About: MYND zinc finger

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In molecular biology the MYND-type zinc finger domain is a conserved protein domain. The MYND domain (myeloid, Nervy, and DEAF-1) is present in a large group of proteins that includes (PDCD2), , and predicted proteins from Drosophila, mammals, Caenorhabditis elegans, yeast, and plants. The MYND domain consists of a cluster of cysteine and histidine residues, arranged with an invariant spacing to form a potential zinc-binding motif. Mutating conserved cysteine residues in the DEAF-1 MYND domain does not abolish DNA binding, which suggests that the MYND domain might be involved in protein-protein interactions. Indeed, the MYND domain of ETO/MTG8 interacts directly with the N-CoR and SMRT co-repressors. Aberrant recruitment of co-repressor complexes and inappropriate transcriptional repressi

Attributes	Values
rdf:type	Thing Biomolecule Biomolecule Protein yago:Abstraction100002137 yago:Family108078020 yago:Group100031264 yago:Organization108008335 yago:YagoLegalActor yago:YagoLegalActorGeo yago:YagoPermanentlyLocatedEntity protein yago:SocialGroup107950920 yago:Unit108189659
rdfs:label	MYND zinc finger (en)
rdfs:comment	In molecular biology the MYND-type zinc finger domain is a conserved protein domain. The MYND domain (myeloid, Nervy, and DEAF-1) is present in a large group of proteins that includes (PDCD2), , and predicted proteins from Drosophila, mammals, Caenorhabditis elegans, yeast, and plants. The MYND domain consists of a cluster of cysteine and histidine residues, arranged with an invariant spacing to form a potential zinc-binding motif. Mutating conserved cysteine residues in the DEAF-1 MYND domain does not abolish DNA binding, which suggests that the MYND domain might be involved in protein-protein interactions. Indeed, the MYND domain of ETO/MTG8 interacts directly with the N-CoR and SMRT co-repressors. Aberrant recruitment of co-repressor complexes and inappropriate transcriptional repressi (en)
name	zf-MYND (en)
foaf:depiction
dct:subject	Protein domains
Wikipage page ID	32008778 (xsd:integer)
Wikipage revision ID	994931245 (xsd:integer)
Link from a Wikipage to another Wikipage	Caenorhabditis elegans Protein-protein interaction Proteins Nuclear receptor Nuclear receptor co-repressor 2 PDCD2 RUNX1 Conserved sequence Leukemia Mammal Mammalia Co-repressor Transcription (biology) DEAF-1 Cysteine Drosophila Chromosomal translocation Protein domain Residue (chemistry) Protein domains Histidine Acute myelogenous leukemia Adenovirus Yeast Zinc finger Plants N-CoR Repressor PLZF Leukemogenesis ETO/MTG8 dbr:Nervy_(gene) dbr:RP-8
sameAs	MYND zinc finger MYND zinc finger MYND zinc finger
dbp:wikiPageUsesTemplate	dbt:ELM dbt:Infobox_protein_family dbt:InterPro_content dbt:Reflist
thumbnail	wiki-commons:Special:FilePath/PDB_2dj8_EBI.jpg?width=300
caption	solution structure of zf-mynd domain of protein cbfa2ti (en)
InterPro	IPR002893 (en)
Pfam	PF01753 (en)
Pfam clan	CL0175 (en)
symbol	zf-MYND (en)
has abstract	In molecular biology the MYND-type zinc finger domain is a conserved protein domain. The MYND domain (myeloid, Nervy, and DEAF-1) is present in a large group of proteins that includes (PDCD2), , and predicted proteins from Drosophila, mammals, Caenorhabditis elegans, yeast, and plants. The MYND domain consists of a cluster of cysteine and histidine residues, arranged with an invariant spacing to form a potential zinc-binding motif. Mutating conserved cysteine residues in the DEAF-1 MYND domain does not abolish DNA binding, which suggests that the MYND domain might be involved in protein-protein interactions. Indeed, the MYND domain of ETO/MTG8 interacts directly with the N-CoR and SMRT co-repressors. Aberrant recruitment of co-repressor complexes and inappropriate transcriptional repression is believed to be a general mechanism of leukemogenesis caused by the t(8;21) translocations that fuse ETO with the acute myelogenous leukemia 1 (AML1) protein. ETO has been shown to be a co-repressor recruited by the promyelocytic leukemia zinc finger (PLZF) protein. A divergent MYND domain present in the adenovirus E1A binding protein BS69 was also shown to interact with N-CoR and mediate transcriptional repression. The current evidence suggests that the MYND motif in mammalian proteins constitutes a protein-protein interaction domain that functions as a co-repressor-recruiting interface. (en)
gold:hypernym	Domain
prov:wasDerivedFrom	wikipedia-en:MYND_zinc_finger?oldid=994931245&ns=0
page length (characters) of wiki page	5071 (xsd:nonNegativeInteger)
Symbol	zf-MYND
foaf:isPrimaryTopicOf	wikipedia-en:MYND_zinc_finger
is Link from a Wikipage to another Wikipage of	EGLN1 MYND finger MYND-type
is Wikipage redirect of	MYND finger MYND-type
is foaf:primaryTopic of	wikipedia-en:MYND_zinc_finger

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