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Protein

Ubiquitin carboxyl-terminal hydrolase CYLD

Gene

CYLD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (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. 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. 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). 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 (PubMed:26670046, PubMed:26997266).By similarity12 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).1 Publication

Enzyme regulationi

Inhibited by phosphorylation at serine residues.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei601NucleophilePROSITE-ProRule annotation1 Publication1
Metal bindingi788Zinc 11
Metal bindingi791Zinc 11
Metal bindingi799Zinc 21
Metal bindingi802Zinc 21
Metal bindingi817Zinc 11
Metal bindingi820Zinc 11
Metal bindingi825Zinc 21
Metal bindingi833Zinc 21
Active sitei871Proton acceptor1 Publication1

GO - Molecular functioni

  • Lys63-specific deubiquitinase activity Source: UniProtKB
  • proline-rich region binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • thiol-dependent ubiquitin-specific protease activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • innate immune response Source: UniProtKB
  • necroptotic process Source: GO_Central
  • negative regulation of canonical Wnt signaling pathway Source: UniProtKB
  • negative regulation of NF-kappaB import into nucleus Source: UniProtKB
  • negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • negative regulation of type I interferon production Source: Reactome
  • nucleotide-binding oligomerization domain containing signaling pathway Source: Reactome
  • positive regulation of extrinsic apoptotic signaling pathway Source: UniProtKB
  • protein K63-linked deubiquitination Source: UniProtKB
  • protein linear deubiquitination Source: UniProtKB
  • regulation of cilium assembly Source: UniProtKB
  • regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
  • regulation of microtubule cytoskeleton organization Source: UniProtKB
  • regulation of mitotic cell cycle Source: UniProtKB
  • regulation of tumor necrosis factor-mediated signaling pathway Source: UniProtKB
  • ubiquitin-dependent protein catabolic process Source: InterPro
  • Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Cell cycle, Immunity, Innate immunity, Ubl conjugation pathway, Wnt signaling pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:HS01450-MONOMER.
ReactomeiR-HSA-168638. NOD1/2 Signaling Pathway.
R-HSA-5357786. TNFR1-induced proapoptotic signaling.
R-HSA-5357905. Regulation of TNFR1 signaling.
R-HSA-5357956. TNFR1-induced NFkappaB signaling pathway.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-936440. Negative regulators of RIG-I/MDA5 signaling.
SIGNORiQ9NQC7.

Protein family/group databases

MEROPSiC67.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase CYLD (EC:3.4.19.121 Publication)
Alternative name(s):
Deubiquitinating enzyme CYLD
Ubiquitin thioesterase CYLD
Ubiquitin-specific-processing protease CYLD
Gene namesi
Name:CYLD1 PublicationImported
Synonyms:CYLD1, KIAA08491 Publication
ORF Names:HSPC057
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:2584. CYLD.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • ciliary basal body Source: UniProtKB
  • ciliary tip Source: UniProtKB
  • cytosol Source: UniProtKB
  • extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  • microtubule Source: UniProtKB-KW
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • spindle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Microtubule

Pathology & Biotechi

Involvement in diseasei

Cylindromatosis, familial (FCYL)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:132700
Multiple familial trichoepithelioma 1 (MFT1)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal 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.
See also OMIM:601606
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_045967747E → G in MFT1 and BRSS. 1 PublicationCorresponds to variant rs121908389dbSNPEnsembl.1
Brooke-Spiegler syndrome (BRSS)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:605041
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_045967747E → G in MFT1 and BRSS. 1 PublicationCorresponds to variant rs121908389dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi418S → 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. 1 Publication1
Mutagenesisi418S → E: Abolishes deubiquitination of TRAF2; when associated with E-422; E-432; E-436; E-439; E-441 and E-444. 1 Publication1
Mutagenesisi422S → 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. 1 Publication1
Mutagenesisi422S → E: Abolishes deubiquitination of TRAF2; when associated with E-418; E-432; E-436; E-439; E-441 and E-444. 1 Publication1
Mutagenesisi432S → 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. 1 Publication1
Mutagenesisi432S → E: Abolishes deubiquitination of TRAF2; when associated with E-418; E-422; E-436; E-439; E-441 and E-444. 1 Publication1
Mutagenesisi436S → 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. 1 Publication1
Mutagenesisi436S → E: Abolishes deubiquitination of TRAF2; when associated with E-418; E-422; E-432; E-439; E-441 and E-444. 1 Publication1
Mutagenesisi439S → A: Loss of phosphorylation; when associated with A-418; A-422; A-432; A-436; A-441 and A-444. 1 Publication1
Mutagenesisi439S → E: Abolishes deubiquitination of TRAF2; when associated with E-418; E-422; E-432; E-436; E-441 and E-444. 1 Publication1
Mutagenesisi441S → A: Loss of phosphorylation; when associated with A-418; A-422; A-432; A-436; A-439 and A-444. 1 Publication1
Mutagenesisi441S → E: Abolishes deubiquitination of TRAF2; when associated with E-418; E-422; E-432; E-436; E-439 and E-444. 1 Publication1
Mutagenesisi444S → A: Loss of phosphorylation; when associated with A-418; A-422; A-432; A-436; A-439 and A-441. 1 Publication1
Mutagenesisi444S → E: Abolishes deubiquitination of TRAF2; when associated with E-418; E-422; E-432; E-436; E-439 and E-441. 1 Publication1
Mutagenesisi457S → A: Abolishes binding to TRAF2. 1 Publication1
Mutagenesisi601C → A or S: Loss of deubiquitinating activity. 4 Publications1
Mutagenesisi871H → N: Loss of deubiquitinating activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Tumor suppressor

Organism-specific databases

DisGeNETi1540.
MalaCardsiCYLD.
MIMi132700. phenotype.
601606. phenotype.
605041. phenotype.
OpenTargetsiENSG00000083799.
Orphaneti211. Familial cylindromatosis.
867. Familial multiple trichoepithelioma.
PharmGKBiPA27084.

Polymorphism and mutation databases

BioMutaiCYLD.
DMDMi51316104.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000806981 – 956Ubiquitin carboxyl-terminal hydrolase CYLDAdd BLAST956

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei387PhosphoserineCombined sources1
Modified residuei418PhosphoserineCombined sources1 Publication1
Modified residuei422PhosphoserineCombined sources1

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.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NQC7.
PaxDbiQ9NQC7.
PeptideAtlasiQ9NQC7.
PRIDEiQ9NQC7.

PTM databases

iPTMnetiQ9NQC7.
PhosphoSitePlusiQ9NQC7.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiENSG00000083799.
CleanExiHS_CYLD.
ExpressionAtlasiQ9NQC7. baseline and differential.
GenevisibleiQ9NQC7. HS.

Organism-specific databases

HPAiCAB011713.
HPA050095.
HPA058854.

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. 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 similarity). Interacts with CEP350 (PubMed:25134987). Interacts with RNF31 (PubMed:26997266).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DDX58O957862EBI-2117940,EBI-995350
HDAC6Q9UBN74EBI-2117940,EBI-301697
ITCHQ96J023EBI-2117940,EBI-1564678
ITCHQ96J02-22EBI-2117940,EBI-6672198
TUBA1AQ71U366EBI-2117940,EBI-302552

GO - Molecular functioni

  • proline-rich region binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107920. 62 interactors.
IntActiQ9NQC7. 28 interactors.
MINTiMINT-6804518.
STRINGi9606.ENSP00000308928.

Structurei

Secondary structure

1956
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi130 – 134Combined sources5
Beta strandi136 – 139Combined sources4
Beta strandi141 – 149Combined sources9
Beta strandi154 – 157Combined sources4
Beta strandi163 – 167Combined sources5
Beta strandi169 – 171Combined sources3
Turni191 – 193Combined sources3
Beta strandi194 – 197Combined sources4
Helixi199 – 201Combined sources3
Beta strandi202 – 204Combined sources3
Beta strandi235 – 240Combined sources6
Beta strandi243 – 253Combined sources11
Turni259 – 261Combined sources3
Beta strandi264 – 272Combined sources9
Beta strandi278 – 280Combined sources3
Beta strandi283 – 285Combined sources3
Beta strandi293 – 298Combined sources6
Helixi299 – 301Combined sources3
Beta strandi302 – 304Combined sources3
Turni463 – 465Combined sources3
Beta strandi466 – 468Combined sources3
Beta strandi474 – 478Combined sources5
Beta strandi480 – 482Combined sources3
Beta strandi486 – 492Combined sources7
Beta strandi495 – 497Combined sources3
Beta strandi501 – 508Combined sources8
Beta strandi514 – 518Combined sources5
Beta strandi531 – 535Combined sources5
Helixi536 – 538Combined sources3
Beta strandi539 – 541Combined sources3
Helixi584 – 586Combined sources3
Beta strandi588 – 591Combined sources4
Helixi601 – 611Combined sources11
Beta strandi612 – 614Combined sources3
Helixi615 – 617Combined sources3
Helixi618 – 622Combined sources5
Helixi633 – 642Combined sources10
Helixi645 – 650Combined sources6
Beta strandi652 – 654Combined sources3
Helixi656 – 669Combined sources14
Helixi682 – 690Combined sources9
Turni691 – 694Combined sources4
Beta strandi699 – 704Combined sources6
Beta strandi710 – 713Combined sources4
Helixi730 – 741Combined sources12
Beta strandi743 – 747Combined sources5
Beta strandi750 – 755Combined sources6
Beta strandi760 – 764Combined sources5
Beta strandi773 – 775Combined sources3
Helixi778 – 780Combined sources3
Beta strandi781 – 784Combined sources4
Turni789 – 791Combined sources3
Helixi800 – 802Combined sources3
Turni806 – 811Combined sources6
Helixi818 – 824Combined sources7
Helixi828 – 830Combined sources3
Helixi844 – 846Combined sources3
Beta strandi859 – 868Combined sources10
Beta strandi871 – 877Combined sources7
Beta strandi879 – 881Combined sources3
Beta strandi885 – 889Combined sources5
Beta strandi905 – 908Combined sources4
Helixi911 – 914Combined sources4
Helixi920 – 925Combined sources6
Helixi928 – 930Combined sources3
Helixi935 – 940Combined sources6
Beta strandi944 – 948Combined sources5
Helixi950 – 952Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IXDNMR-A460-550[»]
1WHLNMR-A125-206[»]
1WHMNMR-A228-304[»]
2VHFX-ray2.80A/B583-956[»]
ProteinModelPortaliQ9NQC7.
SMRiQ9NQC7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NQC7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini153 – 198CAP-Gly 1PROSITE-ProRule annotationAdd BLAST46
Domaini253 – 286CAP-Gly 2PROSITE-ProRule annotationAdd BLAST34
Domaini492 – 535CAP-Gly 3PROSITE-ProRule annotationAdd BLAST44
Domaini592 – 950USPAdd BLAST359

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni106 – 593Interaction with TRIP1 PublicationAdd BLAST488
Regioni394 – 469Interaction with TRAF2Add BLAST76
Regioni470 – 554Interaction with IKBKG/NEMO1 PublicationAdd BLAST85

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

eggNOGiKOG3556. Eukaryota.
ENOG410XP6I. LUCA.
GeneTreeiENSGT00390000018123.
HOGENOMiHOG000006796.
HOVERGENiHBG051281.
InParanoidiQ9NQC7.
KOiK08601.
OMAiCTDGTFK.
OrthoDBiEOG091G015D.
PhylomeDBiQ9NQC7.
TreeFamiTF318734.

Family and domain databases

Gene3Di2.30.30.190. 3 hits.
InterProiIPR000938. CAP-Gly_domain.
IPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
[Graphical view]
PfamiPF01302. CAP_GLY. 2 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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NQC7-1) [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

        10         20         30         40         50
MSSGLWSQEK VTSPYWEERI FYLLLQECSV TDKQTQKLLK VPKGSIGQYI
60 70 80 90 100
QDRSVGHSRI PSAKGKKNQI GLKILEQPHA VLFVDEKDVV EINEKFTELL
110 120 130 140 150
LAITNCEERF SLFKNRNRLS KGLQIDVGCP VKVQLRSGEE KFPGVVRFRG
160 170 180 190 200
PLLAERTVSG IFFGVELLEE GRGQGFTDGV YQGKQLFQCD EDCGVFVALD
210 220 230 240 250
KLELIEDDDT ALESDYAGPG DTMQVELPPL EINSRVSLKV GETIESGTVI
260 270 280 290 300
FCDVLPGKES LGYFVGVDMD NPIGNWDGRF DGVQLCSFAC VESTILLHIN
310 320 330 340 350
DIIPALSESV TQERRPPKLA FMSRGVGDKG SSSHNKPKAT GSTSDPGNRN
360 370 380 390 400
RSELFYTLNG SSVDSQPQSK SKNTWYIDEV AEDPAKSLTE ISTDFDRSSP
410 420 430 440 450
PLQPPPVNSL TTENRFHSLP FSLTKMPNTN GSIGHSPLSL SAQSVMEELN
460 470 480 490 500
TAPVQESPPL AMPPGNSHGL EVGSLAEVKE NPPFYGVIRW IGQPPGLNEV
510 520 530 540 550
LAGLELEDEC AGCTDGTFRG TRYFTCALKK ALFVKLKSCR PDSRFASLQP
560 570 580 590 600
VSNQIERCNS LAFGGYLSEV VEENTPPKME KEGLEIMIGK KKGIQGHYNS
610 620 630 640 650
CYLDSTLFCL FAFSSVLDTV LLRPKEKNDV EYYSETQELL RTEIVNPLRI
660 670 680 690 700
YGYVCATKIM KLRKILEKVE AASGFTSEEK DPEEFLNILF HHILRVEPLL
710 720 730 740 750
KIRSAGQKVQ DCYFYQIFME KNEKVGVPTI QQLLEWSFIN SNLKFAEAPS
760 770 780 790 800
CLIIQMPRFG KDFKLFKKIF PSLELNITDL LEDTPRQCRI CGGLAMYECR
810 820 830 840 850
ECYDDPDISA GKIKQFCKTC NTQVHLHPKR LNHKYNPVSL PKDLPDWDWR
860 870 880 890 900
HGCIPCQNME LFAVLCIETS HYVAFVKYGK DDSAWLFFDS MADRDGGQNG
910 920 930 940 950
FNIPQVTPCP EVGEYLKMSL EDLHSLDSRR IQGCARRLLC DAYMCMYQSP

TMSLYK
Length:956
Mass (Da):107,316
Last modified:October 1, 2000 - v1
Checksum:i01831F9A83424631
GO
Isoform 2 (identifier: Q9NQC7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     305-307: Missing.

Show »
Length:953
Mass (Da):107,044
Checksum:i0CCB3D21E2FF8851
GO

Sequence cautioni

The sequence AAF29029 differs from that shown. Reason: Frameshift at positions 776, 808 and 932.Curated
The sequence BAA74872 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_045967747E → G in MFT1 and BRSS. 1 PublicationCorresponds to variant rs121908389dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_011277305 – 307Missing in isoform 2. 2 Publications3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ250014 mRNA. Translation: CAB93533.1.
AB020656 mRNA. Translation: BAA74872.2. Different initiation.
BC012342 mRNA. Translation: AAH12342.1.
AF161542 mRNA. Translation: AAF29029.1. Frameshift.
CCDSiCCDS42164.1. [Q9NQC7-2]
CCDS45482.1. [Q9NQC7-1]
RefSeqiNP_001035814.1. NM_001042355.1. [Q9NQC7-2]
NP_001035877.1. NM_001042412.1. [Q9NQC7-2]
NP_056062.1. NM_015247.2. [Q9NQC7-1]
XP_005255869.1. XM_005255812.2. [Q9NQC7-2]
XP_006721212.1. XM_006721149.1. [Q9NQC7-2]
XP_011521209.1. XM_011522907.2. [Q9NQC7-2]
XP_016878466.1. XM_017022977.1. [Q9NQC7-2]
XP_016878467.1. XM_017022978.1. [Q9NQC7-2]
XP_016878468.1. XM_017022979.1. [Q9NQC7-2]
XP_016878469.1. XM_017022980.1. [Q9NQC7-2]
UniGeneiHs.578973.

Genome annotation databases

EnsembliENST00000311559; ENSP00000308928; ENSG00000083799. [Q9NQC7-1]
ENST00000398568; ENSP00000381574; ENSG00000083799. [Q9NQC7-2]
ENST00000427738; ENSP00000392025; ENSG00000083799. [Q9NQC7-1]
ENST00000564326; ENSP00000454515; ENSG00000083799. [Q9NQC7-2]
ENST00000569418; ENSP00000457576; ENSG00000083799. [Q9NQC7-2]
GeneIDi1540.
KEGGihsa:1540.
UCSCiuc002egq.2. human. [Q9NQC7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ250014 mRNA. Translation: CAB93533.1.
AB020656 mRNA. Translation: BAA74872.2. Different initiation.
BC012342 mRNA. Translation: AAH12342.1.
AF161542 mRNA. Translation: AAF29029.1. Frameshift.
CCDSiCCDS42164.1. [Q9NQC7-2]
CCDS45482.1. [Q9NQC7-1]
RefSeqiNP_001035814.1. NM_001042355.1. [Q9NQC7-2]
NP_001035877.1. NM_001042412.1. [Q9NQC7-2]
NP_056062.1. NM_015247.2. [Q9NQC7-1]
XP_005255869.1. XM_005255812.2. [Q9NQC7-2]
XP_006721212.1. XM_006721149.1. [Q9NQC7-2]
XP_011521209.1. XM_011522907.2. [Q9NQC7-2]
XP_016878466.1. XM_017022977.1. [Q9NQC7-2]
XP_016878467.1. XM_017022978.1. [Q9NQC7-2]
XP_016878468.1. XM_017022979.1. [Q9NQC7-2]
XP_016878469.1. XM_017022980.1. [Q9NQC7-2]
UniGeneiHs.578973.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IXDNMR-A460-550[»]
1WHLNMR-A125-206[»]
1WHMNMR-A228-304[»]
2VHFX-ray2.80A/B583-956[»]
ProteinModelPortaliQ9NQC7.
SMRiQ9NQC7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107920. 62 interactors.
IntActiQ9NQC7. 28 interactors.
MINTiMINT-6804518.
STRINGi9606.ENSP00000308928.

Protein family/group databases

MEROPSiC67.001.

PTM databases

iPTMnetiQ9NQC7.
PhosphoSitePlusiQ9NQC7.

Polymorphism and mutation databases

BioMutaiCYLD.
DMDMi51316104.

Proteomic databases

MaxQBiQ9NQC7.
PaxDbiQ9NQC7.
PeptideAtlasiQ9NQC7.
PRIDEiQ9NQC7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311559; ENSP00000308928; ENSG00000083799. [Q9NQC7-1]
ENST00000398568; ENSP00000381574; ENSG00000083799. [Q9NQC7-2]
ENST00000427738; ENSP00000392025; ENSG00000083799. [Q9NQC7-1]
ENST00000564326; ENSP00000454515; ENSG00000083799. [Q9NQC7-2]
ENST00000569418; ENSP00000457576; ENSG00000083799. [Q9NQC7-2]
GeneIDi1540.
KEGGihsa:1540.
UCSCiuc002egq.2. human. [Q9NQC7-1]

Organism-specific databases

CTDi1540.
DisGeNETi1540.
GeneCardsiCYLD.
HGNCiHGNC:2584. CYLD.
HPAiCAB011713.
HPA050095.
HPA058854.
MalaCardsiCYLD.
MIMi132700. phenotype.
601606. phenotype.
605018. gene.
605041. phenotype.
neXtProtiNX_Q9NQC7.
OpenTargetsiENSG00000083799.
Orphaneti211. Familial cylindromatosis.
867. Familial multiple trichoepithelioma.
PharmGKBiPA27084.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3556. Eukaryota.
ENOG410XP6I. LUCA.
GeneTreeiENSGT00390000018123.
HOGENOMiHOG000006796.
HOVERGENiHBG051281.
InParanoidiQ9NQC7.
KOiK08601.
OMAiCTDGTFK.
OrthoDBiEOG091G015D.
PhylomeDBiQ9NQC7.
TreeFamiTF318734.

Enzyme and pathway databases

BioCyciZFISH:HS01450-MONOMER.
ReactomeiR-HSA-168638. NOD1/2 Signaling Pathway.
R-HSA-5357786. TNFR1-induced proapoptotic signaling.
R-HSA-5357905. Regulation of TNFR1 signaling.
R-HSA-5357956. TNFR1-induced NFkappaB signaling pathway.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-936440. Negative regulators of RIG-I/MDA5 signaling.
SIGNORiQ9NQC7.

Miscellaneous databases

ChiTaRSiCYLD. human.
EvolutionaryTraceiQ9NQC7.
GeneWikiiCYLD_(gene).
GenomeRNAii1540.
PROiQ9NQC7.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000083799.
CleanExiHS_CYLD.
ExpressionAtlasiQ9NQC7. baseline and differential.
GenevisibleiQ9NQC7. HS.

Family and domain databases

Gene3Di2.30.30.190. 3 hits.
InterProiIPR000938. CAP-Gly_domain.
IPR001394. Peptidase_C19_UCH.
IPR018200. USP_CS.
IPR028889. USP_dom.
[Graphical view]
PfamiPF01302. CAP_GLY. 2 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]
ProtoNetiSearch...

Entry informationi

Entry nameiCYLD_HUMAN
AccessioniPrimary (citable) accession number: Q9NQC7
Secondary accession number(s): O94934
, Q7L3N6, Q96EH0, Q9NZX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: October 1, 2000
Last modified: November 30, 2016
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.