Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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

 CYLD_MOUSE              Reviewed;         952 AA.
Q80TQ2; Q80VB3; Q8BXZ3; Q8BYL9; Q8CGB0;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 2.
27-SEP-2017, entry version 135.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase CYLD;
EC=3.4.19.12 {ECO:0000250|UniProtKB:Q9NQC7};
AltName: Full=Deubiquitinating enzyme CYLD;
AltName: Full=Ubiquitin thioesterase CYLD;
AltName: Full=Ubiquitin-specific-processing protease CYLD;
Name=Cyld; Synonyms=Cyld1, Kiaa0849;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-620 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Cerebellum, and Hypothalamus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=FVB/N; TISSUE=Mammary gland;
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).
[4]
FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH BCL3, AND SUBCELLULAR
LOCATION.
PubMed=16713561; DOI=10.1016/j.cell.2006.03.041;
Massoumi R., Chmielarska K., Hennecke K., Pfeifer A., Fassler R.;
"Cyld inhibits tumor cell proliferation by blocking Bcl-3-dependent
NF-kappaB signaling.";
Cell 125:665-677(2006).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16501569; DOI=10.1038/ni1315;
Reiley W.W., Zhang M., Jin W., Losiewicz M., Donohue K.B.,
Norbury C.C., Sun S.C.;
"Regulation of T cell development by the deubiquitinating enzyme
CYLD.";
Nat. Immunol. 7:411-417(2006).
[6]
FUNCTION, INTERACTION WITH MAP3K7, AND DISRUPTION PHENOTYPE.
PubMed=17548520; DOI=10.1084/jem.20062694;
Reiley W.W., Jin W., Lee A.J., Wright A., Wu X., Tewalt E.F.,
Leonard T.O., Norbury C.C., Fitzpatrick L., Zhang M., Sun S.C.;
"Deubiquitinating enzyme CYLD negatively regulates the ubiquitin-
dependent kinase Tak1 and prevents abnormal T cell responses.";
J. Exp. Med. 204:1475-1485(2007).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18643924; DOI=10.1111/j.1462-5822.2008.01204.x;
Lim J.H., Ha U.H., Woo C.H., Xu H., Li J.D.;
"CYLD is a crucial negative regulator of innate immune response in
Escherichia coli pneumonia.";
Cell. Microbiol. 10:2247-2256(2008).
[8]
DISRUPTION PHENOTYPE, FUNCTION, INTERACTION WITH SQSTM1,
IDENTIFICATION IN A COMPLEX WITH TRAF6 AND SQSTM1, AND INDUCTION.
PubMed=18382763; DOI=10.1172/JCI34257;
Jin W., Chang M., Paul E.M., Babu G., Lee A.J., Reiley W., Wright A.,
Zhang M., You J., Sun S.C.;
"Deubiquitinating enzyme CYLD negatively regulates RANK signaling and
osteoclastogenesis in mice.";
J. Clin. Invest. 118:1858-1866(2008).
[9]
FUNCTION.
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Kidney;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
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).
[12]
FUNCTION, AND SUBCELLULAR LOCATION.
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).
-!- 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. Contributes to the regulation of cell survival,
proliferation and differentiation via its effects on NF-kappa-B
activation. Negative regulator of Wnt signaling. Inhibits HDAC6
and thereby promotes acetylation of alpha-tubulin and
stabilization of microtubules. Plays a role in the regulation of
microtubule dynamics, and thereby contributes to the regulation of
cell proliferation, cell polarization, cell migration, and
angiogenesis. Required for normal cell cycle progress and normal
cytokinesis. Inhibits nuclear translocation of NF-kappa-B (By
similarity). Plays a role in the regulation of inflammation and
the innate immune response, via its effects on NF-kappa-B
activation. 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. 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
(PubMed:25134987). 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
(By similarity). {ECO:0000250|UniProtKB:Q9NQC7,
ECO:0000269|PubMed:16501569, ECO:0000269|PubMed:16713561,
ECO:0000269|PubMed:17548520, ECO:0000269|PubMed:18382763,
ECO:0000269|PubMed:18643924, ECO:0000269|PubMed:19893491,
ECO:0000269|PubMed:20194890, ECO:0000269|PubMed:25134987}.
-!- 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:0000250|UniProtKB:Q9NQC7}.
-!- 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 (By
similarity). 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. Interacts with
CEP350 (By similarity). Interacts with RNF31 (By similarity).
{ECO:0000250|UniProtKB:Q9NQC7, ECO:0000269|PubMed:16713561,
ECO:0000269|PubMed:17548520, ECO:0000269|PubMed:18382763,
ECO:0000269|PubMed:19893491}.
-!- INTERACTION:
Q9Z2F6:Bcl3; NbExp=5; IntAct=EBI-943859, EBI-943884;
Q9Z2V5:Hdac6; NbExp=3; IntAct=EBI-943859, EBI-1009256;
Q8C863:Itch; NbExp=2; IntAct=EBI-943859, EBI-851782;
P68369:Tuba1a; NbExp=5; IntAct=EBI-943859, EBI-400542;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
Cytoplasm, cytoskeleton. Cell membrane
{ECO:0000250|UniProtKB:Q9NQC7}; Peripheral membrane protein
{ECO:0000250|UniProtKB:Q9NQC7}; Cytoplasmic side
{ECO:0000250|UniProtKB:Q9NQC7}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:Q9NQC7}. Cytoplasm, cytoskeleton, spindle
{ECO:0000250|UniProtKB:Q9NQC7}. Cytoplasm, cytoskeleton, cilium
basal body {ECO:0000269|PubMed:25134987}. Note=Detected at the
microtubule cytoskeleton during interphase (By similarity).
Detected at the midbody during telophase (By similarity). During
metaphase, it remains localized to the centrosome but is also
present along the spindle (By similarity).
{ECO:0000250|UniProtKB:Q9NQC7, ECO:0000269|PubMed:25134987}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=2;
IsoId=Q80TQ2-1; Sequence=Displayed;
Name=1;
IsoId=Q80TQ2-2; Sequence=VSP_011278;
Name=3;
IsoId=Q80TQ2-3; Sequence=VSP_011279, VSP_011280;
-!- INDUCTION: Up-regulated by TNFRSF11A.
{ECO:0000269|PubMed:18382763}.
-!- 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 (By similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: No obvious phenotype, but mice are highly
susceptible to carcinogens and are prone to chemically induced
skin tumors. The number of natural killer T-cells is much reduced.
Animals are highly susceptible to bacteria-induced pneumonia, due
to an over active innate immune response. Animals spontaneously
develop colonic inflammation, due to constitutive expression of
several proinflammatory genes in the colon. Animals exhibit
abnormal osteoclast differentiation, leading to osteoporosis.
{ECO:0000269|PubMed:16501569, ECO:0000269|PubMed:16713561,
ECO:0000269|PubMed:17548520, ECO:0000269|PubMed:18382763,
ECO:0000269|PubMed:18643924}.
-!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC65671.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AK122389; BAC65671.1; ALT_INIT; mRNA.
EMBL; AK039054; BAC30222.1; -; mRNA.
EMBL; AK042764; BAC31357.1; -; mRNA.
EMBL; BC042438; AAH42438.1; -; mRNA.
EMBL; BC049879; AAH49879.1; -; mRNA.
CCDS; CCDS22513.1; -. [Q80TQ2-1]
CCDS; CCDS52633.1; -. [Q80TQ2-2]
RefSeq; NP_001121642.1; NM_001128170.2. [Q80TQ2-2]
RefSeq; NP_001121643.1; NM_001128171.2. [Q80TQ2-1]
RefSeq; NP_775545.1; NM_173369.3. [Q80TQ2-1]
RefSeq; XP_006531477.1; XM_006531414.1. [Q80TQ2-2]
RefSeq; XP_006531478.1; XM_006531415.1. [Q80TQ2-2]
RefSeq; XP_006531479.1; XM_006531416.3. [Q80TQ2-2]
RefSeq; XP_006531480.1; XM_006531417.2. [Q80TQ2-2]
RefSeq; XP_006531481.1; XM_006531418.2. [Q80TQ2-2]
RefSeq; XP_011246825.1; XM_011248523.2. [Q80TQ2-2]
RefSeq; XP_011246826.1; XM_011248524.1. [Q80TQ2-2]
RefSeq; XP_011246827.1; XM_011248525.2. [Q80TQ2-2]
RefSeq; XP_017168478.1; XM_017312989.1. [Q80TQ2-2]
UniGene; Mm.490395; -.
ProteinModelPortal; Q80TQ2; -.
SMR; Q80TQ2; -.
BioGrid; 216612; 15.
DIP; DIP-35656N; -.
IntAct; Q80TQ2; 4.
MINT; MINT-7561827; -.
STRING; 10090.ENSMUSP00000096119; -.
MEROPS; C67.001; -.
iPTMnet; Q80TQ2; -.
PhosphoSitePlus; Q80TQ2; -.
SwissPalm; Q80TQ2; -.
EPD; Q80TQ2; -.
PaxDb; Q80TQ2; -.
PeptideAtlas; Q80TQ2; -.
PRIDE; Q80TQ2; -.
Ensembl; ENSMUST00000098519; ENSMUSP00000096119; ENSMUSG00000036712. [Q80TQ2-2]
Ensembl; ENSMUST00000109626; ENSMUSP00000105254; ENSMUSG00000036712. [Q80TQ2-1]
Ensembl; ENSMUST00000209532; ENSMUSP00000147654; ENSMUSG00000036712. [Q80TQ2-2]
Ensembl; ENSMUST00000209559; ENSMUSP00000147426; ENSMUSG00000036712. [Q80TQ2-1]
Ensembl; ENSMUST00000211554; ENSMUSP00000148037; ENSMUSG00000036712. [Q80TQ2-1]
GeneID; 74256; -.
KEGG; mmu:74256; -.
UCSC; uc009mrt.3; mouse. [Q80TQ2-1]
UCSC; uc033jgq.1; mouse. [Q80TQ2-3]
UCSC; uc033jgr.1; mouse. [Q80TQ2-2]
CTD; 1540; -.
MGI; MGI:1921506; Cyld.
eggNOG; KOG3556; Eukaryota.
eggNOG; ENOG410XP6I; LUCA.
GeneTree; ENSGT00390000018123; -.
HOGENOM; HOG000006796; -.
HOVERGEN; HBG051281; -.
InParanoid; Q80TQ2; -.
KO; K08601; -.
OrthoDB; EOG091G015D; -.
PhylomeDB; Q80TQ2; -.
BRENDA; 3.4.19.12; 3474.
Reactome; R-MMU-168638; NOD1/2 Signaling Pathway.
Reactome; R-MMU-5357786; TNFR1-induced proapoptotic signaling.
Reactome; R-MMU-5357905; Regulation of TNFR1 signaling.
Reactome; R-MMU-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
Reactome; R-MMU-936440; Negative regulators of DDX58/IFIH1 signaling.
PRO; PR:Q80TQ2; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000036712; -.
CleanEx; MM_CYLD; -.
ExpressionAtlas; Q80TQ2; baseline and differential.
Genevisible; Q80TQ2; MM.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
GO; GO:0097542; C:ciliary tip; IDA:UniProtKB.
GO; GO:0005881; C:cytoplasmic microtubule; IEA:Ensembl.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISO:MGI.
GO; GO:0030496; C:midbody; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005819; C:spindle; ISS:UniProtKB.
GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IDA:MGI.
GO; GO:0061578; F:Lys63-specific deubiquitinase activity; IDA:MGI.
GO; GO:0070064; F:proline-rich region binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0043369; P:CD4-positive or CD8-positive, alpha-beta T cell lineage commitment; IMP:MGI.
GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI.
GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
GO; GO:0070266; P:necroptotic process; IGI:MGI.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
GO; GO:0042347; P:negative regulation of NF-kappaB import into nucleus; ISS:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:0045581; P:negative regulation of T cell differentiation; IDA:MGI.
GO; GO:1903829; P:positive regulation of cellular protein localization; IDA:MGI.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0045582; P:positive regulation of T cell differentiation; IMP:MGI.
GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; IMP:MGI.
GO; GO:0016579; P:protein deubiquitination; IMP:MGI.
GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
GO; GO:1990108; P:protein linear deubiquitination; ISS:UniProtKB.
GO; GO:0045577; P:regulation of B cell differentiation; IMP:MGI.
GO; GO:1902017; P:regulation of cilium assembly; IMP:UniProtKB.
GO; GO:2001242; P:regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISO:MGI.
GO; GO:0007346; P:regulation of mitotic cell cycle; ISO:MGI.
GO; GO:0043393; P:regulation of protein binding; IDA:MGI.
GO; GO:0050856; P:regulation of T cell receptor signaling pathway; ISO:MGI.
GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; ISS:UniProtKB.
GO; GO:1901026; P:ripoptosome assembly involved in necroptotic process; IMP:MGI.
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; 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;
Alternative splicing; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Cytoskeleton; Hydrolase; Immunity;
Innate immunity; Membrane; Metal-binding; Microtubule; Phosphoprotein;
Protease; Reference proteome; Repeat; Thiol protease;
Ubl conjugation pathway; Wnt signaling pathway; Zinc.
CHAIN 1 952 Ubiquitin carboxyl-terminal hydrolase
CYLD.
/FTId=PRO_0000080699.
DOMAIN 153 198 CAP-Gly 1. {ECO:0000255|PROSITE-
ProRule:PRU00045}.
DOMAIN 253 286 CAP-Gly 2. {ECO:0000255|PROSITE-
ProRule:PRU00045}.
DOMAIN 488 531 CAP-Gly 3. {ECO:0000255|PROSITE-
ProRule:PRU00045}.
DOMAIN 588 946 USP.
REGION 106 589 Interaction with TRIP. {ECO:0000250}.
REGION 390 465 Interaction with TRAF2. {ECO:0000250}.
REGION 466 680 Interaction with IKBKG/NEMO.
{ECO:0000250}.
ACT_SITE 597 597 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10092}.
ACT_SITE 867 867 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10092}.
METAL 784 784 Zinc 1. {ECO:0000250}.
METAL 787 787 Zinc 1. {ECO:0000250}.
METAL 795 795 Zinc 2. {ECO:0000250}.
METAL 798 798 Zinc 2. {ECO:0000250}.
METAL 813 813 Zinc 1. {ECO:0000250}.
METAL 816 816 Zinc 1. {ECO:0000250}.
METAL 821 821 Zinc 2. {ECO:0000250}.
METAL 829 829 Zinc 2. {ECO:0000250}.
MOD_RES 383 383 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NQC7}.
MOD_RES 414 414 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 418 418 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NQC7}.
VAR_SEQ 304 304 P -> PALS (in isoform 1).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_011278.
VAR_SEQ 305 318 DSVTQERRPPKLAF -> GTSKNILDQQLKGK (in
isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_011279.
VAR_SEQ 319 952 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_011280.
CONFLICT 403 403 M -> V (in Ref. 2; BAC30222).
{ECO:0000305}.
SEQUENCE 952 AA; 106586 MW; 0AC0C7D4FF215A9C CRC64;
MSSGLWSQEK VTSPYWEERI FYLLLQECSV TDKQTQKLLK VPKGSIGQYI QDRSVGHSRV
PSTKGKKNQI GLKILEQPHA VLFVDEKDVV EINEKFTELL LAITNCEERL SLFRNRLRLS
KGLQVDVGSP VKVQLRSGEE KFPGVVRFRG PLLAERTVSG IFFGVELLEE GRGQGFTDGV
YQGKQLFQCD EDCGVFVALD KLELIEDDDN GLESDFAGPG DTMQVEPPPL EINSRVSLKV
GESTESGTVI FCDVLPGKES LGYFVGVDMD NPIGNWDGRF DGVQLCSFAS VESTILLHIN
DIIPDSVTQE RRPPKLAFMS RGVGDKGSSS HNKPKVTGST SDPGSRNRSE LFYTLNGSSV
DSQQSKSKNP WYIDEVAEDP AKSLTEMSSD FGHSSPPPQP PSMNSLSSEN RFHSLPFSLT
KMPNTNGSMA HSPLSLSVQS VMGELNSTPV QESPPLPISS GNAHGLEVGS LAEVKENPPF
YGVIRWIGQP PGLSDVLAGL ELEDECAGCT DGTFRGTRYF TCALKKALFV KLKSCRPDSR
FASLQPVSNQ IERCNSLAFG GYLSEVVEEN TPPKMEKEGL EIMIGKKKGI QGHYNSCYLD
STLFCLFAFS SALDTVLLRP KEKNDIEYYS ETQELLRTEI VNPLRIYGYV CATKIMKLRK
ILEKVEAASG FTSEEKDPEE FLNILFHDIL RVEPLLKIRS AGQKVQDCNF YQIFMEKNEK
VGVPTIQQLL EWSFINSNLK FAEAPSCLII QMPRFGKDFK LFKKIFPSLE LNITDLLEDT
PRQCRICGGL AMYECRECYD DPDISAGKIK QFCKTCSTQV HLHPRRLNHS YHPVSLPKDL
PDWDWRHGCI PCQKMELFAV LCIETSHYVA FVKYGKDDSA WLFFDSMADR DGGQNGFNIP
QVTPCPEVGE YLKMSLEDLH SLDSRRIQGC ARRLLCDAYM CMYQSPTMSL YK


Related products :

Catalog number Product name Quantity
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
EIAAB10294 Cyld,Cyld1,Deubiquitinating enzyme CYLD,Kiaa0849,Mouse,Mus musculus,Ubiquitin carboxyl-terminal hydrolase CYLD,Ubiquitin thiolesterase CYLD,Ubiquitin-specific-processing protease CYLD
EIAAB10291 CYLD,CYLD1,Deubiquitinating enzyme CYLD,Homo sapiens,HSPC057,Human,KIAA0849,Ubiquitin carboxyl-terminal hydrolase CYLD,Ubiquitin thiolesterase CYLD,Ubiquitin-specific-processing protease CYLD
I0179 Ubiquitin carboxyl-terminal hydrolase CYLD (CYLD), Mouse, ELISA Kit 96T
CSB-EL006380HU Human Ubiquitin carboxyl-terminal hydrolase CYLD(CYLD) ELISA kit 96T
CSB-EL006380RA Rat Ubiquitin carboxyl-terminal hydrolase CYLD(CYLD) ELISA kit SpeciesRat 96T
CSB-EL006380BO Bovine Ubiquitin carboxyl-terminal hydrolase CYLD(CYLD) ELISA kit 96T
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
I0180 Ubiquitin carboxyl-terminal hydrolase CYLD (CYLD), Rat, ELISA Kit 96T
CSB-EL006380RA Rat Ubiquitin carboxyl-terminal hydrolase CYLD(CYLD) ELISA kit 96T
CYLD_RAT ELISA Kit FOR Ubiquitin carboxyl-terminal hydrolase CYLD; organism: Rat; gene name: Cyld 96T
CSB-EL006380BO Bovine Ubiquitin carboxyl-terminal hydrolase CYLD(CYLD) ELISA kit SpeciesBovine 96T
CSB-EL006380MO Mouse Ubiquitin carboxyl-terminal hydrolase CYLD(CYLD) ELISA kit SpeciesMouse 96T
CSB-EL006380HU Human Ubiquitin carboxyl-terminal hydrolase CYLD(CYLD) ELISA kit SpeciesHuman 96T
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
EIAAB44981 Deubiquitinating enzyme 12,Mouse,Mus musculus,Ubh1,Ubiquitin carboxyl-terminal hydrolase 12,Ubiquitin thiolesterase 12,Ubiquitin-hydrolyzing enzyme 1,Ubiquitin-specific-processing protease 12,Usp12


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur