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Q80TQ2

- CYLD_MOUSE

UniProt

Q80TQ2 - CYLD_MOUSE

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Protein

Ubiquitin carboxyl-terminal hydrolase CYLD

Gene
Cyld, Cyld1, Kiaa0849
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.7 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 – 5971Nucleophile By similarity
Metal bindingi784 – 7841Zinc 1 By similarity
Metal bindingi787 – 7871Zinc 1 By similarity
Metal bindingi795 – 7951Zinc 2 By similarity
Metal bindingi798 – 7981Zinc 2 By similarity
Metal bindingi813 – 8131Zinc 1 By similarity
Metal bindingi816 – 8161Zinc 1 By similarity
Metal bindingi821 – 8211Zinc 2 By similarity
Metal bindingi829 – 8291Zinc 2 By similarity
Active sitei867 – 8671Proton acceptor By similarity

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
Complete GO annotation...

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; Peripheral membrane protein; Cytoplasmic side By similarity
Note: Detected at the microtubule cytoskeleton during interphase. Detected at the midbody during telophase.2 Publications

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
Complete GO annotation...

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 – 4141Phosphoserine By 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.

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 SQSTM1.4 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.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni106 – 589484Interaction with TRIP By similarityAdd
BLAST
Regioni390 – 46576Interaction with TRAF2 By similarityAdd
BLAST
Regioni466 – 680215Interaction with IKBKG/NEMO By similarityAdd
BLAST

Sequence similaritiesi

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

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei304 – 3041P → PALS in isoform 1. VSP_011278
Alternative sequencei305 – 31814DSVTQ…PKLAF → GTSKNILDQQLKGK in isoform 3. VSP_011279Add
BLAST
Alternative sequencei319 – 952634Missing in isoform 3. VSP_011280Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti403 – 4031M → V in BAC30222. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 107 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

Similar proteinsi