NamePeptidyl-prolyl cis-trans isomerase NIMA-interacting 1
Synonyms
  • 5.2.1.8
  • Peptidyl-prolyl cis-trans isomerase Pin1
  • PPIase Pin1
  • Rotamase Pin1
Gene NamePIN1
OrganismHuman
Amino acid sequence
>lcl|BSEQ0017209|Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
MADEEKLPPGWEKRMSRSSGRVYYFNHITNASQWERPSGNSSSGGKNGQGEPARVRCSHL
LVKHSQSRRPSSWRQEKITRTKEEALELINGYIQKIKSGEEDFESLASQFSDCSSAKARG
DLGAFSRGQMQKPFEDASFALRTGEMSGPVFTDSGIHIILRTE
Number of residues163
Molecular Weight18243.13
Theoretical pI9.18
GO Classification
Functions
  • GTPase activating protein binding
  • mitogen-activated protein kinase kinase binding
  • phosphoserine binding
  • phosphothreonine binding
  • peptidyl-prolyl cis-trans isomerase activity
Processes
  • cell cycle
  • negative regulation of transforming growth factor beta receptor signaling pathway
  • innate immune response
  • negative regulation of type I interferon production
  • positive regulation of protein phosphorylation
  • positive regulation of ubiquitin-protein transferase activity
  • positive regulation of GTPase activity
  • cytokine-mediated signaling pathway
  • regulation of cytokinesis
  • regulation of mitotic nuclear division
  • negative regulation of cell motility
  • negative regulation of neuron apoptotic process
  • positive regulation of cell growth involved in cardiac muscle cell development
  • positive regulation of protein dephosphorylation
  • regulation of pathway-restricted SMAD protein phosphorylation
  • protein peptidyl-prolyl isomerization
  • negative regulation of ERK1 and ERK2 cascade
  • positive regulation of neuron apoptotic process
Components
  • midbody
  • cytosol
  • nuclear speck
  • nucleoplasm
  • neuron projection
  • mitochondrion
  • nucleus
General FunctionPhosphothreonine binding
Specific FunctionPeptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs in a subset of proteins, resulting in conformational changes in the proteins (PubMed:21497122, PubMed:22033920). Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK (PubMed:16644721). 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 (PubMed:15664191). Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner (PubMed:17828269). Acts as a regulator of JNK cascade by binding to phosphorylated FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation: degradation of FBXW7 leads to subsequent stabilization of JUN (PubMed:22608923).
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID1332710
UniProtKB IDQ13526
UniProtKB Entry NamePIN1_HUMAN
Cellular LocationNucleus
Gene sequence
>lcl|BSEQ0017210|Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1)
ATGGCGGACGAGGAGAAGCTGCCGCCCGGCTGGGAGAAGCGCATGAGCCGCAGCTCAGGC
CGAGTGTACTACTTCAACCACATCACTAACGCCAGCCAGTGGGAGCGGCCCAGCGGCAAC
AGCAGCAGTGGTGGCAAAAACGGGCAGGGGGAGCCTGCCAGGGTCCGCTGCTCGCACCTG
CTGGTGAAGCACAGCCAGTCACGGCGGCCCTCGTCCTGGCGGCAGGAGAAGATCACCCGG
ACCAAGGAGGAGGCCCTGGAGCTGATCAACGGCTACATCCAGAAGATCAAGTCGGGAGAG
GAGGACTTTGAGTCTCTGGCCTCACAGTTCAGCGACTGCAGCTCAGCCAAGGCCAGGGGA
GACCTGGGTGCCTTCAGCAGAGGTCAGATGCAGAAGCCATTTGAAGACGCCTCGTTTGCG
CTGCGGACGGGGGAGATGAGCGGGCCCGTGTTCACGGATTCCGGCATCCACATCATCCTC
CGCACTGAGTGA
GenBank Gene IDU49070
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDHGNC:8988
Chromosome Location19
Locus19p13
References
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