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Q5RED8

- CYLD_PONAB

UniProt

Q5RED8 - CYLD_PONAB

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Protein

Ubiquitin carboxyl-terminal hydrolase CYLD

Gene

CYLD

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript 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 (By similarity).By similarity

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 sitei601 – 6011NucleophilePROSITE-ProRule annotation
Metal bindingi788 – 7881Zinc 1By similarity
Metal bindingi791 – 7911Zinc 1By similarity
Metal bindingi799 – 7991Zinc 2By similarity
Metal bindingi802 – 8021Zinc 2By similarity
Metal bindingi817 – 8171Zinc 1By similarity
Metal bindingi820 – 8201Zinc 1By similarity
Metal bindingi825 – 8251Zinc 2By similarity
Metal bindingi833 – 8331Zinc 2By similarity
Active sitei871 – 8711Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. ubiquitin-specific protease activity Source: UniProtKB
  2. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. negative regulation of canonical Wnt signaling pathway Source: UniProtKB
  2. negative regulation of NF-kappaB import into nucleus Source: UniProtKB
  3. negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
  4. protein K63-linked deubiquitination Source: UniProtKB
  5. ubiquitin-dependent protein catabolic process Source: InterPro
  6. 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

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
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

Cytoplasm By similarity. Cytoplasmperinuclear region By similarity. Cytoplasmcytoskeleton By similarity. 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 (By similarity).By similarity

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. microtubule Source: UniProtKB-KW
  3. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 956956Ubiquitin carboxyl-terminal hydrolase CYLDPRO_0000326148Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei418 – 4181PhosphoserineBy 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

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).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ5RED8.
SMRiQ5RED8. Positions 125-206, 228-307, 457-550, 583-956.
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
Domaini492 – 53544CAP-Gly 3PROSITE-ProRule annotationAdd
BLAST
Domaini592 – 950359USPAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni106 – 593488Interaction with TRIPAdd
BLAST
Regioni394 – 46976Interaction with TRAF2Add
BLAST
Regioni470 – 684215Interaction with IKBKG/NEMOAdd
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

HOGENOMiHOG000006796.
HOVERGENiHBG051281.
InParanoidiQ5RED8.
KOiK08601.

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]

Sequencei

Sequence statusi: Complete.

Q5RED8-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MSSGLWSQDK VTSPYWEERV FYLLLQECSV TDKQTQKLLK VPKGSIGQYI
60 70 80 90 100
QDRSVGHSRI PSAKGKKNRI 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 STENRFHSLP 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):107,302
Last modified:December 21, 2004 - v1
Checksum:iADDCE3C7241D828B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR857591 mRNA. Translation: CAH89869.1.
RefSeqiNP_001124871.1. NM_001131399.1.
UniGeneiPab.1922.

Genome annotation databases

GeneIDi100171734.
KEGGipon:100171734.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR857591 mRNA. Translation: CAH89869.1 .
RefSeqi NP_001124871.1. NM_001131399.1.
UniGenei Pab.1922.

3D structure databases

ProteinModelPortali Q5RED8.
SMRi Q5RED8. Positions 125-206, 228-307, 457-550, 583-956.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi C67.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100171734.
KEGGi pon:100171734.

Organism-specific databases

CTDi 1540.

Phylogenomic databases

HOGENOMi HOG000006796.
HOVERGENi HBG051281.
InParanoidi Q5RED8.
KOi K08601.

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. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain cortex.

Entry informationi

Entry nameiCYLD_PONAB
AccessioniPrimary (citable) accession number: Q5RED8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: December 21, 2004
Last modified: October 29, 2014
This is version 65 of the entry and version 1 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. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3