Heat shock protein 1 (chaperonin)
mammalian protein found in Mus musculus
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Heat shock protein 1 (chaperonin)
Summary
Heat shock protein 1 (chaperonin) is a protein[1].
Key Facts
- Heat shock protein 1 (chaperonin)'s instance of is recorded as protein[2].
- Heat shock protein 1 (chaperonin)'s UniProt protein ID is recorded as P63038[3].
- Heat shock protein 1 (chaperonin)'s part of is recorded as Chaperonin Cpn60[4].
- Heat shock protein 1 (chaperonin)'s part of is recorded as GroEL-like apical domain superfamily[5].
- Heat shock protein 1 (chaperonin)'s part of is recorded as GroEL-like equatorial domain superfamily[6].
- Heat shock protein 1 (chaperonin)'s part of is recorded as TCP-1-like chaperonin intermediate domain superfamily[7].
- Heat shock protein 1 (chaperonin)'s part of is recorded as membrane protein[8].
- Heat shock protein 1 (chaperonin)'s part of is recorded as Chaperonin Cpn60, conserved site, protein family[9].
- Heat shock protein 1 (chaperonin)'s has part is recorded as Chaperonin Cpn60, conserved site[10].
- Heat shock protein 1 (chaperonin)'s RefSeq protein ID is recorded as NP_034607[11].
- Heat shock protein 1 (chaperonin)'s RefSeq protein ID is recorded as NP_001343441[12].
- Heat shock protein 1 (chaperonin)'s molecular function is recorded as nucleotide binding[13].
- Heat shock protein 1 (chaperonin)'s molecular function is recorded as ATP binding[14].
- Heat shock protein 1 (chaperonin)'s molecular function is recorded as protease binding[15].
- Heat shock protein 1 (chaperonin)'s molecular function is recorded as insulin binding[16].
- Heat shock protein 1 (chaperonin)'s molecular function is recorded as protein heterodimerization activity[17].
- Heat shock protein 1 (chaperonin)'s molecular function is recorded as hydrolase activity[18].
- Heat shock protein 1 (chaperonin)'s molecular function is recorded as protein folding chaperone activity[19].
- Heat shock protein 1 (chaperonin)'s molecular function is recorded as unfolded protein binding[20].
- Heat shock protein 1 (chaperonin)'s molecular function is recorded as lipopolysaccharide binding[21].
- Heat shock protein 1 (chaperonin)'s molecular function is recorded as p53 binding[22].
- Heat shock protein 1 (chaperonin)'s molecular function is recorded as double-stranded RNA binding[23].
- Heat shock protein 1 (chaperonin)'s molecular function is recorded as high-density lipoprotein particle binding[24].
- Heat shock protein 1 (chaperonin)'s molecular function is recorded as enzyme binding[25].
- Heat shock protein 1 (chaperonin)'s molecular function is recorded as ubiquitin protein ligase binding[26].