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Entry version 188 (02 Dec 2020)
Sequence version 1 (01 Nov 1998)
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Protein

Caspase-8

Gene

Casp8

Organism
Mus musculus (Mouse)
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

Thiol protease that plays a key role in programmed cell death by acting as a molecular switch for apoptosis, necroptosis and pyroptosis, and is required to prevent tissue damage during embryonic development and adulthood (PubMed:18455983, PubMed:30361383, PubMed:30381458, PubMed:31511692, PubMed:31748744). Initiator protease that induces extrinsic apoptosis by mediating cleavage and activation of effector caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death (PubMed:9654089, PubMed:9837723, PubMed:24813849, PubMed:24813850). Cleaves and activates effector caspases CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10 (By similarity). Binding to the adapter molecule FADD recruits it to either receptor TNFRSF6/FAS mediated or TNFRSF1A (PubMed:29440439). The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation (By similarity). The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases (By similarity). Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC (By similarity). In addition to extrinsic apoptosis, also acts as a negative regulator of necroptosis: acts by cleaving RIPK1 at 'Asp-325', which is crucial to inhibit RIPK1 kinase activity, limiting TNF-induced apoptosis, necroptosis and inflammatory response (PubMed:31511692). Also able to initiate pyroptosis by mediating cleavage and activation of gasdermin-D (GSDMD): GSDMD cleavage promoting release of the N-terminal moiety (Gasdermin-D, N-terminal) that binds to membranes and forms pores, triggering pyroptosis (PubMed:30361383, PubMed:30381458). Initiates pyroptosis following inactivation of MAP3K7/TAK1 (PubMed:30361383, PubMed:30381458). May participate in the Granzyme B (GZMB) cell death pathways (By similarity). Cleaves PARP1 (By similarity).By similarity10 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

CASP8 activity is restricted by RIPK1.2 Publications
(Microbial infection) Inhibited by baculovirus p35 protein P35.1 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 sitei319By similarity1
Active sitei3622 Publications1

<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

GO - Biological processi

<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 processApoptosis

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.22.61, 3474

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-111465, Apoptotic cleavage of cellular proteins
R-MMU-140534, Caspase activation via Death Receptors in the presence of ligand
R-MMU-168638, NOD1/2 Signaling Pathway
R-MMU-2562578, TRIF-mediated programmed cell death
R-MMU-264870, Caspase-mediated cleavage of cytoskeletal proteins
R-MMU-3371378, Regulation by c-FLIP
R-MMU-5213460, RIPK1-mediated regulated necrosis
R-MMU-5218900, CASP8 activity is inhibited
R-MMU-5357905, Regulation of TNFR1 signaling
R-MMU-5660668, CLEC7A/inflammasome pathway
R-MMU-5675482, Regulation of necroptotic cell death
R-MMU-69416, Dimerization of procaspase-8
R-MMU-75108, Activation, myristolyation of BID and translocation to mitochondria
R-MMU-75153, Apoptotic execution phase
R-MMU-75157, FasL/ CD95L signaling
R-MMU-75158, TRAIL signaling

Protein family/group databases

MEROPS protease database

More...
MEROPSi
C14.009

<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:
Caspase-82 Publications (EC:3.4.22.612 Publications)
Short name:
CASP-82 Publications
Cleaved into the following 2 chains:
Caspase-8 subunit p181 Publication
Caspase-8 subunit p101 Publication
<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:Casp82 PublicationsImported
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 1

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1261423, Casp8

<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

Cytoplasm, Nucleus

<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 describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Embryonic lethality at lethality at E10.5 (PubMed:9729047). Embryos display impaired heart muscle development and congested accumulation of erythrocytes (PubMed:9729047). Perinatal lethality observed in Ripk1 knockout mice is rescued in knockout mice lacking both Ripk1 and Casp8; mice however die the first days of postnatal life (PubMed:24813849). Only mice lacking Ripk1, Ripk3 and Casp8 survive past weaning and rescue lethality caused by the absence of Ripk1 (PubMed:24813849, PubMed:24813850).3 Publications

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>Mutagenesisi212D → A: Loss of autocatalytic cleavage; when associated with A-218; A-225 and A-387. 1 Publication1
Mutagenesisi218D → A: Loss of autocatalytic cleavage; when associated with A-212; A-225 and A-387. 1 Publication1
Mutagenesisi225D → A: Loss of autocatalytic cleavage; when associated with A-212; A-218 and A-387. 1 Publication1
Mutagenesisi362C → A: Loss of kinase ativity. Knockin mice show embryonic lethality caused by endothelial cell necroptosis leading to cardiovascular defects. Mlkl deficiency rescues the cardiovascular phenotype of knockin mice, but causes perinatal lethality caused by induction of pyroptosis. 2 Publications1
Mutagenesisi387D → A: Loss of autocatalytic cleavage; when associated with A-212; A-218 and A-225. 1 Publication1

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_00000046321 – 2181 PublicationAdd BLAST218
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000004633219 – 376Caspase-8 subunit p181 PublicationAdd BLAST158
PropeptideiPRO_0000004634377 – 3871 PublicationAdd BLAST11
ChainiPRO_0000004635388 – 480Caspase-8 subunit p101 PublicationAdd BLAST93

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 residuei188PhosphoserineCombined sources1
Modified residuei213PhosphoserineCombined sources1
Modified residuei226N6-acetyllysineCombined sources1
Modified residuei336PhosphotyrosineBy similarity1
Modified residuei389Phosphoserine; by CDK1By similarity1

<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

Generation of the subunits requires association with the death-inducing signaling complex (DISC), whereas additional processing is likely due to the autocatalytic activity of the activated protease (PubMed:31511692). GZMB and CASP10 can be involved in these processing events (By similarity).By similarity1 Publication
(Microbial infection) Proteolytically cleaved by the cowpox virus CRMA death inhibitory protein.1 Publication
Phosphorylation on Ser-389 during mitosis by CDK1 inhibits activation by proteolysis and prevents apoptosis. This phosphorylation occurs in cancer cell lines, as well as in primary breast tissues and lymphocytes (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei218 – 219Cleavage; by autocatalytic cleavage1 Publication2
Sitei387 – 388Cleavage; by autocatalytic cleavage1 Publication2

Keywords - PTMi

Acetylation, Phosphoprotein, Zymogen

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
O89110

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

More...
PaxDbi
O89110

PeptideAtlas

More...
PeptideAtlasi
O89110

PRoteomics IDEntifications database

More...
PRIDEi
O89110

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O89110

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

More...
PhosphoSitePlusi
O89110

<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

Expressed in a wide variety of tissues. Highest expression in spleen, thymus, lung, liver and kidney. Lower expression in heart, brain, testis and skeletal muscle.2 Publications

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

In the embryo, highest expression occurs at day 7.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000026029, Expressed in jejunum and 267 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O89110, MM

<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

Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 18 kDa (p18) and a 10 kDa (p10) subunit (By similarity).

Interacts with CFLAR and PEA15 (By similarity).

Interacts with RFFL and RNF34; negatively regulate CASP8 through proteasomal degradation (By similarity).

Interacts with TNFAIP8L2 (PubMed:18455983).

Interacts with CASP8AP2 (PubMed:17245429).

Interacts with NOL3; decreases CASP8 activity in a mitochondria localization- and phosphorylation-dependent manner and this interaction is dissociated by calcium (PubMed:15383280).

Interacts with UBR2 (By similarity).

Interacts with RIPK1 (PubMed:31519887).

Interacts with FADD (PubMed:29440439).

Interacts with stimulated TNFRSF10B; this interaction is followed by CASP8 proteolytic cleavage and activation (By similarity).

By similarity5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
198500, 19 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1914, Ripoptosome
CPX-3663, Caspase-8 complex

Database of interacting proteins

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DIPi
DIP-37435N

Protein interaction database and analysis system

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IntActi
O89110, 8 interactors

Molecular INTeraction database

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MINTi
O89110

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000027189

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
O89110, 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

3D structure databases

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

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SMRi
O89110

Database of comparative protein structure models

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ModBasei
Search...

<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>Domaini3 – 80DED 1PROSITE-ProRule annotationAdd BLAST78
Domaini101 – 177DED 2PROSITE-ProRule annotationAdd BLAST77

<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 C14A family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3573, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000160319

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_036904_4_2_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O89110

Identification of Orthologs from Complete Genome Data

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OMAi
SDKVYRM

Database for complete collections of gene phylogenies

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PhylomeDBi
O89110

TreeFam database of animal gene trees

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TreeFami
TF102023

Family and domain databases

Conserved Domains Database

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CDDi
cd00032, CASc, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR029030, Caspase-like_dom_sf
IPR033139, Caspase_cys_AS
IPR016129, Caspase_his_AS
IPR011029, DEATH-like_dom_sf
IPR001875, DED_dom
IPR002398, Pept_C14
IPR002138, Pept_C14_p10
IPR001309, Pept_C14_p20
IPR015917, Pept_C14A

The PANTHER Classification System

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PANTHERi
PTHR10454, PTHR10454, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF01335, DED, 2 hits

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00376, IL1BCENZYME

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00115, CASc, 1 hit
SM00031, DED, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47986, SSF47986, 2 hits
SSF52129, SSF52129, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01122, CASPASE_CYS, 1 hit
PS01121, CASPASE_HIS, 1 hit
PS50207, CASPASE_P10, 1 hit
PS50208, CASPASE_P20, 1 hit
PS50168, DED, 2 hits

<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>Sequence (1+)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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

O89110-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDFQSCLYAI AEELGSEDLA ALKFLCLDYI PHKKQETIED AQKLFLRLRE
60 70 80 90 100
KGMLEEGNLS FLKELLFHIS RWDLLVNFLD CNREEMVREL RDPDNAQISP
110 120 130 140 150
YRVMLFKLSE EVSELELRSF KFLLNNEIPK CKLEDDLSLL EIFVEMEKRT
160 170 180 190 200
MLAENNLETL KSICDQVNKS LLGKIEDYER SSTERRMSLE GREELPPSVL
210 220 230 240 250
DEMSLKMAEL CDSPREQDSE SRTSDKVYQM KNKPRGYCLI INNHDFSKAR
260 270 280 290 300
EDITQLRKMK DRKGTDCDKE ALSKTFKELH FEIVSYDDCT ANEIHEILEG
310 320 330 340 350
YQSADHKNKD CFICCILSHG DKGVVYGTDG KEASIYDLTS YFTGSKCPSL
360 370 380 390 400
SGKPKIFFIQ ACQGSNFQKG VPDEAGFEQQ NHTLEVDSSS HKNYIPDEAD
410 420 430 440 450
FLLGMATVKN CVSYRDPVNG TWYIQSLCQS LRERCPQGDD ILSILTGVNY
460 470 480
DVSNKDDRRN KGKQMPQPTF TLRKKLFFPP
Length:480
Mass (Da):55,357
Last modified:November 1, 1998 - 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:i045268AE3DE5ED4F
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WQT6A0A087WQT6_MOUSE
Caspase-8
Casp8
500Annotation score:

Annotation score:3 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti68 – 71HISR → PHPVG in CAA04196 (Ref. 4) Curated4
Sequence conflicti94 – 99DNAQIS → RQCPRFL in CAA04196 (Ref. 4) Curated6
Sequence conflicti96A → V in CAA07677 (PubMed:9837723).Curated1
Sequence conflicti103 – 107VMLFK → SCSFR in CAA04196 (Ref. 4) Curated5
Sequence conflicti475K → N in CAA04196 (Ref. 4) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AF067841 AF067840 Genomic DNA Translation: AAC40132.1
AF067834 mRNA Translation: AAC40131.1
AJ007749 mRNA Translation: CAA07677.1
BC006737 mRNA Translation: AAH06737.1
BC049955 mRNA Translation: AAH49955.1
AJ000641 mRNA Translation: CAA04196.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS14979.1

NCBI Reference Sequences

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RefSeqi
NP_001073595.1, NM_001080126.1
NP_033942.1, NM_009812.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000027189; ENSMUSP00000027189; ENSMUSG00000026029
ENSMUST00000165549; ENSMUSP00000127375; ENSMUSG00000026029

Database of genes from NCBI RefSeq genomes

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GeneIDi
12370

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:12370

UCSC genome browser

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UCSCi
uc007bcs.1, mouse

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF067841 AF067840 Genomic DNA Translation: AAC40132.1
AF067834 mRNA Translation: AAC40131.1
AJ007749 mRNA Translation: CAA07677.1
BC006737 mRNA Translation: AAH06737.1
BC049955 mRNA Translation: AAH49955.1
AJ000641 mRNA Translation: CAA04196.1
CCDSiCCDS14979.1
RefSeqiNP_001073595.1, NM_001080126.1
NP_033942.1, NM_009812.2

3D structure databases

SMRiO89110
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi198500, 19 interactors
ComplexPortaliCPX-1914, Ripoptosome
CPX-3663, Caspase-8 complex
DIPiDIP-37435N
IntActiO89110, 8 interactors
MINTiO89110
STRINGi10090.ENSMUSP00000027189

Protein family/group databases

MEROPSiC14.009

PTM databases

iPTMnetiO89110
PhosphoSitePlusiO89110

Proteomic databases

EPDiO89110
PaxDbiO89110
PeptideAtlasiO89110
PRIDEiO89110

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
697, 1454 antibodies

Genome annotation databases

EnsembliENSMUST00000027189; ENSMUSP00000027189; ENSMUSG00000026029
ENSMUST00000165549; ENSMUSP00000127375; ENSMUSG00000026029
GeneIDi12370
KEGGimmu:12370
UCSCiuc007bcs.1, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
841
MGIiMGI:1261423, Casp8

Phylogenomic databases

eggNOGiKOG3573, Eukaryota
GeneTreeiENSGT00940000160319
HOGENOMiCLU_036904_4_2_1
InParanoidiO89110
OMAiSDKVYRM
PhylomeDBiO89110
TreeFamiTF102023

Enzyme and pathway databases

BRENDAi3.4.22.61, 3474
ReactomeiR-MMU-111465, Apoptotic cleavage of cellular proteins
R-MMU-140534, Caspase activation via Death Receptors in the presence of ligand
R-MMU-168638, NOD1/2 Signaling Pathway
R-MMU-2562578, TRIF-mediated programmed cell death
R-MMU-264870, Caspase-mediated cleavage of cytoskeletal proteins
R-MMU-3371378, Regulation by c-FLIP
R-MMU-5213460, RIPK1-mediated regulated necrosis
R-MMU-5218900, CASP8 activity is inhibited
R-MMU-5357905, Regulation of TNFR1 signaling
R-MMU-5660668, CLEC7A/inflammasome pathway
R-MMU-5675482, Regulation of necroptotic cell death
R-MMU-69416, Dimerization of procaspase-8
R-MMU-75108, Activation, myristolyation of BID and translocation to mitochondria
R-MMU-75153, Apoptotic execution phase
R-MMU-75157, FasL/ CD95L signaling
R-MMU-75158, TRAIL signaling

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
12370, 4 hits in 19 CRISPR screens

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

More...
ChiTaRSi
Casp8, mouse

Protein Ontology

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PROi
PR:O89110
RNActiO89110, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000026029, Expressed in jejunum and 267 other tissues
GenevisibleiO89110, MM

Family and domain databases

CDDicd00032, CASc, 1 hit
InterProiView protein in InterPro
IPR029030, Caspase-like_dom_sf
IPR033139, Caspase_cys_AS
IPR016129, Caspase_his_AS
IPR011029, DEATH-like_dom_sf
IPR001875, DED_dom
IPR002398, Pept_C14
IPR002138, Pept_C14_p10
IPR001309, Pept_C14_p20
IPR015917, Pept_C14A
PANTHERiPTHR10454, PTHR10454, 1 hit
PfamiView protein in Pfam
PF01335, DED, 2 hits
PRINTSiPR00376, IL1BCENZYME
SMARTiView protein in SMART
SM00115, CASc, 1 hit
SM00031, DED, 2 hits
SUPFAMiSSF47986, SSF47986, 2 hits
SSF52129, SSF52129, 1 hit
PROSITEiView protein in PROSITE
PS01122, CASPASE_CYS, 1 hit
PS01121, CASPASE_HIS, 1 hit
PS50207, CASPASE_P10, 1 hit
PS50208, CASPASE_P20, 1 hit
PS50168, DED, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

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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 nameiCASP8_MOUSE
<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: O89110
Secondary accession number(s): O35669
<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: November 15, 2002
Last sequence update: November 1, 1998
Last modified: December 2, 2020
This is version 188 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

<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

Reference proteome

Documents

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