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Entry version 175 (13 Feb 2019)
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

Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

  • Strict requirement for Asp at position P1 and has a preferred cleavage sequence of (Leu/Asp/Val)-Glu-Thr-Asp-|-(Gly/Ser/Ala). EC:3.4.22.61

<p>This subsection of the ‘Function’ 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 CRMA and P35.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei362By similarity1

<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-3371378 Regulation by c-FLIP
R-MMU-5213460 RIPK1-mediated regulated necrosis
R-MMU-5218900 CASP8 activity is inhibited
R-MMU-5660668 CLEC7A/inflammasome pathway
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_and_taxonomy_section">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-8 (EC:3.4.22.61)
Short name:
CASP-8
Cleaved into the following 2 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:Casp8
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<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_processing_section">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 – 218By similarityAdd BLAST218
<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_0000004633219 – 376Caspase-8 subunit p18Add BLAST158
PropeptideiPRO_0000004634377 – 387By similarityAdd BLAST11
ChainiPRO_0000004635388 – 480Caspase-8 subunit p10Add 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_processing_section">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. GZMB and CASP10 can be involved in these processing events (By similarity).By similarity
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

Keywords - PTMi

Acetylation, Phosphoprotein, Zymogen

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O89110

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O89110

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

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PaxDbi
O89110

PeptideAtlas

More...
PeptideAtlasi
O89110

PRoteomics IDEntifications database

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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.

<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.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000026029 Expressed in 249 organ(s), highest expression level in jejunum

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O89110 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
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_section">'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_section">'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 FADD, 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).By similarity3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
198500, 6 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

More...
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

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O89110

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...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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_and_domains_section">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
ENOG410ZQIE LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000160319

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000276884

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG050803

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O89110

KEGG Orthology (KO)

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KOi
K04398

Identification of Orthologs from Complete Genome Data

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OMAi
RVMLFQI

Database of Orthologous Groups

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OrthoDBi
939331at2759

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
IPR033170 Caspase-8
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
PTHR10454:SF162 PTHR10454:SF162, 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

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SUPFAMi
SSF47986 SSF47986, 2 hits
SSF52129 SSF52129, 1 hit

PROSITE; a protein domain and family database

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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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF067841
, AF067835, AF067836, AF067837, AF067838, AF067839, 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

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.336851

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
, AF067835, AF067836, AF067837, AF067838, AF067839, 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
UniGeneiMm.336851

3D structure databases

ProteinModelPortaliO89110
SMRiO89110
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198500, 6 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
jPOSTiO89110
PaxDbiO89110
PeptideAtlasiO89110
PRIDEiO89110

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
841
MGIiMGI:1261423 Casp8

Phylogenomic databases

eggNOGiKOG3573 Eukaryota
ENOG410ZQIE LUCA
GeneTreeiENSGT00940000160319
HOGENOMiHOG000276884
HOVERGENiHBG050803
InParanoidiO89110
KOiK04398
OMAiRVMLFQI
OrthoDBi939331at2759
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-3371378 Regulation by c-FLIP
R-MMU-5213460 RIPK1-mediated regulated necrosis
R-MMU-5218900 CASP8 activity is inhibited
R-MMU-5660668 CLEC7A/inflammasome pathway
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

Protein Ontology

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PROi
PR:O89110

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000026029 Expressed in 249 organ(s), highest expression level in jejunum
ExpressionAtlasiO89110 baseline and differential
GenevisibleiO89110 MM

Family and domain databases

CDDicd00032 CASc, 1 hit
InterProiView protein in InterPro
IPR033170 Caspase-8
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
PTHR10454:SF162 PTHR10454:SF162, 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
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<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_and_isoforms">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: February 13, 2019
This is version 175 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

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
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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