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Q80TQ2

- CYLD_MOUSE

UniProt

Q80TQ2 - CYLD_MOUSE

Protein

Ubiquitin carboxyl-terminal hydrolase CYLD

Gene

Cyld

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (16 Aug 2004)
      Previous versions | rss
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    Functioni

    Protease 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.By similarity7 Publications

    Catalytic activityi

    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).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei597 – 5971NucleophilePROSITE-ProRule annotation
    Metal bindingi784 – 7841Zinc 1By similarity
    Metal bindingi787 – 7871Zinc 1By similarity
    Metal bindingi795 – 7951Zinc 2By similarity
    Metal bindingi798 – 7981Zinc 2By similarity
    Metal bindingi813 – 8131Zinc 1By similarity
    Metal bindingi816 – 8161Zinc 1By similarity
    Metal bindingi821 – 8211Zinc 2By similarity
    Metal bindingi829 – 8291Zinc 2By similarity
    Active sitei867 – 8671Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. Lys63-specific deubiquitinase activity Source: RefGenome
    2. protein binding Source: UniProtKB
    3. ubiquitin-specific protease activity Source: UniProtKB
    4. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. necroptotic process Source: MGI
    2. negative regulation of canonical Wnt signaling pathway Source: UniProtKB
    3. negative regulation of NF-kappaB import into nucleus Source: UniProtKB
    4. negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
    5. negative regulation of T cell differentiation Source: MGI
    6. positive regulation of extrinsic apoptotic signaling pathway Source: RefGenome
    7. protein deubiquitination Source: MGI
    8. protein K63-linked deubiquitination Source: UniProtKB
    9. regulation of intrinsic apoptotic signaling pathway Source: RefGenome
    10. regulation of microtubule cytoskeleton organization Source: Ensembl
    11. regulation of mitotic cell cycle Source: RefGenome
    12. ripoptosome assembly involved in necroptotic process Source: MGI
    13. ubiquitin-dependent protein catabolic process Source: InterPro
    14. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway, Wnt signaling pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_198532. Negative regulators of RIG-I/MDA5 signaling.
    REACT_211125. NOD1/2 Signaling Pathway.

    Protein family/group databases

    MEROPSiC67.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase CYLD (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme CYLD
    Ubiquitin thioesterase CYLD
    Ubiquitin-specific-processing protease CYLD
    Gene namesi
    Name:Cyld
    Synonyms:Cyld1, Kiaa0849
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:1921506. Cyld.

    Subcellular locationi

    Cytoplasm. Cytoplasmperinuclear region. Cytoplasmcytoskeleton. Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
    Note: Detected at the microtubule cytoskeleton during interphase. Detected at the midbody during telophase.

    GO - Cellular componenti

    1. cytoplasmic microtubule Source: Ensembl
    2. cytosol Source: UniProtKB
    3. extrinsic component of cytoplasmic side of plasma membrane Source: Ensembl
    4. midbody Source: Ensembl
    5. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Microtubule

    Pathology & Biotechi

    Disruption phenotypei

    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.5 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 952952Ubiquitin carboxyl-terminal hydrolase CYLDPRO_0000080699Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei414 – 4141PhosphoserineBy similarity

    Post-translational modificationi

    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.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ80TQ2.
    PaxDbiQ80TQ2.
    PRIDEiQ80TQ2.

    PTM databases

    PhosphoSiteiQ80TQ2.

    Expressioni

    Inductioni

    Up-regulated by TNFRSF11A.1 Publication

    Gene expression databases

    ArrayExpressiQ80TQ2.
    BgeeiQ80TQ2.
    CleanExiMM_CYLD.
    GenevestigatoriQ80TQ2.

    Interactioni

    Subunit structurei

    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.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Bcl3Q9Z2F65EBI-943859,EBI-943884
    Hdac6Q9Z2V53EBI-943859,EBI-1009256
    ItchQ8C8632EBI-943859,EBI-851782
    Tuba1aP683695EBI-943859,EBI-400542

    Protein-protein interaction databases

    BioGridi216612. 13 interactions.
    IntActiQ80TQ2. 4 interactions.
    MINTiMINT-7561827.

    Structurei

    3D structure databases

    ProteinModelPortaliQ80TQ2.
    SMRiQ80TQ2. Positions 125-206, 228-306, 453-546, 579-952.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini153 – 19846CAP-Gly 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini253 – 28634CAP-Gly 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini488 – 53144CAP-Gly 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini588 – 946359USPAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni106 – 589484Interaction with TRIPBy similarityAdd
    BLAST
    Regioni390 – 46576Interaction with TRAF2By similarityAdd
    BLAST
    Regioni466 – 680215Interaction with IKBKG/NEMOBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C19 family.Curated
    Contains 3 CAP-Gly domains.PROSITE-ProRule annotation
    Contains 1 USP domain.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG313578.
    GeneTreeiENSGT00390000018123.
    HOGENOMiHOG000006796.
    HOVERGENiHBG051281.
    KOiK08601.
    OrthoDBiEOG72ZCDM.
    PhylomeDBiQ80TQ2.

    Family and domain databases

    Gene3Di2.30.30.190. 3 hits.
    InterProiIPR000938. CAP-Gly_domain.
    IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    [Graphical view]
    PfamiPF01302. CAP_GLY. 3 hits.
    PF00443. UCH. 1 hit.
    [Graphical view]
    SMARTiSM01052. CAP_GLY. 3 hits.
    [Graphical view]
    SUPFAMiSSF74924. SSF74924. 3 hits.
    PROSITEiPS00845. CAP_GLY_1. 1 hit.
    PS50245. CAP_GLY_2. 2 hits.
    PS00972. USP_1. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 2 (identifier: Q80TQ2-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSSGLWSQEK VTSPYWEERI FYLLLQECSV TDKQTQKLLK VPKGSIGQYI    50
    QDRSVGHSRV PSTKGKKNQI GLKILEQPHA VLFVDEKDVV EINEKFTELL 100
    LAITNCEERL SLFRNRLRLS KGLQVDVGSP VKVQLRSGEE KFPGVVRFRG 150
    PLLAERTVSG IFFGVELLEE GRGQGFTDGV YQGKQLFQCD EDCGVFVALD 200
    KLELIEDDDN GLESDFAGPG DTMQVEPPPL EINSRVSLKV GESTESGTVI 250
    FCDVLPGKES LGYFVGVDMD NPIGNWDGRF DGVQLCSFAS VESTILLHIN 300
    DIIPDSVTQE RRPPKLAFMS RGVGDKGSSS HNKPKVTGST SDPGSRNRSE 350
    LFYTLNGSSV DSQQSKSKNP WYIDEVAEDP AKSLTEMSSD FGHSSPPPQP 400
    PSMNSLSSEN RFHSLPFSLT KMPNTNGSMA HSPLSLSVQS VMGELNSTPV 450
    QESPPLPISS GNAHGLEVGS LAEVKENPPF YGVIRWIGQP PGLSDVLAGL 500
    ELEDECAGCT DGTFRGTRYF TCALKKALFV KLKSCRPDSR FASLQPVSNQ 550
    IERCNSLAFG GYLSEVVEEN TPPKMEKEGL EIMIGKKKGI QGHYNSCYLD 600
    STLFCLFAFS SALDTVLLRP KEKNDIEYYS ETQELLRTEI VNPLRIYGYV 650
    CATKIMKLRK ILEKVEAASG FTSEEKDPEE FLNILFHDIL RVEPLLKIRS 700
    AGQKVQDCNF YQIFMEKNEK VGVPTIQQLL EWSFINSNLK FAEAPSCLII 750
    QMPRFGKDFK LFKKIFPSLE LNITDLLEDT PRQCRICGGL AMYECRECYD 800
    DPDISAGKIK QFCKTCSTQV HLHPRRLNHS YHPVSLPKDL PDWDWRHGCI 850
    PCQKMELFAV LCIETSHYVA FVKYGKDDSA WLFFDSMADR DGGQNGFNIP 900
    QVTPCPEVGE YLKMSLEDLH SLDSRRIQGC ARRLLCDAYM CMYQSPTMSL 950
    YK 952
    Length:952
    Mass (Da):106,586
    Last modified:August 16, 2004 - v2
    Checksum:i0AC0C7D4FF215A9C
    GO
    Isoform 1 (identifier: Q80TQ2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         304-304: P → PALS

    Show »
    Length:955
    Mass (Da):106,857
    Checksum:iE8D55AE26D90241F
    GO
    Isoform 3 (identifier: Q80TQ2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         305-318: DSVTQERRPPKLAF → GTSKNILDQQLKGK
         319-952: Missing.

    Show »
    Length:318
    Mass (Da):35,288
    Checksum:i23465D36304356BF
    GO

    Sequence cautioni

    The sequence BAC65671.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti403 – 4031M → V in BAC30222. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei304 – 3041P → PALS in isoform 1. 1 PublicationVSP_011278
    Alternative sequencei305 – 31814DSVTQ…PKLAF → GTSKNILDQQLKGK in isoform 3. 1 PublicationVSP_011279Add
    BLAST
    Alternative sequencei319 – 952634Missing in isoform 3. 1 PublicationVSP_011280Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK122389 mRNA. Translation: BAC65671.1. Different initiation.
    AK039054 mRNA. Translation: BAC30222.1.
    AK042764 mRNA. Translation: BAC31357.1.
    BC042438 mRNA. Translation: AAH42438.1.
    BC049879 mRNA. Translation: AAH49879.1.
    CCDSiCCDS22513.1. [Q80TQ2-1]
    CCDS52633.1. [Q80TQ2-2]
    RefSeqiNP_001121642.1. NM_001128170.2. [Q80TQ2-2]
    NP_001121643.1. NM_001128171.2. [Q80TQ2-1]
    NP_775545.1. NM_173369.3. [Q80TQ2-1]
    XP_006531477.1. XM_006531414.1. [Q80TQ2-2]
    XP_006531478.1. XM_006531415.1. [Q80TQ2-2]
    XP_006531479.1. XM_006531416.1. [Q80TQ2-2]
    XP_006531480.1. XM_006531417.1. [Q80TQ2-2]
    XP_006531481.1. XM_006531418.1. [Q80TQ2-2]
    UniGeneiMm.490395.

    Genome annotation databases

    EnsembliENSMUST00000098519; ENSMUSP00000096119; ENSMUSG00000036712. [Q80TQ2-2]
    ENSMUST00000109626; ENSMUSP00000105254; ENSMUSG00000036712. [Q80TQ2-1]
    GeneIDi74256.
    KEGGimmu:74256.
    UCSCiuc009mrt.2. mouse. [Q80TQ2-1]
    uc009mrw.2. mouse. [Q80TQ2-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK122389 mRNA. Translation: BAC65671.1 . Different initiation.
    AK039054 mRNA. Translation: BAC30222.1 .
    AK042764 mRNA. Translation: BAC31357.1 .
    BC042438 mRNA. Translation: AAH42438.1 .
    BC049879 mRNA. Translation: AAH49879.1 .
    CCDSi CCDS22513.1. [Q80TQ2-1 ]
    CCDS52633.1. [Q80TQ2-2 ]
    RefSeqi NP_001121642.1. NM_001128170.2. [Q80TQ2-2 ]
    NP_001121643.1. NM_001128171.2. [Q80TQ2-1 ]
    NP_775545.1. NM_173369.3. [Q80TQ2-1 ]
    XP_006531477.1. XM_006531414.1. [Q80TQ2-2 ]
    XP_006531478.1. XM_006531415.1. [Q80TQ2-2 ]
    XP_006531479.1. XM_006531416.1. [Q80TQ2-2 ]
    XP_006531480.1. XM_006531417.1. [Q80TQ2-2 ]
    XP_006531481.1. XM_006531418.1. [Q80TQ2-2 ]
    UniGenei Mm.490395.

    3D structure databases

    ProteinModelPortali Q80TQ2.
    SMRi Q80TQ2. Positions 125-206, 228-306, 453-546, 579-952.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 216612. 13 interactions.
    IntActi Q80TQ2. 4 interactions.
    MINTi MINT-7561827.

    Protein family/group databases

    MEROPSi C67.001.

    PTM databases

    PhosphoSitei Q80TQ2.

    Proteomic databases

    MaxQBi Q80TQ2.
    PaxDbi Q80TQ2.
    PRIDEi Q80TQ2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000098519 ; ENSMUSP00000096119 ; ENSMUSG00000036712 . [Q80TQ2-2 ]
    ENSMUST00000109626 ; ENSMUSP00000105254 ; ENSMUSG00000036712 . [Q80TQ2-1 ]
    GeneIDi 74256.
    KEGGi mmu:74256.
    UCSCi uc009mrt.2. mouse. [Q80TQ2-1 ]
    uc009mrw.2. mouse. [Q80TQ2-2 ]

    Organism-specific databases

    CTDi 1540.
    MGIi MGI:1921506. Cyld.
    Rougei Search...

    Phylogenomic databases

    eggNOGi NOG313578.
    GeneTreei ENSGT00390000018123.
    HOGENOMi HOG000006796.
    HOVERGENi HBG051281.
    KOi K08601.
    OrthoDBi EOG72ZCDM.
    PhylomeDBi Q80TQ2.

    Enzyme and pathway databases

    Reactomei REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
    REACT_211125. NOD1/2 Signaling Pathway.

    Miscellaneous databases

    NextBioi 340262.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q80TQ2.
    Bgeei Q80TQ2.
    CleanExi MM_CYLD.
    Genevestigatori Q80TQ2.

    Family and domain databases

    Gene3Di 2.30.30.190. 3 hits.
    InterProi IPR000938. CAP-Gly_domain.
    IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    [Graphical view ]
    Pfami PF01302. CAP_GLY. 3 hits.
    PF00443. UCH. 1 hit.
    [Graphical view ]
    SMARTi SM01052. CAP_GLY. 3 hits.
    [Graphical view ]
    SUPFAMi SSF74924. SSF74924. 3 hits.
    PROSITEi PS00845. CAP_GLY_1. 1 hit.
    PS50245. CAP_GLY_2. 2 hits.
    PS00972. USP_1. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
      DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    2. "The transcriptional landscape of the mammalian genome."
      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.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-620 (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Cerebellum and Hypothalamus.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: FVB/N.
      Tissue: Mammary gland.
    4. "Cyld inhibits tumor cell proliferation by blocking Bcl-3-dependent NF-kappaB signaling."
      Massoumi R., Chmielarska K., Hennecke K., Pfeifer A., Fassler R.
      Cell 125:665-677(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH BCL3, SUBCELLULAR LOCATION.
    5. "Regulation of T cell development by the deubiquitinating enzyme CYLD."
      Reiley W.W., Zhang M., Jin W., Losiewicz M., Donohue K.B., Norbury C.C., Sun S.C.
      Nat. Immunol. 7:411-417(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    6. "Deubiquitinating enzyme CYLD negatively regulates the ubiquitin-dependent kinase Tak1 and prevents abnormal T cell responses."
      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.
      J. Exp. Med. 204:1475-1485(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MAP3K7, DISRUPTION PHENOTYPE.
    7. "CYLD is a crucial negative regulator of innate immune response in Escherichia coli pneumonia."
      Lim J.H., Ha U.H., Woo C.H., Xu H., Li J.D.
      Cell. Microbiol. 10:2247-2256(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    8. "Deubiquitinating enzyme CYLD negatively regulates RANK signaling and osteoclastogenesis in mice."
      Jin W., Chang M., Paul E.M., Babu G., Lee A.J., Reiley W., Wright A., Zhang M., You J., Sun S.C.
      J. Clin. Invest. 118:1858-1866(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION, INTERACTION WITH SQSTM1, IDENTIFICATION IN A COMPLEX WITH TRAF6 AND SQSTM1, INDUCTION.
    9. "CYLD regulates angiogenesis by mediating vascular endothelial cell migration."
      Gao J., Sun L., Huo L., Liu M., Li D., Zhou J.
      Blood 115:4130-4137(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "CYLD negatively regulates cell-cycle progression by inactivating HDAC6 and increasing the levels of acetylated tubulin."
      Wickstrom S.A., Masoumi K.C., Khochbin S., Fassler R., Massoumi R.
      EMBO J. 29:131-144(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HDAC6, BCL3 AND MICROTUBULES, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiCYLD_MOUSE
    AccessioniPrimary (citable) accession number: Q80TQ2
    Secondary accession number(s): Q80VB3
    , Q8BXZ3, Q8BYL9, Q8CGB0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 108 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3