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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.
17-JUN-2020, entry version 183.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase CYLD;
EC=3.4.19.12 {ECO:0000269|PubMed:18313383, ECO:0000269|PubMed:27458237, ECO:0000269|PubMed:27591049};
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, ACTIVITY 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]
INTERACTION WITH SPATA2.
PubMed=27307491; DOI=10.15252/embj.201694300;
Wagner S.A., Satpathy S., Beli P., Choudhary C.;
"SPATA2 links CYLD to the TNF-alpha receptor signaling complex and
modulates the receptor signaling outcomes.";
EMBO J. 35:1868-1884(2016).
[28]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH SPATA2, AND MUTAGENESIS OF
CYS-601.
PubMed=27458237; DOI=10.15252/embr.201642592;
Schlicher L., Wissler M., Preiss F., Brauns-Schubert P., Jakob C.,
Dumit V., Borner C., Dengjel J., Maurer U.;
"SPATA2 promotes CYLD activity and regulates TNF-induced NF-kappaB
signaling and cell death.";
EMBO Rep. 17:1485-1497(2016).
[29]
INTERACTION WITH SPATA2.
PubMed=27545878; DOI=10.1016/j.celrep.2016.07.086;
Kupka S., De Miguel D., Draber P., Martino L., Surinova S., Rittinger K.,
Walczak H.;
"SPATA2-Mediated Binding of CYLD to HOIP Enables CYLD Recruitment to
Signaling Complexes.";
Cell Rep. 16:2271-2280(2016).
[30]
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).
[31]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH SPATA2, AND MUTAGENESIS OF
LEU-622.
PubMed=27591049; DOI=10.1016/j.molcel.2016.08.001;
Elliott P.R., Leske D., Hrdinka M., Bagola K., Fiil B.K., McLaughlin S.H.,
Wagstaff J., Volkmar N., Christianson J.C., Kessler B.M., Freund S.M.,
Komander D., Gyrd-Hansen M.;
"SPATA2 links CYLD to LUBAC, activates CYLD, and controls LUBAC
signaling.";
Mol. Cell 63:990-1005(2016).
[32]
FUNCTION, TISSUE SPECIFICITY, AND UBIQUITINATION.
PubMed=29291351; DOI=10.1038/nm.4461;
Ji Y.X., Huang Z., Yang X., Wang X., Zhao L.P., Wang P.X., Zhang X.J.,
Alves-Bezerra M., Cai L., Zhang P., Lu Y.X., Bai L., Gao M.M., Zhao H.,
Tian S., Wang Y., Huang Z.X., Zhu X.Y., Zhang Y., Gong J., She Z.G., Li F.,
Cohen D.E., Li H.;
"The deubiquitinating enzyme cylindromatosis mitigates nonalcoholic
steatohepatitis.";
Nat. Med. 24:213-223(2018).
[33]
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).
[34]
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.
[35]
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).
[36]
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'- and linear
'Met-1'-linked polyubiquitin chains and is involved in NF-kappa-B
activation and TNF-alpha-induced necroptosis (PubMed:18636086,
PubMed:26670046, PubMed:27458237, PubMed:26997266, PubMed:27591049,
PubMed:29291351, PubMed:18313383). 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 (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-alpha-induced
necroptosis: recruited to the LUBAC complex via interaction with SPATA2
and restricts linear polyubiquitin formation on target proteins
(PubMed:26997266, PubMed:26670046, PubMed:27458237, PubMed:27591049).
Regulates innate immunity by restricting linear polyubiquitin formation
on RIPK2 in response to NOD2 stimulation (PubMed:26997266). Involved in
TNF-alpha-induced necroptosis by removing linear ('Met-1'-linked)
polyubiquitin chains from RIPK1, thereby regulating the kinase activity
of RIPK1 (By similarity). Removes 'Lys-63' linked polyubiquitin chain
of MAP3K7, which inhibits phosphorylation and blocks downstream
activation of the JNK-p38 kinase cascades (PubMed:29291351).
{ECO:0000250|UniProtKB:Q80TQ2, ECO:0000269|PubMed:12917689,
ECO:0000269|PubMed:12917690, ECO:0000269|PubMed:12917691,
ECO:0000269|PubMed:17495026, ECO:0000269|PubMed:18222923,
ECO:0000269|PubMed:18313383, ECO:0000269|PubMed:18636086,
ECO:0000269|PubMed:19893491, ECO:0000269|PubMed:20194890,
ECO:0000269|PubMed:20227366, ECO:0000269|PubMed:26670046,
ECO:0000269|PubMed:26997266, ECO:0000269|PubMed:27458237,
ECO:0000269|PubMed:27591049, ECO:0000269|PubMed:29291351}.
-!- CATALYTIC ACTIVITY:
Reaction=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).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:18313383,
ECO:0000269|PubMed:27458237, ECO:0000269|PubMed:27591049};
-!- ACTIVITY 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) (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 DDX58 (PubMed:17495026, PubMed:18636086,
PubMed:20227366). 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 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-alpha-induced necroptosis
(PubMed:27307491, PubMed:27458237, PubMed:27545878, PubMed:27591049).
{ECO:0000250|UniProtKB:Q80TQ2, ECO:0000269|PubMed:12917689,
ECO:0000269|PubMed:12917690, ECO:0000269|PubMed:12917691,
ECO:0000269|PubMed:14676304, ECO:0000269|PubMed:15341735,
ECO:0000269|PubMed:17495026, ECO:0000269|PubMed:18636086,
ECO:0000269|PubMed:19893491, ECO:0000269|PubMed:20227366,
ECO:0000269|PubMed:25134987, ECO:0000269|PubMed:26997266,
ECO:0000269|PubMed:27307491, ECO:0000269|PubMed:27458237,
ECO:0000269|PubMed:27545878, ECO:0000269|PubMed:27591049}.
-!- INTERACTION:
Q9NQC7; O95786: DDX58; NbExp=2; IntAct=EBI-2117940, EBI-995350;
Q9NQC7; Q9UBN7: HDAC6; NbExp=4; IntAct=EBI-2117940, EBI-301697;
Q9NQC7; Q96J02: ITCH; NbExp=3; IntAct=EBI-2117940, EBI-1564678;
Q9NQC7; Q96J02-2: ITCH; NbExp=2; IntAct=EBI-2117940, EBI-6672198;
Q9NQC7; Q71U36: TUBA1A; NbExp=6; IntAct=EBI-2117940, EBI-302552;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18313383}.
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,
ECO:0000269|PubMed:29291351}.
-!- PTM: Ubiquitinated. Polyubiquitinated in hepatocytes treated with
palmitic acid. Ubiquitination is mediated by E3 ligase TRIM47 and leads
to proteasomal degradation. {ECO:0000269|PubMed:29291351}.
-!- 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; Evidence={ECO:0000305};
Sequence=BAA74872.2; Type=Erroneous initiation; Note=Extended N-terminus.; 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]
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; -.
SMR; Q9NQC7; -.
BioGRID; 107920; 639.
CORUM; Q9NQC7; -.
IntAct; Q9NQC7; 56.
MINT; Q9NQC7; -.
STRING; 9606.ENSP00000392025; -.
MEROPS; C67.001; -.
iPTMnet; Q9NQC7; -.
PhosphoSitePlus; Q9NQC7; -.
BioMuta; CYLD; -.
DMDM; 51316104; -.
jPOST; Q9NQC7; -.
MassIVE; Q9NQC7; -.
MaxQB; Q9NQC7; -.
PaxDb; Q9NQC7; -.
PeptideAtlas; Q9NQC7; -.
PRIDE; Q9NQC7; -.
ProteomicsDB; 82139; -. [Q9NQC7-1]
ProteomicsDB; 82140; -. [Q9NQC7-2]
Antibodypedia; 3193; 292 antibodies.
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; ENSG00000083799; Low tissue specificity.
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; -.
InParanoid; Q9NQC7; -.
KO; K08601; -.
OMA; FNGVQLC; -.
OrthoDB; 119442at2759; -.
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; -.
BioGRID-ORCS; 1540; 15 hits in 790 CRISPR screens.
ChiTaRS; CYLD; human.
EvolutionaryTrace; Q9NQC7; -.
GeneWiki; CYLD_(gene); -.
GenomeRNAi; 1540; -.
Pharos; Q9NQC7; Tbio.
PRO; PR:Q9NQC7; -.
Proteomes; UP000005640; Chromosome 16.
RNAct; Q9NQC7; protein.
Bgee; ENSG00000083799; Expressed in caudate nucleus and 228 other tissues.
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:0046329; P:negative regulation of JNK cascade; IDA:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:1903753; P:negative regulation of p38MAPK cascade; IDA:UniProtKB.
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; IDA:UniProtKB.
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:0050727; P:regulation of inflammatory response; IDA: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:0060544; P:regulation of necroptotic process; IDA: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; IPR038765; Papain-like_cys_pep_sf.
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; SSF54001; SSF54001; 1.
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; Cytoplasm; Cytoskeleton; Disease mutation; Hydrolase;
Immunity; Innate immunity; Membrane; Metal-binding; Microtubule;
Phosphoprotein; Protease; Reference proteome; Repeat; Thiol protease;
Tumor suppressor; Ubl conjugation; Ubl conjugation pathway;
Wnt signaling pathway; Zinc.
CHAIN 1..956
/note="Ubiquitin carboxyl-terminal hydrolase CYLD"
/id="PRO_0000080698"
DOMAIN 153..198
/note="CAP-Gly 1"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
DOMAIN 253..286
/note="CAP-Gly 2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
DOMAIN 492..535
/note="CAP-Gly 3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
DOMAIN 592..950
/note="USP"
REGION 106..593
/note="Interaction with TRIP"
/evidence="ECO:0000269|PubMed:14676304"
REGION 394..469
/note="Interaction with TRAF2"
REGION 470..554
/note="Interaction with IKBKG/NEMO"
/evidence="ECO:0000269|PubMed:15341735"
REGION 781..833
/note="B-box"
/evidence="ECO:0000269|PubMed:18313383,
ECO:0000269|PubMed:27591049"
ACT_SITE 601
/note="Nucleophile"
/evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
ECO:0000269|PubMed:18313383"
ACT_SITE 871
/note="Proton acceptor"
/evidence="ECO:0000305|PubMed:18313383"
METAL 788
/note="Zinc 1"
METAL 791
/note="Zinc 1"
METAL 799
/note="Zinc 2"
METAL 802
/note="Zinc 2"
METAL 817
/note="Zinc 1"
METAL 820
/note="Zinc 1"
METAL 825
/note="Zinc 2"
METAL 833
/note="Zinc 2"
MOD_RES 387
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:24275569"
MOD_RES 418
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15870263"
MOD_RES 422
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
VAR_SEQ 305..307
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:10048485,
ECO:0000303|PubMed:15489334"
/id="VSP_011277"
VARIANT 747
/note="E -> G (in MFT1 and BRSS; dbSNP:rs121908389)"
/evidence="ECO:0000269|PubMed:14632188"
/id="VAR_045967"
MUTAGEN 418
/note="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."
/evidence="ECO:0000269|PubMed:15870263"
MUTAGEN 418
/note="S->E: Abolishes deubiquitination of TRAF2; when
associated with E-422; E-432; E-436; E-439; E-441 and E-
444."
/evidence="ECO:0000269|PubMed:15870263"
MUTAGEN 422
/note="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."
/evidence="ECO:0000269|PubMed:15870263"
MUTAGEN 422
/note="S->E: Abolishes deubiquitination of TRAF2; when
associated with E-418; E-432; E-436; E-439; E-441 and E-
444."
/evidence="ECO:0000269|PubMed:15870263"
MUTAGEN 432
/note="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."
/evidence="ECO:0000269|PubMed:15870263"
MUTAGEN 432
/note="S->E: Abolishes deubiquitination of TRAF2; when
associated with E-418; E-422; E-436; E-439; E-441 and E-
444."
/evidence="ECO:0000269|PubMed:15870263"
MUTAGEN 436
/note="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."
/evidence="ECO:0000269|PubMed:15870263"
MUTAGEN 436
/note="S->E: Abolishes deubiquitination of TRAF2; when
associated with E-418; E-422; E-432; E-439; E-441 and E-
444."
/evidence="ECO:0000269|PubMed:15870263"
MUTAGEN 439
/note="S->A: Loss of phosphorylation; when associated with
A-418; A-422; A-432; A-436; A-441 and A-444."
/evidence="ECO:0000269|PubMed:15870263"
MUTAGEN 439
/note="S->E: Abolishes deubiquitination of TRAF2; when
associated with E-418; E-422; E-432; E-436; E-441 and E-
444."
/evidence="ECO:0000269|PubMed:15870263"
MUTAGEN 441
/note="S->A: Loss of phosphorylation; when associated with
A-418; A-422; A-432; A-436; A-439 and A-444."
/evidence="ECO:0000269|PubMed:15870263"
MUTAGEN 441
/note="S->E: Abolishes deubiquitination of TRAF2; when
associated with E-418; E-422; E-432; E-436; E-439 and E-
444."
/evidence="ECO:0000269|PubMed:15870263"
MUTAGEN 444
/note="S->A: Loss of phosphorylation; when associated with
A-418; A-422; A-432; A-436; A-439 and A-441."
/evidence="ECO:0000269|PubMed:15870263"
MUTAGEN 444
/note="S->E: Abolishes deubiquitination of TRAF2; when
associated with E-418; E-422; E-432; E-436; E-439 and E-
441."
/evidence="ECO:0000269|PubMed:15870263"
MUTAGEN 457
/note="S->A: Abolishes binding to TRAF2."
/evidence="ECO:0000269|PubMed:12917691"
MUTAGEN 601
/note="C->A,S: Loss of deubiquitinating activity."
/evidence="ECO:0000269|PubMed:12917689,
ECO:0000269|PubMed:12917690, ECO:0000269|PubMed:17495026,
ECO:0000269|PubMed:18313383, ECO:0000269|PubMed:27458237"
MUTAGEN 622
/note="L->D: Impaired interaction with SPATA2."
/evidence="ECO:0000269|PubMed:27591049"
MUTAGEN 871
/note="H->N: Loss of deubiquitinating activity."
/evidence="ECO:0000269|PubMed:12917691"
STRAND 130..134
/evidence="ECO:0000244|PDB:1WHL"
STRAND 136..139
/evidence="ECO:0000244|PDB:1WHL"
STRAND 141..149
/evidence="ECO:0000244|PDB:1WHL"
STRAND 154..157
/evidence="ECO:0000244|PDB:1WHL"
STRAND 163..167
/evidence="ECO:0000244|PDB:1WHL"
STRAND 169..171
/evidence="ECO:0000244|PDB:1WHL"
TURN 191..193
/evidence="ECO:0000244|PDB:1WHL"
STRAND 194..197
/evidence="ECO:0000244|PDB:1WHL"
HELIX 199..201
/evidence="ECO:0000244|PDB:1WHL"
STRAND 202..204
/evidence="ECO:0000244|PDB:1WHL"
STRAND 235..240
/evidence="ECO:0000244|PDB:1WHM"
STRAND 243..253
/evidence="ECO:0000244|PDB:1WHM"
TURN 259..261
/evidence="ECO:0000244|PDB:1WHM"
STRAND 264..272
/evidence="ECO:0000244|PDB:1WHM"
STRAND 278..280
/evidence="ECO:0000244|PDB:1WHM"
STRAND 283..285
/evidence="ECO:0000244|PDB:1WHM"
STRAND 293..298
/evidence="ECO:0000244|PDB:1WHM"
HELIX 299..301
/evidence="ECO:0000244|PDB:1WHM"
STRAND 302..304
/evidence="ECO:0000244|PDB:1WHM"
TURN 463..465
/evidence="ECO:0000244|PDB:1IXD"
STRAND 466..468
/evidence="ECO:0000244|PDB:1IXD"
STRAND 474..478
/evidence="ECO:0000244|PDB:1IXD"
STRAND 480..482
/evidence="ECO:0000244|PDB:1IXD"
STRAND 486..492
/evidence="ECO:0000244|PDB:1IXD"
STRAND 495..497
/evidence="ECO:0000244|PDB:1IXD"
STRAND 501..508
/evidence="ECO:0000244|PDB:1IXD"
STRAND 514..518
/evidence="ECO:0000244|PDB:1IXD"
STRAND 531..535
/evidence="ECO:0000244|PDB:1IXD"
HELIX 536..538
/evidence="ECO:0000244|PDB:1IXD"
STRAND 539..541
/evidence="ECO:0000244|PDB:1IXD"
HELIX 584..586
/evidence="ECO:0000244|PDB:2VHF"
STRAND 588..591
/evidence="ECO:0000244|PDB:2VHF"
HELIX 601..611
/evidence="ECO:0000244|PDB:2VHF"
STRAND 612..614
/evidence="ECO:0000244|PDB:2VHF"
HELIX 615..617
/evidence="ECO:0000244|PDB:2VHF"
HELIX 618..622
/evidence="ECO:0000244|PDB:2VHF"
HELIX 633..642
/evidence="ECO:0000244|PDB:2VHF"
HELIX 645..650
/evidence="ECO:0000244|PDB:2VHF"
STRAND 652..654
/evidence="ECO:0000244|PDB:2VHF"
HELIX 656..669
/evidence="ECO:0000244|PDB:2VHF"
HELIX 682..690
/evidence="ECO:0000244|PDB:2VHF"
TURN 691..694
/evidence="ECO:0000244|PDB:2VHF"
STRAND 699..704
/evidence="ECO:0000244|PDB:2VHF"
STRAND 710..713
/evidence="ECO:0000244|PDB:2VHF"
HELIX 730..741
/evidence="ECO:0000244|PDB:2VHF"
STRAND 743..747
/evidence="ECO:0000244|PDB:2VHF"
STRAND 750..755
/evidence="ECO:0000244|PDB:2VHF"
STRAND 760..764
/evidence="ECO:0000244|PDB:2VHF"
STRAND 773..775
/evidence="ECO:0000244|PDB:2VHF"
HELIX 778..780
/evidence="ECO:0000244|PDB:2VHF"
STRAND 781..784
/evidence="ECO:0000244|PDB:2VHF"
TURN 789..791
/evidence="ECO:0000244|PDB:2VHF"
HELIX 800..802
/evidence="ECO:0000244|PDB:2VHF"
TURN 806..811
/evidence="ECO:0000244|PDB:2VHF"
HELIX 818..824
/evidence="ECO:0000244|PDB:2VHF"
HELIX 828..830
/evidence="ECO:0000244|PDB:2VHF"
HELIX 844..846
/evidence="ECO:0000244|PDB:2VHF"
STRAND 859..868
/evidence="ECO:0000244|PDB:2VHF"
STRAND 871..877
/evidence="ECO:0000244|PDB:2VHF"
STRAND 879..881
/evidence="ECO:0000244|PDB:2VHF"
STRAND 885..889
/evidence="ECO:0000244|PDB:2VHF"
STRAND 905..908
/evidence="ECO:0000244|PDB:2VHF"
HELIX 911..914
/evidence="ECO:0000244|PDB:2VHF"
HELIX 920..925
/evidence="ECO:0000244|PDB:2VHF"
HELIX 928..930
/evidence="ECO:0000244|PDB:2VHF"
HELIX 935..940
/evidence="ECO:0000244|PDB:2VHF"
STRAND 944..948
/evidence="ECO:0000244|PDB:2VHF"
HELIX 950..952
/evidence="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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EIAAB10293 Bos taurus,Bovine,CYLD,CYLD1,Deubiquitinating enzyme CYLD,Ubiquitin carboxyl-terminal hydrolase CYLD,Ubiquitin thiolesterase CYLD,Ubiquitin-specific-processing protease CYLD
EIAAB10292 Cyld,Cyld1,Deubiquitinating enzyme CYLD,Rat,Rattus norvegicus,Ubiquitin carboxyl-terminal hydrolase CYLD,Ubiquitin thiolesterase CYLD,Ubiquitin-specific-processing protease CYLD
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CSB-EL006380RA Rat Ubiquitin carboxyl-terminal hydrolase CYLD(CYLD) ELISA kit SpeciesRat 96T
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I0178 Ubiquitin carboxyl-terminal hydrolase CYLD (CYLD), Human, ELISA Kit 96T
I0177 Ubiquitin carboxyl-terminal hydrolase CYLD (CYLD), Bovine, ELISA Kit 96T
CSB-EL006380MO Mouse Ubiquitin carboxyl-terminal hydrolase CYLD(CYLD) ELISA kit 96T
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EIAAB45096 Deubiquitinating enzyme 7,HAUSP,Herpesvirus-associated ubiquitin-specific protease,Homo sapiens,Human,Ubiquitin carboxyl-terminal hydrolase 7,Ubiquitin thioesterase 7,Ubiquitin-specific-processing pro
EIAAB45055 Deubiquitinating enzyme 4,Rat,Rattus norvegicus,Ubiquitin carboxyl-terminal hydrolase 4,Ubiquitin thioesterase 4,Ubiquitin-specific-processing protease 4,Usp4
EIAAB44991 Deubiquitinating enzyme 16,Homo sapiens,Human,MSTP039,Ubiquitin carboxyl-terminal hydrolase 16,Ubiquitin thiolesterase 16,Ubiquitin-processing protease UBP-M,Ubiquitin-specific-processing protease 16,
EIAAB45002 41 kDa ubiquitin-specific protease,Deubiquitinating enzyme 2,Rat,Rattus norvegicus,Ubiquitin carboxyl-terminal hydrolase 2,Ubiquitin thiolesterase 2,Ubiquitin-specific-processing protease 2,Ubiquitin-
EIAAB45093 Chicken,Deubiquitinating enzyme 7,Gallus gallus,Ubiquitin carboxyl-terminal hydrolase 7,Ubiquitin thioesterase 7,Ubiquitin-specific-processing protease 7,USP7
EIAAB45022 Deubiquitinating enzyme 27,Homo sapiens,Human,Ubiquitin carboxyl-terminal hydrolase 22-like,Ubiquitin carboxyl-terminal hydrolase 27,Ubiquitin thiolesterase 27,Ubiquitin-specific-processing protease 2
EIAAB45023 Deubiquitinating enzyme 27,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase 27,Ubiquitin thiolesterase 27,Ubiquitin-specific-processing protease 27,Usp27,Usp27x,X-linked ubiquitin carboxyl-ter
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Pathways :
WP457: TNF-alpha NF-kB Signaling Pathway
WP1449: Regulation of toll-like receptor signaling pathway
WP1047: TNF-alpha NF-kB Signaling Pathway
WP1163: TNF-alpha NF-kB Signaling Pathway
WP2199: Seed Development
WP811: TNF-alpha NF-kB Signaling Pathway
WP929: TNF-alpha NF-kB Signaling Pathway
WP1369: TNF-alpha NF-kB Signaling Pathway
WP246: TNF-alpha NF-kB Signaling Pathway
WP2292: Chemokine signaling pathway
WP2359: Parkin-Ubiquitin Proteasomal System pathway
WP211: BMP signaling pathway
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP142: mRNA processing
WP2349: vitamin B3 (niacin), NAD and NADP biosynthesis pathway
WP2344: vitamin B6 (pyridoxine, pyridoxal, pyridoxamine) biosynthesis and salvage pathway
WP1000: Arachidonate Epoxygenase Epoxide Hydrolase
WP1838: Interleukin-1 processing
WP1890: Processing of Capped Intronless Pre-mRNA
WP1116: Arachidonate Epoxygenase Epoxide Hydrolase
WP529: mRNA processing
WP1229: mRNA processing
WP793: mRNA processing
WP1285: Arachidonate Epoxygenase Epoxide Hydrolase

Related Genes :
[CYLD CYLD1 KIAA0849 HSPC057] Ubiquitin carboxyl-terminal hydrolase CYLD (EC 3.4.19.12) (Deubiquitinating enzyme CYLD) (Ubiquitin thioesterase CYLD) (Ubiquitin-specific-processing protease CYLD)
[Cyld Cyld1 Kiaa0849] Ubiquitin carboxyl-terminal hydrolase CYLD (EC 3.4.19.12) (Deubiquitinating enzyme CYLD) (Ubiquitin thioesterase CYLD) (Ubiquitin-specific-processing protease CYLD)
[Cyld Cyld1] Ubiquitin carboxyl-terminal hydrolase CYLD (EC 3.4.19.12) (Deubiquitinating enzyme CYLD) (Ubiquitin thioesterase CYLD) (Ubiquitin-specific-processing protease CYLD)
[CYLD CYLD1] Ubiquitin carboxyl-terminal hydrolase CYLD (EC 3.4.19.12) (Deubiquitinating enzyme CYLD) (Ubiquitin thioesterase CYLD) (Ubiquitin-specific-processing protease CYLD)
[CYLD CYLD1] Ubiquitin carboxyl-terminal hydrolase CYLD (EC 3.4.19.12) (Deubiquitinating enzyme CYLD) (Ubiquitin thioesterase CYLD) (Ubiquitin-specific-processing protease CYLD)
[USP17L2 DUB3 USP17 USP17H USP17I USP17J USP17K USP17L USP17M] Ubiquitin carboxyl-terminal hydrolase 17 (USP17) (EC 3.4.19.12) (Deubiquitinating enzyme 17-like protein 2) (Deubiquitinating protein 3) (DUB-3) (Ubiquitin carboxyl-terminal hydrolase 17-like protein 2) (Ubiquitin thioesterase 17-like protein 2) (Ubiquitin-specific-processing protease 17-like protein 2)
[USP7 HAUSP] Ubiquitin carboxyl-terminal hydrolase 7 (EC 3.4.19.12) (Deubiquitinating enzyme 7) (Herpesvirus-associated ubiquitin-specific protease) (Ubiquitin thioesterase 7) (Ubiquitin-specific-processing protease 7)
[USP9X DFFRX FAM USP9] Probable ubiquitin carboxyl-terminal hydrolase FAF-X (EC 3.4.19.12) (Deubiquitinating enzyme FAF-X) (Fat facets in mammals) (hFAM) (Fat facets protein-related, X-linked) (Ubiquitin thioesterase FAF-X) (Ubiquitin-specific protease 9, X chromosome) (Ubiquitin-specific-processing protease FAF-X)
[USP15 KIAA0529] Ubiquitin carboxyl-terminal hydrolase 15 (EC 3.4.19.12) (Deubiquitinating enzyme 15) (Ubiquitin thioesterase 15) (Ubiquitin-specific-processing protease 15) (Unph-2) (Unph4)
[USP25 USP21] Ubiquitin carboxyl-terminal hydrolase 25 (EC 3.4.19.12) (Deubiquitinating enzyme 25) (USP on chromosome 21) (Ubiquitin thioesterase 25) (Ubiquitin-specific-processing protease 25)
[USP11 UHX1] Ubiquitin carboxyl-terminal hydrolase 11 (EC 3.4.19.12) (Deubiquitinating enzyme 11) (Ubiquitin thioesterase 11) (Ubiquitin-specific-processing protease 11)
[USP10 KIAA0190] Ubiquitin carboxyl-terminal hydrolase 10 (EC 3.4.19.12) (Deubiquitinating enzyme 10) (Ubiquitin thioesterase 10) (Ubiquitin-specific-processing protease 10)
[USP28 KIAA1515] Ubiquitin carboxyl-terminal hydrolase 28 (EC 3.4.19.12) (Deubiquitinating enzyme 28) (Ubiquitin thioesterase 28) (Ubiquitin-specific-processing protease 28)
[UBP3 YER151C] Ubiquitin carboxyl-terminal hydrolase 3 (EC 3.4.19.12) (Deubiquitinating enzyme 3) (Ubiquitin thioesterase 3) (Ubiquitin-specific-processing protease 3)
[USP22 KIAA1063 USP3L] Ubiquitin carboxyl-terminal hydrolase 22 (EC 3.4.19.12) (Deubiquitinating enzyme 22) (Ubiquitin thioesterase 22) (Ubiquitin-specific-processing protease 22)
[Usp25] Ubiquitin carboxyl-terminal hydrolase 25 (EC 3.4.19.12) (Deubiquitinating enzyme 25) (Ubiquitin thioesterase 25) (Ubiquitin-specific-processing protease 25) (mUSP25)
[USP6 HRP1 TRE2] Ubiquitin carboxyl-terminal hydrolase 6 (EC 3.4.19.12) (Deubiquitinating enzyme 6) (Proto-oncogene TRE-2) (Ubiquitin thioesterase 6) (Ubiquitin-specific-processing protease 6)
[USP44] Ubiquitin carboxyl-terminal hydrolase 44 (EC 3.4.19.12) (Deubiquitinating enzyme 44) (Ubiquitin thioesterase 44) (Ubiquitin-specific-processing protease 44)
[scny Usp36 CG5505] Ubiquitin carboxyl-terminal hydrolase 36 (EC 3.4.19.12) (Deubiquitinating enzyme 36) (Protein scrawny) (Ubiquitin thioesterase 36) (Ubiquitin-specific-processing protease 36)
[USP45] Ubiquitin carboxyl-terminal hydrolase 45 (EC 3.4.19.12) (Deubiquitinating enzyme 45) (Ubiquitin thioesterase 45) (Ubiquitin-specific-processing protease 45)
[OTULIN FAM105B] Ubiquitin thioesterase otulin (EC 3.4.19.12) (Deubiquitinating enzyme otulin) (OTU domain-containing deubiquitinase with linear linkage specificity) (Ubiquitin thioesterase Gumby)
[Usp10 Kiaa0190 Ode-1 Uchrp] Ubiquitin carboxyl-terminal hydrolase 10 (EC 3.4.19.12) (Deubiquitinating enzyme 10) (Ubiquitin thioesterase 10) (Ubiquitin-specific-processing protease 10)
[ubp9 SPBC1703.12] Probable ubiquitin carboxyl-terminal hydrolase 9 (EC 3.4.19.12) (Deubiquitinating enzyme 9) (Ubiquitin thioesterase 9) (Ubiquitin-specific-processing protease 9)
[Usp15 ubp109] Ubiquitin carboxyl-terminal hydrolase 15 (EC 3.4.19.12) (Deubiquitinating enzyme 15) (Ubiquitin carboxyl-terminal hydrolase of 109 kDa) (Ubiquitin thioesterase 15) (Ubiquitin-specific-processing protease 15)
[USP9Y DFFRY] Probable ubiquitin carboxyl-terminal hydrolase FAF-Y (EC 3.4.19.12) (Deubiquitinating enzyme FAF-Y) (Fat facets protein-related, Y-linked) (Ubiquitin thioesterase FAF-Y) (Ubiquitin-specific protease 9, Y chromosome) (Ubiquitin-specific-processing protease FAF-Y)
[Usp44] Ubiquitin carboxyl-terminal hydrolase 44 (EC 3.4.19.12) (Deubiquitinating enzyme 44) (Ubiquitin thioesterase 44) (Ubiquitin-specific-processing protease 44)
[USP51] Ubiquitin carboxyl-terminal hydrolase 51 (EC 3.4.19.12) (Deubiquitinating enzyme 51) (Ubiquitin thioesterase 51) (Ubiquitin-specific-processing protease 51)
[Usp10] Ubiquitin carboxyl-terminal hydrolase 10 (EC 3.4.19.12) (Deubiquitinating enzyme 10) (Ubiquitin thioesterase 10) (Ubiquitin-specific-processing protease 10)
[Usp15 Kiaa0529] Ubiquitin carboxyl-terminal hydrolase 15 (EC 3.4.19.12) (Deubiquitinating enzyme 15) (Ubiquitin thioesterase 15) (Ubiquitin-specific-processing protease 15)
[faf CG1945] Probable ubiquitin carboxyl-terminal hydrolase FAF (EC 3.4.19.12) (Protein fat facets) (Ubiquitin thioesterase FAF) (Ubiquitin-specific-processing protease FAF) (Deubiquitinating enzyme FAF)

Bibliography :
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