Scj1p YMR214W
fungal protein found in Saccharomyces cerevisiae S288c
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Scj1p YMR214W
Summary
Scj1p YMR214W is a protein[1].
Key Facts
- Scj1p YMR214W's instance of is recorded as protein[2].
- Scj1p YMR214W's subclass of is recorded as protein[3].
- Scj1p YMR214W's UniProt protein ID is recorded as P25303[4].
- Scj1p YMR214W's part of is recorded as HSP40/DnaJ peptide-binding[5].
- Scj1p YMR214W's part of is recorded as Chaperone J-domain superfamily[6].
- Scj1p YMR214W's part of is recorded as Heat shock protein DnaJ, cysteine-rich domain superfamily[7].
- Scj1p YMR214W's part of is recorded as Chaperone DnaJ, C-terminal domain, protein family[8].
- Scj1p YMR214W's part of is recorded as Heat shock protein DnaJ, cysteine-rich domain, protein family[9].
- Scj1p YMR214W's part of is recorded as DnaJ domain, protein family[10].
- Scj1p YMR214W's part of is recorded as DnaJ domain, conserved site, protein family[11].
- Scj1p YMR214W's has part is recorded as DnaJ domain, conserved site[12].
- Scj1p YMR214W's has part is recorded as Chaperone DnaJ, C-terminal[13].
- Scj1p YMR214W's has part is recorded as DnaJ domain[14].
- Scj1p YMR214W's has part is recorded as Heat shock protein DnaJ, cysteine-rich domain[15].
- Scj1p YMR214W's RefSeq protein ID is recorded as NP_013941[16].
- Scj1p YMR214W's molecular function is recorded as metal ion binding[17].
- Scj1p YMR214W's molecular function is recorded as heat shock protein binding[18].
- Scj1p YMR214W's molecular function is recorded as chaperone binding[19].
- Scj1p YMR214W's molecular function is recorded as unfolded protein binding[20].
- Scj1p YMR214W's molecular function is recorded as protein binding[21].
- Scj1p YMR214W's cell component is recorded as endoplasmic reticulum lumen[22].
- Scj1p YMR214W's cell component is recorded as endoplasmic reticulum[23].
- Scj1p YMR214W's cell component is recorded as endoplasmic reticulum[24].
- Scj1p YMR214W's biological process is recorded as protein transport[25].
- Scj1p YMR214W's biological process is recorded as protein folding[26].