Protein family
Protein sequence
Protein function
Catalytic activity
EC number
EC number description
3.5.3.15
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amidines;
protein-arginine deiminase
PDB | Resolution (Å) | PDB name |
---|---|---|
4N20 | 1.657 | Crystal structure of Protein Arginine Deiminase 2 (0 mM Ca2+) |
4N22 | 1.889 | Crystal structure of Protein Arginine Deiminase 2 (50 uM Ca2+) |
4N24 | 1.968 | Crystal structure of Protein Arginine Deiminase 2 (100 uM Ca2+) |
4N25 | 1.931 | Crystal structure of Protein Arginine Deiminase 2 (250 uM Ca2+) |
4N26 | 1.943 | Crystal structure of Protein Arginine Deiminase 2 (500 uM Ca2+) |
4N28 | 1.879 | Crystal structure of Protein Arginine Deiminase 2 (1 mM Ca2+) |
4N2A | 1.7 | Crystal structure of Protein Arginine Deiminase 2 (5 mM Ca2+) |
4N2B | 1.69 | Crystal structure of Protein Arginine Deiminase 2 (10 mM Ca2+) |
4N2C | 3.022 | Crystal structure of Protein Arginine Deiminase 2 (F221/222A, 10 mM Ca2+) |
4N2D | 2.0 | Crystal structure of Protein Arginine Deiminase 2 (D123N, 0 mM Ca2+) |
4N2E | 1.858 | Crystal structure of Protein Arginine Deiminase 2 (D123N, 10 mM Ca2+) |
4N2F | 1.8 | Crystal structure of Protein Arginine Deiminase 2 (D169A, 0 mM Ca2+) |
4N2G | 1.85 | Crystal structure of Protein Arginine Deiminase 2 (D169A, 10 mM Ca2+) |
4N2H | 1.808 | Crystal structure of Protein Arginine Deiminase 2 (D177A, 0 mM Ca2+) |
4N2I | 1.9 | Crystal structure of Protein Arginine Deiminase 2 (D177A, 10 mM Ca2+) |
4N2K | 1.57 | Crystal structure of Protein Arginine Deiminase 2 (Q350A, 0 mM Ca2+) |
4N2L | 2.1 | Crystal structure of Protein Arginine Deiminase 2 (Q350A, 10 mM Ca2+) |
4N2M | 1.599 | Crystal structure of Protein Arginine Deiminase 2 (E354A, 0 mM Ca2+) |
4N2N | 1.8 | Crystal structure of Protein Arginine Deiminase 2 (E354A, 10 mM Ca2+) |
GO ontology | GO term | GO description |
---|---|---|
Biological Process | GO:1990830 | cellular response to leukemia inhibitory factor |
Biological Process | GO:0006338 | chromatin remodeling |
Biological Process | GO:0030520 | intracellular estrogen receptor signaling pathway |
Biological Process | GO:0070100 | negative regulation of chemokine-mediated signaling pathway |
Biological Process | GO:1901624 | negative regulation of lymphocyte chemotaxis |
Biological Process | GO:0021762 | substantia nigra development |
Biological Process | GO:0045815 | transcription initiation-coupled chromatin remodeling |
Molecular Function | GO:0005509 | calcium ion binding |
Molecular Function | GO:0140798 | histone H3R26 arginine deiminase activity |
Molecular Function | GO:0140794 | histone arginine deiminase activity |
Molecular Function | GO:0030331 | nuclear estrogen receptor binding |
Molecular Function | GO:0042803 | protein homodimerization activity |
Molecular Function | GO:0004668 | protein-arginine deiminase activity |
Cellular Component | GO:0035578 | azurophil granule lumen |
Cellular Component | GO:0005737 | cytoplasm |
Cellular Component | GO:0005829 | cytosol |
Cellular Component | GO:0000791 | euchromatin |
Cellular Component | GO:0070062 | extracellular exosome |
Cellular Component | GO:0005576 | extracellular region |
InterPro | InterPro name |
---|---|
IPR004303 | Protein-arginine deiminase |
IPR008972 | Cupredoxin |
IPR013530 | Protein-arginine deiminase, C-terminal |
IPR013732 | Protein-arginine deiminase (PAD), N-terminal |
IPR013733 | Protein-arginine deiminase (PAD), central domain |
IPR036556 | Protein-arginine deiminase, central domain superfamily |
IPR038685 | PAD, N-terminal domain superfamily |
Pfam | Pfam name |
---|---|
PF03068 | Protein-arginine deiminase (PAD) |
PF08526 | Protein-arginine deiminase (PAD) N-terminal domain |
PF08527 | Protein-arginine deiminase (PAD) middle domain |
Reactome | Reactome Name | Node type | Reactome Root | Reactome Root Name |
---|---|---|---|---|
R-HSA-3247509 | Chromatin modifying enzymes | Internal node | R-HSA-4839726 | Chromatin organization |
R-HSA-6798695 | Neutrophil degranulation | Leaf | R-HSA-168256 | Immune System |
Location | ECO term | Pubmed |
---|---|---|
Cytoplasm | ECO:0000269 | PubMed:12392711 |