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Ubiquitin carboxyl-terminal hydrolase CYLD (EC 3.4.19.12) (Deubiquitinating enzyme CYLD) (Ubiquitin thioesterase CYLD) (Ubiquitin-specific-processing protease CYLD)

 CYLD_HUMAN              Reviewed;         956 AA.
Q9NQC7; O94934; Q7L3N6; Q96EH0; Q9NZX9;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 161.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase CYLD;
EC=3.4.19.12 {ECO:0000269|PubMed:18313383};
AltName: Full=Deubiquitinating enzyme CYLD;
AltName: Full=Ubiquitin thioesterase CYLD;
AltName: Full=Ubiquitin-specific-processing protease CYLD;
Name=CYLD {ECO:0000303|PubMed:12917689, ECO:0000312|HGNC:HGNC:2584};
Synonyms=CYLD1, KIAA0849 {ECO:0000303|PubMed:10048485};
ORFNames=HSPC057;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
INVOLVEMENT IN FAMILIAL CYLINDROMATOSIS.
PubMed=10835629; DOI=10.1038/76006;
Bignell G.R., Brown C., Biggs P.J., Lakhani S.R., Jones C., Hansen J.,
Blair E., Hofmann B., Siebert R., Turner G., Evans D.G.,
Schrander-Stumpel C., Beemer F.A., Van Den Ouweland A., Halley D.,
Delpech B., Cleveland M.G., Leigh I., Leisti J., Rasmussen S.,
Wallace M.R., Fenske C., Banerjee P., Oiso N., Chaggar R., Merrett S.,
Leonard N., Huber M., Hohl D., Chapman P., Burn J., Swift S.,
Smith A., Ashworth A., Stratton M.R.;
"Identification of the familial cylindromatosis tumor suppressor
gene.";
Nat. Genet. 25:160-165(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=10048485; DOI=10.1093/dnares/5.6.355;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"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.";
DNA Res. 5:355-364(1998).
[3]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 397-956.
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[6]
FUNCTION, INTERACTION WITH IKBKG/NEMO, AND MUTAGENESIS OF CYS-601.
PubMed=12917689; DOI=10.1038/nature01803;
Trompouki E., Hatzivassiliou E., Tsichritzis T., Farmer H.,
Ashworth A., Mosialos G.;
"CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB
activation by TNFR family members.";
Nature 424:793-796(2003).
[7]
FUNCTION, INTERACTION WITH IKBKG/NEMO, AND MUTAGENESIS OF CYS-601.
PubMed=12917690; DOI=10.1038/nature01811;
Brummelkamp T.R., Nijman S.M.B., Dirac A.M.G., Bernards R.;
"Loss of the cylindromatosis tumour suppressor inhibits apoptosis by
activating NF-kappaB.";
Nature 424:797-801(2003).
[8]
FUNCTION, INTERACTION WITH IKBKG/NEMO AND TRAF2, AND MUTAGENESIS OF
SER-457 AND HIS-871.
PubMed=12917691; DOI=10.1038/nature01802;
Kovalenko A., Chable-Bessia C., Cantarella G., Israeel A., Wallach D.,
Courtois G.;
"The tumour suppressor CYLD negatively regulates NF-kappaB signalling
by deubiquitination.";
Nature 424:801-805(2003).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TRIP.
PubMed=14676304; DOI=10.1084/jem.20031187;
Regamey A., Hohl D., Liu J.W., Roger T., Kogerman P., Toftgaard R.,
Huber M.;
"The tumor suppressor CYLD interacts with TRIP and regulates
negatively nuclear factor kappaB activation by tumor necrosis
factor.";
J. Exp. Med. 198:1959-1964(2003).
[10]
FUNCTION, INTERACTION WITH TRAF2, ENZYME REGULATION, MUTAGENESIS OF
SER-418; SER-422; SER-432; SER-436; SER-439; SER-441 AND SER-444, AND
PHOSPHORYLATION AT SER-418.
PubMed=15870263; DOI=10.1128/MCB.25.10.3886-3895.2005;
Reiley W., Zhang M., Wu X., Granger E., Sun S.C.;
"Regulation of the deubiquitinating enzyme CYLD by IkappaB kinase
gamma-dependent phosphorylation.";
Mol. Cell. Biol. 25:3886-3895(2005).
[11]
FUNCTION, MUTAGENESIS OF CYS-601, INTERACTION WITH PLK1, AND
SUBCELLULAR LOCATION.
PubMed=17495026; DOI=10.1073/pnas.0703268104;
Stegmeier F., Sowa M.E., Nalepa G., Gygi S.P., Harper J.W.,
Elledge S.J.;
"The tumor suppressor CYLD regulates entry into mitosis.";
Proc. Natl. Acad. Sci. U.S.A. 104:8869-8874(2007).
[12]
FUNCTION, SUBUNIT, AND INTERACTION WITH DDX58; MAVS; TBK1 AND IKKE.
PubMed=18636086; DOI=10.1038/embor.2008.136;
Friedman C.S., O'Donnell M.A., Legarda-Addison D., Ng A.,
Cardenas W.B., Yount J.S., Moran T.M., Basler C.F., Komuro A.,
Horvath C.M., Xavier R., Ting A.T.;
"The tumour suppressor CYLD is a negative regulator of RIG-I-mediated
antiviral response.";
EMBO Rep. 9:930-936(2008).
[13]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18222923; DOI=10.1074/jbc.M708470200;
Gao J., Huo L., Sun X., Liu M., Li D., Dong J.T., Zhou J.;
"The tumor suppressor CYLD regulates microtubule dynamics and plays a
role in cell migration.";
J. Biol. Chem. 283:8802-8809(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20194890; DOI=10.1182/blood-2009-10-248526;
Gao J., Sun L., Huo L., Liu M., Li D., Zhou J.;
"CYLD regulates angiogenesis by mediating vascular endothelial cell
migration.";
Blood 115:4130-4137(2010).
[16]
FUNCTION, INTERACTION WITH HDAC6; BCL3 AND MICROTUBULES, AND
SUBCELLULAR LOCATION.
PubMed=19893491; DOI=10.1038/emboj.2009.317;
Wickstrom S.A., Masoumi K.C., Khochbin S., Fassler R., Massoumi R.;
"CYLD negatively regulates cell-cycle progression by inactivating
HDAC6 and increasing the levels of acetylated tubulin.";
EMBO J. 29:131-144(2010).
[17]
FUNCTION, AND INTERACTION WITH DVL1 AND DVL3.
PubMed=20227366; DOI=10.1016/j.molcel.2010.01.035;
Tauriello D.V., Haegebarth A., Kuper I., Edelmann M.J., Henraat M.,
Canninga-van Dijk M.R., Kessler B.M., Clevers H., Maurice M.M.;
"Loss of the tumor suppressor CYLD enhances Wnt/beta-catenin signaling
through K63-linked ubiquitination of Dvl.";
Mol. Cell 37:607-619(2010).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-418 AND SER-422, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[20]
SUBCELLULAR LOCATION, AND INTERACTION WITH CEP350.
PubMed=25134987; DOI=10.1038/ncomms5585;
Eguether T., Ermolaeva M.A., Zhao Y., Bonnet M.C., Jain A.,
Pasparakis M., Courtois G., Tassin A.M.;
"The deubiquitinating enzyme CYLD controls apical docking of basal
bodies in ciliated epithelial cells.";
Nat. Commun. 5:4585-4585(2014).
[21]
INVOLVEMENT IN FCYL, AND INVOLVEMENT IN BRSS.
PubMed=12190880; DOI=10.1046/j.1523-1747.2002.01839.x;
Poblete Gutierrez P., Eggermann T., Hoeller D., Jugert F.K.,
Beermann T., Grussendorf-Conen E.-I., Zerres K., Merk H.F., Frank J.;
"Phenotype diversity in familial cylindromatosis: a frameshift
mutation in the tumor suppressor gene CYLD underlies different tumors
of skin appendages.";
J. Invest. Dermatol. 119:527-531(2002).
[22]
INVOLVEMENT IN BRSS.
PubMed=12950348; DOI=10.1046/j.1365-2230.2003.01344.x;
Scheinfeld N., Hu G., Gill M., Austin C., Celebi J.T.;
"Identification of a recurrent mutation in the CYLD gene in Brooke-
Spiegler syndrome.";
Clin. Exp. Dermatol. 28:539-541(2003).
[23]
INVOLVEMENT IN MFT1.
PubMed=16307661; DOI=10.1111/j.1365-2133.2005.06960.x;
Liang Y.H., Gao M., Sun L.D., Liu L.J., Cui Y., Yang S., Fan X.,
Wang J., Xiao F.L., Zhang X.J.;
"Two novel CYLD gene mutations in Chinese families with
trichoepithelioma and a literature review of 16 families with
trichoepithelioma reported in China.";
Br. J. Dermatol. 153:1213-1215(2005).
[24]
INVOLVEMENT IN BRSS.
PubMed=15854031; DOI=10.1111/j.0022-202X.2005.23688.x;
Bowen S., Gill M., Lee D.A., Fisher G., Geronemus R.G., Vazquez M.E.,
Celebi J.T.;
"Mutations in the CYLD gene in Brooke-Spiegler syndrome, familial
cylindromatosis, and multiple familial trichoepithelioma: lack of
genotype-phenotype correlation.";
J. Invest. Dermatol. 124:919-920(2005).
[25]
INVOLVEMENT IN FCYL, AND INVOLVEMENT IN MFT1.
PubMed=16922728; DOI=10.1111/j.1399-0004.2006.00667.x;
Young A.L., Kellermayer R., Szigeti R., Teszas A., Azmi S.,
Celebi J.T.;
"CYLD mutations underlie Brooke-Spiegler, familial cylindromatosis,
and multiple familial trichoepithelioma syndromes.";
Clin. Genet. 70:246-249(2006).
[26]
FUNCTION.
PubMed=26670046; DOI=10.1016/j.celrep.2015.11.009;
Draber P., Kupka S., Reichert M., Draberova H., Lafont E.,
de Miguel D., Spilgies L., Surinova S., Taraborrelli L., Hartwig T.,
Rieser E., Martino L., Rittinger K., Walczak H.;
"LUBAC-recruited CYLD and A20 regulate gene activation and cell death
by exerting opposing effects on linear ubiquitin in signaling
complexes.";
Cell Rep. 13:2258-2272(2015).
[27]
FUNCTION, AND INTERACTION WITH RNF31.
PubMed=26997266; DOI=10.1016/j.celrep.2016.02.062;
Hrdinka M., Fiil B.K., Zucca M., Leske D., Bagola K., Yabal M.,
Elliott P.R., Damgaard R.B., Komander D., Jost P.J., Gyrd-Hansen M.;
"CYLD limits Lys63- and Met1-linked ubiquitin at receptor complexes to
regulate innate immune signaling.";
Cell Rep. 14:2846-2858(2016).
[28]
STRUCTURE BY NMR OF 460-550, AND INTERACTION WITH IKBKG.
PubMed=15341735; DOI=10.1016/j.str.2004.07.012;
Saito K., Kigawa T., Koshiba S., Sato K., Matsuo Y., Sakamoto A.,
Takagi T., Shirouzu M., Yabuki T., Nunokawa E., Seki E., Matsuda T.,
Aoki M., Miyata Y., Hirakawa N., Inoue M., Terada T., Nagase T.,
Kikuno R., Nakayama M., Ohara O., Tanaka A., Yokoyama S.;
"The CAP-Gly domain of CYLD associates with the proline-rich sequence
in NEMO/IKKgamma.";
Structure 12:1719-1728(2004).
[29]
STRUCTURE BY NMR OF 125-304.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the 1st and 2nd CAP-Gly domains in human
cylindromatosis tumor suppressor CYLD.";
Submitted (NOV-2004) to the PDB data bank.
[30]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 583-956 IN COMPLEX WITH ZINC
IONS, FUNCTION, ACTIVE SITE, MUTAGENESIS OF CYS-601, CATALYTIC
ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=18313383; DOI=10.1016/j.molcel.2007.12.018;
Komander D., Lord C.J., Scheel H., Swift S., Hofmann K., Ashworth A.,
Barford D.;
"The structure of the CYLD USP domain explains its specificity for
Lys63-linked polyubiquitin and reveals a B box module.";
Mol. Cell 29:451-464(2008).
[31]
VARIANT MFT1 GLY-747, AND VARIANT BRSS GLY-747.
PubMed=14632188; DOI=10.1046/j.1523-1747.2003.12514.x;
Hu G., Oender M., Gill M., Aksakal B., Oeztas M., Guerer M.A.,
Celebi J.T.;
"A novel missense mutation in CYLD in a family with Brooke-Spiegler
syndrome.";
J. Invest. Dermatol. 121:732-734(2003).
-!- FUNCTION: Deubiquitinase that specifically cleaves 'Lys-63'-linked
polyubiquitin chains. Has endodeubiquitinase activity. Plays an
important role in the regulation of pathways leading to NF-kappa-B
activation (PubMed:12917689, PubMed:12917691). 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. 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. 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). Also
able to remove linear ('Met-1'-linked) polyubiquitin chains to
regulate innate immunity: recruited to the LUBAC complex and,
together with OTULIN, restricts linear polyubiquitin formation on
RIPK2 in response to NOD2 stimulation (PubMed:26670046,
PubMed:26997266). {ECO:0000250|UniProtKB:Q80TQ2,
ECO:0000269|PubMed:12917689, ECO:0000269|PubMed:12917690,
ECO:0000269|PubMed:12917691, ECO:0000269|PubMed:14676304,
ECO:0000269|PubMed:17495026, ECO:0000269|PubMed:18222923,
ECO:0000269|PubMed:18636086, ECO:0000269|PubMed:19893491,
ECO:0000269|PubMed:20194890, ECO:0000269|PubMed:20227366,
ECO:0000269|PubMed:26670046, ECO:0000269|PubMed:26997266}.
-!- CATALYTIC ACTIVITY: 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).
{ECO:0000269|PubMed:18313383}.
-!- ENZYME REGULATION: Inhibited by phosphorylation at serine
residues. {ECO:0000269|PubMed:15870263}.
-!- SUBUNIT: Interacts (via CAP-Gly domain) with IKBKG/NEMO (via
proline-rich C-terminal region). Interacts with TRAF2 and TRIP.
Interacts with PLK1, DVL1, DVL3, MAVS, TBK1, IKKE and DDX58.
Interacts (via CAP-Gly domain) with microtubules. Interacts with
HDAC6 and BCL3. Interacts with SQSTM1 and MAP3K7. Identified in a
complex with TRAF6 and SQSTM1 (By similarity). Interacts with
CEP350 (PubMed:25134987). Interacts with RNF31 (PubMed:26997266).
{ECO:0000250, ECO:0000269|PubMed:25134987,
ECO:0000269|PubMed:26997266}.
-!- INTERACTION:
O95786:DDX58; NbExp=2; IntAct=EBI-2117940, EBI-995350;
Q9UBN7:HDAC6; NbExp=4; IntAct=EBI-2117940, EBI-301697;
Q96J02:ITCH; NbExp=3; IntAct=EBI-2117940, EBI-1564678;
Q96J02-2:ITCH; NbExp=2; IntAct=EBI-2117940, EBI-6672198;
Q71U36:TUBA1A; NbExp=6; IntAct=EBI-2117940, EBI-302552;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane
protein; Cytoplasmic side. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000269|PubMed:25134987}.
Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:25134987}.
Cytoplasm, cytoskeleton, cilium basal body
{ECO:0000250|UniProtKB:Q80TQ2}. Note=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). {ECO:0000250|UniProtKB:Q80TQ2,
ECO:0000269|PubMed:25134987}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NQC7-1; Sequence=Displayed;
Name=2;
IsoId=Q9NQC7-2; Sequence=VSP_011277;
-!- TISSUE SPECIFICITY: 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. {ECO:0000269|PubMed:10835629}.
-!- PTM: Phosphorylated on several serine residues by IKKA and/or IKKB
in response to immune stimuli. Phosphorylation requires IKBKG.
Phosphorylation abolishes TRAF2 deubiquitination, interferes with
the activation of Jun kinases, and strongly reduces CD40-dependent
gene activation by NF-kappa-B. {ECO:0000269|PubMed:15870263}.
-!- DISEASE: Cylindromatosis, familial (FCYL) [MIM:132700]: 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.
{ECO:0000269|PubMed:12190880, ECO:0000269|PubMed:16922728}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Multiple familial trichoepithelioma 1 (MFT1)
[MIM:601606]: 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. {ECO:0000269|PubMed:14632188,
ECO:0000269|PubMed:16307661, ECO:0000269|PubMed:16922728}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Brooke-Spiegler syndrome (BRSS) [MIM:605041]: 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.
{ECO:0000269|PubMed:12190880, ECO:0000269|PubMed:12950348,
ECO:0000269|PubMed:14632188, ECO:0000269|PubMed:15854031}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF29029.1; Type=Frameshift; Positions=776, 808, 932; Evidence={ECO:0000305};
Sequence=BAA74872.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CYLDID40232ch16q12.html";
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EMBL; AJ250014; CAB93533.1; -; mRNA.
EMBL; AB020656; BAA74872.2; ALT_INIT; mRNA.
EMBL; BC012342; AAH12342.1; -; mRNA.
EMBL; AF161542; AAF29029.1; ALT_FRAME; mRNA.
CCDS; CCDS42164.1; -. [Q9NQC7-2]
CCDS; CCDS45482.1; -. [Q9NQC7-1]
RefSeq; NP_001035814.1; NM_001042355.1. [Q9NQC7-2]
RefSeq; NP_001035877.1; NM_001042412.1. [Q9NQC7-2]
RefSeq; NP_056062.1; NM_015247.2. [Q9NQC7-1]
RefSeq; XP_005255869.1; XM_005255812.2. [Q9NQC7-2]
RefSeq; XP_006721212.1; XM_006721149.1. [Q9NQC7-2]
RefSeq; XP_011521209.1; XM_011522907.2. [Q9NQC7-2]
RefSeq; XP_016878466.1; XM_017022977.1. [Q9NQC7-2]
RefSeq; XP_016878467.1; XM_017022978.1. [Q9NQC7-2]
RefSeq; XP_016878468.1; XM_017022979.1. [Q9NQC7-2]
RefSeq; XP_016878469.1; XM_017022980.1. [Q9NQC7-2]
UniGene; Hs.578973; -.
PDB; 1IXD; NMR; -; A=460-550.
PDB; 1WHL; NMR; -; A=125-206.
PDB; 1WHM; NMR; -; A=228-304.
PDB; 2VHF; X-ray; 2.80 A; A/B=583-956.
PDBsum; 1IXD; -.
PDBsum; 1WHL; -.
PDBsum; 1WHM; -.
PDBsum; 2VHF; -.
ProteinModelPortal; Q9NQC7; -.
SMR; Q9NQC7; -.
BioGrid; 107920; 67.
CORUM; Q9NQC7; -.
IntAct; Q9NQC7; 29.
MINT; MINT-6804518; -.
STRING; 9606.ENSP00000308928; -.
MEROPS; C67.001; -.
iPTMnet; Q9NQC7; -.
PhosphoSitePlus; Q9NQC7; -.
BioMuta; CYLD; -.
DMDM; 51316104; -.
MaxQB; Q9NQC7; -.
PaxDb; Q9NQC7; -.
PeptideAtlas; Q9NQC7; -.
PRIDE; Q9NQC7; -.
Ensembl; ENST00000311559; ENSP00000308928; ENSG00000083799. [Q9NQC7-1]
Ensembl; ENST00000398568; ENSP00000381574; ENSG00000083799. [Q9NQC7-2]
Ensembl; ENST00000427738; ENSP00000392025; ENSG00000083799. [Q9NQC7-1]
Ensembl; ENST00000564326; ENSP00000454515; ENSG00000083799. [Q9NQC7-2]
Ensembl; ENST00000569418; ENSP00000457576; ENSG00000083799. [Q9NQC7-2]
GeneID; 1540; -.
KEGG; hsa:1540; -.
UCSC; uc002egq.2; human. [Q9NQC7-1]
CTD; 1540; -.
DisGeNET; 1540; -.
EuPathDB; HostDB:ENSG00000083799.17; -.
GeneCards; CYLD; -.
HGNC; HGNC:2584; CYLD.
HPA; CAB011713; -.
HPA; HPA050095; -.
MalaCards; CYLD; -.
MIM; 132700; phenotype.
MIM; 601606; phenotype.
MIM; 605018; gene.
MIM; 605041; phenotype.
neXtProt; NX_Q9NQC7; -.
OpenTargets; ENSG00000083799; -.
Orphanet; 211; Familial cylindromatosis.
Orphanet; 867; Familial multiple trichoepithelioma.
PharmGKB; PA27084; -.
eggNOG; KOG3556; Eukaryota.
eggNOG; ENOG410XP6I; LUCA.
GeneTree; ENSGT00390000018123; -.
HOGENOM; HOG000006796; -.
HOVERGEN; HBG051281; -.
InParanoid; Q9NQC7; -.
KO; K08601; -.
OMA; YWEERIF; -.
OrthoDB; EOG091G015D; -.
PhylomeDB; Q9NQC7; -.
TreeFam; TF318734; -.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
Reactome; R-HSA-5357786; TNFR1-induced proapoptotic signaling.
Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
SIGNOR; Q9NQC7; -.
ChiTaRS; CYLD; human.
EvolutionaryTrace; Q9NQC7; -.
GeneWiki; CYLD_(gene); -.
GenomeRNAi; 1540; -.
PRO; PR:Q9NQC7; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000083799; -.
CleanEx; HS_CYLD; -.
ExpressionAtlas; Q9NQC7; baseline and differential.
Genevisible; Q9NQC7; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
GO; GO:0097542; C:ciliary tip; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005819; C:spindle; IDA:UniProtKB.
GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IEA:Ensembl.
GO; GO:0061578; F:Lys63-specific deubiquitinase activity; IDA:UniProtKB.
GO; GO:0070064; F:proline-rich region binding; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:UniProtKB.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; TAS:Reactome.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0043369; P:CD4-positive or CD8-positive, alpha-beta T cell lineage commitment; IEA:Ensembl.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0048872; P:homeostasis of number of cells; IEA:Ensembl.
GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
GO; GO:0070266; P:necroptotic process; IBA:GO_Central.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
GO; GO:0042347; P:negative regulation of NF-kappaB import into nucleus; IDA:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0045581; P:negative regulation of T cell differentiation; IEA:Ensembl.
GO; GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome.
GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
GO; GO:1903829; P:positive regulation of cellular protein localization; IEA:Ensembl.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0045582; P:positive regulation of T cell differentiation; IEA:Ensembl.
GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; IEA:Ensembl.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0070536; P:protein K63-linked deubiquitination; IDA:UniProtKB.
GO; GO:1990108; P:protein linear deubiquitination; IDA:UniProtKB.
GO; GO:0045577; P:regulation of B cell differentiation; IEA:Ensembl.
GO; GO:1902017; P:regulation of cilium assembly; ISS:UniProtKB.
GO; GO:2001242; P:regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:UniProtKB.
GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0043393; P:regulation of protein binding; IEA:Ensembl.
GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; IDA:UniProtKB.
GO; GO:1901026; P:ripoptosome assembly involved in necroptotic process; IEA:Ensembl.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
Gene3D; 2.30.30.190; -; 3.
InterPro; IPR036859; CAP-Gly_dom_sf.
InterPro; IPR000938; CAP-Gly_domain.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
Pfam; PF01302; CAP_GLY; 2.
Pfam; PF00443; UCH; 1.
SMART; SM01052; CAP_GLY; 3.
SUPFAM; SSF74924; SSF74924; 3.
PROSITE; PS00845; CAP_GLY_1; 1.
PROSITE; PS50245; CAP_GLY_2; 2.
PROSITE; PS00972; USP_1; 1.
PROSITE; PS50235; USP_3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Cell membrane;
Cell projection; Complete proteome; Cytoplasm; Cytoskeleton;
Disease mutation; Hydrolase; Immunity; Innate immunity; Membrane;
Metal-binding; Microtubule; Phosphoprotein; Protease;
Reference proteome; Repeat; Thiol protease; Tumor suppressor;
Ubl conjugation pathway; Wnt signaling pathway; Zinc.
CHAIN 1 956 Ubiquitin carboxyl-terminal hydrolase
CYLD.
/FTId=PRO_0000080698.
DOMAIN 153 198 CAP-Gly 1. {ECO:0000255|PROSITE-
ProRule:PRU00045}.
DOMAIN 253 286 CAP-Gly 2. {ECO:0000255|PROSITE-
ProRule:PRU00045}.
DOMAIN 492 535 CAP-Gly 3. {ECO:0000255|PROSITE-
ProRule:PRU00045}.
DOMAIN 592 950 USP.
REGION 106 593 Interaction with TRIP.
{ECO:0000269|PubMed:14676304}.
REGION 394 469 Interaction with TRAF2.
REGION 470 554 Interaction with IKBKG/NEMO.
{ECO:0000269|PubMed:15341735}.
ACT_SITE 601 601 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10092,
ECO:0000269|PubMed:18313383}.
ACT_SITE 871 871 Proton acceptor.
{ECO:0000305|PubMed:18313383}.
METAL 788 788 Zinc 1.
METAL 791 791 Zinc 1.
METAL 799 799 Zinc 2.
METAL 802 802 Zinc 2.
METAL 817 817 Zinc 1.
METAL 820 820 Zinc 1.
METAL 825 825 Zinc 2.
METAL 833 833 Zinc 2.
MOD_RES 387 387 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 418 418 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15870263}.
MOD_RES 422 422 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 305 307 Missing (in isoform 2).
{ECO:0000303|PubMed:10048485,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_011277.
VARIANT 747 747 E -> G (in MFT1 and BRSS;
dbSNP:rs121908389).
{ECO:0000269|PubMed:14632188}.
/FTId=VAR_045967.
MUTAGEN 418 418 S->A: Reduced phosphorylation; when
associated with A-422; A-432 and A-436.
Loss of phosphorylation; when associated
with A-422; A-432; A-436; A-439; A-441
and A-444. {ECO:0000269|PubMed:15870263}.
MUTAGEN 418 418 S->E: Abolishes deubiquitination of
TRAF2; when associated with E-422; E-432;
E-436; E-439; E-441 and E-444.
{ECO:0000269|PubMed:15870263}.
MUTAGEN 422 422 S->A: Reduced phosphorylation; when
associated with A-418; A-432 and A-436.
Loss of phosphorylation; when associated
with A-418; A-432; A-436; A-439; A-441
and A-444. {ECO:0000269|PubMed:15870263}.
MUTAGEN 422 422 S->E: Abolishes deubiquitination of
TRAF2; when associated with E-418; E-432;
E-436; E-439; E-441 and E-444.
{ECO:0000269|PubMed:15870263}.
MUTAGEN 432 432 S->A: Slightly reduced phosphorylation;
when associated with A-436. Reduced
phosphorylation; when associated with A-
418; A-422 and A-436. Loss of
phosphorylation; when associated with A-
418; A-422; A-436; A-439; A-441 and A-
444. {ECO:0000269|PubMed:15870263}.
MUTAGEN 432 432 S->E: Abolishes deubiquitination of
TRAF2; when associated with E-418; E-422;
E-436; E-439; E-441 and E-444.
{ECO:0000269|PubMed:15870263}.
MUTAGEN 436 436 S->A: Slightly reduced phosphorylation;
when associated with A-432. Reduced
phosphorylation; when associated with A-
418; A-422 and A-432. Loss of
phosphorylation; when associated with A-
418; A-422; A-432; A-439; A-441 and A-
444. {ECO:0000269|PubMed:15870263}.
MUTAGEN 436 436 S->E: Abolishes deubiquitination of
TRAF2; when associated with E-418; E-422;
E-432; E-439; E-441 and E-444.
{ECO:0000269|PubMed:15870263}.
MUTAGEN 439 439 S->A: Loss of phosphorylation; when
associated with A-418; A-422; A-432; A-
436; A-441 and A-444.
{ECO:0000269|PubMed:15870263}.
MUTAGEN 439 439 S->E: Abolishes deubiquitination of
TRAF2; when associated with E-418; E-422;
E-432; E-436; E-441 and E-444.
{ECO:0000269|PubMed:15870263}.
MUTAGEN 441 441 S->A: Loss of phosphorylation; when
associated with A-418; A-422; A-432; A-
436; A-439 and A-444.
{ECO:0000269|PubMed:15870263}.
MUTAGEN 441 441 S->E: Abolishes deubiquitination of
TRAF2; when associated with E-418; E-422;
E-432; E-436; E-439 and E-444.
{ECO:0000269|PubMed:15870263}.
MUTAGEN 444 444 S->A: Loss of phosphorylation; when
associated with A-418; A-422; A-432; A-
436; A-439 and A-441.
{ECO:0000269|PubMed:15870263}.
MUTAGEN 444 444 S->E: Abolishes deubiquitination of
TRAF2; when associated with E-418; E-422;
E-432; E-436; E-439 and E-441.
{ECO:0000269|PubMed:15870263}.
MUTAGEN 457 457 S->A: Abolishes binding to TRAF2.
{ECO:0000269|PubMed:12917691}.
MUTAGEN 601 601 C->A,S: Loss of deubiquitinating
activity. {ECO:0000269|PubMed:12917689,
ECO:0000269|PubMed:12917690,
ECO:0000269|PubMed:17495026,
ECO:0000269|PubMed:18313383}.
MUTAGEN 871 871 H->N: Loss of deubiquitinating activity.
{ECO:0000269|PubMed:12917691}.
STRAND 130 134 {ECO:0000244|PDB:1WHL}.
STRAND 136 139 {ECO:0000244|PDB:1WHL}.
STRAND 141 149 {ECO:0000244|PDB:1WHL}.
STRAND 154 157 {ECO:0000244|PDB:1WHL}.
STRAND 163 167 {ECO:0000244|PDB:1WHL}.
STRAND 169 171 {ECO:0000244|PDB:1WHL}.
TURN 191 193 {ECO:0000244|PDB:1WHL}.
STRAND 194 197 {ECO:0000244|PDB:1WHL}.
HELIX 199 201 {ECO:0000244|PDB:1WHL}.
STRAND 202 204 {ECO:0000244|PDB:1WHL}.
STRAND 235 240 {ECO:0000244|PDB:1WHM}.
STRAND 243 253 {ECO:0000244|PDB:1WHM}.
TURN 259 261 {ECO:0000244|PDB:1WHM}.
STRAND 264 272 {ECO:0000244|PDB:1WHM}.
STRAND 278 280 {ECO:0000244|PDB:1WHM}.
STRAND 283 285 {ECO:0000244|PDB:1WHM}.
STRAND 293 298 {ECO:0000244|PDB:1WHM}.
HELIX 299 301 {ECO:0000244|PDB:1WHM}.
STRAND 302 304 {ECO:0000244|PDB:1WHM}.
TURN 463 465 {ECO:0000244|PDB:1IXD}.
STRAND 466 468 {ECO:0000244|PDB:1IXD}.
STRAND 474 478 {ECO:0000244|PDB:1IXD}.
STRAND 480 482 {ECO:0000244|PDB:1IXD}.
STRAND 486 492 {ECO:0000244|PDB:1IXD}.
STRAND 495 497 {ECO:0000244|PDB:1IXD}.
STRAND 501 508 {ECO:0000244|PDB:1IXD}.
STRAND 514 518 {ECO:0000244|PDB:1IXD}.
STRAND 531 535 {ECO:0000244|PDB:1IXD}.
HELIX 536 538 {ECO:0000244|PDB:1IXD}.
STRAND 539 541 {ECO:0000244|PDB:1IXD}.
HELIX 584 586 {ECO:0000244|PDB:2VHF}.
STRAND 588 591 {ECO:0000244|PDB:2VHF}.
HELIX 601 611 {ECO:0000244|PDB:2VHF}.
STRAND 612 614 {ECO:0000244|PDB:2VHF}.
HELIX 615 617 {ECO:0000244|PDB:2VHF}.
HELIX 618 622 {ECO:0000244|PDB:2VHF}.
HELIX 633 642 {ECO:0000244|PDB:2VHF}.
HELIX 645 650 {ECO:0000244|PDB:2VHF}.
STRAND 652 654 {ECO:0000244|PDB:2VHF}.
HELIX 656 669 {ECO:0000244|PDB:2VHF}.
HELIX 682 690 {ECO:0000244|PDB:2VHF}.
TURN 691 694 {ECO:0000244|PDB:2VHF}.
STRAND 699 704 {ECO:0000244|PDB:2VHF}.
STRAND 710 713 {ECO:0000244|PDB:2VHF}.
HELIX 730 741 {ECO:0000244|PDB:2VHF}.
STRAND 743 747 {ECO:0000244|PDB:2VHF}.
STRAND 750 755 {ECO:0000244|PDB:2VHF}.
STRAND 760 764 {ECO:0000244|PDB:2VHF}.
STRAND 773 775 {ECO:0000244|PDB:2VHF}.
HELIX 778 780 {ECO:0000244|PDB:2VHF}.
STRAND 781 784 {ECO:0000244|PDB:2VHF}.
TURN 789 791 {ECO:0000244|PDB:2VHF}.
HELIX 800 802 {ECO:0000244|PDB:2VHF}.
TURN 806 811 {ECO:0000244|PDB:2VHF}.
HELIX 818 824 {ECO:0000244|PDB:2VHF}.
HELIX 828 830 {ECO:0000244|PDB:2VHF}.
HELIX 844 846 {ECO:0000244|PDB:2VHF}.
STRAND 859 868 {ECO:0000244|PDB:2VHF}.
STRAND 871 877 {ECO:0000244|PDB:2VHF}.
STRAND 879 881 {ECO:0000244|PDB:2VHF}.
STRAND 885 889 {ECO:0000244|PDB:2VHF}.
STRAND 905 908 {ECO:0000244|PDB:2VHF}.
HELIX 911 914 {ECO:0000244|PDB:2VHF}.
HELIX 920 925 {ECO:0000244|PDB:2VHF}.
HELIX 928 930 {ECO:0000244|PDB:2VHF}.
HELIX 935 940 {ECO:0000244|PDB:2VHF}.
STRAND 944 948 {ECO:0000244|PDB:2VHF}.
HELIX 950 952 {ECO:0000244|PDB:2VHF}.
SEQUENCE 956 AA; 107316 MW; 01831F9A83424631 CRC64;
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


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