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UniProtKB - O08738 (CASP6_MOUSE)

Entry version 181 (23 Feb 2022)
Sequence version 1 (01 Jul 1997)
Previous versions | rss
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Protein

Caspase-6

Gene

Casp6

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

Cysteine protease that plays essential roles in programmed cell death, axonal degeneration, development and innate immunity (PubMed:18981099, PubMed:22555455, PubMed:23695670, PubMed:32298652).

Acts as a non-canonical executioner caspase during apoptosis: localizes in the nucleus and cleaves the nuclear structural protein NUMA1 and lamin A/LMNA thereby inducing nuclear shrinkage and fragmentation (By similarity).

Lamin-A/LMNA cleavage is required for chromatin condensation and nuclear disassembly during apoptotic execution (By similarity).

Acts as a regulator of liver damage by promoting hepatocyte apoptosis: in absence of phosphorylation by AMP-activated protein kinase (AMPK), catalyzes cleavage of BID, leading to cytochrome c release, thereby participating in nonalcoholic steatohepatitis (PubMed:32029622).

Cleaves PARK7/DJ-1 in cells undergoing apoptosis (PubMed:22555455).

Involved in intrinsic apoptosis by mediating cleavage of RIPK1 (By similarity).

Furthermore, cleaves many transcription factors such as NF-kappa-B and cAMP response element-binding protein/CREBBP (By similarity).

Cleaves phospholipid scramblase proteins XKR4 and XKR9 (PubMed:25231987).

In addition to apoptosis, involved in different forms of programmed cell death (PubMed:32298652).

Plays an essential role in defense against viruses by acting as a central mediator of the ZBP1-mediated pyroptosis, apoptosis, and necroptosis (PANoptosis), independently of its cysteine protease activity (PubMed:32298652).

PANoptosis is a unique inflammatory programmed cell death, which provides a molecular scaffold that allows the interactions and activation of machinery required for inflammasome/pyroptosis, apoptosis and necroptosis (PubMed:32298652).

Mechanistically, interacts with RIPK3 and enhances the interaction between RIPK3 and ZBP1, leading to ZBP1-mediated inflammasome activation and cell death (PubMed:32298652).

Plays an essential role in axon degeneration during axon pruning which is the remodeling of axons during neurogenesis but not apoptosis (PubMed:23695670).

Regulates B-cell programs both during early development and after antigen stimulation (PubMed:18981099, PubMed:29863787).

By similarity7 Publications

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

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

During activation, the N-terminal disordered prodomain is removed by cleavage. Concomitantly, double cleavage gives rise to a large 18-kDa and a small 11-kDa subunit. The two large and two small subunits then assemble to form the active CASP6 complex. Can be cleaved and activated by different caspases, depending on the context. Cleaved and activated by caspase-8 (CASP8) and subsequently by caspase-3 (CASP3). Can also undergo autoactivation by mediating autocleavage at Asp-162 and Asp-175, while it is not able to cleave its N-terminal disordered prodomain. Intramolecular cleavage at Asp-175 is a prerequisite for CASP6 self-activation. Cleaved and activated by CASP1 in neurons, possibly in the context of inflammation. Phosphorylation at Ser-239 inhibits autocleavage, preventing caspase activation.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 sitei104By similarity1
Active sitei1461 Publication1

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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

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

Molecular functionHydrolase, Protease, Thiol protease
Biological processApoptosis

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.4.22.59, 3474

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-111465, Apoptotic cleavage of cellular proteins
R-MMU-264870, Caspase-mediated cleavage of cytoskeletal proteins
R-MMU-352238, Breakdown of the nuclear lamina

Protein family/group databases

MEROPS protease database

More...MEROPSi		C14.005

<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-61 Publication (EC:3.4.22.592 Publications)
Short name:
CASP-61 Publication
Alternative name(s):
Apoptotic protease Mch-21 Publication
Cleaved into the following 2 chains:
Caspase-6 subunit p18By similarity
Caspase-6 subunit p11By 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:Casp6Imported
Synonyms:Mch21 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

Organism-specific databases

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

More...MGIi		MGI:1312921, Casp6

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSMUSG00000027997

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

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

Casp6-knockout mice are grossly normal, breed with Mendelian ratio, and are only slightly protected from anti-Fas/CD95-induced cell death (PubMed:11062535). Casp6-deficient neurons undergo apoptosis and exhibit soma and axon degeneration just as wild type neurons (PubMed:23695670). While Casp6-deficiency is able to block axon degeneration with local deprivation, it is incapable of doing so with global deprivation (PubMed:23695670). In addition, B-cell differentiation into plasma cells is accelerated in deletion mutants compared to wild-type (PubMed:18981099, PubMed:29863787). Casp6-knockout mice are more susceptible to influenza virus infection (PubMed:32298652).5 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi146C → A: Does not affect ability to promote ZBP1-mediated pyroptosis, apoptosis, and necroptosis (PANoptosis). 1 Publication1

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_00000046121 – 5By similarity5
<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_00000046136 – 162Caspase-6 subunit p18By similarityAdd BLAST157
PropeptideiPRO_0000004614163 – 175By similarityAdd BLAST13
ChainiPRO_0000004615176 – 276Caspase-6 subunit p11By similarityAdd BLAST101

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 residuei62PhosphoserineCombined sources1
Modified residuei239PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi246S-palmitoyl cysteineBy similarity1
Lipidationi259S-palmitoyl cysteineBy 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

Phosphorylated by NUAK1; phosphorylation inhibits self-activation. Phosphorylation at Ser-239 by AMP-activated protein kinase (PRKAA1 or PRKAA2) inhibits autocleavage, preventing caspase activation, thereby preventing hepatocyte apoptosis.By similarity
Palmitoylation by ZDHHC17 blocks dimerization and subsequent activation, leading to inhibit the cysteine protease activity.By similarity
Can be cleaved and activated by different caspases, depending on the context. Cleaved and activated by caspase-8 (CASP8) and subsequently by caspase-3 (CASP3). Can also undergo autoactivation by mediating autocleavage at Asp-162 and Asp-175, while it is not able to cleave its N-terminal disordered prodomain. Cleaved and activated by CASP1, possibly in the context of inflammation.By similarity

Keywords - PTMi

Autocatalytic cleavage, Lipoprotein, Palmitate, Phosphoprotein, Zymogen

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		O08738

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		O08738

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

More...PaxDbi		O08738

PeptideAtlas

More...PeptideAtlasi		O08738

PRoteomics IDEntifications database

More...PRIDEi		O08738

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		265440

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O08738

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

More...PhosphoSitePlusi		O08738

SwissPalm database of S-palmitoylation events

More...SwissPalmi		O08738

<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

Highly expressed in lung, liver, kidney, testis, and heart. Lower levels in spleen, skeletal muscle and brain. Expressed in neurons.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000027997, Expressed in stomach and 277 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O08738, MM

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

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

Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 18 kDa (p18) and a 11 kDa (p11) subunit.

Interacts with BIRC6/bruce.

Interacts with RIPK3.

By similarity

Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 18 kDa (Caspase-6 subunit p18) and a 11 kDa (Caspase-6 subunit p11) subunit.

By similarity

Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 18 kDa (Caspase-6 subunit p18) and a 11 kDa (Caspase-6 subunit p11) subunit.

By similarity

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		198498, 13 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3944, Caspase-6 complex

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000029626

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		O08738, protein

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

3D structure databases

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

More...SMRi		O08738

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni25 – 27Tri-arginine exositeBy similarity3
Regioni108 – 125130's regionBy similarityAdd BLAST18

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminal disordered prodomain is required to prevent self-activation.By similarity
The Tri-arginine exosite is required to recruit substrates for hydrolysis.By similarity
Undergoes helix-strand structural transitions upon substrate-binding: the 130's region interconverts between an inactive helical state and the canonically active strand state. Other caspases rest constitutively in the strand conformation before and after substrate-binding.By similarity

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3573, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155140

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_036904_2_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O08738

Identification of Orthologs from Complete Genome Data

More...OMAi		ACRGSQH

Database of Orthologous Groups

More...OrthoDBi		984395at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		O08738

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
IPR029030, Caspase-like_dom_sf
IPR037554, Caspase_6
IPR033139, Caspase_cys_AS
IPR016129, Caspase_his_AS
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:SF206, PTHR10454:SF206, 1 hit

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

Superfamily database of structural and functional annotation

More...SUPFAMi		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

<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.

O08738-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTETDGFYKS REVFDPAEQY KMDHKRRGVA LIFNHERFFW HLTLPERRGT 
        60         70         80         90        100
NADRDNLTRR FSDLGFEVKC FNDLRAEELL LKIHEVSTSS HIDADCFICV 
       110        120        130        140        150
FLSHGEGNHV YAYDAKIEIQ TLTGLFKGDK CQSLVGKPKI FIIQACRGSQ 
       160        170        180        190        200
HDVPVVPLDM VDHQTDKLDN VTQVDAASVY TLPAGADFLM CYSVAEGYYS 
       210        220        230        240        250
HRETVNGSWY IQDLCEMLAR YGSSLEFTEL LTLVNRKVSQ RRVDFCKDPD 
       260        270 
AIGKKQVPCF ASMLTKKLHF CPKPSK
Length:276
Mass (Da):31,595
Last modified:July 1, 1997 - 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:i5965DE9321126B6C
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
Y13087 mRNA Translation: CAA73529.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS17838.1

NCBI Reference Sequences

More...RefSeqi		NP_033941.3, NM_009811.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000029626; ENSMUSP00000029626; ENSMUSG00000027997

Database of genes from NCBI RefSeq genomes

More...GeneIDi		12368

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:12368

UCSC genome browser

More...UCSCi		uc008riq.3, 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
Y13087 mRNA Translation: CAA73529.1
CCDSiCCDS17838.1
RefSeqiNP_033941.3, NM_009811.4

3D structure databases

SMRiO08738
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi198498, 13 interactors
ComplexPortaliCPX-3944, Caspase-6 complex
STRINGi10090.ENSMUSP00000029626

Protein family/group databases

MEROPSiC14.005

PTM databases

iPTMnetiO08738
PhosphoSitePlusiO08738
SwissPalmiO08738

Proteomic databases

EPDiO08738
jPOSTiO08738
PaxDbiO08738
PeptideAtlasiO08738
PRIDEiO08738
ProteomicsDBi265440

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		1733, 1146 antibodies from 43 providers

The DNASU plasmid repository

More...DNASUi		12368

Genome annotation databases

EnsembliENSMUST00000029626; ENSMUSP00000029626; ENSMUSG00000027997
GeneIDi12368
KEGGimmu:12368
UCSCiuc008riq.3, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		839
MGIiMGI:1312921, Casp6
VEuPathDBiHostDB:ENSMUSG00000027997

Phylogenomic databases

eggNOGiKOG3573, Eukaryota
GeneTreeiENSGT00940000155140
HOGENOMiCLU_036904_2_0_1
InParanoidiO08738
OMAiACRGSQH
OrthoDBi984395at2759
PhylomeDBiO08738
TreeFamiTF102023

Enzyme and pathway databases

BRENDAi3.4.22.59, 3474
ReactomeiR-MMU-111465, Apoptotic cleavage of cellular proteins
R-MMU-264870, Caspase-mediated cleavage of cytoskeletal proteins
R-MMU-352238, Breakdown of the nuclear lamina

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		12368, 0 hits in 50 CRISPR screens

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

More...ChiTaRSi		Casp6, mouse

Protein Ontology

More...PROi		PR:O08738
RNActiO08738, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000027997, Expressed in stomach and 277 other tissues
GenevisibleiO08738, MM

Family and domain databases

CDDicd00032, CASc, 1 hit
InterProiView protein in InterPro
IPR029030, Caspase-like_dom_sf
IPR037554, Caspase_6
IPR033139, Caspase_cys_AS
IPR016129, Caspase_his_AS
IPR002398, Pept_C14
IPR002138, Pept_C14_p10
IPR001309, Pept_C14_p20
IPR015917, Pept_C14A
PANTHERiPTHR10454, PTHR10454, 1 hit
PTHR10454:SF206, PTHR10454:SF206, 1 hit
PRINTSiPR00376, IL1BCENZYME
SMARTiView protein in SMART
SM00115, CASc, 1 hit
SUPFAMiSSF52129, 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

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 nameiCASP6_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: O08738
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: February 23, 2022
This is version 181 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families
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