Details for: CYLD

Gene ID: 1540

Symbol: CYLD

Ensembl ID: ENSG00000083799

Description: CYLD lysine 63 deubiquitinase

Associated with

Other Information

Genular Protein ID: 1057081307

Symbol: CYLD_HUMAN

Name: Ubiquitin carboxyl-terminal hydrolase CYLD

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 10835629

Title: Identification of the familial cylindromatosis tumor suppressor gene.

PubMed ID: 10835629

DOI: 10.1038/76006

PubMed ID: 10048485

Title: Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.

PubMed ID: 10048485

DOI: 10.1093/dnares/5.6.355

PubMed ID: 12168954

Title: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones.

PubMed ID: 12168954

DOI: 10.1093/dnares/9.3.99

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 11042152

Title: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells.

PubMed ID: 11042152

DOI: 10.1101/gr.140200

PubMed ID: 12917689

Title: CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members.

PubMed ID: 12917689

DOI: 10.1038/nature01803

PubMed ID: 12917690

Title: Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-kappaB.

PubMed ID: 12917690

DOI: 10.1038/nature01811

PubMed ID: 12917691

Title: The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination.

PubMed ID: 12917691

DOI: 10.1038/nature01802

PubMed ID: 14676304

Title: The tumor suppressor CYLD interacts with TRIP and regulates negatively nuclear factor kappaB activation by tumor necrosis factor.

PubMed ID: 14676304

DOI: 10.1084/jem.20031187

PubMed ID: 15870263

Title: Regulation of the deubiquitinating enzyme CYLD by IkappaB kinase gamma-dependent phosphorylation.

PubMed ID: 15870263

DOI: 10.1128/mcb.25.10.3886-3895.2005

PubMed ID: 17495026

Title: The tumor suppressor CYLD regulates entry into mitosis.

PubMed ID: 17495026

DOI: 10.1073/pnas.0703268104

PubMed ID: 18636086

Title: The tumour suppressor CYLD is a negative regulator of RIG-I-mediated antiviral response.

PubMed ID: 18636086

DOI: 10.1038/embor.2008.136

PubMed ID: 18222923

Title: The tumor suppressor CYLD regulates microtubule dynamics and plays a role in cell migration.

PubMed ID: 18222923

DOI: 10.1074/jbc.m708470200

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 20194890

Title: CYLD regulates angiogenesis by mediating vascular endothelial cell migration.

PubMed ID: 20194890

DOI: 10.1182/blood-2009-10-248526

PubMed ID: 19893491

Title: CYLD negatively regulates cell-cycle progression by inactivating HDAC6 and increasing the levels of acetylated tubulin.

PubMed ID: 19893491

DOI: 10.1038/emboj.2009.317

PubMed ID: 20227366

Title: Loss of the tumor suppressor CYLD enhances Wnt/beta-catenin signaling through K63-linked ubiquitination of Dvl.

PubMed ID: 20227366

DOI: 10.1016/j.molcel.2010.01.035

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25134987

Title: The deubiquitinating enzyme CYLD controls apical docking of basal bodies in ciliated epithelial cells.

PubMed ID: 25134987

DOI: 10.1038/ncomms5585

PubMed ID: 12190880

Title: Phenotype diversity in familial cylindromatosis: a frameshift mutation in the tumor suppressor gene CYLD underlies different tumors of skin appendages.

PubMed ID: 12190880

DOI: 10.1046/j.1523-1747.2002.01839.x

PubMed ID: 12950348

Title: Identification of a recurrent mutation in the CYLD gene in Brooke-Spiegler syndrome.

PubMed ID: 12950348

DOI: 10.1046/j.1365-2230.2003.01344.x

PubMed ID: 16307661

Title: Two novel CYLD gene mutations in Chinese families with trichoepithelioma and a literature review of 16 families with trichoepithelioma reported in China.

PubMed ID: 16307661

DOI: 10.1111/j.1365-2133.2005.06960.x

PubMed ID: 15854031

Title: Mutations in the CYLD gene in Brooke-Spiegler syndrome, familial cylindromatosis, and multiple familial trichoepithelioma: lack of genotype-phenotype correlation.

PubMed ID: 15854031

DOI: 10.1111/j.0022-202x.2005.23688.x

PubMed ID: 16922728

Title: CYLD mutations underlie Brooke-Spiegler, familial cylindromatosis, and multiple familial trichoepithelioma syndromes.

PubMed ID: 16922728

DOI: 10.1111/j.1399-0004.2006.00667.x

PubMed ID: 26670046

Title: LUBAC-recruited CYLD and A20 regulate gene activation and cell death by exerting opposing effects on linear ubiquitin in signaling complexes.

PubMed ID: 26670046

DOI: 10.1016/j.celrep.2015.11.009

PubMed ID: 27307491

Title: SPATA2 links CYLD to the TNF-alpha receptor signaling complex and modulates the receptor signaling outcomes.

PubMed ID: 27307491

DOI: 10.15252/embj.201694300

PubMed ID: 27458237

Title: SPATA2 promotes CYLD activity and regulates TNF-induced NF-kappaB signaling and cell death.

PubMed ID: 27458237

DOI: 10.15252/embr.201642592

PubMed ID: 27545878

Title: SPATA2-Mediated Binding of CYLD to HOIP Enables CYLD Recruitment to Signaling Complexes.

PubMed ID: 27545878

DOI: 10.1016/j.celrep.2016.07.086

PubMed ID: 26997266

Title: CYLD limits Lys63- and Met1-linked ubiquitin at receptor complexes to regulate innate immune signaling.

PubMed ID: 26997266

DOI: 10.1016/j.celrep.2016.02.062

PubMed ID: 27591049

Title: SPATA2 links CYLD to LUBAC, activates CYLD, and controls LUBAC signaling.

PubMed ID: 27591049

DOI: 10.1016/j.molcel.2016.08.001

PubMed ID: 29291351

Title: The deubiquitinating enzyme cylindromatosis mitigates nonalcoholic steatohepatitis.

PubMed ID: 29291351

DOI: 10.1038/nm.4461

PubMed ID: 34497368

Title: TRIM15 and CYLD regulate ERK activation via lysine-63-linked polyubiquitination.

PubMed ID: 34497368

DOI: 10.1038/s41556-021-00732-8

PubMed ID: 15341735

Title: The CAP-Gly domain of CYLD associates with the proline-rich sequence in NEMO/IKKgamma.

PubMed ID: 15341735

DOI: 10.1016/j.str.2004.07.012

PubMed ID: 18313383

Title: The structure of the CYLD USP domain explains its specificity for Lys63-linked polyubiquitin and reveals a B box module.

PubMed ID: 18313383

DOI: 10.1016/j.molcel.2007.12.018

PubMed ID: 14632188

Title: A novel missense mutation in CYLD in a family with Brooke-Spiegler syndrome.

PubMed ID: 14632188

DOI: 10.1046/j.1523-1747.2003.12514.x

PubMed ID: 23338750

Title: Frontotemporal dementia-amyotrophic lateral sclerosis syndrome locus on chromosome 16p12.1-q12.2: genetic, clinical and neuropathological analysis.

PubMed ID: 23338750

DOI: 10.1007/s00401-013-1078-9

PubMed ID: 32666117

Title: CYLD variants in frontotemporal dementia associated with severe memory impairment in a Portuguese cohort.

PubMed ID: 32666117

DOI: 10.1093/brain/awaa183

PubMed ID: 32185393

Title: CYLD is a causative gene for frontotemporal dementia - amyotrophic lateral sclerosis.

PubMed ID: 32185393

DOI: 10.1093/brain/awaa039

Sequence Information:

  • Length: 956
  • Mass: 107316
  • Checksum: 01831F9A83424631
  • Sequence:
  • MSSGLWSQEK VTSPYWEERI FYLLLQECSV TDKQTQKLLK VPKGSIGQYI QDRSVGHSRI 
    PSAKGKKNQI GLKILEQPHA VLFVDEKDVV EINEKFTELL LAITNCEERF SLFKNRNRLS 
    KGLQIDVGCP VKVQLRSGEE KFPGVVRFRG PLLAERTVSG IFFGVELLEE GRGQGFTDGV 
    YQGKQLFQCD EDCGVFVALD KLELIEDDDT ALESDYAGPG DTMQVELPPL EINSRVSLKV 
    GETIESGTVI FCDVLPGKES LGYFVGVDMD NPIGNWDGRF DGVQLCSFAC VESTILLHIN 
    DIIPALSESV TQERRPPKLA FMSRGVGDKG SSSHNKPKAT GSTSDPGNRN RSELFYTLNG 
    SSVDSQPQSK SKNTWYIDEV AEDPAKSLTE ISTDFDRSSP PLQPPPVNSL TTENRFHSLP 
    FSLTKMPNTN GSIGHSPLSL SAQSVMEELN TAPVQESPPL AMPPGNSHGL EVGSLAEVKE 
    NPPFYGVIRW IGQPPGLNEV LAGLELEDEC AGCTDGTFRG TRYFTCALKK ALFVKLKSCR 
    PDSRFASLQP VSNQIERCNS LAFGGYLSEV VEENTPPKME KEGLEIMIGK KKGIQGHYNS 
    CYLDSTLFCL FAFSSVLDTV LLRPKEKNDV EYYSETQELL RTEIVNPLRI YGYVCATKIM 
    KLRKILEKVE AASGFTSEEK DPEEFLNILF HHILRVEPLL KIRSAGQKVQ DCYFYQIFME 
    KNEKVGVPTI QQLLEWSFIN SNLKFAEAPS CLIIQMPRFG KDFKLFKKIF PSLELNITDL 
    LEDTPRQCRI CGGLAMYECR ECYDDPDISA GKIKQFCKTC NTQVHLHPKR LNHKYNPVSL 
    PKDLPDWDWR HGCIPCQNME LFAVLCIETS HYVAFVKYGK DDSAWLFFDS MADRDGGQNG 
    FNIPQVTPCP EVGEYLKMSL EDLHSLDSRR IQGCARRLLC DAYMCMYQSP TMSLYK

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.