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InterPro-Version: 108.0
InterPro-Version-Minor: 0
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{
"metadata": {
"accession": "IPR020684",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0004674",
"name": "protein serine/threonine kinase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0030036",
"name": "actin cytoskeleton organization",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"pirsf": {
"PIRSF037568": "Rho-associated protein kinase"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR020684",
"name": "Rho-associated protein kinase 1/2",
"type": "Family",
"children": []
},
"name": {
"name": "Rho-associated protein kinase 1/2",
"short": "ROCK1/ROCK2"
},
"description": [
{
"text": "<p>Eukaryotic protein kinases [[cite:PUB00001530], [cite:PUB00003568], [cite:PUB00003569], [cite:PUB00005115]] are enzymes that belong to a very extensive family of proteins which share a conserved catalytic core common with both serine/threonine and tyrosine protein kinases.</p>\n\n<p>Rho kinases are serine/threonine kinases that are important in cell migration, cell proliferation and cell survival. Disorders of the central nervous system including stroke, inflammatory and demyelinating diseases, Alzheimer's disease and neuropathic pain may be linked to abnormal activation of Rho kinases [[cite:PUB00035008]].</p>\r\n<p>This entry represents a set of Rho-associated, coiled-coil-containing, protein kinases. They phosphorylate a large number of important signalling proteins and help regulate the assembly of the actin cytoskeleton. Proteins in this entry have been shown to play a role in smooth muscle formation, and promote the formation of stress fibres and of focal adhesion complexes [[cite:PUB00035531], [cite:PUB00035532]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00035532": {
"PMID": 12832488,
"ISBN": null,
"volume": "23",
"issue": "14",
"year": 2003,
"title": "Targeted disruption of the mouse rho-associated kinase 2 gene results in intrauterine growth retardation and fetal death.",
"URL": null,
"raw_pages": "5043-55",
"medline_journal": "Mol Cell Biol",
"ISO_journal": "Mol. Cell. Biol.",
"authors": [
"Thumkeo D",
"Keel J",
"Ishizaki T",
"Hirose M",
"Nonomura K",
"Oshima H",
"Oshima M",
"Taketo MM",
"Narumiya S."
],
"DOI_URL": "http://dx.doi.org/10.1128/MCB.23.14.5043-5055.2003"
},
"PUB00035531": {
"PMID": 8772201,
"ISBN": null,
"volume": "392",
"issue": "2",
"year": 1996,
"title": "ROCK-I and ROCK-II, two isoforms of Rho-associated coiled-coil forming protein serine/threonine kinase in mice.",
"URL": null,
"raw_pages": "189-93",
"medline_journal": "FEBS Lett",
"ISO_journal": "FEBS Lett.",
"authors": [
"Nakagawa O",
"Fujisawa K",
"Ishizaki T",
"Saito Y",
"Nakao K",
"Narumiya S."
],
"DOI_URL": "http://dx.doi.org/10.1016/0014-5793(96)00811-3"
},
"PUB00035008": {
"PMID": 15864268,
"ISBN": null,
"volume": "4",
"issue": "5",
"year": 2005,
"title": "Rho kinase, a promising drug target for neurological disorders.",
"URL": null,
"raw_pages": "387-98",
"medline_journal": "Nat Rev Drug Discov",
"ISO_journal": null,
"authors": [
"Mueller BK",
"Mack H",
"Teusch N."
],
"DOI_URL": "http://dx.doi.org/10.1038/nrd1719"
},
"PUB00005115": {
"PMID": 3291115,
"ISBN": null,
"volume": "241",
"issue": "4861",
"year": 1988,
"title": "The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.",
"URL": null,
"raw_pages": "42-52",
"medline_journal": "Science",
"ISO_journal": "Science",
"authors": [
"Hanks SK",
"Quinn AM",
"Hunter T."
],
"DOI_URL": "http://www.sciencemag.org/cgi/content/abstract/241/4861/42"
},
"PUB00001530": {
"PMID": 7768349,
"ISBN": null,
"volume": "9",
"issue": "8",
"year": 1995,
"title": "Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification.",
"URL": null,
"raw_pages": "576-96",
"medline_journal": "FASEB J",
"ISO_journal": "FASEB J.",
"authors": [
"Hanks SK",
"Hunter T."
],
"DOI_URL": "http://www.fasebj.org/cgi/content/abstract/9/8/576"
},
"PUB00003569": {
"PMID": 1956325,
"ISBN": null,
"volume": "200",
"issue": null,
"year": 1991,
"title": "Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members.",
"URL": null,
"raw_pages": "38-62",
"medline_journal": "Methods Enzymol",
"ISO_journal": "Meth. Enzymol.",
"authors": [
"Hanks SK",
"Quinn AM."
],
"DOI_URL": "http://dx.doi.org/10.1016/0076-6879(91)00126-H"
},
"PUB00003568": {
"PMID": 1835513,
"ISBN": null,
"volume": "200",
"issue": null,
"year": 1991,
"title": "Protein kinase classification.",
"URL": null,
"raw_pages": "3-37",
"medline_journal": "Methods Enzymol",
"ISO_journal": "Meth. Enzymol.",
"authors": [
"Hunter T."
],
"DOI_URL": "http://dx.doi.org/10.1016/0076-6879(91)00125-G"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 1885,
"pathways": 50,
"proteins": 1885,
"proteomes": 594,
"sets": 0,
"structural_models": {
"alphafold": 22,
"bfvd": 0
},
"structures": 0,
"taxa": 1948
},
"entry_annotations": {},
"cross_references": {
"ec": {
"displayName": "ENZYME",
"description": "ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.",
"rank": 19,
"accessions": [
{
"accession": "2.7.11.39",
"url": "https://enzyme.expasy.org/EC/2.7.11.39"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
