{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P49959","secondaryAccessions":["B3KTC7","O43475"],"uniProtkbId":"MRE11_HUMAN","entryAudit":{"firstPublicDate":"1996-10-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2001-09-26","entryVersion":245,"sequenceVersion":3},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Double-strand break repair protein MRE11"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26240375"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27889449"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29670289"}],"value":"3.1.-.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8530104"}],"value":"Meiotic recombination 11 homolog 1"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8530104"}],"value":"MRE11 homolog 1"}]},{"fullName":{"value":"Meiotic recombination 11 homolog A"},"shortNames":[{"value":"MRE11 homolog A"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8530104"},{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:7230"}],"value":"MRE11"},"synonyms":[{"value":"HNGS1"},{"value":"MRE11A"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q61216"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10888888"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11741547"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14657032"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15064416"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15790808"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16622404"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22078559"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23080121"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24316220"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26240375"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27814491"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27889449"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28867292"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29670289"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30464262"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30612738"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30787182"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31353207"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31537797"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36050397"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36563124"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37696958"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38128537"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9590181"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9651580"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9705271"}],"value":"Core component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:11741547, PubMed:14657032, PubMed:22078559, PubMed:23080121, PubMed:24316220, PubMed:26240375, PubMed:27889449, PubMed:28867292, PubMed:29670289, PubMed:30464262, PubMed:30612738, PubMed:31353207, PubMed:37696958, PubMed:38128537, PubMed:9590181, PubMed:9651580, PubMed:9705271). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (PubMed:24316220, PubMed:28867292, PubMed:31353207, PubMed:38128537). The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (PubMed:24316220, PubMed:27889449, PubMed:28867292, PubMed:36050397, PubMed:38128537). Within the MRN complex, MRE11 possesses both single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity (PubMed:11741547, PubMed:22078559, PubMed:24316220, PubMed:26240375, PubMed:27889449, PubMed:29670289, PubMed:31353207, PubMed:36563124, PubMed:9590181, PubMed:9651580, PubMed:9705271). After DSBs, MRE11 is loaded onto DSBs sites and cleaves DNA by cooperating with RBBP8/CtIP to initiate end resection (PubMed:27814491, PubMed:27889449, PubMed:30787182). MRE11 first endonucleolytically cleaves the 5' strand at DNA DSB ends to prevent non-homologous end joining (NHEJ) and licence HR (PubMed:24316220). It then generates a single-stranded DNA gap via 3' to 5' exonucleolytic degradation to create entry sites for EXO1- and DNA2-mediated 5' to 3' long-range resection, which is required for single-strand invasion and recombination (PubMed:24316220, PubMed:28867292). RBBP8/CtIP specifically promotes the endonuclease activity of MRE11 to clear protein-DNA adducts and generate clean double-strand break ends (PubMed:27814491, PubMed:27889449, PubMed:30787182). MRE11 endonuclease activity is also enhanced by AGER/RAGE (By similarity). The MRN complex is also required for DNA damage signaling via activation of the ATM and ATR kinases: the nuclease activity of MRE11 is not required to activate ATM and ATR (PubMed:14657032, PubMed:15064416, PubMed:15790808, PubMed:16622404). The MRN complex is also required for the processing of R-loops (PubMed:31537797). The MRN complex is involved in the activation of the cGAS-STING pathway induced by DNA damage during tumorigenesis: the MRN complex acts by displacing CGAS from nucleosome sequestration, thereby activating it (By similarity). In telomeres the MRN complex may modulate t-loop formation (PubMed:10888888)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"MRE11 contains two DNA-binding domains (DBDs), enabling it to bind both single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA)"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22078559"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36577401"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24316220"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27814491"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27889449"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29670289"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30464262"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30787182"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31353207"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37696958"}],"value":"Interaction with SAMHD1 stimulates the double-strand-specific 3'-5' exonuclease activity (PubMed:29670289). RBBP8/CtIP specifically promotes the endonuclease activity to clear protein-DNA adducts and generate clean double-strand break ends (PubMed:27814491, PubMed:27889449, PubMed:30787182). DYNLL1-binding inhibits the activity of MRE11 (PubMed:30464262, PubMed:37696958). MRE11 activity is inhibited by C1QBP: in absence of DNA damage, C1QBP interacts with unphosphorylated MRE11, preventing formation and activity of the MRN complex (PubMed:31353207). The mirin-derivative PFM39, specifically inhibits the 3'-5' exonuclease activity (PubMed:24316220). The N-alkylated mirin-derivatives PFM03 and PFM01 specifically inhibit the endonuclease activity (PubMed:24316220)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q61216"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10783165"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10839544"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10888888"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15456891"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15723659"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15916964"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18469862"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26215093"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26807646"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27568553"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28834754"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28867292"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29651020"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29670289"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30464262"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30612738"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31353207"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33918759"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36577401"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37696958"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9590181"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9651580"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9705271"}],"value":"Component of the MRN complex composed of two heterodimers RAD50 and MRE11 associated with a single NBN (PubMed:10839544, PubMed:26215093, PubMed:28867292, PubMed:9590181, PubMed:9651580, PubMed:9705271). The MRN complexes dimerize on DNA to form joined MRN-MRN oligomers required for DNA double-strand break repair (PubMed:36577401). As part of the MRN complex, interacts with MCM9; the interaction recruits the complex to DNA repair sites (PubMed:26215093). Component of the BASC complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM, BLM, RAD50, MRE11 and NBN (PubMed:10783165). Found in a complex with TERF2 (PubMed:10888888). Interacts with DCLRE1C/Artemis and DCLRE1B/Apollo (PubMed:15456891, PubMed:15723659, PubMed:18469862). Interacts with ATF2 (PubMed:15916964). Interacts with EXD2 (PubMed:26807646). Interacts with MRNIP (PubMed:27568553). Interacts with SAMHD1; leading to stimulate 3'-5' exonuclease activity (PubMed:28834754, PubMed:29670289). Interacts (when ubiquitinated) with UBQLN4 (via its UBA domain) (PubMed:30612738). Interacts with CYREN (via XLF motif) (By similarity). Interacts with GFI1; promoting methylation by PRMT1 (PubMed:29651020). Interacts with DYNLL1; inhibiting the activity of MRE11 (PubMed:30464262, PubMed:37696958). Interacts with C1QBP and RAD50; interaction takes place in absence of DNA damage to form the MRC (MRE11-RAD50-C1QBP) complex that inhibits the activity of MRE11 (PubMed:31353207). Interacts with AGER/RAGE (PubMed:33918759). AGER is recruited to DNA double-strand break sites where it enhances MRE11 endonuclease activity to promote DNA repair (By similarity)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20943970"}],"value":"(Microbial infection) Interacts with herpes simplex virus 1 protein UL12 (PubMed:20943970)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P49959","intActId":"EBI-396513"},"interactantTwo":{"uniProtKBAccession":"Q9BXW9","geneName":"FANCD2","intActId":"EBI-359343"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P49959","intActId":"EBI-396513"},"interactantTwo":{"uniProtKBAccession":"P16104","geneName":"H2AX","intActId":"EBI-494830"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P49959","intActId":"EBI-396513"},"interactantTwo":{"uniProtKBAccession":"P42858","geneName":"HTT","intActId":"EBI-466029"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P49959","intActId":"EBI-396513"},"interactantTwo":{"uniProtKBAccession":"P49959","geneName":"MRE11","intActId":"EBI-396513"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P49959","intActId":"EBI-396513"},"interactantTwo":{"uniProtKBAccession":"O60934","geneName":"NBN","intActId":"EBI-494844"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P49959","intActId":"EBI-396513"},"interactantTwo":{"uniProtKBAccession":"O75943","geneName":"RAD17","intActId":"EBI-968231"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P49959","intActId":"EBI-396513"},"interactantTwo":{"uniProtKBAccession":"Q99708","geneName":"RBBP8","intActId":"EBI-745715"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P49959","intActId":"EBI-396513"},"interactantTwo":{"uniProtKBAccession":"P03243-1","intActId":"EBI-1927377"},"numberOfExperiments":2,"organismDiffer":true}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15916964"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26240375"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28512243"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30612738"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36050397"}],"value":"Localizes to DNA double-strand breaks (DSBs)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10783165"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26215093"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15916964"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26215093"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26240375"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28512243"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30612738"}],"value":"Chromosome","id":"SL-0468"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10888888"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36050397"}],"value":"Chromosome, telomere","id":"SL-0276"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["P49959-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["P49959-2"],"sequenceIds":["VSP_003262"],"isoformSequenceStatus":"Described"},{"name":{"value":"3"},"isoformIds":["P49959-3"],"sequenceIds":["VSP_057350"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16601701"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26240375"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28512243"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31353207"}],"value":"Phosphorylated by ATM at Ser-676 and Ser-678 in response to DNA damage, promoting MRE11 activity: phosphorylation activates MRE11 by preventing the interaction between MRE11 and the C1QBP inhibitor (PubMed:16601701, PubMed:26240375, PubMed:31353207). Phosphorylation at Ser-649 by PLK1 primes for phosphorylation at Ser-688 by CK2, inhibiting recruitment of the MRN complex to DNA damage sites (PubMed:28512243)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15741314"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29651020"}],"value":"Asymmetric dimethylation by PRMT1 promotes MRE11 exonuclease activity"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38128537"}],"value":"Lactylation at Lys-673 by CREBBP/CBP in response to DNA damage promotes DNA binding and MRE11 activity"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38128537"}],"value":"Acetylated on lysine residues by KAT2A /GCN5"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30612738"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36563124"}],"value":"Ubiquitinated following DNA damage (PubMed:30612738). Ubiquitination triggers interaction with UBQLN4, leading to MRE11 removal from chromatin and degradation by the proteasome (PubMed:30612738). Ubiquitinated at Lys-339 and Lys-480 by RNF126 via 'Lys-27'- and 'Lys-29'-linked polyubiquitin chains, promoting the exonuclease activity of MRE11 (PubMed:36563124)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36050397"}],"value":"SUMOylated by PIAS1, stabilizing MRE11 on chromatin during end resection (PubMed:36050397). DeSUMOylated by SENP3 following removal from DNA double-strand breaks (DSBs) (PubMed:36050397)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30783677"}],"value":"Ufmylation at Lys-282 promotes MRE11 activity and is required for activation of the ATM and ATR kinases by the MRN complex"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12124628"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14657032"}],"value":"(Microbial infection) Following infection by adenovirus E4, ubiquitinated and degraded by a SCF-like E3 ubiquitin ligase complex containing viral proteins E1B-55K and E4-ORF6"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Ataxia-telangiectasia-like disorder 1","diseaseAccession":"DI-00140","acronym":"ATLD1","description":"A rare disorder characterized by progressive cerebellar ataxia, dysarthria, abnormal eye movements, and absence of telangiectasia. ATLD patients show normal levels of total IgG, IgA and IgM, although there may be reduced levels of specific functional antibodies. At the cellular level, ATLD exhibits hypersensitivity to ionizing radiation and radioresistant DNA synthesis.","diseaseCrossReference":{"database":"MIM","id":"604391"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10612394"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11371508"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15269180"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15574463"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19732584"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23080121"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24332946"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22863007"}],"value":"Defects in MRE11 can be a cause of nephronophthisis-related ciliopathies (NPHP-RC), a group of recessive diseases that affect kidney, retina and brain. A homozygous truncating mutation MRE11 has been found in patients with cerebellar vermis hypoplasia, ataxia and dysarthria"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the MRE11/RAD32 family"}],"commentType":"SIMILARITY"},{"commentType":"WEB RESOURCE","resourceName":"Atlas of Genetics and Cytogenetics in Oncology and Haematology","resourceUrl":"https://atlasgeneticsoncology.org/gene/247/MRE11","ftp":false},{"commentType":"WEB RESOURCE","resourceName":"MRE11base","resourceUrl":"https://databases.lovd.nl/shared/genes/MRE11A","ftp":false,"note":"MRE11A mutation db"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"19413330"},{"evidenceCode":"ECO:0007744","source":"PubMed","id":"22223895"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":708,"modifier":"EXACT"}},"description":"Double-strand break repair protein MRE11","featureId":"PRO_0000138672"},{"type":"Region","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"Interaction with NBN","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22078559"}]},{"type":"Region","location":{"start":{"value":507,"modifier":"EXACT"},"end":{"value":540,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":556,"modifier":"EXACT"},"end":{"value":614,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":651,"modifier":"EXACT"},"end":{"value":708,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Motif","location":{"start":{"value":570,"modifier":"EXACT"},"end":{"value":594,"modifier":"EXACT"}},"description":"GAR","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15741314"}]},{"type":"Compositional 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