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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR001841",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"profile": {
"PS50089": "Zinc finger RING-type profile"
},
"pfam": {
"PF14634": "zinc-RING finger domain",
"PF17121": "Zinc finger, C3HC4 type (RING finger)",
"PF17122": "Zinc-finger",
"PF17123": "RING-like zinc finger",
"PF13923": "Zinc finger, C3HC4 type (RING finger)",
"PF13639": "Ring finger domain"
},
"smart": {
"SM00184": "Ring finger"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR001841",
"name": "Zinc finger, RING-type",
"type": "Domain",
"children": [
{
"accession": "IPR018957",
"name": "Zinc finger, C3HC4 RING-type",
"type": "Domain",
"children": [
{
"accession": "IPR045859",
"name": "Peroxisome biogenesis factor 2, HC subclass-RING finger domain",
"type": "Domain",
"children": []
},
{
"accession": "IPR058558",
"name": "V(D)J recombination-activating protein 1, RING finger, HC subclass",
"type": "Domain",
"children": []
}
]
},
{
"accession": "IPR024766",
"name": "Zinc finger, RING-H2-type",
"type": "Domain",
"children": []
},
{
"accession": "IPR024991",
"name": "Anaphase-promoting complex subunit 11, RING-H2 finger",
"type": "Domain",
"children": []
},
{
"accession": "IPR027133",
"name": "TNF receptor-associated factor 2, C3HC3D-type RING zinc finger",
"type": "Domain",
"children": []
},
{
"accession": "IPR027139",
"name": "TNF receptor-associated factor 6, C3HC3D-type RING zinc finger",
"type": "Domain",
"children": []
},
{
"accession": "IPR027370",
"name": "Zinc finger, RING-type, eukaryotic",
"type": "Domain",
"children": [
{
"accession": "IPR027726",
"name": "E3 ubiquitin-protein ligase Trim36, RING finger, HC subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR033491",
"name": "Probable E3 ubiquitin-protein ligase MID2, RING finger, HC subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR042667",
"name": "E3 ubiquitin-protein ligase TRIM63, RING finger, HC subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR042716",
"name": "E3 ubiquitin-protein ligase RNF114, RING finger, HC subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR042752",
"name": "TRIM54, RING finger, HC subclass",
"type": "Domain",
"children": []
}
]
},
{
"accession": "IPR027934",
"name": "Cellulose synthase, RING-type zinc finger",
"type": "Domain",
"children": []
},
{
"accession": "IPR028511",
"name": "E3 ubiquitin-protein ligase SH3RF2, RING finger, HC subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR032043",
"name": "E3 ubiquitin-protein ligase Msl2, zinc RING finger",
"type": "Domain",
"children": []
},
{
"accession": "IPR033609",
"name": "E3 ubiquitin-protein ligase RNF152, RING finger domain",
"type": "Domain",
"children": []
},
{
"accession": "IPR035691",
"name": "ORC ubiquitin ligase 1, RING finger",
"type": "Domain",
"children": []
},
{
"accession": "IPR039503",
"name": "BARD1, Zinc finger, RING-type",
"type": "Domain",
"children": []
},
{
"accession": "IPR039520",
"name": "E3 ubiquitin-protein ligase CBL-B, RING finger, HC subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR039571",
"name": "RNF126, RING finger, H2 subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR039804",
"name": "Listerin, zinc finger, RING-type",
"type": "Domain",
"children": []
},
{
"accession": "IPR040089",
"name": "RNF26, C3HC5-type zinc finger",
"type": "Domain",
"children": []
},
{
"accession": "IPR040100",
"name": "RING finger protein 208, HC type RING finger",
"type": "Domain",
"children": []
},
{
"accession": "IPR040178",
"name": "E3 ubiquitin-protein ligase RNF220, RING finger",
"type": "Domain",
"children": []
},
{
"accession": "IPR040380",
"name": "HAKAI-like, RING finger, HC subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR041888",
"name": "ZN598/HEL22, RING finger",
"type": "Domain",
"children": []
},
{
"accession": "IPR042656",
"name": "E3 ubiquitin-protein ligase TRIM68, RING finger, HC subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR042699",
"name": "E3 ubiquitin-protein ligase TRIM58, RING finger, HC subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR042712",
"name": "E3 ubiquitin-protein ligase RNF149, RING finger, H2 subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR042713",
"name": "TIF1-beta, RING finger, HC subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR042741",
"name": "RING1 , RING finger, HC subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR042765",
"name": "TRIM42, RING-HC finger",
"type": "Domain",
"children": []
},
{
"accession": "IPR042784",
"name": "TRIM10, RING-HC finger",
"type": "Domain",
"children": []
},
{
"accession": "IPR042823",
"name": "E3 ubiquitin-protein ligase Dma1/Dma2, RING finger, H2 subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR042843",
"name": "DTX3L, RING-HC finger",
"type": "Domain",
"children": []
},
{
"accession": "IPR043295",
"name": "RNF4, RING finger, HC subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR043400",
"name": "RNF141, RING finger, HC subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR044080",
"name": "MDM2, modified RING finger, HC subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR044110",
"name": "RNF146, RING finger, HC subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR045195",
"name": "LOG2-like, modified RING finger, C3HC5-type",
"type": "Domain",
"children": []
},
{
"accession": "IPR045317",
"name": "E3 ubiquitin-protein ligase RGLG1/2, RING finger",
"type": "Domain",
"children": []
},
{
"accession": "IPR045903",
"name": "E3 ubiquitin-protein ligase ZNRF3, zinc finger, RING-type",
"type": "Domain",
"children": []
},
{
"accession": "IPR045907",
"name": "E3 ubiquitin-protein ligase RNF43, Zinc finger, RING-type",
"type": "Domain",
"children": []
},
{
"accession": "IPR047243",
"name": "BRCA1-associated protein, RING finger, H2 subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR047466",
"name": "E3 ubiquitin-protein ligase UHRF2, RING finger, HC subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR047498",
"name": "E3 ubiquitin-protein ligase ORTHRUS 1/2-like, first RING finger, HC subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR047529",
"name": "E3 ubiquitin-protein ligase ORTHRUS 1-5, second RING finger, HC subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR047559",
"name": "Heme-oxidized IRP2 ubiquitin ligase 1, modified RING finger, HC subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR047563",
"name": "Ankyrin repeat and IBR domain-containing protein 1, RING finger, HC subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR047823",
"name": "RNF145, RING finger, H2 subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR047986",
"name": "E3 ubiquitin-protein ligase RNF182, RING finger, HC subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR048025",
"name": "RING finger protein 24, RING finger, H2 subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR048217",
"name": "RING-type E3 ubiquitin transferase BIG BROTHER, RING finger, H2 subclass",
"type": "Domain",
"children": []
},
{
"accession": "IPR049440",
"name": "TNF receptor-associated factor 3/5, RING domain",
"type": "Domain",
"children": [
{
"accession": "IPR027128",
"name": "TNF receptor-associated factor 3, C3HC3D-type RING zinc finger",
"type": "Domain",
"children": []
}
]
},
{
"accession": "IPR049548",
"name": "E3 ubiquitin-protein ligase Sina-like, RING finger",
"type": "Domain",
"children": []
},
{
"accession": "IPR056760",
"name": "E3 ubiquitin-protein ligase XB3-like, RING finger",
"type": "Domain",
"children": []
},
{
"accession": "IPR056939",
"name": "Vps8, RING finger",
"type": "Domain",
"children": []
},
{
"accession": "IPR058051",
"name": "Synoviolin-like, RING finger",
"type": "Domain",
"children": []
},
{
"accession": "IPR058746",
"name": "Topors, zinc finger, RING-type",
"type": "Domain",
"children": []
}
]
},
"name": {
"name": "Zinc finger, RING-type",
"short": "Znf_RING"
},
"description": [
{
"text": "<p>This entry represents RING-type zinc finger domains. The RING-finger is a specialised type of Zn-finger of 40 to 60 residues that binds two atoms of zinc, and is probably involved in mediating protein-protein interactions [[cite:PUB00005712], [cite:PUB00001094], [cite:PUB00006216]]. There are two different variants, the C3HC4-type and a C3H2C3-type, which are clearly related despite the different cysteine/histidine pattern. The latter type is sometimes referred to as 'RING-H2 finger'. The RING domain is a protein interaction domain that has been implicated in a range of diverse biological processes. E3 ubiquitin-protein ligase, in Homo sapiens [swissprot:Q06587], activity is intrinsic to the RING domain of c-Cbl and is likely to be a general function of this domain. E3 ubiquitin-protein ligases determine the substrate specificity for ubiquitylation and have been classified into HECT and RING-finger families. Various RING fingers also exhibit binding to E2 ubiquitin-conjugating enzymes (Ubc's) [[cite:PUB00006474], [cite:PUB00006565], [cite:PUB00006516]].</p>\n\n<p>Several 3D-structures for RING-fingers are known [[cite:PUB00001094], [cite:PUB00006216]]. The 3D structure of the zinc ligation system is unique to the RING domain and is referred to as the 'cross-brace' motif. The spacing of the cysteines in such a domain is C-x(2)-C-x(9 to 39)-C-x(1 to 3)-H-x(2 to 3)-C-x(2)-C-x(4 to 48)-C-x(2)-C. Metal ligand pairs one and three co-ordinate to bind one zinc ion, whilst pairs two and four bind the second.</p>\n\n<p>Note that in the older literature, some RING-fingers are denoted as LIM-domains. The LIM-domain Zn-finger is a fundamentally different family, albeit with similar Cys-spacing (see [interpro:IPR001781]).</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [[cite:PUB00035807], [cite:PUB00035805], [cite:PUB00035806], [cite:PUB00035804], [cite:PUB00014077]]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few [[cite:PUB00035812]]. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00035807": {
"PMID": 10529348,
"ISBN": null,
"volume": "293",
"issue": "2",
"year": 1999,
"title": "Zinc finger peptides for the regulation of gene expression.",
"URL": null,
"raw_pages": "215-8",
"medline_journal": "J Mol Biol",
"ISO_journal": "J. Mol. Biol.",
"authors": [
"Klug A."
],
"DOI_URL": "http://dx.doi.org/10.1006/jmbi.1999.3007"
},
"PUB00035805": {
"PMID": 15963892,
"ISBN": null,
"volume": "15",
"issue": "3",
"year": 2005,
"title": "Multiple modes of RNA recognition by zinc finger proteins.",
"URL": null,
"raw_pages": "367-73",
"medline_journal": "Curr Opin Struct Biol",
"ISO_journal": "Curr. Opin. Struct. Biol.",
"authors": [
"Hall TM."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.sbi.2005.04.004"
},
"PUB00035806": {
"PMID": 15718139,
"ISBN": null,
"volume": "15",
"issue": "1",
"year": 2005,
"title": "Zinc finger proteins: getting a grip on RNA.",
"URL": null,
"raw_pages": "94-8",
"medline_journal": "Curr Opin Struct Biol",
"ISO_journal": "Curr. Opin. Struct. Biol.",
"authors": [
"Brown RS."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.sbi.2005.01.006"
},
"PUB00006516": {
"PMID": 10577187,
"ISBN": null,
"volume": "286",
"issue": "5438",
"year": 1999,
"title": "A new finger on the protein destruction button.",
"URL": null,
"raw_pages": "223, 225",
"medline_journal": "Science",
"ISO_journal": "Science",
"authors": [
"Barinaga M."
],
"DOI_URL": "http://dx.doi.org/10.1126/science.286.5438.223"
},
"PUB00006216": {
"PMID": 8744354,
"ISBN": null,
"volume": "21",
"issue": "6",
"year": 1996,
"title": "Does this have a familiar RING?",
"URL": null,
"raw_pages": "208-14",
"medline_journal": "Trends Biochem Sci",
"ISO_journal": "Trends Biochem. Sci.",
"authors": [
"Saurin AJ",
"Borden KL",
"Boddy MN",
"Freemont PS."
],
"DOI_URL": "http://dx.doi.org/10.1016/0968-0004(96)10036-0"
},
"PUB00005712": {
"PMID": 8317827,
"ISBN": null,
"volume": "684",
"issue": null,
"year": 1993,
"title": "The RING finger. A novel protein sequence motif related to the zinc finger.",
"URL": null,
"raw_pages": "174-92",
"medline_journal": "Ann N Y Acad Sci",
"ISO_journal": "Ann. N. Y. Acad. Sci.",
"authors": [
"Freemont PS."
],
"DOI_URL": "http://www.annalsnyas.org/cgi/content/abstract/684/1/174"
},
"PUB00035812": {
"PMID": 11179890,
"ISBN": null,
"volume": "11",
"issue": "1",
"year": 2001,
"title": "Zinc finger proteins: new insights into structural and functional diversity.",
"URL": null,
"raw_pages": "39-46",
"medline_journal": "Curr Opin Struct Biol",
"ISO_journal": "Curr. Opin. Struct. Biol.",
"authors": [
"Laity JH",
"Lee BM",
"Wright PE."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0959-440X(00)00167-6"
},
"PUB00035804": {
"PMID": 17210253,
"ISBN": null,
"volume": "32",
"issue": "2",
"year": 2007,
"title": "Sticky fingers: zinc-fingers as protein-recognition motifs.",
"URL": null,
"raw_pages": "63-70",
"medline_journal": "Trends Biochem Sci",
"ISO_journal": "Trends Biochem. Sci.",
"authors": [
"Gamsjaeger R",
"Liew CK",
"Loughlin FE",
"Crossley M",
"Mackay JP."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.tibs.2006.12.007"
},
"PUB00001094": {
"PMID": 8804826,
"ISBN": null,
"volume": "6",
"issue": "3",
"year": 1996,
"title": "The RING finger domain: a recent example of a sequence-structure family.",
"URL": null,
"raw_pages": "395-401",
"medline_journal": "Curr Opin Struct Biol",
"ISO_journal": "Curr. Opin. Struct. Biol.",
"authors": [
"Borden KL",
"Freemont PS."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0959-440X(96)80060-1"
},
"PUB00014077": {
"PMID": 12665246,
"ISBN": null,
"volume": "54",
"issue": "6",
"year": 2002,
"title": "Zinc fingers--folds for many occasions.",
"URL": null,
"raw_pages": "351-5",
"medline_journal": "IUBMB Life",
"ISO_journal": "IUBMB Life",
"authors": [
"Matthews JM",
"Sunde M."
],
"DOI_URL": "http://dx.doi.org/10.1080/15216540216035"
},
"PUB00006565": {
"PMID": 10514377,
"ISBN": null,
"volume": "286",
"issue": "5438",
"year": 1999,
"title": "The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase.",
"URL": null,
"raw_pages": "309-12",
"medline_journal": "Science",
"ISO_journal": "Science",
"authors": [
"Joazeiro CA",
"Wing SS",
"Huang H",
"Leverson JD",
"Hunter T",
"Liu YC."
],
"DOI_URL": "http://dx.doi.org/10.1126/science.286.5438.309"
},
"PUB00006474": {
"PMID": 10662664,
"ISBN": null,
"volume": "10",
"issue": "2",
"year": 2000,
"title": "RING for destruction?",
"URL": null,
"raw_pages": "R84-7",
"medline_journal": "Curr Biol",
"ISO_journal": "Curr. Biol.",
"authors": [
"Freemont PS."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0960-9822(00)00287-6"
},
"PUB00014857": {
"PMID": 12944364,
"ISBN": null,
"volume": "134",
"issue": "1",
"year": 2003,
"title": "Ubiquitylation as a quality control system for intracellular proteins.",
"URL": null,
"raw_pages": "1-8",
"medline_journal": "J Biochem",
"ISO_journal": "J. Biochem.",
"authors": [
"Hatakeyama S",
"Nakayama KI."
],
"DOI_URL": "http://dx.doi.org/10.1093/jb/mvg106"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR013083",
"name": "Zinc finger, RING/FYVE/PHD-type",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 5325,
"interactions": 25,
"matches": 820304,
"pathways": 938,
"proteins": 766300,
"proteomes": 4094,
"sets": 0,
"structural_models": {
"alphafold": 642976,
"bfvd": 601
},
"structures": 578,
"taxa": 23559
},
"entry_annotations": {
"alignment:seed": 71,
"alignment:full": 7812
},
"cross_references": {
"prositedoc": {
"displayName": "PROSITE Doc",
"description": "PROSITE is a database of protein families and domains.",
"rank": 18,
"accessions": [
{
"accession": "PDOC00449",
"url": "http://prosite.expasy.org/PDOC00449"
}
]
},
"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": [
{
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"url": "https://enzyme.expasy.org/EC/2.3.2"
},
{
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"url": "https://enzyme.expasy.org/EC/2.3.2.27"
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]
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},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "3zvz",
"name": "PHD finger of human UHRF1"
}
}
}
