Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1

NamePeptidyl-prolyl cis-trans isomerase NIMA-interacting 1
Synonyms5.2.1.8 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
peptidyl-prolyl cis-trans isomerase activity
phosphoserine binding
phosphothreonine binding
Processes
    positive regulation of GTPase activity
cytokine-mediated signaling pathway
negative regulation of transforming growth factor beta receptor signaling pathway
regulation of cytokinesis
negative regulation of type I interferon production
regulation of mitotic nuclear division
positive regulation of ubiquitin-protein transferase activity
negative regulation of neuron apoptotic process
cell cycle
positive regulation of protein dephosphorylation
protein peptidyl-prolyl isomerization
innate immune response
negative regulation of ERK1 and ERK2 cascade
negative regulation of cell motility
positive regulation of protein phosphorylation
positive regulation of neuron apoptotic process
positive regulation of cell growth involved in cardiac muscle cell development
regulation of pathway-restricted SMAD protein phosphorylation
Components
    nuclear speck
mitochondrion
nucleus
cytosol
nucleoplasm
neuron projection
midbody
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).
Transmembrane Regions
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 IDNone
GenAtlas ID
HGNC IDHGNC:8988
Chromosome Location19
Locus19p13
References
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FRCD ID Name Exact Mass Structure




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