{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q99708","secondaryAccessions":["A6NKN2","A8K8W6","E7ETY1","O75371","Q8NHQ3"],"uniProtkbId":"CTIP_HUMAN","entryAudit":{"firstPublicDate":"2000-12-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2006-10-17","entryVersion":217,"sequenceVersion":2},"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":"DNA endonuclease RBBP8"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19202191"}],"value":"3.1.-.-"}]},"alternativeNames":[{"fullName":{"value":"CtBP-interacting protein"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"31802118"}],"value":"CtIP"}]},{"fullName":{"value":"Retinoblastoma-binding protein 8"},"shortNames":[{"value":"RBBP-8"}]},{"fullName":{"value":"Retinoblastoma-interacting protein and myosin-like"},"shortNames":[{"value":"RIM"}]},{"fullName":{"value":"Sporulation in the absence of SPO11 protein 2 homolog"},"shortNames":[{"value":"SAE2"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:9891"}],"value":"RBBP8"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"31802118"}],"value":"CTIP"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q80YR6"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15485915"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16581787"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16818604"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17965729"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19202191"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19759395"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20064462"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23273981"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26721387"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27814491"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27889449"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30601117"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30787182"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31802118"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33836577"}],"value":"Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in DNA-end resection, the first step of double-strand break (DSB) repair through the homologous recombination (HR) pathway (PubMed:17965729, PubMed:19202191, PubMed:19759395, PubMed:20064462, PubMed:23273981, PubMed:26721387, PubMed:27814491, PubMed:27889449, PubMed:30787182, PubMed:31802118). HR is restricted to S and G2 phases of the cell cycle and preferentially repairs DSBs resulting from replication fork collapse (PubMed:17965729, PubMed:19202191, PubMed:23273981, PubMed:27814491, PubMed:27889449, PubMed:30787182). Key determinant of DSB repair pathway choice, as it commits cells to HR by preventing classical non-homologous end-joining (NHEJ) (PubMed:19202191). Specifically promotes the endonuclease activity of the MRN complex to clear DNA ends containing protein adducts: recruited to DSBs by NBN following phosphorylation by CDK1, and promotes the endonuclease activity of MRE11 to clear protein-DNA adducts and generate clean double-strand break ends (PubMed:27814491, PubMed:27889449, PubMed:30787182, PubMed:33836577). Functions downstream of the MRN complex and ATM, promotes ATR activation and its recruitment to DSBs in the S/G2 phase facilitating the generation of ssDNA (PubMed:16581787, PubMed:17965729, PubMed:19759395, PubMed:20064462). Component of the BRCA1-RBBP8 complex that regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage (PubMed:15485915, PubMed:16818604). During immunoglobulin heavy chain class-switch recombination, promotes microhomology-mediated alternative end joining (A-NHEJ) and plays an essential role in chromosomal translocations (By similarity). Binds preferentially to DNA Y-junctions and to DNA substrates with blocked ends and promotes intermolecular DNA bridging (PubMed:30601117)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10764811"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11751867"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14654780"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15084581"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15485915"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16101277"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16818604"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17965729"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19759395"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23353824"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23623683"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25349192"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25558984"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26502057"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26721387"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26807646"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27561354"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28834754"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29042561"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30601117"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31802118"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34129781"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9535825"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9721205"}],"value":"Homotetramer; formed by antiparallel association of helical extensions protruding from the N-termini of two parallel coiled-coil dimers (PubMed:15084581, PubMed:25558984, PubMed:30601117, PubMed:34129781). Forms a dumbbell-shaped particle in which polar globular domains are held about 30 nm apart by a central rod (PubMed:30601117). Homotetramerization is required for DNA-end resection and repair (PubMed:25558984). Interacts (via the PXDLS motif) with CTBP1; the interaction is disrupted via binding of the adenovirus E1A to CTBP1 (PubMed:9535825). Component of the BRCA1-RBBP8 complex. Interacts (the Ser-327 phosphorylated form) with BRCA1 (via the C-terminal BRCT domains): the interaction occurs in the G2 phase, ubiquitinates RBBP8 and involves RBBP8 in BRCA1-dependent G2/M checkpoint control on DNA damage (PubMed:10764811, PubMed:15485915, PubMed:16101277, PubMed:16818604, PubMed:17965729, PubMed:23623683). Interacts with RB1 (PubMed:9721205). Interacts with the MRN complex; interacts directly with MRE11; the interaction is required for efficient homologous recombination (HR) and regulation of the MRN complex (PubMed:19759395, PubMed:23623683, PubMed:25558984). Interacts directly with RAD50 (PubMed:19759395, PubMed:25558984). Interacts (when phosphorylated by CDK1) with NBN; promoting association with the MRN complex (PubMed:19759395, PubMed:25558984). Interacts with LM04 (via the LIM zinc-binding 1 domain) (PubMed:11751867, PubMed:23353824). Interacts with SIAH1 (PubMed:14654780). Interacts with RNF138 (PubMed:26502057). Interacts with EXD2 (PubMed:26807646). Interacts with CUL3 and KLHL15; this interaction leads to RBBP8 proteasomal degradation (PubMed:27561354). Directly interacts with PIN1; this interaction depends upon RBBP8 phosphorylation, predominantly at Thr-315 (PubMed:23623683). Interacts with FZR1; this interaction leads to APC/C-mediated RBBP8 proteasomal degradation (PubMed:25349192). Interacts with AUNIP; leading to recruitment of RBBP8 to sites of DNA damage (PubMed:10764811, PubMed:11751867, PubMed:14654780, PubMed:15084581, PubMed:15485915, PubMed:16818604, PubMed:17965729, PubMed:19759395, PubMed:23623683, PubMed:25349192, PubMed:26502057, PubMed:26807646, PubMed:27561354, PubMed:29042561, PubMed:9535825, PubMed:9721205). Interacts with SAMHD1 (PubMed:28834754). Interacts with HDGFL2 (PubMed:26721387). Interacts with HELLS; the interaction leads to recruitment of RBBP8/CtIP to sites of DNA breaks (PubMed:31802118)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q99708","intActId":"EBI-745715"},"interactantTwo":{"uniProtKBAccession":"P38398","geneName":"BRCA1","intActId":"EBI-349905"},"numberOfExperiments":15,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99708","intActId":"EBI-745715"},"interactantTwo":{"uniProtKBAccession":"Q9NVH0","geneName":"EXD2","intActId":"EBI-11324738"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99708","intActId":"EBI-745715"},"interactantTwo":{"uniProtKBAccession":"Q9UQ84","geneName":"EXO1","intActId":"EBI-944667"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99708","intActId":"EBI-745715"},"interactantTwo":{"uniProtKBAccession":"P49959","geneName":"MRE11","intActId":"EBI-396513"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99708","intActId":"EBI-745715"},"interactantTwo":{"uniProtKBAccession":"O60934","geneName":"NBN","intActId":"EBI-494844"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99708","intActId":"EBI-745715"},"interactantTwo":{"uniProtKBAccession":"O75475","geneName":"PSIP1","intActId":"EBI-1801773"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99708","intActId":"EBI-745715"},"interactantTwo":{"uniProtKBAccession":"P06400","geneName":"RB1","intActId":"EBI-491274"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99708","intActId":"EBI-745715"},"interactantTwo":{"uniProtKBAccession":"Q99708","geneName":"RBBP8","intActId":"EBI-745715"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99708-2","intActId":"EBI-10203615"},"interactantTwo":{"uniProtKBAccession":"P25800","geneName":"LMO1","intActId":"EBI-8639312"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99708-2","intActId":"EBI-10203615"},"interactantTwo":{"uniProtKBAccession":"P61968","geneName":"LMO4","intActId":"EBI-2798728"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99708-2","intActId":"EBI-10203615"},"interactantTwo":{"uniProtKBAccession":"Q13526","geneName":"PIN1","intActId":"EBI-714158"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q99708-2","intActId":"EBI-10203615"},"interactantTwo":{"uniProtKBAccession":"Q08999","geneName":"RBL2","intActId":"EBI-971439"},"numberOfExperiments":3,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10764811"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16818604"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25349192"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27814491"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27889449"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33836577"}],"value":"Associates with sites of DNA damage in S/G2 phase (PubMed:10764811, PubMed:25349192). Recruited to DSBs by the MRE11-RAD50-NBN (MRN) complex following phosphorylation by CDK1, which promotes interaction with NBN (PubMed:27814491, PubMed:27889449, PubMed:33836577). Ubiquitinated RBBP8 binds to chromatin following DNA damage (PubMed:16818604)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10764811"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17965729"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23623683"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10764811"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16818604"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27814491"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27889449"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29042561"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33836577"}],"value":"Chromosome","id":"SL-0468"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q99708-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q99708-2"],"sequenceIds":["VSP_043220"],"isoformSequenceStatus":"Described"},{"name":{"value":"3"},"isoformIds":["Q99708-3"],"sequenceIds":["VSP_045247","VSP_045248"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18171986"}],"value":"Expressed in ER-positive breast cancer lines, but tends to be down-regulated ER-negative cells (at protein level)"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18171986"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25349192"}],"value":"Expression is cell-cycle regulated. Levels increase as dividing cells traverse the G1/S boundary (PubMed:18171986). The protein is degraded by the proteasome pathway during mitotic exit. Also degraded in response to DNA damage in G2 cells; this degradation is mediated by the E3 FZR1/APC/C complex (PubMed:25349192)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9535825"}],"value":"The PXDLS motif binds to a cleft in CtBP proteins"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20064462"}],"value":"The damage-recruitment motif is required for DNA binding and translocation to sites of DNA damage"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10910365"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15485915"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17965729"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19202191"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23273981"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23623683"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27814491"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27889449"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30601117"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33836577"}],"value":"Hyperphosphorylation upon ionizing radiation results in dissociation from BRCA1 (PubMed:10910365, PubMed:17965729). Phosphorylation at Thr-847 by CDK1 is essential for the recruitment to DNA and the DNA repair function (PubMed:19202191, PubMed:27814491, PubMed:27889449). Phosphorylation at Thr-847 and Thr-859 promote interaction with NBN and recruitment to double-strand breaks (DSBs) (PubMed:23273981, PubMed:27814491, PubMed:27889449, PubMed:33836577). Phosphorylated on Ser-327 as cells enter G2 phase (PubMed:15485915). This phosphorylation is required for binding BRCA1 and for the G2/M DNA damage transition checkpoint control (PubMed:15485915). Phosphorylation at Thr-315, probably catalyzed by CDK2, is required for PIN1-binding, while phosphorylation at Ser-276 serves as a PIN1 isomerization site (PubMed:23623683). Phosphorylation at Thr-315 is cell-cycle dependent (PubMed:23623683). It steadily increases during S phase, peaks at late S/G2 phase, and drops at G1 (PubMed:23623683). Phosphorylation is not required for tetramerization (PubMed:30601117). Binds to DNA more strongly when dephosphorylated (PubMed:30601117)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14654780"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16818604"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25349192"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26502057"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27561354"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35219381"}],"value":"Ubiquitinated (PubMed:14654780, PubMed:16818604, PubMed:27561354). Ubiquitination at multiple sites by BRCA1 (via its N-terminal RING domain) does not lead to its proteasomal degradation but instead the ubiquitinated RBBP8 binds to chromatin following DNA damage and may play a role in G2/M checkpoint control (PubMed:16818604). Ubiquitinated by RNF138 at its N-terminus (PubMed:26502057). Ubiquitinated through 'Lys-48' by the E3 CUL3-KLHL15 complex; this modification leads to proteasomal degradation (PubMed:27561354, PubMed:35219381). Ubiquitinated by the E3 FZR1/APC/C complex; this modification leads to proteasomal degradation (PubMed:25349192)"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Seckel syndrome 2","diseaseAccession":"DI-03353","acronym":"SCKL2","description":"A rare autosomal recessive disorder characterized by proportionate dwarfism of prenatal onset associated with low birth weight, growth retardation, severe microcephaly with a bird-headed like appearance, and intellectual disability.","diseaseCrossReference":{"database":"MIM","id":"606744"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21998596"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24389050"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Jawad syndrome","diseaseAccession":"DI-03354","acronym":"JWDS","description":"A syndrome characterized by congenital microcephaly, moderately severe intellectual disability, and symmetrical digital anomalies. Digital malformations of variable degree include hallux valgus, syndactyly of toes 4 and 5, short fifth fingers, single flexion crease of fifth fingers, polydactyly and synpolydactyly.","diseaseCrossReference":{"database":"MIM","id":"251255"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21998596"}]},"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":"18171986"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21799032"}],"value":"Genetic variability in RBBP8 is noted as a factor in BRCA1-associated breast cancer risk (PubMed:21799032). Associated with sensitivity to tamoxifen in certain breast cancer cell lines (PubMed:18171986)"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25558984"}],"value":"Binds one Zn(2+) atom per dimer. Zn(2+)-binding is not required for homotetramerization"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the COM1/SAE2/CtIP family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"20829486"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"30975768"}],"value":"Upon DNA damage, was shown to interact with SIRT6 resulting in its deacetylation. However, this study was later retracted"}],"commentType":"CAUTION"},{"commentType":"WEB RESOURCE","resourceName":"Atlas of Genetics and Cytogenetics in Oncology and Haematology","resourceUrl":"https://atlasgeneticsoncology.org/gene/42066/RBBP8","ftp":false}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":897,"modifier":"EXACT"}},"description":"DNA endonuclease RBBP8","featureId":"PRO_0000097179"},{"type":"Region","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"Essential for binding to the MRN complex and for RPA focus formation on DNA damage"},{"type":"Region","location":{"start":{"value":45,"modifier":"EXACT"},"end":{"value":160,"modifier":"EXACT"}},"description":"Required for interaction with LMO4, probably by stabilizing the interaction through RPPB8 dimerization","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23353824"}]},{"type":"Region","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":325,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":419,"modifier":"EXACT"},"end":{"value":464,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":509,"modifier":"EXACT"},"end":{"value":557,"modifier":"EXACT"}},"description":"Damage-recruitment motif","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20064462"}]},{"type":"Region","location":{"start":{"value":641,"modifier":"EXACT"},"end":{"value":685,"modifier":"EXACT"}},"description":"Required for interaction with LMO4, probably by making physical contact with LMO4","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23353824"}]},{"type":"Region","location":{"start":{"value":704,"modifier":"EXACT"},"end":{"value":723,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":873,"modifier":"EXACT"},"end":{"value":897,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Coiled coil","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34129781"}]},{"type":"Coiled coil","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34129781"}]},{"type":"Motif","location":{"start":{"value":490,"modifier":"EXACT"},"end":{"value":494,"modifier":"EXACT"}},"description":"PXDLS motif","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9535825"}]},{"type":"Motif","location":{"start":{"value":840,"modifier":"EXACT"},"end":{"value":842,"modifier":"EXACT"}},"description":"KLHL15-binding","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27561354"}]},{"type":"Compositional bias","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":307,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":420,"modifier":"EXACT"},"end":{"value":436,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Modified residue","location":{"start":{"value":233,"modifier":"EXACT"},"end":{"value":233,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"23186163"}]},{"type":"Modified residue","location":{"start":{"value":276,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23623683"}]},{"type":"Modified residue","location":{"start":{"value":315,"modifier":"EXACT"},"end":{"value":315,"modifier":"EXACT"}},"description":"Phosphothreonine; 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