PIN4

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Protein (peptidylprolyl cis/trans isomerase) NIMA-interacting, 4 (parvulin)
PDB rendering based on 1eq3.
Available structures: 1eq3, 1fjd
Identifiers
Symbol(s) PIN4; EPVH; MGC138486; PAR14
External IDs OMIM: 300252 MGI: 1916963 HomoloGene: 4532
Orthologs
Human Mouse
Entrez 5303 69713


Refseq XM_001126085 (mRNA)
XP_001126085 (protein)		 XM_135990 (mRNA)
XP_135990 (protein)
Pubmed search [1] [2]

Protein (peptidylprolyl cis/trans isomerase) NIMA-interacting, 4 (parvulin), also known as PIN4, is a human gene.[1]


[edit] References

  1. ^ Entrez Gene: PIN4 protein (peptidylprolyl cis/trans isomerase) NIMA-interacting, 4 (parvulin).

[edit] Further reading

  • Uchida T, Fujimori F, Tradler T, et al. (1999). "Identification and characterization of a 14 kDa human protein as a novel parvulin-like peptidyl prolyl cis/trans isomerase.". FEBS Lett. 446 (2-3): 278–82. PMID 10100858. 
  • Rulten S, Thorpe J, Kay J (1999). "Identification of eukaryotic parvulin homologues: a new subfamily of peptidylprolyl cis-trans isomerases.". Biochem. Biophys. Res. Commun. 259 (3): 557–62. doi:10.1006/bbrc.1999.0828. PMID 10364457. 
  • Sekerina E, Rahfeld JU, Müller J, et al. (2000). "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 (4): 1003–17. doi:10.1006/jmbi.2000.4013. PMID 10966801. 
  • Terada T, Shirouzu M, Fukumori Y, et al. (2001). "Solution structure of the human parvulin-like peptidyl prolyl cis/trans isomerase, hPar14.". J. Mol. Biol. 305 (4): 917–26. doi:10.1006/jmbi.2000.4293. PMID 11162102. 
  • Suzuki Y, Tsunoda T, Sese J, et al. (2001). "Identification and characterization of the potential promoter regions of 1031 kinds of human genes.". Genome Res. 11 (5): 677–84. doi:10.1101/gr.164001. PMID 11337467. 
  • Fujiyama S, Yanagida M, Hayano T, et al. (2002). "Isolation and proteomic characterization of human Parvulin-associating preribosomal ribonucleoprotein complexes.". J. Biol. Chem. 277 (26): 23773–80. doi:10.1074/jbc.M201181200. PMID 11960984. 
  • Surmacz TA, Bayer E, Rahfeld JU, et al. (2002). "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 (2): 235–47. PMID 12144781. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Reimer T, Weiwad M, Schierhorn A, et al. (2003). "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 (5): 955–66. PMID 12860119. 
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334. 
  • Mueller JW, Kessler D, Neumann D, et al. (2006). "Characterization of novel elongated Parvulin isoforms that are ubiquitously expressed in human tissues and originate from alternative transcription initiation.". BMC Mol. Biol. 7: 9. doi:10.1186/1471-2199-7-9. PMID 16522211. 
  • Kessler D, Papatheodorou P, Stratmann T, et al. (2007). "The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in Hominidae.". BMC Biol. 5: 37. doi:10.1186/1741-7007-5-37. PMID 17875217. 
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