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- Table of Contents
4 Q&As
Facts about Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1.
21). Displays a preference for acidic residues located N-terminally to the proline bond to be isomerized.
Human | |
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Gene Name: | PIN1 |
Uniprot: | Q13526 |
Entrez: | 5300 |
Belongs to: |
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No superfamily |
dod; EC 5.2.1.8; peptidylprolyl cis/trans isomerase, NIMA-interacting 1; peptidyl-prolyl cis/trans isomerase, NIMA-interacting; peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; Peptidyl-prolyl cis-trans isomerase Pin1; Pin1; PPIase Pin1; prolyl isomerase; protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1; protein (peptidylprolyl cis/trans isomerase) NIMA-interacting 1; Rotamase Pin1; UBL5
Mass (kDA):
18.243 kDA
Human | |
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Location: | 19p13.2 |
Sequence: | 19; NC_000019.10 (9835207..9849689) |
The phosphorylated form at Ser-71 is expressed in normal breast tissue cells but not in breast cancer cells.
Nucleus. Nucleus speckle. Cytoplasm. Colocalizes with NEK6 in the nucleus (PubMed:16476580). Mainly localized in the nucleus but phosphorylation at Ser-71 by DAPK1 results in inhibition of its nuclear localization (PubMed:21497122).
PMID: 8606777 by Lu K.P., et al. A human peptidyl-prolyl isomerase essential for regulation of mitosis.
PMID: 11470801 by Kamimoto T., et al. Identification of a novel kinesin-related protein, KRMP1, as a target for mitotic peptidyl-prolyl isomerase Pin1.