Cyld
entrez
74256
canonical
uniprot
Q80TQ2
canonical
ensembl
ENSMUSG00000036712
resolver
ensp
ENSMUSP00000147426
resolver
ensp
ENSMUSP00000147654
resolver
ensp
ENSMUSP00000148037
resolver
ensp
ENSMUSP00000220766
resolver
ensp
ENSMUSP00000220768
resolver
ensp
ENSMUSP00000220769
resolver
ensp
ENSMUSP00000220770
resolver
ensp
ENSMUSP00000220771
resolver
ensp
ENSMUSP00000220772
resolver
ensp
ENSMUSP00000220773
resolver
ensp
ENSMUSP00000220797
resolver
ensp
ENSMUSP00000220798
resolver
genesymbol
Cyld
resolver
genesymbol_syn
Cyld1
resolver
genesymbol_syn
Kiaa0849
resolver
uniprot
A0A1B0GSE5
resolver
uniprot
Q3TJI3
resolver
uniprot
Q80VB3
resolver
uniprot
Q8BXZ3
resolver
uniprot
Q8BYL9
resolver
uniprot
Q8CGB0
resolver
uniprot_entry
CYLD_MOUSE
resolver
uniprot_sec
A0A1B0GSE5
resolver
uniprot_sec
Q3TJI3
resolver
uniprot_sec
Q80VB3
resolver
uniprot_sec
Q8BXZ3
resolver
uniprot_sec
Q8BYL9
resolver
uniprot_sec
Q8CGB0
resolver
amino_acid_sequence
MSSGLWSQEKVTSPYWEERIFYLLLQECSVTDKQTQKLLKVPKGSIGQYIQDRSVGHSRVPSTKGKKNQIGLKILEQPHAVLFVDEKDVVEINEKFTELLLAITNCEERLSLFRNRLRLSKGLQVDVGSPVKVQLRSGEEKFPGVVRFRGPLLAERTVSGIFFGVELLEEGRGQGFTDGVYQGKQLFQCDEDCGVFVALDKLELIEDDDNGLESDFAGPGDTMQVEPPPLEINSRVSLKVGESTESGTVIFCDVLPGKESLGYFVGVDMDNPIGNWDGRFDGVQLCSFASVESTILLHINDIIPDSVTQERRPPKLAFMSRGVGDKGSSSHNKPKVTGSTSDPGSRNRSELFYTLNGSSVDSQQSKSKNPWYIDEVAEDPAKSLTEMSSDFGHSSPPPQPPSMNSLSSENRFHSLPFSLTKMPNTNGSMAHSPLSLSVQSVMGELNSTPVQESPPLPISSGNAHGLEVGSLAEVKENPPFYGVIRWIGQPPGLSDVLAGLELEDECAGCTDGTFRGTRYFTCALKKALFVKLKSCRPDSRFASLQPVSNQIERCNSLAFGGYLSEVVEENTPPKMEKEGLEIMIGKKKGIQGHYNSCYLDSTLFCLFAFSSALDTVLLRPKEKNDIEYYSETQELLRTEIVNPLRIYGYVCATKIMKLRKILEKVEAASGFTSEEKDPEEFLNILFHDILRVEPLLKIRSAGQKVQDCNFYQIFMEKNEKVGVPTIQQLLEWSFINSNLKFAEAPSCLIIQMPRFGKDFKLFKKIFPSLELNITDLLEDTPRQCRICGGLAMYECRECYDDPDISAGKIKQFCKTCSTQVHLHPRRLNHSYHPVSLPKDLPDWDWRHGCIPCQKMELFAVLCIETSHYVAFVKYGKDDSAWLFFDSMADRDGGQNGFNIPQVTPCPEVGEYLKMSLEDLHSLDSRRIQGCARRLLCDAYMCMYQSPTMSLYK
uniprot
proteins
ec_number
3.4.19.12
uniprot
proteins
function
FUNCTION: Deubiquitinase that specifically cleaves 'Lys-63'- and linear 'Met-1'-linked polyubiquitin chains and is involved in NF-kappa-B activation and TNF-induced necroptosis (PubMed:17548520, PubMed:28701375, PubMed:29291351, PubMed:32185393, PubMed:32424362). Negatively regulates NF-kappa-B activation by deubiquitinating upstream signaling factors (PubMed:16713561). Contributes to the regulation of cell survival, proliferation and differentiation via its effects on NF-kappa-B activation (PubMed:16713561). Negative regulator of Wnt signaling. 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:16713561, PubMed:19893491, PubMed:20194890). Required for normal cell cycle progress and normal cytokinesis (PubMed:19893491). 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 (By similarity). Dispensable for the maturation of intrathymic natural killer cells, but required for the continued survival of immature natural killer cells (PubMed:16501569, PubMed:18643924). Negatively regulates TNFRSF11A signaling and osteoclastogenesis (PubMed:18382763). 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). Ability to remove linear ('Met-1'-linked) polyubiquitin chains regulates innate immunity and TNF-induced necroptosis: recruited to the LUBAC complex via interaction with SPATA2 and restricts linear polyubiquitin formation on target proteins (PubMed:28701375). Regulates innate immunity by restricting linear polyubiquitin formation on RIPK2 in response to NOD2 stimulation (By similarity). Involved in TNF-induced necroptosis by removing linear ('Met-1'-linked) polyubiquitin chains from RIPK1, thereby regulating the kinase activity of RIPK1 (PubMed:28701375). Negatively regulates intestinal inflammation by removing 'Lys-63' linked polyubiquitin chain of NLRP6, thereby reducing the interaction between NLRP6 and PYCARD/ASC and formation of the NLRP6 inflammasome (PubMed:32424362). Does not catalyze deubiquitination of heterotypic 'Lys-63'-/'Lys-48'-linked branched ubiquitin chains (By similarity). Removes 'Lys-63' linked polyubiquitin chain of MAP3K7, which inhibits phosphorylation and blocks downstream activation of the JNK-p38 kinase cascades (PubMed:17548520, PubMed:29291351). Also removes 'Lys-63'-linked polyubiquitin chains of MAP3K1 and MA3P3K3, which inhibit their interaction with MAP2K1 and MAP2K2 (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, ECO:0000269|PubMed:28701375, ECO:0000269|PubMed:29291351, ECO:0000269|PubMed:32185393, ECO:0000269|PubMed:32424362}.
uniprot
proteins
mass_dalton
106586
uniprot
proteins
mutagenesis
MUTAGEN 597; /note="C->A: Loss of deubiquitinating activity."; /evidence="ECO:0000269|PubMed:32424362"; MUTAGEN 677; /note="D->G: Decreased inhibition of NF-kappa-B."; /evidence="ECO:0000269|PubMed:32185393"; MUTAGEN 715; /note="M->V: Increased inhibition of NF-kappa-B."; /evidence="ECO:0000269|PubMed:32185393
uniprot
proteins
post_translational_modification
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. Phosphorylation at Ser-414 by IKKE/IKBKE inhibits the deubiquitinase activity, leading to activation by NF-kappa-B. {ECO:0000250|UniProtKB:Q9NQC7}.
uniprot
proteins
protein_family
Peptidase C19 family
uniprot
proteins
pubmed
12693553
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16501569
uniprot
proteins
pubmed
16713561
uniprot
proteins
pubmed
17548520
uniprot
proteins
pubmed
18382763
uniprot
proteins
pubmed
18643924
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19893491
uniprot
proteins
pubmed
20194890
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
25134987
uniprot
proteins
pubmed
28701375
uniprot
proteins
pubmed
29291351
uniprot
proteins
pubmed
32185393
uniprot
proteins
pubmed
32424362
uniprot
proteins
sequence_length
952
uniprot
proteins
subcellular_location
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}.
uniprot
proteins