A protein-arginine deiminase type-2 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9Y2J8]
EC 3.5.3.15;
PAD-H19;
Peptidylarginine deiminase II;
Protein-arginine deiminase type II
Timeframe | Studies on this Protein(%) | All Drugs % |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 0 (0.00) | 29.6817 |
2010's | 1 (100.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
---|---|---|---|---|---|
streptonigrin | Homo sapiens (human) | IC50 | 26.1000 | 1 | 1 |
This protein enables 6 target(s):
Target | Category | Definition |
---|---|---|
protein-arginine deiminase activity | molecular function | Catalysis of the reaction: H2O + L-arginyl-[protein] = L-citrullyl-[protein] + NH4+, resulting in citrullination of the target protein. This reaction is calcium-dependent. [PMID:27393304] |
calcium ion binding | molecular function | Binding to a calcium ion (Ca2+). [GOC:ai] |
nuclear estrogen receptor binding | molecular function | Binding to a nuclear estrogen receptor. [GOC:ai] |
protein homodimerization activity | molecular function | Binding to an identical protein to form a homodimer. [GOC:jl] |
histone H3R26 arginine deiminase activity | molecular function | Catalysis of the reaction: H2O + histone H3 L-arginyl (position 26)= histone H3 L-citrullyl (position 26) + NH4+, resulting in histone H3 citrullination at position 26. [PMID:15339660] |
histone arginine deiminase activity | molecular function | Catalysis of the reaction: H2O + histone 3 L-arginyl = histone 3 L-citrullyl + NH4+, resulting in histone citrullination. [PMID:15339660] |
This protein is located in 5 target(s):
Target | Category | Definition |
---|---|---|
extracellular region | cellular component | The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite. [GOC:go_curators] |
cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
cytosol | cellular component | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl] |
azurophil granule lumen | cellular component | The volume enclosed by the membrane of an azurophil granule, a primary lysosomal granule found in neutrophil granulocytes that contains a wide range of hydrolytic enzymes and is released into the extracellular fluid. [GOC:bf, PMID:17152095] |
extracellular exosome | cellular component | A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. [GOC:BHF, GOC:mah, GOC:vesicles, PMID:15908444, PMID:17641064, PMID:19442504, PMID:19498381, PMID:22418571, PMID:24009894] |
This protein is active in 2 target(s):
Target | Category | Definition |
---|---|---|
nucleus | cellular component | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators] |
cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
This protein is part of 1 target(s):
Target | Category | Definition |
---|---|---|
euchromatin | cellular component | A dispersed and relatively uncompacted form of chromatin that is in a transcription-competent conformation. [PMID:32017156] |
This protein is involved in 7 target(s):
Target | Category | Definition |
---|---|---|
substantia nigra development | biological process | The progression of the substantia nigra over time from its initial formation until its mature state. The substantia nigra is the layer of gray substance that separates the posterior parts of the cerebral peduncles (tegmentum mesencephali) from the anterior parts; it normally includes a posterior compact part with many pigmented cells (pars compacta) and an anterior reticular part whose cells contain little pigment (pars reticularis). [GO_REF:0000021, GOC:cls, GOC:dgh, GOC:dph, GOC:jid, ISBN:0838580343, ISBN:0878937420] |
intracellular estrogen receptor signaling pathway | biological process | The series of molecular signals initiated by estrogen binding to its nuclear receptor inside the cell, and ending with the regulation of a downstream cellular process, e.g. transcription. [GOC:mah, GOC:signaling] |
transcription initiation-coupled chromatin remodeling | biological process | An epigenetic mechanism of regulation of gene expression that involves chromatin remodeling to capacitate gene expression by either modifying the chromatin fiber, the nucleosomal histones, or the DNA. [PMID:34414474] |
negative regulation of chemokine-mediated signaling pathway | biological process | Any process that decreases the rate, frequency or extent of a chemokine-mediated signaling pathway. [GOC:mah] |
negative regulation of lymphocyte chemotaxis | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of lymphocyte chemotaxis. [GOC:TermGenie] |
cellular response to leukemia inhibitory factor | biological process | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a leukemia inhibitory factor stimulus. [PMID:12801913] |
chromatin remodeling | biological process | A dynamic process of chromatin reorganization resulting in changes to chromatin structure. These changes allow DNA metabolic processes such as transcriptional regulation, DNA recombination, DNA repair, and DNA replication. [GOC:jid, GOC:vw, PMID:12042764, PMID:12697820] |