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MGP002298

UniProt Annotations

Entry Information
Gene Namepeptidylprolyl cis/trans isomerase, NIMA-interacting 1
Protein EntryPIN1_HUMAN
UniProt IDQ13526
SpeciesHuman
Comments
Comment typeDescription
Catalytic ActivityPeptidylproline (omega=180) = peptidylproline (omega=0).
DomainThe WW domain is required for the interaction with STIL and KIF20B.
FunctionEssential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzes pSer/Thr-Pro cis/trans isomerizations. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation. Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner. {ECO:0000269|PubMed:15664191, ECO:0000269|PubMed:16644721, ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:21497122, ECO:0000269|PubMed:22033920}.
InteractionP78563:ADARB1; NbExp=12; IntAct=EBI-714158, EBI-2967304; P05067-4:APP; NbExp=2; IntAct=EBI-714158, EBI-302641; P85298-4:ARHGAP8; NbExp=25; IntAct=EBI-714158, EBI-9523517; Q15131:CDK10; NbExp=5; IntAct=EBI-714158, EBI-1646959; P31424-2:Grm5 (xeno); NbExp=3; IntAct=EBI-714158, EBI-8830305; Q3UVX5:Grm5 (xeno); NbExp=2; IntAct=EBI-714158, EBI-8795045; P51617:IRAK1; NbExp=10; IntAct=EBI-714158, EBI-358664; P31938:Map2k1 (xeno); NbExp=4; IntAct=EBI-714158, EBI-298860; Q63932:Map2k2 (xeno); NbExp=12; IntAct=EBI-714158, EBI-397724; Q9HC98:NEK6; NbExp=3; IntAct=EBI-714158, EBI-740364; P46531:NOTCH1; NbExp=9; IntAct=EBI-714158, EBI-636374; Q13950:RUNX2; NbExp=7; IntAct=EBI-714158, EBI-976402; Q13342:SP140; NbExp=4; IntAct=EBI-714158, EBI-2865100; Q9BR01:SULT4A1; NbExp=4; IntAct=EBI-714158, EBI-6690555; P04637:TP53; NbExp=12; IntAct=EBI-714158, EBI-366083;
PtmPhosphorylation at Ser-71 by DAPK1 results in inhibition of its catalytic activity, nuclear localization, and its ability to induce centrosome amplification, chromosome instability and cell transformation. {ECO:0000269|PubMed:17525332, ECO:0000269|PubMed:21497122}.
SimilarityContains 1 PpiC domain. {ECO:0000255|PROSITE- ProRule:PRU00278}.
SimilarityContains 1 WW domain. {ECO:0000255|PROSITE- ProRule:PRU00224}.
Subcellular LocationNucleus. Nucleus speckle. Cytoplasm. Note=Colocalizes with NEK6 in the nucleus. Mainly localized in the nucleus but phosphorylation at Ser-71 by DAPK1 results in inhibition of its nuclear localization.
SubunitInteracts with STIL. Interacts with KIF20B. Interacts with NEK6. Interacts (via WW domain) with PRKX. Interacts with BTK. Interacts (via PpiC domain) with DAPK1. Interacts with the phosphorylated form of RAF1. Interacts (via WW domain) with ATCAY; upon NGF stimulation. Interacts with PML (isoform PML-4) and BCL- 6. {ECO:0000269|PubMed:11470801, ECO:0000269|PubMed:15664191, ECO:0000269|PubMed:16476580, ECO:0000269|PubMed:16644721, ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:18628984, ECO:0000269|PubMed:19367327, ECO:0000269|PubMed:21497122, ECO:0000269|PubMed:22033920}.
Tissue SpecificityThe phosphorylated form at Ser-71 is expressed in normal breast tissue cells but not in breast cancer cells. {ECO:0000269|PubMed:17828269, ECO:0000269|PubMed:21497122}.
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