Sec17p YBL050W
fungal protein found in Saccharomyces cerevisiae S288c
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Sec17p YBL050W
Summary
Sec17p YBL050W is a protein[1].
Key Facts
- Sec17p YBL050W's instance of is recorded as protein[2].
- Sec17p YBL050W's UniProt protein ID is recorded as P32602[3].
- Sec17p YBL050W's part of is recorded as Tetratricopeptide-like helical domain superfamily[4].
- Sec17p YBL050W's part of is recorded as soluble NSF attachment protein[5].
- Sec17p YBL050W's part of is recorded as synaptosomal vesicle fusion pore[6].
- Sec17p YBL050W's part of is recorded as membrane protein[7].
- Sec17p YBL050W's RefSeq protein ID is recorded as NP_009503[8].
- Sec17p YBL050W's molecular function is recorded as ATPase activator activity[9].
- Sec17p YBL050W's molecular function is recorded as soluble NSF attachment protein activity[10].
- Sec17p YBL050W's molecular function is recorded as syntaxin binding[11].
- Sec17p YBL050W's molecular function is recorded as soluble NSF attachment protein activity[12].
- Sec17p YBL050W's cell component is recorded as membrane[13].
- Sec17p YBL050W's cell component is recorded as cytosol[14].
- Sec17p YBL050W's cell component is recorded as extrinsic component of membrane[15].
- Sec17p YBL050W's cell component is recorded as SNARE complex[16].
- Sec17p YBL050W's cell component is recorded as vacuolar membrane[17].
- Sec17p YBL050W's cell component is recorded as SNARE complex[18].
- Sec17p YBL050W's cell component is recorded as fungal-type vacuole membrane[19].
- Sec17p YBL050W's biological process is recorded as autophagy[20].
- Sec17p YBL050W's biological process is recorded as vacuole fusion, non-autophagic[21].
- Sec17p YBL050W's biological process is recorded as vesicle-mediated transport[22].
- Sec17p YBL050W's biological process is recorded as vesicle fusion with Golgi apparatus[23].
- Sec17p YBL050W's biological process is recorded as protein transport[24].
- Sec17p YBL050W's biological process is recorded as SNARE complex disassembly[25].
- Sec17p YBL050W's biological process is recorded as positive regulation of ATP-dependent activity[26].