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UniProtKB - Q9NQC7 (CYLD_HUMAN)

Entry version 181 (26 Feb 2020)
Sequence version 1 (01 Oct 2000)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Deubiquitinase that specifically cleaves 'Lys-63'- and linear 'Met-1'-linked polyubiquitin chains and is involved in NF-kappa-B activation and TNF-alpha-induced necroptosis (PubMed:18636086, PubMed:26670046, PubMed:27458237, PubMed:26997266, PubMed:27591049, PubMed:29291351, PubMed:18313383). 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 (PubMed:18636086). 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 (By similarity). 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). Ability to remove linear ('Met-1'-linked) polyubiquitin chains regulates innate immunity and TNF-alpha-induced necroptosis: recruited to the LUBAC complex via interaction with SPATA2 and restricts linear polyubiquitin formation on target proteins (PubMed:26997266, PubMed:26670046, PubMed:27458237, PubMed:27591049). Regulates innate immunity by restricting linear polyubiquitin formation on RIPK2 in response to NOD2 stimulation (PubMed:26997266). Involved in TNF-alpha-induced necroptosis by removing linear ('Met-1'-linked) polyubiquitin chains from RIPK1, thereby regulating the kinase activity of RIPK1 (By similarity). Removes 'Lys-63' linked polyubiquitin chain of MAP3K7, which inhibits phosphorylation and blocks downstream activation of the JNK-p38 kinase cascades (PubMed:29291351).By similarity15 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by phosphorylation at serine residues.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei601NucleophilePROSITE-ProRule annotation1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Protease, Thiol protease
Biological processCell cycle, Immunity, Innate immunity, Ubl conjugation pathway, Wnt signaling pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-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 DDX58/IFIH1 signaling

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q9NQC7

Protein family/group databases

MEROPS protease database

More...MEROPSi		C67.001

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase CYLD (EC:3.4.19.123 Publications)
Alternative name(s):
Deubiquitinating enzyme CYLD
Ubiquitin thioesterase CYLD
Ubiquitin-specific-processing protease CYLD
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CYLD1 PublicationImported
Synonyms:CYLD1, KIAA08491 Publication
ORF Names:HSPC057
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 16

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:2584 CYLD

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		605018 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9NQC7

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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.
Related information in OMIM
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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_045967747E → G in MFT1 and BRSS. 1 PublicationCorresponds to variant dbSNP:rs121908389EnsemblClinVar.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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_045967747E → G in MFT1 and BRSS. 1 PublicationCorresponds to variant dbSNP:rs121908389EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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. 5 Publications1
Mutagenesisi622L → D: Impaired interaction with SPATA2. 1 Publication1
Mutagenesisi871H → N: Loss of deubiquitinating activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Tumor suppressor

Organism-specific databases

DisGeNET

More...DisGeNETi		1540

MalaCards human disease database

More...MalaCardsi		CYLD
MIMi132700 phenotype
601606 phenotype
605041 phenotype

Open Targets

More...OpenTargetsi		ENSG00000083799

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		211 Familial cylindromatosis
867 Familial multiple trichoepithelioma

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA27084

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q9NQC7 Tbio

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		CYLD

Domain mapping of disease mutations (DMDM)

More...DMDMi		51316104

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000806981 – 956Ubiquitin carboxyl-terminal hydrolase CYLDAdd BLAST956

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei387PhosphoserineCombined sources1
Modified residuei418PhosphoserineCombined sources1 Publication1
Modified residuei422PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Ubiquitinated. Polyubiquitinated in hepatocytes treated with palmitic acid. Ubiquitination is mediated by E3 ligase TRIM47 and leads to proteasomal degradation.1 Publication
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, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q9NQC7

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q9NQC7

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q9NQC7

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q9NQC7

PeptideAtlas

More...PeptideAtlasi		Q9NQC7

PRoteomics IDEntifications database

More...PRIDEi		Q9NQC7

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		82139 [Q9NQC7-1]
82140 [Q9NQC7-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9NQC7

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q9NQC7

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000083799 Expressed in caudate nucleus and 228 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9NQC7 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9NQC7 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB011713
HPA050095

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts (via CAP-Gly domain) with IKBKG/NEMO (via proline-rich C-terminal region) (PubMed:12917689, PubMed:12917690, PubMed:12917691, PubMed:15341735).

Interacts with TRAF2 and TRIP (PubMed:12917691, PubMed:14676304).

Interacts with PLK1, DVL1, DVL3, MAVS, TBK1, IKKE and DDX58 (PubMed:17495026, PubMed:18636086, PubMed:20227366).

Interacts (via CAP-Gly domain) with microtubules (PubMed:19893491).

Interacts with HDAC6 and BCL3 (PubMed:19893491).

Interacts with MAP3K7 (By similarity).

Identified in a complex with TRAF6 and SQSTM1 (By similarity).

Interacts with CEP350 (PubMed:25134987).

Interacts with RNF31; the interaction is indirect and is mediated via SPATA2 (PubMed:26997266).

Interacts with SPATA2 (via the PUB domain); the interaction is direct and recruits CYLD to the LUBAC complex, thereby regulating TNF-alpha-induced necroptosis (PubMed:27307491, PubMed:27458237, PubMed:27545878, PubMed:27591049).

By similarity15 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		107920, 634 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q9NQC7

Protein interaction database and analysis system

More...IntActi		Q9NQC7, 36 interactors

Molecular INTeraction database

More...MINTi		Q9NQC7

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000392025

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q9NQC7 protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1956
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q9NQC7

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q9NQC7

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>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
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni106 – 593Interaction with TRIP1 PublicationAdd BLAST488
Regioni394 – 469Interaction with TRAF2Add BLAST76
Regioni470 – 554Interaction with IKBKG/NEMO1 PublicationAdd BLAST85
Regioni781 – 833B-box2 PublicationsAdd BLAST53

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase C19 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3556 Eukaryota
ENOG410XP6I LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00390000018123

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9NQC7

KEGG Orthology (KO)

More...KOi		K08601

Identification of Orthologs from Complete Genome Data

More...OMAi		RNIPCKG

Database of Orthologous Groups

More...OrthoDBi		119442at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9NQC7

TreeFam database of animal gene trees

More...TreeFami		TF318734

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.30.30.190, 3 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR036859 CAP-Gly_dom_sf
IPR000938 CAP-Gly_domain
IPR038765 Papain-like_cys_pep_sf
IPR001394 Peptidase_C19_UCH
IPR018200 USP_CS
IPR028889 USP_dom

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01302 CAP_GLY, 2 hits
PF00443 UCH, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM01052 CAP_GLY, 3 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF54001 SSF54001, 1 hit
SSF74924 SSF74924, 3 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00845 CAP_GLY_1, 1 hit
PS50245 CAP_GLY_2, 2 hits
PS00972 USP_1, 1 hit
PS50235 USP_3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 7 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9NQC7-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H3BS09H3BS09_HUMAN
Ubiquitin carboxyl-terminal hydrola...
CYLD
771Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3KRR7J3KRR7_HUMAN
Ubiquitin carboxyl-terminal hydrola...
CYLD
910Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H3BSW9H3BSW9_HUMAN
Ubiquitin carboxyl-terminal hydrola...
CYLD
304Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H3BTB8H3BTB8_HUMAN
Ubiquitin carboxyl-terminal hydrola...
CYLD
166Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3QKR2J3QKR2_HUMAN
Ubiquitin carboxyl-terminal hydrola...
CYLD
104Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H3BPZ5H3BPZ5_HUMAN
Ubiquitin carboxyl-terminal hydrola...
CYLD
33Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
I3L117I3L117_HUMAN
Ubiquitin carboxyl-terminal hydrola...
CYLD
66Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAF29029 differs from that shown. Reason: Frameshift.Curated
The sequence BAA74872 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_045967747E → G in MFT1 and BRSS. 1 PublicationCorresponds to variant dbSNP:rs121908389EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_011277305 – 307Missing in isoform 2. 2 Publications3

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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.

The Consensus CDS (CCDS) project

More...CCDSi		CCDS42164.1 [Q9NQC7-2]
CCDS45482.1 [Q9NQC7-1]

NCBI Reference Sequences

More...RefSeqi		NP_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]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000311559; ENSP00000308928; ENSG00000083799 [Q9NQC7-1]
ENST00000398568; ENSP00000381574; ENSG00000083799 [Q9NQC7-2]
ENST00000427738; ENSP00000392025; ENSG00000083799 [Q9NQC7-1]
ENST00000564326; ENSP00000454515; ENSG00000083799 [Q9NQC7-2]
ENST00000569418; ENSP00000457576; ENSG00000083799 [Q9NQC7-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		1540

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:1540

UCSC genome browser

More...UCSCi		uc002egq.2 human [Q9NQC7-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IXDNMR-A460-550[»]
1WHLNMR-A125-206[»]
1WHMNMR-A228-304[»]
2VHFX-ray2.80A/B583-956[»]
SMRiQ9NQC7
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi107920, 634 interactors
CORUMiQ9NQC7
IntActiQ9NQC7, 36 interactors
MINTiQ9NQC7
STRINGi9606.ENSP00000392025

Protein family/group databases

MEROPSiC67.001

PTM databases

iPTMnetiQ9NQC7
PhosphoSitePlusiQ9NQC7

Polymorphism and mutation databases

BioMutaiCYLD
DMDMi51316104

Proteomic databases

jPOSTiQ9NQC7
MassIVEiQ9NQC7
MaxQBiQ9NQC7
PaxDbiQ9NQC7
PeptideAtlasiQ9NQC7
PRIDEiQ9NQC7
ProteomicsDBi82139 [Q9NQC7-1]
82140 [Q9NQC7-2]

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

Comparative Toxicogenomics Database

More...CTDi		1540
DisGeNETi1540

GeneCards: human genes, protein and diseases

More...GeneCardsi		CYLD
HGNCiHGNC:2584 CYLD
HPAiCAB011713
HPA050095
MalaCardsiCYLD
MIMi132700 phenotype
601606 phenotype
605018 gene
605041 phenotype
neXtProtiNX_Q9NQC7
OpenTargetsiENSG00000083799
Orphaneti211 Familial cylindromatosis
867 Familial multiple trichoepithelioma
PharmGKBiPA27084

Human Unidentified Gene-Encoded large proteins database

More...HUGEi		Search...

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3556 Eukaryota
ENOG410XP6I LUCA
GeneTreeiENSGT00390000018123
InParanoidiQ9NQC7
KOiK08601
OMAiRNIPCKG
OrthoDBi119442at2759
PhylomeDBiQ9NQC7
TreeFamiTF318734

Enzyme and pathway databases

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 DDX58/IFIH1 signaling
SIGNORiQ9NQC7

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		CYLD human
EvolutionaryTraceiQ9NQC7

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		CYLD_(gene)

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		1540
PharosiQ9NQC7 Tbio

Protein Ontology

More...PROi		PR:Q9NQC7
RNActiQ9NQC7 protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000083799 Expressed in caudate nucleus and 228 other tissues
ExpressionAtlasiQ9NQC7 baseline and differential
GenevisibleiQ9NQC7 HS

Family and domain databases

Gene3Di2.30.30.190, 3 hits
InterProiView protein in InterPro
IPR036859 CAP-Gly_dom_sf
IPR000938 CAP-Gly_domain
IPR038765 Papain-like_cys_pep_sf
IPR001394 Peptidase_C19_UCH
IPR018200 USP_CS
IPR028889 USP_dom
PfamiView protein in Pfam
PF01302 CAP_GLY, 2 hits
PF00443 UCH, 1 hit
SMARTiView protein in SMART
SM01052 CAP_GLY, 3 hits
SUPFAMiSSF54001 SSF54001, 1 hit
SSF74924 SSF74924, 3 hits
PROSITEiView protein in PROSITE
PS00845 CAP_GLY_1, 1 hit
PS50245 CAP_GLY_2, 2 hits
PS00972 USP_1, 1 hit
PS50235 USP_3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCYLD_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9NQC7
Secondary accession number(s): O94934
, Q7L3N6, Q96EH0, Q9NZX9
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: October 1, 2000
Last modified: February 26, 2020
This is version 181 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

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