UniProtKB - P49662 (CASP4_HUMAN)
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- BLAST>sp|P49662|CASP4_HUMAN Caspase-4 OS=Homo sapiens OX=9606 GN=CASP4 PE=1 SV=1 MAEGNHRKKPLKVLESLGKDFLTGVLDNLVEQNVLNWKEEEKKKYYDAKTEDKVRVMADS MQEKQRMAGQMLLQTFFNIDQISPNKKAHPNMEAGPPESGESTDALKLCPHEEFLRLCKE RAEEIYPIKERNNRTRLALIICNTEFDHLPPRNGADFDITGMKELLEGLDYSVDVEENLT ARDMESALRAFATRPEHKSSDSTFLVLMSHGILEGICGTVHDEKKPDVLLYDTIFQIFNN RNCLSLKDKPKVIIVQACRGANRGELWVRDSPASLEVASSQSSENLEEDAVYKTHVEKDF IAFCSSTPHNVSWRDSTMGSIFITQLITCFQKYSWCCHLEEVFRKVQQSFETPRAKAQMP TIERLSMTRYFYLFPGN
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Protein
Caspase-4
Gene
CASP4
Organism
Homo sapiens (Human)
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>Select a section on the left to see content.
<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
Inflammatory caspase (PubMed:7797510, PubMed:23516580, PubMed:25119034). Essential effector of NLRP3 inflammasome-dependent CASP1 activation and IL1B and IL18 secretion in response to non-canonical activators, such as UVB radiation, cholera enterotoxin subunit B and cytosolic LPS (PubMed:22246630, PubMed:26174085, PubMed:26173988, PubMed:26508369, PubMed:25964352). Independently of NLRP3 inflammasome and CASP1, promotes pyroptosis, through GSDMD cleavage and activation, and IL1A, IL18 and HMGB1 release in response to non-canonical inflammasome activators (PubMed:24879791, PubMed:25964352). Plays a crucial role in the restriction of Salmonella typhimurium replication in colonic epithelial cells during infection (PubMed:25121752). In later stages of the infection, LPS from cytosolic Salmonella triggers CASP4 activation, which ultimately results in pyroptosis of infected cells and their extrusion into the gut lumen, as well as in IL18 secretion. Pyroptosis limits bacterial replication, while cytokine secretion promotes the recruitment and activation of immune cells and triggers mucosal inflammation. Involved in LPS-induced IL6 secretion; this activity may not require caspase enzymatic activity (PubMed:26508369). Involved in cell death induced by endoplasmic reticulum stress and by treatment with cytotoxic APP peptides found Alzheimer's patient brains (PubMed:15123740, PubMed:22246630, PubMed:23661706). Activated by direct binding to LPS without the need of an upstream sensor (PubMed:25119034). Does not directly process IL1B (PubMed:7743998, PubMed:7797592, PubMed:7797510). During non-canonical inflammasome activation, cuts CGAS and may play a role in the regulation of antiviral innate immune activation (PubMed:28314590).15 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"A novel human protease similar to the interleukin-1 beta converting enzyme induces apoptosis in transfected cells."
Faucheu C., Diu A., Chan A.W.E., Blanchet A.-M., Miossec C., Herve F., Collard-Dutilleul V., Gu Y., Aldape R.A., Lippke J.A., Rocher C., Su M.S.-S., Livingston D.J., Hercend T., Lalanne J.-L.
EMBO J. 14:1914-1922(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF CYS-258, 3D-STRUCTURE MODELING, AUTOCATALYSIS, TISSUE SPECIFICITY. - Ref.2"Molecular cloning and pro-apoptotic activity of ICErelII and ICErelIII, members of the ICE/CED-3 family of cysteine proteases."
Munday N.A., Vaillancourt J.P., Ali A., Casano F.J., Miller D.K., Molineaux S.M., Yamin T.-T., Yu V.L., Nicholson D.W.
J. Biol. Chem. 270:15870-15876(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY. - Ref.3"Identification and characterization of ICH-2, a novel member of the interleukin-1 beta-converting enzyme family of cysteine proteases."
Kamens J., Paskind M., Hugunin M., Talanian R.V., Allen H., Banach D., Bump N.J., Hackett M.C., Johnston C.G., Li P., Mankovich J.A., Terranova M., Ghayur T.
J. Biol. Chem. 270:15250-15256(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AUTOCATALYTIC CLEAVAGE AT ASP-289, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.12"Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death."
Hitomi J., Katayama T., Eguchi Y., Kudo T., Taniguchi M., Koyama Y., Manabe T., Yamagishi S., Bando Y., Imaizumi K., Tsujimoto Y., Tohyama M.
J. Cell Biol. 165:347-356(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, CLEAVAGE IN RESPONSE TO ENDOPLASMIC RETICULUM STRESS. - Ref.17"Caspase-4 is required for activation of inflammasomes."
Sollberger G., Strittmatter G.E., Kistowska M., French L.E., Beer H.D.
J. Immunol. 188:1992-2000(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH CASP1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-258. - Ref.19"Transmembrane protein 214 (TMEM214) mediates endoplasmic reticulum stress-induced caspase 4 enzyme activation and apoptosis."
Li C., Wei J., Li Y., He X., Zhou Q., Yan J., Zhang J., Liu Y., Liu Y., Shu H.B.
J. Biol. Chem. 288:17908-17917(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TMEM214, MUTAGENESIS OF CYS-258. - Ref.20"The E. coli effector protein NleF is a caspase inhibitor."
Blasche S., Mortl M., Steuber H., Siszler G., Nisa S., Schwarz F., Lavrik I., Gronewold T.M., Maskos K., Donnenberg M.S., Ullmann D., Uetz P., Kogl M.
PLoS ONE 8:E58937-E58937(2013) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH E.COLI NLEF (MICROBIAL INFECTION), CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION (MICROBIAL INFECTION). - Ref.21"Noncanonical inflammasome activation of caspase-4/caspase-11 mediates epithelial defenses against enteric bacterial pathogens."
Knodler L.A., Crowley S.M., Sham H.P., Yang H., Wrande M., Ma C., Ernst R.K., Steele-Mortimer O., Celli J., Vallance B.A.
Cell Host Microbe 16:249-256(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION BY LPS. - Ref.22"A critical role for human caspase-4 in endotoxin sensitivity."
Kajiwara Y., Schiff T., Voloudakis G., Gama Sosa M.A., Elder G., Bozdagi O., Buxbaum J.D.
J. Immunol. 193:335-343(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INDUCTION BY LPS. - Ref.23"Inflammatory caspases are innate immune receptors for intracellular LPS."
Shi J., Zhao Y., Wang Y., Gao W., Ding J., Li P., Hu L., Shao F.
Nature 514:187-192(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, OLIGOMERIZATION, INTERACTION WITH LPS, ENZYME REGULATION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF CYS-258. - Ref.24"Caspase-4 mediates non-canonical activation of the NLRP3 inflammasome in human myeloid cells."
Schmid-Burgk J.L., Gaidt M.M., Schmidt T., Ebert T.S., Bartok E., Hornung V.
Eur. J. Immunol. 45:2911-2917(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.25"NLRP3 inflammasome activation downstream of cytoplasmic LPS recognition by both caspase-4 and caspase-5."
Baker P.J., Boucher D., Bierschenk D., Tebartz C., Whitney P.G., D'Silva D.B., Tanzer M.C., Monteleone M., Robertson A.A., Cooper M.A., Alvarez-Diaz S., Herold M.J., Bedoui S., Schroder K., Masters S.L.
Eur. J. Immunol. 45:2918-2926(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.26"Human caspase-4 and caspase-5 regulate the one-step non-canonical inflammasome activation in monocytes."
Vigano E., Diamond C.E., Spreafico R., Balachander A., Sobota R.M., Mortellaro A.
Nat. Commun. 6:8761-8761(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INDUCTION BY LPS. - Ref.29"Human caspase-4 mediates noncanonical inflammasome activation against gram-negative bacterial pathogens."
Casson C.N., Yu J., Reyes V.M., Taschuk F.O., Yadav A., Copenhaver A.M., Nguyen H.T., Collman R.G., Shin S.
Proc. Natl. Acad. Sci. U.S.A. 112:6688-6693(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INDUCTION BY LPS AND IFNB1. - Ref.30"Inflammasome activation triggers caspase-1-mediated cleavage of cGAS to regulate responses to DNA virus infection."
Wang Y., Ning X., Gao P., Wu S., Sha M., Lv M., Zhou X., Gao J., Fang R., Meng G., Su X., Jiang Z.
Immunity 46:393-404(2017) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, MUTAGENESIS OF CYS-258.
<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. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
Strict requirement for Asp at the P1 position. It has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|- but also cleaves at Asp-Glu-Val-Asp-|-.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.20"The E. coli effector protein NleF is a caspase inhibitor."
Blasche S., Mortl M., Steuber H., Siszler G., Nisa S., Schwarz F., Lavrik I., Gronewold T.M., Maskos K., Donnenberg M.S., Ullmann D., Uetz P., Kogl M.
PLoS ONE 8:E58937-E58937(2013) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH E.COLI NLEF (MICROBIAL INFECTION), CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION (MICROBIAL INFECTION).
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
Activated by homooligomerization induced by direct binding to cytosolic LPS, in a TLR4-independent manner (PubMed:25119034).1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.23"Inflammatory caspases are innate immune receptors for intracellular LPS."
Shi J., Zhao Y., Wang Y., Gao W., Ding J., Li P., Hu L., Shao F.
Nature 514:187-192(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, OLIGOMERIZATION, INTERACTION WITH LPS, ENZYME REGULATION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF CYS-258.
(Microbial infection) Inhibited by the effector protein NleF produced by pathogenic E.coli; this inhibits apoptosis (PubMed:23516580).1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.20"The E. coli effector protein NleF is a caspase inhibitor."
Blasche S., Mortl M., Steuber H., Siszler G., Nisa S., Schwarz F., Lavrik I., Gronewold T.M., Maskos K., Donnenberg M.S., Ullmann D., Uetz P., Kogl M.
PLoS ONE 8:E58937-E58937(2013) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH E.COLI NLEF (MICROBIAL INFECTION), CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION (MICROBIAL INFECTION).
<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
Values obtained using the partial C-terminal enzyme sequence of 105-377.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.3"Identification and characterization of ICH-2, a novel member of the interleukin-1 beta-converting enzyme family of cysteine proteases."
Kamens J., Paskind M., Hugunin M., Talanian R.V., Allen H., Banach D., Bump N.J., Hackett M.C., Johnston C.G., Li P., Mankovich J.A., Terranova M., Ghayur T.
J. Biol. Chem. 270:15250-15256(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AUTOCATALYTIC CLEAVAGE AT ASP-289, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=681 µM for synthetic peptide acetyl-YVAD-p-nitroanilide1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.3"Identification and characterization of ICH-2, a novel member of the interleukin-1 beta-converting enzyme family of cysteine proteases."
Kamens J., Paskind M., Hugunin M., Talanian R.V., Allen H., Banach D., Bump N.J., Hackett M.C., Johnston C.G., Li P., Mankovich J.A., Terranova M., Ghayur T.
J. Biol. Chem. 270:15250-15256(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AUTOCATALYTIC CLEAVAGE AT ASP-289, BIOPHYSICOCHEMICAL PROPERTIES.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 sitei | 210 | By similarity | 1 | |
| <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 sitei | 258 | 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<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
- CARD domain binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- cysteine-type endopeptidase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- cysteine-type endopeptidase activity involved in apoptotic process Source: GO_Central
<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 - Biological processi
- apoptotic process Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- cellular response to amyloid-beta Source: ParkinsonsUK-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- inflammatory response Source: UniProtKB-KW
- innate immune response Source: UniProtKB-KW
- intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of tumor necrosis factor-mediated signaling pathway Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- proteolysis Source: ProtInc <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- regulation of apoptotic process Source: InterPro
- regulation of inflammatory response Source: GO_Central
<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 function | Hydrolase, Protease, Thiol protease |
| Biological process | Immunity, Inflammatory response, Innate immunity, Necrosis |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.4.22.57 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-168638 NOD1/2 Signaling Pathway |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P49662 |
Protein family/group databases
MEROPS protease database More...MEROPSi | C14.007 |
<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-4 (EC:3.4.22.571 Publication<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Short name: CASP-4 Alternative name(s): ICE and Ced-3 homolog 21 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Short name: ICH-21 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
ICE(rel)-II1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Mih11 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Protease TX1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
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:CASP4 Synonyms:ICH2 |
| <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>Organismi | Homo sapiens (Human) |
| <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 identifieri | 9606 [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 lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <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 |
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Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000196954.12 |
Human Gene Nomenclature Database More...HGNCi | HGNC:1505 CASP4 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 602664 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P49662 |
<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
Mitochondrion
- Mitochondrion 2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.12"Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death."
Hitomi J., Katayama T., Eguchi Y., Kudo T., Taniguchi M., Koyama Y., Manabe T., Yamagishi S., Bando Y., Imaizumi K., Tsujimoto Y., Tohyama M.
J. Cell Biol. 165:347-356(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, CLEAVAGE IN RESPONSE TO ENDOPLASMIC RETICULUM STRESS. - Ref.19"Transmembrane protein 214 (TMEM214) mediates endoplasmic reticulum stress-induced caspase 4 enzyme activation and apoptosis."
Li C., Wei J., Li Y., He X., Zhou Q., Yan J., Zhang J., Liu Y., Liu Y., Shu H.B.
J. Biol. Chem. 288:17908-17917(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TMEM214, MUTAGENESIS OF CYS-258.
- Mitochondrion 2 Publications
Endoplasmic reticulum
- Endoplasmic reticulum membrane 2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.12"Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death."
Hitomi J., Katayama T., Eguchi Y., Kudo T., Taniguchi M., Koyama Y., Manabe T., Yamagishi S., Bando Y., Imaizumi K., Tsujimoto Y., Tohyama M.
J. Cell Biol. 165:347-356(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, CLEAVAGE IN RESPONSE TO ENDOPLASMIC RETICULUM STRESS. - Ref.19"Transmembrane protein 214 (TMEM214) mediates endoplasmic reticulum stress-induced caspase 4 enzyme activation and apoptosis."
Li C., Wei J., Li Y., He X., Zhou Q., Yan J., Zhang J., Liu Y., Liu Y., Shu H.B.
J. Biol. Chem. 288:17908-17917(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TMEM214, MUTAGENESIS OF CYS-258.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.19"Transmembrane protein 214 (TMEM214) mediates endoplasmic reticulum stress-induced caspase 4 enzyme activation and apoptosis."
Li C., Wei J., Li Y., He X., Zhou Q., Yan J., Zhang J., Liu Y., Liu Y., Shu H.B.
J. Biol. Chem. 288:17908-17917(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TMEM214, MUTAGENESIS OF CYS-258.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.19"Transmembrane protein 214 (TMEM214) mediates endoplasmic reticulum stress-induced caspase 4 enzyme activation and apoptosis."
Li C., Wei J., Li Y., He X., Zhou Q., Yan J., Zhang J., Liu Y., Liu Y., Shu H.B.
J. Biol. Chem. 288:17908-17917(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TMEM214, MUTAGENESIS OF CYS-258.
- Endoplasmic reticulum membrane 2 Publications
Extracellular region or secreted
- Secreted 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.17"Caspase-4 is required for activation of inflammasomes."
Sollberger G., Strittmatter G.E., Kistowska M., French L.E., Beer H.D.
J. Immunol. 188:1992-2000(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH CASP1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-258.
- Secreted 1 Publication
Cytosol
- cytosol 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.19"Transmembrane protein 214 (TMEM214) mediates endoplasmic reticulum stress-induced caspase 4 enzyme activation and apoptosis."
Li C., Wei J., Li Y., He X., Zhou Q., Yan J., Zhang J., Liu Y., Liu Y., Shu H.B.
J. Biol. Chem. 288:17908-17917(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TMEM214, MUTAGENESIS OF CYS-258.
- Inflammasome 2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.23"Inflammatory caspases are innate immune receptors for intracellular LPS."
Shi J., Zhao Y., Wang Y., Gao W., Ding J., Li P., Hu L., Shao F.
Nature 514:187-192(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, OLIGOMERIZATION, INTERACTION WITH LPS, ENZYME REGULATION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF CYS-258. - Ref.26"Human caspase-4 and caspase-5 regulate the one-step non-canonical inflammasome activation in monocytes."
Vigano E., Diamond C.E., Spreafico R., Balachander A., Sobota R.M., Mortellaro A.
Nat. Commun. 6:8761-8761(2015) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INDUCTION BY LPS.
Note: Predominantly localizes to the endoplasmic reticulum (ER). Association with the ER membrane requires TMEM214 (PubMed:15123740). Released in the extracellular milieu by keratinocytes following UVB irradiation (PubMed:22246630).2 Publications- cytosol 1 Publication
- Ref.12"Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death."
Hitomi J., Katayama T., Eguchi Y., Kudo T., Taniguchi M., Koyama Y., Manabe T., Yamagishi S., Bando Y., Imaizumi K., Tsujimoto Y., Tohyama M.
J. Cell Biol. 165:347-356(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, CLEAVAGE IN RESPONSE TO ENDOPLASMIC RETICULUM STRESS. - Ref.17"Caspase-4 is required for activation of inflammasomes."
Sollberger G., Strittmatter G.E., Kistowska M., French L.E., Beer H.D.
J. Immunol. 188:1992-2000(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH CASP1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-258.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Cytosol
- AIM2 inflammasome complex Source: GO_Central
- cytosol Source: HPA
- IPAF inflammasome complex Source: GO_Central
- NLRP3 inflammasome complex Source: GO_Central
Endoplasmic reticulum
- endoplasmic reticulum Source: ParkinsonsUK-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- endoplasmic reticulum membrane Source: UniProtKB-SubCell
Extracellular region or secreted
- extracellular region Source: UniProtKB-SubCell
Mitochondrion
- mitochondrion Source: ParkinsonsUK-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Plasma Membrane
- plasma membrane Source: HPA
Other locations
- protein-containing complex Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<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>Keywords - Cellular componenti
Cytoplasm, Endoplasmic reticulum, Inflammasome, Membrane, Mitochondrion, Secreted<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
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi | 258 | C → A: Loss of enzymatic activity. Loss of LPS-induced pyroptosis. No effect on the interaction with LPS. Decrease in cell death induced by TMEM214 overexpression. Does not support IL1B and IL18 secretion following UVB irradiation. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi | 258 | C → S: Loss of autocatalysis. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Organism-specific databases
DisGeNET More...DisGeNETi | 837 |
Open Targets More...OpenTargetsi | ENSG00000196954 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA26088 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL2226 |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 1620 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | CASP4 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 1352420 |
<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 key | Position(s) | DescriptionActions | Graphical view | Length | |
|---|---|---|---|---|---|
| <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_0000004596 | 1 – ?80 | Sequence analysisAdd BLAST | 80 | ||
| <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_0000004597 | ?81 – 270 | Caspase-4 subunit 1Add BLAST | 190 | ||
| <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_0000004598 | 271 – 289 | Sequence analysis1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 19 | ||
| <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_0000004599 | 290 – 377 | Caspase-4 subunit 2Add BLAST | 88 | ||
| Isoform 2 (identifier: P49662-2) | |||||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | RemovedCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||||
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length | |
|---|---|---|---|---|---|
| <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 residuei | 83 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Isoform 2 (identifier: P49662-2) | |||||
| <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 residuei | 2 | N-acetylalanineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
<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
In response to activation signals, including endoplasmic reticulum stress or treatment with amyloid-beta A4 protein fragments (such as amyloid-beta protein 40), undergoes autoproteolytic cleavage.3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"A novel human protease similar to the interleukin-1 beta converting enzyme induces apoptosis in transfected cells."
Faucheu C., Diu A., Chan A.W.E., Blanchet A.-M., Miossec C., Herve F., Collard-Dutilleul V., Gu Y., Aldape R.A., Lippke J.A., Rocher C., Su M.S.-S., Livingston D.J., Hercend T., Lalanne J.-L.
EMBO J. 14:1914-1922(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF CYS-258, 3D-STRUCTURE MODELING, AUTOCATALYSIS, TISSUE SPECIFICITY. - Ref.3"Identification and characterization of ICH-2, a novel member of the interleukin-1 beta-converting enzyme family of cysteine proteases."
Kamens J., Paskind M., Hugunin M., Talanian R.V., Allen H., Banach D., Bump N.J., Hackett M.C., Johnston C.G., Li P., Mankovich J.A., Terranova M., Ghayur T.
J. Biol. Chem. 270:15250-15256(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AUTOCATALYTIC CLEAVAGE AT ASP-289, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.12"Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death."
Hitomi J., Katayama T., Eguchi Y., Kudo T., Taniguchi M., Koyama Y., Manabe T., Yamagishi S., Bando Y., Imaizumi K., Tsujimoto Y., Tohyama M.
J. Cell Biol. 165:347-356(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, CLEAVAGE IN RESPONSE TO ENDOPLASMIC RETICULUM STRESS.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Sitei | 289 – 290 | Cleavage; by autolysis1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 2 |
<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>Keywords - PTMi
Acetylation, Phosphoprotein, ZymogenProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P49662 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P49662 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P49662 |
PeptideAtlas More...PeptideAtlasi | P49662 |
PRoteomics IDEntifications database More...PRIDEi | P49662 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 56043 56044 [P49662-2] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P49662 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P49662 |
<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
Widely expressed, including in keratinocytes and colonic and small intestinal epithelial cells (at protein level). Not detected in brain.6 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"A novel human protease similar to the interleukin-1 beta converting enzyme induces apoptosis in transfected cells."
Faucheu C., Diu A., Chan A.W.E., Blanchet A.-M., Miossec C., Herve F., Collard-Dutilleul V., Gu Y., Aldape R.A., Lippke J.A., Rocher C., Su M.S.-S., Livingston D.J., Hercend T., Lalanne J.-L.
EMBO J. 14:1914-1922(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF CYS-258, 3D-STRUCTURE MODELING, AUTOCATALYSIS, TISSUE SPECIFICITY. - Ref.2"Molecular cloning and pro-apoptotic activity of ICErelII and ICErelIII, members of the ICE/CED-3 family of cysteine proteases."
Munday N.A., Vaillancourt J.P., Ali A., Casano F.J., Miller D.K., Molineaux S.M., Yamin T.-T., Yu V.L., Nicholson D.W.
J. Biol. Chem. 270:15870-15876(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY. - Ref.3"Identification and characterization of ICH-2, a novel member of the interleukin-1 beta-converting enzyme family of cysteine proteases."
Kamens J., Paskind M., Hugunin M., Talanian R.V., Allen H., Banach D., Bump N.J., Hackett M.C., Johnston C.G., Li P., Mankovich J.A., Terranova M., Ghayur T.
J. Biol. Chem. 270:15250-15256(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AUTOCATALYTIC CLEAVAGE AT ASP-289, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.11"Expression analysis of the human caspase-1 subfamily reveals specific regulation of the CASP5 gene by lipopolysaccharide and interferon-gamma."
Lin X.Y., Choi M.S., Porter A.G.
J. Biol. Chem. 275:39920-39926(2000) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY. - Ref.17"Caspase-4 is required for activation of inflammasomes."
Sollberger G., Strittmatter G.E., Kistowska M., French L.E., Beer H.D.
J. Immunol. 188:1992-2000(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH CASP1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-258. - Ref.21"Noncanonical inflammasome activation of caspase-4/caspase-11 mediates epithelial defenses against enteric bacterial pathogens."
Knodler L.A., Crowley S.M., Sham H.P., Yang H., Wrande M., Ma C., Ernst R.K., Steele-Mortimer O., Celli J., Vallance B.A.
Cell Host Microbe 16:249-256(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION BY LPS.
<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
In peripheral blood mononuclear cells and purified monocytes, up-regulated by bacterial lipopolysaccharides (LPS) and interferon-beta/IFNB1 at the mRNA level (PubMed:16893518, PubMed:24879791). However, this increase is not observed at the protein level, which remains constant in monocytes and other cell types following LPS treatment (PubMed:25121752) (PubMed:26508369). In monocyte-derived macrophages, some up-regulation at the protein level is observed following treatment with LPS and IFNB1 (PubMed:25964352). In SH-EP1 neuroblastoma cell line, up-regulated by NF-kappa-B RELA/p65 at both mRNA and protein levels.3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.13"Identification of a novel exon encoding the amino-terminus of the predominant caspase-5 variants."
Eckhart L., Kittel C., Gawlas S., Gruber F., Mildner M., Jilma B., Tschachler E.
Biochem. Biophys. Res. Commun. 348:682-688(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION BY LPS. - Ref.22"A critical role for human caspase-4 in endotoxin sensitivity."
Kajiwara Y., Schiff T., Voloudakis G., Gama Sosa M.A., Elder G., Bozdagi O., Buxbaum J.D.
J. Immunol. 193:335-343(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INDUCTION BY LPS. - Ref.28"NF-kappaB regulates caspase-4 expression and sensitizes neuroblastoma cells to Fas-induced apoptosis."
Yang H.J., Wang M., Wang L., Cheng B.F., Lin X.Y., Feng Z.W.
PLoS ONE 10:E0117953-E0117953(2015) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION BY NF-KAPPA-B.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000196954 |
CleanEx database of gene expression profiles More...CleanExi | HS_CASP4 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P49662 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P49662 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB037167 HPA027588 |
<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
Upon direct LPS-binding, forms large homooligomers, resulting in its activation. These oligomers are often referred to as 'non-canonical inflammasomes' (PubMed:25119034). Active as a heterotetramer consisting of two anti-parallel arranged heterodimers, each one formed by a small and a large subunit (By similarity). In its precursor form, interacts with TMEM214; this interaction is required for association with the endoplasmic reticulum membrane (PubMed:23661706). Interacts with CASP1 (PubMed:22246630). Interacts with NOD2 (PubMed:18511561).By similarity4 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.15"A NOD2-NALP1 complex mediates caspase-1-dependent IL-1beta secretion in response to Bacillus anthracis infection and muramyl dipeptide."
Hsu L.C., Ali S.R., McGillivray S., Tseng P.H., Mariathasan S., Humke E.W., Eckmann L., Powell J.J., Nizet V., Dixit V.M., Karin M.
Proc. Natl. Acad. Sci. U.S.A. 105:7803-7808(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH NOD2. - Ref.17"Caspase-4 is required for activation of inflammasomes."
Sollberger G., Strittmatter G.E., Kistowska M., French L.E., Beer H.D.
J. Immunol. 188:1992-2000(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH CASP1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-258. - Ref.19"Transmembrane protein 214 (TMEM214) mediates endoplasmic reticulum stress-induced caspase 4 enzyme activation and apoptosis."
Li C., Wei J., Li Y., He X., Zhou Q., Yan J., Zhang J., Liu Y., Liu Y., Shu H.B.
J. Biol. Chem. 288:17908-17917(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TMEM214, MUTAGENESIS OF CYS-258. - Ref.23"Inflammatory caspases are innate immune receptors for intracellular LPS."
Shi J., Zhao Y., Wang Y., Gao W., Ding J., Li P., Hu L., Shao F.
Nature 514:187-192(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, OLIGOMERIZATION, INTERACTION WITH LPS, ENZYME REGULATION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF CYS-258.
(Microbial infection) Interacts with NleF protein from pathogenic E.coli; this interaction leads to enzyme inhibition.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.20"The E. coli effector protein NleF is a caspase inhibitor."
Blasche S., Mortl M., Steuber H., Siszler G., Nisa S., Schwarz F., Lavrik I., Gronewold T.M., Maskos K., Donnenberg M.S., Ullmann D., Uetz P., Kogl M.
PLoS ONE 8:E58937-E58937(2013) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH E.COLI NLEF (MICROBIAL INFECTION), CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION (MICROBIAL INFECTION).
<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
- CARD domain binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 107287, 34 interactors |
Database of interacting proteins More...DIPi | DIP-44806N |
Protein interaction database and analysis system More...IntActi | P49662, 41 interactors |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000388566 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P49662 |
<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 | P49662 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P49662 |
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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Domaini | 1 – 91 | CARDPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 91 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Regioni | 1 – 59 | Required for LPS-bindingBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi Add BLAST | 59 |
<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 CARD domain mediates LPS recognition and homooligomerization.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.23"Inflammatory caspases are innate immune receptors for intracellular LPS."
Shi J., Zhao Y., Wang Y., Gao W., Ding J., Li P., Hu L., Shao F.
Nature 514:187-192(2014) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, OLIGOMERIZATION, INTERACTION WITH LPS, ENZYME REGULATION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF CYS-258.
<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 ENOG410ZQIE LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00910000144131 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000234399 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG076981 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P49662 |
KEGG Orthology (KO) More...KOi | K04394 |
Identification of Orthologs from Complete Genome Data More...OMAi | FFNIDQI |
Database of Orthologous Groups More...OrthoDBi | EOG091G07NO |
Database for complete collections of gene phylogenies More...PhylomeDBi | P49662 |
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 IPR001315 CARD IPR029030 Caspase-like_dom_sf IPR033139 Caspase_cys_AS IPR016129 Caspase_his_AS IPR011029 DEATH-like_dom_sf IPR002138 Pept_C14_p10 IPR001309 Pept_C14_p20 IPR015917 Pept_C14A |
Pfam protein domain database More...Pfami | View protein in Pfam PF00619 CARD, 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 SM00114 CARD, 1 hit SM00115 CASc, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF47986 SSF47986, 1 hit SSF52129 SSF52129, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50209 CARD, 1 hit 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_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>Sequences (5)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 describes 5 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
Isoform 1 (identifier: P49662-1) [UniParc]FASTAAdd to basketAdded to basketShow »
Also known as: Alpha
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
10 20 30 40 50
MAEGNHRKKP LKVLESLGKD FLTGVLDNLV EQNVLNWKEE EKKKYYDAKT
60 70 80 90 100
EDKVRVMADS MQEKQRMAGQ MLLQTFFNID QISPNKKAHP NMEAGPPESG
110 120 130 140 150
ESTDALKLCP HEEFLRLCKE RAEEIYPIKE RNNRTRLALI ICNTEFDHLP
160 170 180 190 200
PRNGADFDIT GMKELLEGLD YSVDVEENLT ARDMESALRA FATRPEHKSS
210 220 230 240 250
DSTFLVLMSH GILEGICGTV HDEKKPDVLL YDTIFQIFNN RNCLSLKDKP
260 270 280 290 300
KVIIVQACRG ANRGELWVRD SPASLEVASS QSSENLEEDA VYKTHVEKDF
310 320 330 340 350
IAFCSSTPHN VSWRDSTMGS IFITQLITCF QKYSWCCHLE EVFRKVQQSF
360 370
ETPRAKAQMP TIERLSMTRY FYLFPGN
Length:377
Mass (Da):43,262
Last modified:February 1, 1996 - 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:iDC7CCEC6E9D483EB
Isoform 2 (identifier: P49662-2) [UniParc]FASTAAdd to basketAdded to basketShow »
Also known as: Gamma, mih1-beta
The sequence of this isoform differs from the canonical sequence as follows:
1-56: Missing.
10 20 30 40 50
MADSMQEKQR MAGQMLLQTF FNIDQISPNK KAHPNMEAGP PESGESTDAL
60 70 80 90 100
KLCPHEEFLR LCKERAEEIY PIKERNNRTR LALIICNTEF DHLPPRNGAD
110 120 130 140 150
FDITGMKELL EGLDYSVDVE ENLTARDMES ALRAFATRPE HKSSDSTFLV
160 170 180 190 200
LMSHGILEGI CGTVHDEKKP DVLLYDTIFQ IFNNRNCLSL KDKPKVIIVQ
210 220 230 240 250
ACRGANRGEL WVRDSPASLE VASSQSSENL EEDAVYKTHV EKDFIAFCSS
260 270 280 290 300
TPHNVSWRDS TMGSIFITQL ITCFQKYSWC CHLEEVFRKV QQSFETPRAK
310 320
AQMPTIERLS MTRYFYLFPG N
Length:321
Mass (Da):36,705
<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:i7336654FD603B65A
Isoform 3 (identifier: P49662-3) [UniParc]FASTAAdd to basketAdded to basket
Also known as: mih1-delta
The sequence of this isoform differs from the canonical sequence as follows:
88-116: AHPNMEAGPPESGESTDALKLCPHEEFLR → GDKLGHRGRNHNLCSAISCSSSEYGGWTT
117-377: Missing.
10 20 30 40 50
MAEGNHRKKP LKVLESLGKD FLTGVLDNLV EQNVLNWKEE EKKKYYDAKT
60 70 80 90 100
EDKVRVMADS MQEKQRMAGQ MLLQTFFNID QISPNKKGDK LGHRGRNHNL
110
CSAISCSSSE YGGWTT
Note: May be due to competing acceptor splice site. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.Curated
Show »Length:116
Mass (Da):13,264
<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:iFD9ED1FF1DF981D3
Isoform 4 (identifier: P49662-4) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
261-263: ANR → GEC
264-377: Missing.
10 20 30 40 50
MAEGNHRKKP LKVLESLGKD FLTGVLDNLV EQNVLNWKEE EKKKYYDAKT
60 70 80 90 100
EDKVRVMADS MQEKQRMAGQ MLLQTFFNID QISPNKKAHP NMEAGPPESG
110 120 130 140 150
ESTDALKLCP HEEFLRLCKE RAEEIYPIKE RNNRTRLALI ICNTEFDHLP
160 170 180 190 200
PRNGADFDIT GMKELLEGLD YSVDVEENLT ARDMESALRA FATRPEHKSS
210 220 230 240 250
DSTFLVLMSH GILEGICGTV HDEKKPDVLL YDTIFQIFNN RNCLSLKDKP
260
KVIIVQACRG GEC
Note: No experimental confirmation available.Curated
Show »Length:263
Mass (Da):30,000
<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:iFED10278B701F0F0
Isoform 5 (identifier: P49662-5) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
125-157: IYPIKERNNRTRLALIICNTEFDHLPPRNGADF → VLCYLYEIEKKEEISLLSFSAPFLTALNDWGWG
158-377: Missing.
10 20 30 40 50
MAEGNHRKKP LKVLESLGKD FLTGVLDNLV EQNVLNWKEE EKKKYYDAKT
60 70 80 90 100
EDKVRVMADS MQEKQRMAGQ MLLQTFFNID QISPNKKAHP NMEAGPPESG
110 120 130 140 150
ESTDALKLCP HEEFLRLCKE RAEEVLCYLY EIEKKEEISL LSFSAPFLTA
LNDWGWG
Note: No experimental confirmation available.Curated
Show »Length:157
Mass (Da):18,111
<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:i65936259DD31435E
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
Isoform 2 : The sequence AAC99851 differs from that shown. Reason: Frameshift at position 19.Combined sources
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
- Ref.18"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 2), CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
The sequence AAC99854 differs from that shown. Reason: Erroneous translation. Erroneous CDS prediction.Curated
The sequence EAW67050 differs from that shown. Reason: Erroneous gene model prediction.Curated
Natural variant
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_043495 | 1 – 56 | Missing in isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 56 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_058177 | 88 – 116 | AHPNM…EEFLR → GDKLGHRGRNHNLCSAISCS SSEYGGWTT in isoform 3. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 29 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_058178 | 117 – 377 | Missing in isoform 3. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 261 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_058179 | 125 – 157 | IYPIK…NGADF → VLCYLYEIEKKEEISLLSFS APFLTALNDWGWG in isoform 5. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 33 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_058180 | 158 – 377 | Missing in isoform 5. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 220 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_058181 | 261 – 263 | ANR → GEC in isoform 4. 2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 3 | |
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_058182 | 264 – 377 | Missing in isoform 4. 2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 114 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | Z48810 mRNA Translation: CAA88750.1 U28014 mRNA Translation: AAA75171.1 U25804 mRNA Translation: AAA86890.1 U28976 mRNA Translation: AAC99850.1 U28977 mRNA Translation: AAC99851.1 Frameshift. U28978 mRNA Translation: AAC99852.1 U28979 mRNA Translation: AAC99853.1 U28979 mRNA Translation: AAC99854.1 Sequence problems. AK057094 mRNA Translation: BAG51861.1 AK296081 mRNA Translation: BAG58837.1 AK304222 mRNA Translation: BAG65094.1 EF636667 Genomic DNA Translation: ABR09278.1 AP001153 Genomic DNA No translation available. AP002004 Genomic DNA No translation available. CH471065 Genomic DNA Translation: EAW67050.1 Sequence problems. CH471065 Genomic DNA Translation: EAW67051.1 CH471065 Genomic DNA Translation: EAW67052.1 BC017839 mRNA Translation: AAH17839.1 AL050391 mRNA Translation: CAB43686.2 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS41704.1 [P49662-2] CCDS8327.1 [P49662-1] |
Protein sequence database of the Protein Information Resource More...PIRi | A57511 |
NCBI Reference Sequences More...RefSeqi | NP_001216.1, NM_001225.3 [P49662-1] NP_150649.1, NM_033306.2 [P49662-2] XP_011541321.1, XM_011543019.1 XP_016873886.1, XM_017018397.1 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.138378 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000393150; ENSP00000376857; ENSG00000196954 [P49662-2] ENST00000444739; ENSP00000388566; ENSG00000196954 [P49662-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 837 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:837 |
UCSC genome browser More...UCSCi | uc001pib.2 human [P49662-1] |
<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>Keywords - Coding sequence diversityi
Alternative splicing, Polymorphism<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
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P49662 | UPI000011F191 | 286 | |||
| P49662-2 | 321 | ||||
| Caspase-4 (Fragment) | 147 |
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P49662 | UPI000011F191 | 286 | |||
| Caspase 4 | 377 | ||||
| Caspase 4 | 377 | ||||
| UPI0006C956BA | 377 | ||||
| UPI000C2B34B7 | 377 | ||||
| +31 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P49662 | UPI000011F191 | 286 | |||
| Caspase 4 | 377 | ||||
| UPI0006C956BA | 377 | ||||
| UPI000C2B34B7 | 377 | ||||
| Caspase 4 | 377 | ||||
| +60 | |||||
<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
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| NIEHS-SNPs |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | Z48810 mRNA Translation: CAA88750.1 U28014 mRNA Translation: AAA75171.1 U25804 mRNA Translation: AAA86890.1 U28976 mRNA Translation: AAC99850.1 U28977 mRNA Translation: AAC99851.1 Frameshift. U28978 mRNA Translation: AAC99852.1 U28979 mRNA Translation: AAC99853.1 U28979 mRNA Translation: AAC99854.1 Sequence problems. AK057094 mRNA Translation: BAG51861.1 AK296081 mRNA Translation: BAG58837.1 AK304222 mRNA Translation: BAG65094.1 EF636667 Genomic DNA Translation: ABR09278.1 AP001153 Genomic DNA No translation available. AP002004 Genomic DNA No translation available. CH471065 Genomic DNA Translation: EAW67050.1 Sequence problems. CH471065 Genomic DNA Translation: EAW67051.1 CH471065 Genomic DNA Translation: EAW67052.1 BC017839 mRNA Translation: AAH17839.1 AL050391 mRNA Translation: CAB43686.2 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS41704.1 [P49662-2] CCDS8327.1 [P49662-1] |
Protein sequence database of the Protein Information Resource More...PIRi | A57511 |
NCBI Reference Sequences More...RefSeqi | NP_001216.1, NM_001225.3 [P49662-1] NP_150649.1, NM_033306.2 [P49662-2] XP_011541321.1, XM_011543019.1 XP_016873886.1, XM_017018397.1 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.138378 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P49662 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P49662 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 107287, 34 interactors |
Database of interacting proteins More...DIPi | DIP-44806N |
Protein interaction database and analysis system More...IntActi | P49662, 41 interactors |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000388566 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P49662 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL2226 |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 1620 |
Protein family/group databases
MEROPS protease database More...MEROPSi | C14.007 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P49662 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P49662 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | CASP4 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 1352420 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P49662 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P49662 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P49662 |
PeptideAtlas More...PeptideAtlasi | P49662 |
PRoteomics IDEntifications database More...PRIDEi | P49662 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 56043 56044 [P49662-2] |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 837 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000393150; ENSP00000376857; ENSG00000196954 [P49662-2] ENST00000444739; ENSP00000388566; ENSG00000196954 [P49662-1] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 837 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:837 |
UCSC genome browser More...UCSCi | uc001pib.2 human [P49662-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 837 |
DisGeNET More...DisGeNETi | 837 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000196954.12 |
GeneCards: human genes, protein and diseases More...GeneCardsi | CASP4 |
Human Gene Nomenclature Database More...HGNCi | HGNC:1505 CASP4 |
Human Protein Atlas More...HPAi | CAB037167 HPA027588 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 602664 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P49662 |
Open Targets More...OpenTargetsi | ENSG00000196954 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA26088 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3573 Eukaryota ENOG410ZQIE LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00910000144131 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000234399 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG076981 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P49662 |
KEGG Orthology (KO) More...KOi | K04394 |
Identification of Orthologs from Complete Genome Data More...OMAi | FFNIDQI |
Database of Orthologous Groups More...OrthoDBi | EOG091G07NO |
Database for complete collections of gene phylogenies More...PhylomeDBi | P49662 |
TreeFam database of animal gene trees More...TreeFami | TF102023 |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.4.22.57 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-168638 NOD1/2 Signaling Pathway |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P49662 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | CASP4 human |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 837 |
Protein Ontology More...PROi | PR:P49662 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000196954 |
CleanEx database of gene expression profiles More...CleanExi | HS_CASP4 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P49662 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P49662 HS |
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 IPR001315 CARD IPR029030 Caspase-like_dom_sf IPR033139 Caspase_cys_AS IPR016129 Caspase_his_AS IPR011029 DEATH-like_dom_sf IPR002138 Pept_C14_p10 IPR001309 Pept_C14_p20 IPR015917 Pept_C14A |
Pfam protein domain database More...Pfami | View protein in Pfam PF00619 CARD, 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 SM00114 CARD, 1 hit SM00115 CASc, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF47986 SSF47986, 1 hit SSF52129 SSF52129, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50209 CARD, 1 hit PS01122 CASPASE_CYS, 1 hit PS01121 CASPASE_HIS, 1 hit PS50207 CASPASE_P10, 1 hit PS50208 CASPASE_P20, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | 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 namei | CASP4_HUMAN | |
| <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>Accessioni | P49662Primary (citable) accession number: P49662 Secondary accession number(s): A2NHL8 , A2NHL9, A2NHM0, B3KPZ9, B4DJH5, B4E2D2, O95601, Q7KYX7, Q9UG96 | |
| <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 historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1996 |
| Last sequence update: | February 1, 1996 | |
| Last modified: | July 18, 2018 | |
| This is version 182 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 statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<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
<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>Keywords - Technical termi
Complete proteome, Reference proteomeDocuments
- Human chromosome 11
Human chromosome 11: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - Peptidase families
Classification of peptidase families and list of entries - SIMILARITY comments
Index of protein domains and families
