PADI4

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Peptidyl arginine deiminase, type IV
File:PBB Protein PADI4 image.jpg
PDB rendering based on 1wd8.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols PADI4 ; PAD; PADI5; PDI4; PDI5
External IDs Template:OMIM5 Template:MGI HomoloGene7883
RNA expression pattern
File:PBB GE PADI4 220001 at tn.png
File:PBB GE PADI4 211413 s at tn.png
File:PBB GE PADI4 211412 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Peptidyl arginine deiminase, type IV, also known as PADI4, is a human gene.[1]

This gene is a member of a gene family which encodes enzymes responsible for the conversion of arginine residues to citrulline residues. This gene may play a role in granulocyte and macrophage development leading to inflammation and immune response.[1]

References

  1. 1.0 1.1 "Entrez Gene: PADI4 peptidyl arginine deiminase, type IV".

Further reading

  • Nakashima K, Hagiwara T, Ishigami A; et al. (1999). "Molecular characterization of peptidylarginine deiminase in HL-60 cells induced by retinoic acid and 1alpha,25-dihydroxyvitamin D(3)". J. Biol. Chem. 274 (39): 27786–92. PMID 10488123.
  • Zhang QH, Ye M, Wu XY; et al. (2001). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Res. 10 (10): 1546–60. PMID 11042152.
  • Asaga H, Nakashima K, Senshu T; et al. (2001). "Immunocytochemical localization of peptidylarginine deiminase in human eosinophils and neutrophils". J. Leukoc. Biol. 70 (1): 46–51. PMID 11435484.
  • Nakashima K, Hagiwara T, Yamada M (2003). "Nuclear localization of peptidylarginine deiminase V and histone deimination in granulocytes". J. Biol. Chem. 277 (51): 49562–8. doi:10.1074/jbc.M208795200. PMID 12393868.
  • 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.
  • Suzuki A, Yamada R, Chang X; et al. (2003). "Functional haplotypes of PADI4, encoding citrullinating enzyme peptidylarginine deiminase 4, are associated with rheumatoid arthritis". Nat. Genet. 34 (4): 395–402. doi:10.1038/ng1206. PMID 12833157.
  • Barton A, Bowes J, Eyre S; et al. (2004). "A functional haplotype of the PADI4 gene associated with rheumatoid arthritis in a Japanese population is not associated in a United Kingdom population". Arthritis Rheum. 50 (4): 1117–21. doi:10.1002/art.20169. PMID 15077293.
  • Chavanas S, Méchin MC, Takahara H; et al. (2004). "Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6". Gene. 330: 19–27. doi:10.1016/j.gene.2003.12.038. PMID 15087120.
  • Arita K, Hashimoto H, Shimizu T; et al. (2004). "Structural basis for Ca(2+)-induced activation of human PAD4". Nat. Struct. Mol. Biol. 11 (8): 777–83. doi:10.1038/nsmb799. PMID 15247907.
  • Hoppe B, Heymann GA, Tolou F; et al. (2005). "High variability of peptidylarginine deiminase 4 (PADI4) in a healthy white population: characterization of six new variants of PADI4 exons 2-4 by a novel haplotype-specific sequencing-based approach". J. Mol. Med. 82 (11): 762–7. doi:10.1007/s00109-004-0584-6. PMID 15338034.
  • Cuthbert GL, Daujat S, Snowden AW; et al. (2004). "Histone deimination antagonizes arginine methylation". Cell. 118 (5): 545–53. doi:10.1016/j.cell.2004.08.020. PMID 15339660.
  • Wang Y, Wysocka J, Sayegh J; et al. (2004). "Human PAD4 regulates histone arginine methylation levels via demethylimination". Science. 306 (5694): 279–83. doi:10.1126/science.1101400. PMID 15345777.
  • 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.
  • Nakayama-Hamada M, Suzuki A, Kubota K; et al. (2005). "Comparison of enzymatic properties between hPADI2 and hPADI4". Biochem. Biophys. Res. Commun. 327 (1): 192–200. doi:10.1016/j.bbrc.2004.11.152. PMID 15629448.
  • Lee YH, Coonrod SA, Kraus WL; et al. (2005). "Regulation of coactivator complex assembly and function by protein arginine methylation and demethylimination". Proc. Natl. Acad. Sci. U.S.A. 102 (10): 3611–6. doi:10.1073/pnas.0407159102. PMID 15731352.
  • Kearney PL, Bhatia M, Jones NG; et al. (2005). "Kinetic characterization of protein arginine deiminase 4: a transcriptional corepressor implicated in the onset and progression of rheumatoid arthritis". Biochemistry. 44 (31): 10570–82. doi:10.1021/bi050292m. PMID 16060666.
  • Ikari K, Kuwahara M, Nakamura T; et al. (2005). "Association between PADI4 and rheumatoid arthritis: a replication study". Arthritis Rheum. 52 (10): 3054–7. doi:10.1002/art.21309. PMID 16200584.
  • Chang X, Han J (2006). "Expression of peptidylarginine deiminase type 4 (PAD4) in various tumors". Mol. Carcinog. 45 (3): 183–96. doi:10.1002/mc.20169. PMID 16355400.
  • Plenge RM, Padyukov L, Remmers EF; et al. (2006). "Replication of putative candidate-gene associations with rheumatoid arthritis in >4,000 samples from North America and Sweden: association of susceptibility with PTPN22, CTLA4, and PADI4". Am. J. Hum. Genet. 77 (6): 1044–60. doi:10.1086/498651. PMID 16380915.
  • Hoppe B, Häupl T, Gruber R; et al. (2006). "Detailed analysis of the variability of peptidylarginine deiminase type 4 in German patients with rheumatoid arthritis: a case-control study". Arthritis Res. Ther. 8 (2): R34. doi:10.1186/ar1889. PMID 16469113.

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