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Peptidyl Prolyl Cis/Trans Isomerase NIMA Interacting Protein 4 (PIN4)

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EPVH; PAR14; PAR17; Parvulin; Eukaryotic Parvulin Homologue ; Parvulin-14; Parvulin-17; Peptidyl-prolyl cis/trans isomerase EPVH

Peptidyl Prolyl Cis/Trans Isomerase NIMA Interacting Protein 4 (PIN4)
CCC B490
HGNC 8992
MGI 1916963
PubMed 11960984
UniProt Q9Y237
Wiki PIN4

  • Sequence analysis predicted that the 131-amino acid PIN4 protein contains a PPIase domain preceded by a 40-amino acid glycine- and lysine-rich N-terminal sequence.

  • PIN4, however, lacks a WW domain, a nuclear localization motif, and residues required for phosphoprotein interactions. Multiple-tissue Northern blot analysis detected variable expression of an approximately 1.0-kb PIN4 transcript in all tissues tested, with notably lower expression in neuronal tissue. Transmission electron microscopy demonstrated preferential localization of PIN4 in the mitochondrial matrix. Functional analysis failed to show PPIase activity, possibly due to proteolytic degradation or different substrate requirements.

Organism species: Homo sapiens (Human)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins RPB490Hu01 Recombinant Peptidyl Prolyl Cis/Trans Isomerase NIMA Interacting Protein 4 (PIN4) Positive Control; Immunogen; SDS-PAGE; WB.
Antibodies PAB490Hu01 Polyclonal Antibody to Peptidyl Prolyl Cis/Trans Isomerase NIMA Interacting Protein 4 (PIN4) WB; IHC; ICC; IP.
Assay Kits n/a CLIA Kit for Peptidyl Prolyl Cis/Trans Isomerase NIMA Interacting Protein 4 (PIN4) CLIA Kit Customized Service Offer
n/a ELISA Kit for Peptidyl Prolyl Cis/Trans Isomerase NIMA Interacting Protein 4 (PIN4) ELISA Kit Customized Service Offer

Organism species: Mus musculus (Mouse)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins n/a Recombinant Peptidyl Prolyl Cis/Trans Isomerase NIMA Interacting Protein 4 (PIN4) Recombinant Protein Customized Service Offer
Antibodies n/a Monoclonal Antibody to Peptidyl Prolyl Cis/Trans Isomerase NIMA Interacting Protein 4 (PIN4) Monoclonal Antibody Customized Service Offer
n/a Polyclonal Antibody to Peptidyl Prolyl Cis/Trans Isomerase NIMA Interacting Protein 4 (PIN4) Polyclonal Antibody Customized Service Offer
Assay Kits n/a CLIA Kit for Peptidyl Prolyl Cis/Trans Isomerase NIMA Interacting Protein 4 (PIN4) CLIA Kit Customized Service Offer
n/a ELISA Kit for Peptidyl Prolyl Cis/Trans Isomerase NIMA Interacting Protein 4 (PIN4) ELISA Kit Customized Service Offer
  1. "Identification of eukaryotic parvulin homologues: a new subfamily of peptidylprolyl cis-trans isomerases."Biochem. Biophys. Res. Commun. 259:557-562(1999) [PubMed] [Europe PMC] [Abstract]
  2. "Identification and characterization of a 14 kDa human protein as a novel parvulin-like peptidyl prolyl cis/trans isomerase."FEBS Lett. 446:278-282(1999) [PubMed] [Europe PMC] [Abstract]
  3. "The DNA sequence of the human X chromosome." Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
  5. "Characterization of novel elongated Parvulin isoforms that are ubiquitously expressed in human tissues and originate from alternative transcription initiation."BMC Mol. Biol. 7:9-9(2006) [PubMed] [Europe PMC] [Abstract]
  6. "The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in Hominidae."BMC Biol. 5:37-37(2007) [PubMed] [Europe PMC] [Abstract]
  7. "Phosphorylation of the N-terminal domain regulates subcellular localization and DNA binding properties of the peptidyl-prolyl cis/trans isomerase hPar14."J. Mol. Biol. 330:955-966(2003) [PubMed] [Europe PMC] [Abstract]
  8. "Complete sequencing and characterization of 21,243 full-length human cDNAs." Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
  9. "The N-terminal basic domain of human parvulin hPar14 is responsible for the entry to the nucleus and high-affinity DNA-binding."J. Mol. Biol. 321:235-247(2002) [PubMed] [Europe PMC] [Abstract]
  10. "Parvulin (Par14), a peptidyl-prolyl cis-trans isomerase, is a novel rRNA processing factor that evolved in the metazoan lineage."Mol. Cell. Proteomics 8:1552-1565(2009) [PubMed] [Europe PMC] [Abstract]
  11. "Initial characterization of the human central proteome."BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
  12. "NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein."J. Mol. Biol. 301:1003-1017(2000) [PubMed] [Europe PMC] [Abstract]
  13. "Solution structure of the human parvulin-like peptidyl prolyl cis/trans isomerase, hPar14."J. Mol. Biol. 305:917-926(2001) [PubMed] [Europe PMC] [Abstract]