Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4

See also: Parvulin 14

PIN4
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1EQ3, 1FJD, 3UI4, 3UI5, 3UI6
Identifiers
Aliases	PIN4 , EPVH, PAR14, PAR17, peptidylprolyl cis/trans isomerase, NIMA-interacting 4
External IDs	OMIM: 300252; MGI: 1916963; HomoloGene: 121907; GeneCards: PIN4; OMA:PIN4 - orthologs
Gene location (Human) Chr. X chromosome (human) [1] Band Xq13.1 Start 72,181,353 bp [1] End 72,302,926 bp [1]
Gene location (Mouse) Chr. X chromosome (mouse) [2] Band X|X D Start 102,119,447 bp [2] End 102,127,669 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in tendon of biceps brachii gingival epithelium amniotic fluid germinal epithelium buccal mucosa cell hair follicle pancreatic epithelial cell pancreatic ductal cell palpebral conjunctiva kidney tubule Top expressed in yolk sac lens epiblast embryo duodenum morula bone marrow urinary bladder embryo dentate gyrus of hippocampal formation granule cell More reference expression data BioGPS n/a
Gene ontology Molecular function DNA binding double-stranded DNA binding protein binding bent DNA binding isomerase activity peptidyl-prolyl cis-trans isomerase activity RNA binding Cellular component cytoplasm mitochondrial matrix spindle preribosome nucleolus extracellular exosome cytoskeleton mitochondrion nucleus Biological process rRNA processing protein peptidyl-prolyl isomerization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5303 69713 Ensembl ENSG00000102309 ENSMUSG00000079480 UniProt Q9Y237 Q9CWW6 RefSeq (mRNA) NM_001170747 NM_006223 NM_027181 RefSeq (protein) NP_001164218 NP_006214 NP_081457 NP_001352019 Location (UCSC) Chr X: 72.18 – 72.3 Mb Chr X: 102.12 – 102.13 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4 is an enzyme that in humans is encoded by the PIN4 gene. ^{[5] [6] [7]}

References

1. GRCh38: Ensembl release 89: ENSG00000102309 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000079480 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Mueller JW, Kessler D, Neumann D, Stratmann T, Papatheodorou P, Hartmann-Fatu C, Bayer P (Mar 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 . PMC   1420321 . PMID   16522211.
6. Kessler D, Papatheodorou P, Stratmann T, Dian EA, Hartmann-Fatu C, Rassow J, Bayer P, Mueller JW (Oct 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 . PMC   2031878 . PMID   17875217.
7. "Entrez Gene: PIN4 protein (peptidylprolyl cis/trans isomerase) NIMA-interacting, 4 (parvulin)".

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. Bibcode:1999FEBSL.446..278U. doi: 10.1016/S0014-5793(99)00239-2 . PMID   10100858. S2CID   45172611.
• 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.gr-1640r. PMC   311086 . 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. doi:10.1016/S0022-2836(02)00615-0. 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. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . 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. doi:10.1016/S0022-2836(03)00713-7. 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. PMC   528928 . PMID   15489334.