PADI2

Peptidyl arginine deiminase, type II
Identifiers
Symbols	PADI2 ; KIAA0994; PAD-H19; PAD2; PDI2
External IDs	Template:OMIM5 Template:MGI HomoloGene: 7214
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO
RNA expression pattern
File:PBB GE PADI2 209791 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 II, also known as PADI2, is a human gene.

This gene encodes a member of the peptidyl arginine deiminase family of enzymes, which catalyze the post-translational deimination of proteins by converting arginine residues into citrullines in the presence of calcium ions. The family members have distinct substrate specificities and tissue-specific expression patterns. The type II enzyme is the most widely expressed family member. Known substrates for this enzyme include myelin basic protein in the central nervous system and vimentin in skeletal muscle and macrophages. This enzyme is thought to play a role in the onset and progression of neurodegenerative human disorders, including Alzheimer disease and multiple sclerosis, and it has also been implicated in glaucoma pathogenesis. This gene exists in a cluster with four other paralogous genes.

Further reading

• Vossenaar ER, Zendman AJ, van Venrooij WJ, Pruijn GJ (2004). "PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease". Bioessays. 25 (11): 1106–18. doi:10.1002/bies.10357. PMID 14579251.CS1 maint: Multiple names: authors list (link)
• Chavanas S, Méchin MC, Nachat R; et al. (2006). "Peptidylarginine deiminases and deimination in biology and pathology: relevance to skin homeostasis". J. Dermatol. Sci. 44 (2): 63–72. doi:10.1016/j.jdermsci.2006.07.004. PMID 16973334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Moscarello MA, Mastronardi FG, Wood DD (2007). "The role of citrullinated proteins suggests a novel mechanism in the pathogenesis of multiple sclerosis". Neurochem. Res. 32 (2): 251–6. doi:10.1007/s11064-006-9144-5. PMID 17031564.CS1 maint: Multiple names: authors list (link)
• Watanabe K, Senshu T (1989). "Isolation and characterization of cDNA clones encoding rat skeletal muscle peptidylarginine deiminase". J. Biol. Chem. 264 (26): 15255–60. PMID 2768262.
• Nagase T, Ishikawa K, Suyama M; et al. (1999). "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 6 (1): 63–70. PMID 10231032.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Venter JC, Adams MD, Myers EW; et al. (2001). "The sequence of the human genome". Science. 291 (5507): 1304–51. doi:10.1126/science.1058040. PMID 11181995.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ishigami A, Ohsawa T, Asaga H; et al. (2002). "Human peptidylarginine deiminase type II: molecular cloning, gene organization, and expression in human skin". Arch. Biochem. Biophys. 407 (1): 25–31. PMID 12392711.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Sambandam T, Belousova M, Accaviti-Loper MA; et al. (2005). "Increased peptidylarginine deiminase type II in hypoxic astrocytes". Biochem. Biophys. Res. Commun. 325 (4): 1324–9. doi:10.1016/j.bbrc.2004.10.173. PMID 15555572.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ishigami A, Ohsawa T, Hiratsuka M; et al. (2005). "Abnormal accumulation of citrullinated proteins catalyzed by peptidylarginine deiminase in hippocampal extracts from patients with Alzheimer's disease". J. Neurosci. Res. 80 (1): 120–8. doi:10.1002/jnr.20431. PMID 15704193.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Gregory SG, Barlow KF, McLay KE; et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. doi:10.1038/nature04727. PMID 16710414.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Bhattacharya SK, Crabb JS, Bonilha VL; et al. (2006). "Proteomics implicates peptidyl arginine deiminase 2 and optic nerve citrullination in glaucoma pathogenesis". Invest. Ophthalmol. Vis. Sci. 47 (6): 2508–14. doi:10.1167/iovs.05-1499. PMID 16723463.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Mastronardi FG, Noor A, Wood DD; et al. (2007). "Peptidyl argininedeiminase 2 CpG island in multiple sclerosis white matter is hypomethylated". J. Neurosci. Res. 85 (9): 2006–16. doi:10.1002/jnr.21329. PMID 17469138.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)