Cyclin L1a
protein found in Danio rerio
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Cyclin L1a
Summary
Cyclin L1a is a protein[1].
Key Facts
- Cyclin L1a's instance of is recorded as protein[2].
- Cyclin L1a's UniProt protein ID is recorded as A4QP43[3].
- Cyclin L1a's part of is recorded as Cyclin-like superfamily[4].
- Cyclin L1a's part of is recorded as Cyclin L1[5].
- Cyclin L1a's part of is recorded as Cyclin-like, protein family[6].
- Cyclin L1a's part of is recorded as Cyclin, N-terminal domain, protein family[7].
- Cyclin L1a's part of is recorded as Cyclin, C-terminal domain, protein family[8].
- Cyclin L1a's has part is recorded as Cyclin-like[9].
- Cyclin L1a's has part is recorded as Cyclin, C-terminal domain[10].
- Cyclin L1a's has part is recorded as Cyclin, N-terminal[11].
- Cyclin L1a's RefSeq protein ID is recorded as NP_001082832[12].
- Cyclin L1a's RefSeq protein ID is recorded as XP_005159279[13].
- Cyclin L1a's RefSeq protein ID is recorded as XP_005159280[14].
- Cyclin L1a's RefSeq protein ID is recorded as XP_005159281[15].
- Cyclin L1a's RefSeq protein ID is recorded as XP_009292089[16].
- Cyclin L1a's molecular function is recorded as cyclin-dependent protein serine/threonine kinase regulator activity[17].
- Cyclin L1a's cell component is recorded as nucleus[18].
- Cyclin L1a's cell component is recorded as cyclin-dependent protein kinase holoenzyme complex[19].
- Cyclin L1a's cell component is recorded as nucleus[20].
- Cyclin L1a's biological process is recorded as regulation of cyclin-dependent protein serine/threonine kinase activity[21].
- Cyclin L1a's biological process is recorded as regulation of transcription, DNA-templated[22].
- Cyclin L1a's biological process is recorded as RNA processing[23].
- Cyclin L1a's biological process is recorded as positive regulation of cyclin-dependent protein serine/threonine kinase activity[24].
- Cyclin L1a's biological process is recorded as positive regulation of transcription by RNA polymerase II[25].
- Cyclin L1a's biological process is recorded as positive regulation of phosphorylation of RNA polymerase II C-terminal domain[26].