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UniProtKB - Q9JHX4 (CASP8_RAT)

Entry version 155 (07 Apr 2021)
Sequence version 1 (01 Oct 2000)
Previous versions | rss
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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

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 (By similarity). 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:10197541). 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:10197541). 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 (By similarity). 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 (By similarity). Initiates pyroptosis following inactivation of MAP3K7/TAK1 (By similarity). Also acts as a regulator of innate immunity by mediating cleavage and inactivation of N4BP1 downstream of TLR3 or TLR4, thereby promoting cytokine production (By similarity). May participate in the Granzyme B (GZMB) cell death pathways (By similarity). Cleaves PARP1 (By similarity).By similarity1 Publication

<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

  • 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 <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.By similarity

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 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

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

Molecular functionHydrolase, Protease, Thiol protease
Biological 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-264870, Caspase-mediated cleavage of cytoskeletal proteins
R-RNO-3371378, Regulation by c-FLIP
R-RNO-5218900, CASP8 activity is inhibited
R-RNO-5357905, Regulation of TNFR1 signaling
R-RNO-5660668, CLEC7A/inflammasome pathway
R-RNO-5675482, Regulation of necroptotic cell death
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%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:3.4.22.61By similarity)
Short name:
CASP-81 Publication
Cleaved into the following 2 chains:
Caspase-8 subunit p18By similarity
Caspase-8 subunit p10By similarity
<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:Casp81 PublicationImported
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<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
  • UP000002494 <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 9
  • UP000234681 Componentsi: Chromosome 9, Unassembled WGS sequence

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

<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_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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000432426219 – 378Caspase-8 subunit p18By similarityAdd BLAST160
PropeptideiPRO_0000432427379 – 388By similarity10
ChainiPRO_0000432428389 – 482Caspase-8 subunit p10By similarityAdd 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%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. 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

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 cleavageBy similarity2
Sitei388 – 389Cleavage; by autocatalytic cleavageBy similarity2

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 thymus and 21 other tissues

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%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 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).

Interacts with RIPK1 (By similarity).

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

By similarity1 Publication

<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

GO - Molecular functioni

Complete GO annotation on QuickGO ...

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

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

More...SMRi		Q9JHX4

Database of comparative protein structure models

More...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>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

Ensembl GeneTree

More...GeneTreei		ENSGT00940000160319

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_036904_4_2_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9JHX4

Identification of Orthologs from Complete Genome Data

More...OMAi		SDKVYRM

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

More...Pfami		View protein in Pfam
PF01335, DED, 2 hits

Protein Motif fingerprint database; a protein domain database

More...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%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>Sequencei

<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.

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

More...EMBLi

GenBank nucleotide sequence database

More...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

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

3D structure databases

SMRiQ9JHX4
ModBaseiSearch...

Protein-protein interaction databases

IntActiQ9JHX4, 2 interactors
STRINGi10116.ENSRNOP00000016613

Protein family/group databases

MEROPSiC14.009

PTM databases

iPTMnetiQ9JHX4
PhosphoSitePlusiQ9JHX4

Proteomic databases

PaxDbiQ9JHX4
PRIDEiQ9JHX4

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
GeneTreeiENSGT00940000160319
HOGENOMiCLU_036904_4_2_1
InParanoidiQ9JHX4
OMAiSDKVYRM
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-264870, Caspase-mediated cleavage of cytoskeletal proteins
R-RNO-3371378, Regulation by c-FLIP
R-RNO-5218900, CASP8 activity is inhibited
R-RNO-5357905, Regulation of TNFR1 signaling
R-RNO-5660668, CLEC7A/inflammasome pathway
R-RNO-5675482, Regulation of necroptotic cell death
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 thymus and 21 other tissues
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

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry 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%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: April 1, 2015
Last sequence update: October 1, 2000
Last modified: April 7, 2021
This is version 155 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. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
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