SMIM11 (formerly C21orf51, FAM165B; also called SMIM11A) is a 58-amino-acid protein encoded on chromosome 21. It has a single predicted helical transmembrane segment near the N terminus (residues 10-32), followed by a lysine-rich segment predicted to form a coiled coil (residues 29-58). On this basis it is predicted to be a single-pass membrane protein with a short charged cytoplasmic or luminal tail. Its membrane, topology and oligomeric state have not been determined experimentally. The transcript is broadly expressed across tissues. Its only reported partners come from a proteome-scale yeast two-hybrid screen: the ER-membrane ceramide synthase CERS4, an isoform of aspartyl/asparaginyl beta-hydroxylase (ASPH), and the cytosolic ubiquilin UBQLN2. No molecular function, biological process or loss-of-function phenotype has been reported.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: HuRI yeast two-hybrid interaction between SMIM11 and an isoform of ASPH. Reason: Single high-throughput Y2H hit with no follow-up. Bare protein binding is uninformative and no specific molecular function can be inferred from it. Removal does not imply that the interaction is false. Supporting Evidence: PMID:32296183 the majority of PPIs in HuRI were found in only one screen |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: HuRI yeast two-hybrid interaction between SMIM11 and CERS4, a multi-pass ER-membrane ceramide synthase. Reason: Single high-throughput Y2H hit with no follow-up. There is no evidence that SMIM11 affects ceramide synthesis or CERS4 activity, so neither an enzyme binding nor a regulator term is supported. Bare protein binding is uninformative. Supporting Evidence: PMID:32296183 the majority of PPIs in HuRI were found in only one screen |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: HuRI yeast two-hybrid interaction between SMIM11 and UBQLN2. Reason: Ubiquilins are cytosolic chaperones for exposed transmembrane domains (PMID:27345149). A UBQLN2 hit for a single-pass transmembrane peptide is therefore expected client recognition, not a function of SMIM11. No informative replacement term is supported. Supporting Evidence: PMID:27345149 We show that Ubiquilin family proteins bind transmembrane domains in the cytosol to prevent aggregation |
| GO:0016020 membrane | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular-location mapping to membrane, based on the single predicted helical transmembrane segment (residues 10-32). Reason: Correct but general. No experiment places SMIM11 in a specific membrane, so a more specific term cannot be assigned. Supporting Evidence: file:human/SMIM11/SMIM11-uniprot.txt SUBCELLULAR LOCATION: Membrane |
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Download this section (compressed HTML)Q: Does the lysine-rich coiled-coil after the transmembrane helix of SMIM11 mediate homo-oligomerization, and on which side of the membrane does it lie?
Experiment: Express tagged SMIM11 at endogenous levels and determine its membrane by co-localization with organelle markers and its topology by selective permeabilization or protease protection. Test oligomerization of the coiled-coil by crosslinking or native gel electrophoresis.
Hypothesis: SMIM11 is a single-pass membrane protein of the ER or plasma membrane whose coiled-coil tail faces the cytosol.
Type: localization and topology mapping
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