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Entry version 142 (13 Feb 2019)
Sequence version 1 (01 Oct 2000)
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Protein

Caspase-8

Gene

Casp8

Organism
Rattus norvegicus (Rat)
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.By similarity

<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).By similarity 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.By similarity

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 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-111465 Apoptotic cleavage of cellular proteins
R-RNO-168638 NOD1/2 Signaling Pathway
R-RNO-3371378 Regulation by c-FLIP
R-RNO-5213460 RIPK1-mediated regulated necrosis
R-RNO-5218900 CASP8 activity is inhibited
R-RNO-5660668 CLEC7A/inflammasome pathway
R-RNO-69416 Dimerization of procaspase-8
R-RNO-75108 Activation, myristolyation of BID and translocation to mitochondria
R-RNO-75153 Apoptotic execution phase
R-RNO-75157 FasL/ CD95L signaling
R-RNO-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-81 PublicationCurated (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:Casp8Imported
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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 9

Organism-specific databases

Rat genome database

More...
RGDi
620945 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_00004324251 – 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_0000432426219 – 378Caspase-8 subunit p18Add BLAST160
PropeptideiPRO_0000432427379 – 388By similarity10
ChainiPRO_0000432428389 – 482Caspase-8 subunit p10Add BLAST94

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 residuei188PhosphoserineBy similarity1
Modified residuei213PhosphoserineBy similarity1
Modified residuei336PhosphotyrosineBy similarity1
Modified residuei390Phosphoserine; 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

Phosphoprotein, Zymogen

Proteomic databases

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

More...
PaxDbi
Q9JHX4

PRoteomics IDEntifications database

More...
PRIDEi
Q9JHX4

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9JHX4

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

More...
PhosphoSitePlusi
Q9JHX4

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000012331 Expressed in 10 organ(s), highest expression level in colon

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q9JHX4 RN

<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 (By similarity). Interacts with CASP8AP2 (By similarity). 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 similarity1 Publication

<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

WithEntry#Exp.IntActNotes
FaddQ8R2E72EBI-4326675,EBI-4326723

GO - Molecular functioni

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
Q9JHX4, 2 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000016613

<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

More...
ProteinModelPortali
Q9JHX4

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

More...
SMRi
Q9JHX4

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
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>Domaini2 – 80DED 1PROSITE-ProRule annotationAdd BLAST79
Domaini100 – 177DED 2PROSITE-ProRule annotationAdd BLAST78

<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

More...
eggNOGi
KOG3573 Eukaryota
ENOG410ZQIE LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000160319

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000276884

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG050803

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9JHX4

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

More...
OrthoDBi
939331at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9JHX4

TreeFam database of animal gene trees

More...
TreeFami
TF102023

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00032 CASc, 1 hit

Integrated resource of protein families, domains and functional sites

More...
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

More...
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

More...
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_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>Sequencei

<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.

Q9JHX4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDFHSCLYDI AERLGNEELA ALKFLCLDHI PQKKQESIND VLVLFQRLQE
60 70 80 90 100
EGMLEEDNLS FLKELLFHIS RRDLLSRVLK SSPEEMVREL QVLGKAQVSA
110 120 130 140 150
YRVMLFKLSE DMDKEDLKSF KFLLITEIPK CKLQDNSSLL DIFVEMEKRT
160 170 180 190 200
ILAENNLVTL KSICFRVNRS LLGRIDDYER SSTERRMSTE GGEELPVSVL
210 220 230 240 250
DEVTIKMQDM WDSPGEQESE SLNSDNVYQM KSKPRGYCLI FNNNNFSKAR
260 270 280 290 300
EDIPKLSNMR DRKGTNYDEE ALSKTFKELH FEIVSFSDCT ASQIHEVLVS
310 320 330 340 350
YQSKDHKGKD CFICCILSHG DKGIVYGTDG KEASIYELTS YFTGSKCPSL
360 370 380 390 400
AGKPKIFFIQ ACQGNNFQKA VPVPDETGLE QEHVLEEDSS SYKNYIPDEA
410 420 430 440 450
DFLLGMATVK NCVSYRDPTR GTWYIQSLCQ SLRERCPRGE DILSILTGVN
460 470 480
YDVSNKDNPR NMGKQMPQPI FTLRKKLFFP PN
Length:482
Mass (Da):55,339
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:i82B4A29330C53264
GO

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

More...
DDBJi
Links Updated
AF279308 mRNA Translation: AAF87778.1
AF288372 mRNA Translation: AAK83055.1
AABR06060567 Genomic DNA No translation available.
AABR06060568 Genomic DNA No translation available.
CH473965 Genomic DNA Translation: EDL98978.1
CH473965 Genomic DNA Translation: EDL98979.1

NCBI Reference Sequences

More...
RefSeqi
NP_071613.1, NM_022277.1
XP_006245077.1, XM_006245015.3

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Rn.54474

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000016613; ENSRNOP00000016613; ENSRNOG00000012331
ENSRNOT00000084498; ENSRNOP00000069982; ENSRNOG00000012331

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
64044

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:64044

UCSC genome browser

More...
UCSCi
RGD:620945 rat

<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
AF279308 mRNA Translation: AAF87778.1
AF288372 mRNA Translation: AAK83055.1
AABR06060567 Genomic DNA No translation available.
AABR06060568 Genomic DNA No translation available.
CH473965 Genomic DNA Translation: EDL98978.1
CH473965 Genomic DNA Translation: EDL98979.1
RefSeqiNP_071613.1, NM_022277.1
XP_006245077.1, XM_006245015.3
UniGeneiRn.54474

3D structure databases

ProteinModelPortaliQ9JHX4
SMRiQ9JHX4
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JHX4, 2 interactors
STRINGi10116.ENSRNOP00000016613

Protein family/group databases

MEROPSiC14.009

PTM databases

iPTMnetiQ9JHX4
PhosphoSitePlusiQ9JHX4

Proteomic databases

PaxDbiQ9JHX4
PRIDEiQ9JHX4

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000016613; ENSRNOP00000016613; ENSRNOG00000012331
ENSRNOT00000084498; ENSRNOP00000069982; ENSRNOG00000012331
GeneIDi64044
KEGGirno:64044
UCSCiRGD:620945 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
841
RGDi620945 Casp8

Phylogenomic databases

eggNOGiKOG3573 Eukaryota
ENOG410ZQIE LUCA
GeneTreeiENSGT00940000160319
HOGENOMiHOG000276884
HOVERGENiHBG050803
InParanoidiQ9JHX4
KOiK04398
OMAiRVMLFQI
OrthoDBi939331at2759
PhylomeDBiQ9JHX4
TreeFamiTF102023

Enzyme and pathway databases

BRENDAi3.4.22.61 5301
ReactomeiR-RNO-111465 Apoptotic cleavage of cellular proteins
R-RNO-168638 NOD1/2 Signaling Pathway
R-RNO-3371378 Regulation by c-FLIP
R-RNO-5213460 RIPK1-mediated regulated necrosis
R-RNO-5218900 CASP8 activity is inhibited
R-RNO-5660668 CLEC7A/inflammasome pathway
R-RNO-69416 Dimerization of procaspase-8
R-RNO-75108 Activation, myristolyation of BID and translocation to mitochondria
R-RNO-75153 Apoptotic execution phase
R-RNO-75157 FasL/ CD95L signaling
R-RNO-75158 TRAIL signaling

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q9JHX4

Gene expression databases

BgeeiENSRNOG00000012331 Expressed in 10 organ(s), highest expression level in colon
GenevisibleiQ9JHX4 RN

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_RAT
<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: Q9JHX4
<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: April 1, 2015
Last sequence update: October 1, 2000
Last modified: February 13, 2019
This is version 142 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
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