoplasm, cytosol. Nucleus. Chromosome
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Graphical Visualization of S-nitrosylation Sites:
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| InterPro ID |
Domain Name |
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IPR011256
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Reg_factor_effector_dom_sf |
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The S-nitrosylation sites of Q9Y6I9
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| No. |
Position |
S-nitrosylated Peptide |
Secondary Structure of S-nitrosylated Peptide |
Solvent Accessibility of nitrosylated Site |
PubMed ID |
| 1 |
182 |
IYQEDQIHFM C PLARQGDFYV |
CCHHHHHHHH H HHHHHHHHHH |
2.14% |
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| 2 |
68 |
GETGRLFTES C SISPKLRSIA |
CCHHHHHHHH H HHHHHHHHHH |
3.22% |
19483679
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| 3 |
94 |
PHMVPPDKCR C AVGSILSEGE |
CCHHHHHHHH H HHHHHHHHHH |
5.15% |
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