{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9NQC7","secondaryAccessions":["O94934","Q7L3N6","Q96EH0","Q9NZX9"],"uniProtkbId":"CYLD_HUMAN","entryAudit":{"firstPublicDate":"2004-08-16","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2000-10-01","entryVersion":212,"sequenceVersion":1},"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":{"value":"Ubiquitin carboxyl-terminal hydrolase CYLD"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18313383"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27458237"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27591049"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27746020"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32185393"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34497368"}],"value":"3.4.19.12"}]},"alternativeNames":[{"fullName":{"value":"Deubiquitinating enzyme CYLD"}},{"fullName":{"value":"Ubiquitin thioesterase CYLD"}},{"fullName":{"value":"Ubiquitin-specific-processing protease CYLD"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"12917689"},{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:2584"}],"value":"CYLD"},"synonyms":[{"value":"CYLD1"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10048485"}],"value":"KIAA0849"}],"orfNames":[{"value":"HSPC057"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q80TQ2"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12917689"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12917690"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12917691"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17495026"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18222923"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18313383"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18636086"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19481526"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19893491"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20194890"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20227366"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26670046"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26997266"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27458237"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27591049"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27746020"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29291351"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32185393"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34497368"}],"value":"Deubiquitinase that specifically cleaves 'Lys-63'- and linear 'Met-1'-linked polyubiquitin chains and is involved in NF-kappa-B activation and TNF-induced necroptosis (PubMed:18313383, PubMed:18636086, PubMed:19481526, PubMed:26670046, PubMed:26997266, PubMed:27458237, PubMed:27591049, PubMed:27746020, PubMed:29291351, PubMed:32185393). Negatively regulates NF-kappa-B activation by deubiquitinating upstream signaling factors (PubMed:12917689, PubMed:12917691, PubMed:19481526, PubMed:32185393). Contributes to the regulation of cell survival, proliferation and differentiation via its effects on NF-kappa-B activation (PubMed:12917690). Negative regulator of Wnt signaling (PubMed:20227366). Inhibits HDAC6 and thereby promotes acetylation of alpha-tubulin and stabilization of microtubules (PubMed:19893491). Plays a role in the regulation of microtubule dynamics, and thereby contributes to the regulation of cell proliferation, cell polarization, cell migration, and angiogenesis (PubMed:18222923, PubMed:20194890). Required for normal cell cycle progress and normal cytokinesis (PubMed:17495026, PubMed:19893491). Inhibits nuclear translocation of NF-kappa-B (PubMed:18636086). Plays a role in the regulation of inflammation and the innate immune response, via its effects on NF-kappa-B activation (PubMed:18636086). Dispensable for the maturation of intrathymic natural killer cells, but required for the continued survival of immature natural killer cells (By similarity). Negatively regulates TNFRSF11A signaling and osteoclastogenesis (By similarity). Involved in the regulation of ciliogenesis, allowing ciliary basal bodies to migrate and dock to the plasma membrane; this process does not depend on NF-kappa-B activation (By similarity). Ability to remove linear ('Met-1'-linked) polyubiquitin chains regulates innate immunity and TNF-induced necroptosis: recruited to the LUBAC complex via interaction with SPATA2 and restricts linear polyubiquitin formation on target proteins (PubMed:26670046, PubMed:26997266, PubMed:27458237, PubMed:27591049). Regulates innate immunity by restricting linear polyubiquitin formation on RIPK2 in response to NOD2 stimulation (PubMed:26997266). Involved in TNF-induced necroptosis by removing linear ('Met-1'-linked) polyubiquitin chains from RIPK1, thereby regulating the kinase activity of RIPK1 (By similarity). Negatively regulates intestinal inflammation by removing 'Lys-63' linked polyubiquitin chain of NLRP6, thereby reducing the interaction between NLRP6 and PYCARD/ASC and formation of the NLRP6 inflammasome (By similarity). Does not catalyze deubiquitination of heterotypic 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains (PubMed:27746020). Removes 'Lys-63' linked polyubiquitin chain of MAP3K7, which inhibits phosphorylation and blocks downstream activation of the JNK-p38 kinase cascades (PubMed:29291351). Also removes 'Lys-63'-linked polyubiquitin chains of MAP3K1 and MA3P3K3, which inhibit their interaction with MAP2K1 and MAP2K2 (PubMed:34497368)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).","ecNumber":"3.4.19.12","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18313383"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19481526"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27458237"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27591049"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27746020"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32185393"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15870263"}],"value":"Inhibited by phosphorylation at serine residues"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q80TQ2"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12917689"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12917690"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12917691"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14676304"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15341735"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17495026"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18636086"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19893491"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20227366"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25134987"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26997266"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27307491"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27458237"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27545878"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27591049"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32185393"}],"value":"Interacts (via CAP-Gly domain) with IKBKG/NEMO (via proline-rich C-terminal region) (PubMed:12917689, PubMed:12917690, PubMed:12917691, PubMed:15341735). Interacts with TRAF2 and TRIP (PubMed:12917691, PubMed:14676304). Interacts with PLK1, DVL1, DVL3, MAVS, TBK1, IKKE and RIGI (PubMed:17495026, PubMed:18636086, PubMed:20227366, PubMed:32185393). Interacts (via CAP-Gly domain) with microtubules (PubMed:19893491). Interacts with HDAC6 and BCL3 (PubMed:19893491). Interacts with MAP3K7 (By similarity). Identified in a complex with TRAF6 and SQSTM1 (By similarity). Interacts with OPTN and SQSTM1 (PubMed:32185393). Interacts with CEP350 (PubMed:25134987). Interacts with RNF31; the interaction is indirect and is mediated via SPATA2 (PubMed:26997266). Interacts with SPATA2 (via the PUB domain); the interaction is direct and recruits CYLD to the LUBAC complex, thereby regulating TNF-induced necroptosis (PubMed:27307491, PubMed:27458237, PubMed:27545878, PubMed:27591049)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q9NQC7","intActId":"EBI-2117940"},"interactantTwo":{"uniProtKBAccession":"Q9UBN7","geneName":"HDAC6","intActId":"EBI-301697"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9NQC7","intActId":"EBI-2117940"},"interactantTwo":{"uniProtKBAccession":"Q96J02","geneName":"ITCH","intActId":"EBI-1564678"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9NQC7","intActId":"EBI-2117940"},"interactantTwo":{"uniProtKBAccession":"Q96J02-2","geneName":"ITCH","intActId":"EBI-6672198"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9NQC7","intActId":"EBI-2117940"},"interactantTwo":{"uniProtKBAccession":"O95786","geneName":"RIGI","intActId":"EBI-995350"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9NQC7","intActId":"EBI-2117940"},"interactantTwo":{"uniProtKBAccession":"Q9UM82","geneName":"SPATA2","intActId":"EBI-744066"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9NQC7","intActId":"EBI-2117940"},"interactantTwo":{"uniProtKBAccession":"Q71U36","geneName":"TUBA1A","intActId":"EBI-302552"},"numberOfExperiments":6,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q80TQ2"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25134987"}],"value":"Detected at the microtubule cytoskeleton during interphase. Detected at the midbody during telophase. During metaphase, it remains localized to the centrosome but is also present along the spindle (PubMed:25134987)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18313383"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32185393"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"value":"Cytoplasm, perinuclear region","id":"SL-0198"}},{"location":{"value":"Cytoplasm, cytoskeleton","id":"SL-0090"}},{"location":{"value":"Cell membrane","id":"SL-0039"},"topology":{"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"value":"Cytoplasmic side","id":"SL-9910"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25134987"}],"value":"Cytoplasm, cytoskeleton, microtubule organizing center, centrosome","id":"SL-0048"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25134987"}],"value":"Cytoplasm, cytoskeleton, spindle","id":"SL-0251"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q80TQ2"}],"value":"Cytoplasm, cytoskeleton, cilium basal body","id":"SL-0087"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q9NQC7-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q9NQC7-2"],"sequenceIds":["VSP_011277"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10835629"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29291351"}],"value":"Detected in fetal brain, testis, and skeletal muscle, and at a lower level in adult brain, leukocytes, liver, heart, kidney, spleen, ovary and lung. Isoform 2 is found in all tissues except kidney"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29291351"}],"value":"Ubiquitinated. Polyubiquitinated in hepatocytes treated with palmitic acid. Ubiquitination is mediated by E3 ligase TRIM47 and leads to proteasomal degradation"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15870263"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19481526"}],"value":"Phosphorylated on several serine residues by IKKA and/or IKKB in response to immune stimuli (PubMed:15870263). Phosphorylation requires IKBKG (PubMed:15870263). Phosphorylation abolishes TRAF2 deubiquitination, interferes with the activation of Jun kinases, and strongly reduces CD40-dependent gene activation by NF-kappa-B (PubMed:15870263). Phosphorylation at Ser-418 by IKKE/IKBKE inhibits the deubiquitinase activity, leading to activation by NF-kappa-B (PubMed:19481526)"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Cylindromatosis, familial","diseaseAccession":"DI-01564","acronym":"FCYL","description":"A disorder characterized by multiple skin tumors that develop from skin appendages, such as hair follicles and sweat glands. Affected individuals typically develop large numbers of tumors called cylindromas that arise predominantly in hairy parts of the body with approximately 90% on the head and neck. In severely affected individuals, cylindromas may combine into a confluent mass which may ulcerate or become infected (turban tumor syndrome). Individuals with familial cylindromatosis occasionally develop other types of tumors including spiradenomas that begin in sweat glands, and trichoepitheliomas arising from hair follicles.","diseaseCrossReference":{"database":"MIM","id":"132700"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12190880"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16922728"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Trichoepithelioma, multiple familial, 1","diseaseAccession":"DI-02007","acronym":"MFT1","description":"An autosomal dominant dermatosis characterized by the presence of many skin tumors predominantly on the face. Since histologic examination shows dermal aggregates of basaloid cells with connection to or differentiation toward hair follicles, this disorder has been thought to represent a benign hamartoma of the pilosebaceous apparatus. Trichoepitheliomas can degenerate into basal cell carcinoma.","diseaseCrossReference":{"database":"MIM","id":"601606"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14632188"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16307661"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16922728"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Brooke-Spiegler syndrome","diseaseAccession":"DI-00201","acronym":"BRSS","description":"An autosomal dominant disorder characterized by the appearance of multiple skin appendage tumors such as cylindroma, trichoepithelioma, and spiradenoma. These tumors are typically located in the head and neck region, appear in early adulthood, and gradually increase in size and number throughout life.","diseaseCrossReference":{"database":"MIM","id":"605041"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12190880"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12950348"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14632188"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15854031"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"commentType":"DISEASE","disease":{"diseaseId":"Frontotemporal dementia and/or amyotrophic lateral sclerosis 8","diseaseAccession":"DI-06000","acronym":"FTDALS8","description":"A neurodegenerative disorder characterized by frontotemporal dementia and/or amyotrophic lateral sclerosis in affected individuals. There is high intrafamilial variation. Frontotemporal dementia is characterized by frontal and temporal lobe atrophy associated with neuronal loss, gliosis, and dementia. Patients exhibit progressive changes in social, behavioral, and/or language function. Amyotrophic lateral sclerosis is characterized by the death of motor neurons in the brain, brainstem, and spinal cord, resulting in fatal paralysis. FTDALS8 is an autosomal dominant form.","diseaseCrossReference":{"database":"MIM","id":"619132"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23338750"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32185393"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32666117"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the peptidase C19 family"}],"commentType":"SIMILARITY"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Frameshift","sequence":"AAF29029.1","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"BAA74872.2","note":"Extended N-terminus.","evidences":[{"evidenceCode":"ECO:0000305"}]},{"commentType":"WEB RESOURCE","resourceName":"Atlas of Genetics and Cytogenetics in Oncology and Haematology","resourceUrl":"https://atlasgeneticsoncology.org/gene/40232/CYLD","ftp":false}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":956,"modifier":"EXACT"}},"description":"Ubiquitin carboxyl-terminal hydrolase CYLD","featureId":"PRO_0000080698"},{"type":"Domain","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"CAP-Gly 1","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00045"}]},{"type":"Domain","location":{"start":{"value":253,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"CAP-Gly 2","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00045"}]},{"type":"Domain","location":{"start":{"value":492,"modifier":"EXACT"},"end":{"value":535,"modifier":"EXACT"}},"description":"CAP-Gly 3","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00045"}]},{"type":"Domain","location":{"start":{"value":592,"modifier":"EXACT"},"end":{"value":950,"modifier":"EXACT"}},"description":"USP"},{"type":"Region","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":593,"modifier":"EXACT"}},"description":"Interaction with TRIP","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14676304"}]},{"type":"Region","location":{"start":{"value":309,"modifier":"EXACT"},"end":{"value":353,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":392,"modifier":"EXACT"},"end":{"value":411,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":394,"modifier":"EXACT"},"end":{"value":469,"modifier":"EXACT"}},"description":"Interaction with TRAF2"},{"type":"Region","location":{"start":{"value":470,"modifier":"EXACT"},"end":{"value":554,"modifier":"EXACT"}},"description":"Interaction with IKBKG/NEMO","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15341735"}]},{"type":"Region","location":{"start":{"value":781,"modifier":"EXACT"},"end":{"value":833,"modifier":"EXACT"}},"description":"B-box","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18313383"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27591049"}]},{"type":"Compositional bias","location":{"start":{"value":330,"modifier":"EXACT"},"end":{"value":349,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":601,"modifier":"EXACT"},"end":{"value":601,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU10092"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18313383"}]},{"type":"Active 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