Crystallin, alpha B
mammalian protein found in Mus musculus
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Crystallin, alpha B
Summary
Crystallin, alpha B is a protein[1].
Key Facts
- Crystallin, alpha B's instance of is recorded as protein[2].
- Crystallin, alpha B's subclass of is recorded as protein[3].
- Crystallin, alpha B's UniProt protein ID is recorded as P23927[4].
- Crystallin, alpha B's part of is recorded as HSP20-like chaperone[5].
- Crystallin, alpha B's part of is recorded as Alpha crystallin/Heat shock protein[6].
- Crystallin, alpha B's part of is recorded as Alpha-crystallin, N-terminal domain, protein family[7].
- Crystallin, alpha B's part of is recorded as Alpha crystallin/Hsp20 domain, protein family[8].
- Crystallin, alpha B's part of is recorded as Alpha-crystallin B chain, ACD domain, protein family[9].
- Crystallin, alpha B's has part is recorded as Alpha crystallin/Hsp20 domain[10].
- Crystallin, alpha B's has part is recorded as Alpha-crystallin, N-terminal[11].
- Crystallin, alpha B's has part is recorded as Alpha-crystallin B chain, ACD domain[12].
- Crystallin, alpha B's RefSeq protein ID is recorded as NP_001276711[13].
- Crystallin, alpha B's RefSeq protein ID is recorded as NP_001276713[14].
- Crystallin, alpha B's RefSeq protein ID is recorded as NP_001276714[15].
- Crystallin, alpha B's RefSeq protein ID is recorded as NP_034094[16].
- Crystallin, alpha B's RefSeq protein ID is recorded as XP_030099896[17].
- Crystallin, alpha B's RefSeq protein ID is recorded as XP_036010485[18].
- Crystallin, alpha B's molecular function is recorded as metal ion binding[19].
- Crystallin, alpha B's molecular function is recorded as protein binding[20].
- Crystallin, alpha B's molecular function is recorded as structural constituent of eye lens[21].
- Crystallin, alpha B's molecular function is recorded as identical protein binding[22].
- Crystallin, alpha B's molecular function is recorded as protein homodimerization activity[23].
- Crystallin, alpha B's molecular function is recorded as unfolded protein binding[24].
- Crystallin, alpha B's molecular function is recorded as amyloid-beta binding[25].
- Crystallin, alpha B's molecular function is recorded as protein-containing complex binding[26].