Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P42574 (CASP3_HUMAN)

Protein

Caspase-3

Gene

CASP3

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>

<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

Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage.2 Publications

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

  • Strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position. EC:3.4.22.56

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by isatin sulfonamides.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei121By similarity1
Active sitei163By similarity1

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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the 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		3.4.22.56 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-111459 Activation of caspases through apoptosome-mediated cleavage
R-HSA-111463 SMAC binds to IAPs
R-HSA-111464 SMAC-mediated dissociation of IAP:caspase complexes
R-HSA-111465 Apoptotic cleavage of cellular proteins
R-HSA-1474228 Degradation of the extracellular matrix
R-HSA-2028269 Signaling by Hippo
R-HSA-205025 NADE modulates death signalling
R-HSA-211227 Activation of DNA fragmentation factor
R-HSA-211736 Stimulation of the cell death response by PAK-2p34
R-HSA-264870 Caspase-mediated cleavage of cytoskeletal proteins
R-HSA-351906 Apoptotic cleavage of cell adhesion proteins
R-HSA-418889 Caspase activation via Dependence Receptors in the absence of ligand
R-HSA-449836 Other interleukin signaling

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P42574

SIGNOR Signaling Network Open Resource

More...SIGNORi		P42574

Protein family/group databases

MEROPS protease database

More...MEROPSi		C14.003

<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-3 (EC:3.4.22.56)
Short name:
CASP-3
Alternative name(s):
Apopain
Cysteine protease CPP32
Short name:
CPP-32
Protein Yama
SREBP cleavage activity 1
Short name:
SCA-1
Cleaved into the following 2 chains:
Caspase-3 subunit p17
Caspase-3 subunit p12
<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:CASP3
Synonyms:CPP32
<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>OrganismiHomo 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 identifieri9606 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000164305.17

Human Gene Nomenclature Database

More...HGNCi		HGNC:1504 CASP3

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		600636 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P42574

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<p>This section 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

Organism-specific databases

DisGeNET

More...DisGeNETi		836

Open Targets

More...OpenTargetsi		ENSG00000164305

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA26087

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2334

Drug and drug target database

More...DrugBanki		DB06862 2-HYDROXY-5-(2-MERCAPTO-ETHYLSULFAMOYL)-BENZOIC ACID
DB08251 4-[5-(2-CARBOXY-1-FORMYL-ETHYLCARBAMOYL)-PYRIDIN-3-YL]-BENZOIC ACID
DB03124 5-[4-(1-Carboxymethyl-2-Oxo-Propylcarbamoyl)-Benzylsulfamoyl]-2-Hydroxy-Benzoic Acid
DB08229 [N-(3-DIBENZYLCARBAMOYL-OXIRANECARBONYL)-HYDRAZINO]-ACETIC ACID
DB05408 IDN-6556
DB07696 methyl (3S)-3-[(tert-butoxycarbonyl)amino]-4-oxopentanoate
DB01017 Minocycline

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		1619

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		CASP3

Domain mapping of disease mutations (DMDM)

More...DMDMi		77416852

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_00000045691 – 99
PropeptideiPRO_000000457010 – 281 PublicationAdd BLAST19
<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_000000457129 – 175Caspase-3 subunit p17Add BLAST147
ChainiPRO_0000004572176 – 277Caspase-3 subunit p12Add BLAST102

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 residuei1N-acetylmethionineCombined sources1
Modified residuei11N6-acetyllysineBy similarity1
Modified residuei26PhosphoserineCombined sources1
Modified residuei163S-nitrosocysteine; in inhibited form1 Publication1

<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

Cleavage by granzyme B, caspase-6, caspase-8 and caspase-10 generates the two active subunits. Additional processing of the propeptides is likely due to the autocatalytic activity of the activated protease. Active heterodimers between the small subunit of caspase-7 protease and the large subunit of caspase-3 also occur and vice versa.
S-nitrosylated on its catalytic site cysteine in unstimulated human cell lines and denitrosylated upon activation of the Fas apoptotic pathway, associated with an increase in intracellular caspase activity. Fas therefore activates caspase-3 not only by inducing the cleavage of the caspase zymogen to its active subunits, but also by stimulating the denitrosylation of its active site thiol.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation, Zymogen

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P42574

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P42574

MaxQB - The MaxQuant DataBase

More...MaxQBi		P42574

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

More...PaxDbi		P42574

PeptideAtlas

More...PeptideAtlasi		P42574

PRoteomics IDEntifications database

More...PRIDEi		P42574

ProteomicsDB human proteome resource

More...ProteomicsDBi		55518

2D gel databases

USC-OGP 2-DE database

More...OGPi		P42574

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P42574

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

More...PhosphoSitePlusi		P42574

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		P42574

<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, spleen, heart, liver and kidney. Moderate levels in brain and skeletal muscle, and low in testis. Also found in many cell lines, highest expression in cells of the immune system.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000164305 Expressed in 194 organ(s), highest expression level in jejunal mucosa

CleanEx database of gene expression profiles

More...CleanExi		HS_CASP3

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P42574 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P42574 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB000091
CAB008381
HPA002643

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

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

Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 17 kDa (p17) and a 12 kDa (p12) subunit. Interacts with BIRC6/bruce.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		107286, 102 interactors

Database of interacting proteins

More...DIPi		DIP-268N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P42574

Protein interaction database and analysis system

More...IntActi		P42574, 54 interactors

Molecular INTeraction database

More...MINTi		P42574

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000311032

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P42574

<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

Secondary structure

1277
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CP3X-ray2.30A/B1-277[»]
1GFWX-ray2.80A29-175[»]
B181-277[»]
1I3OX-ray2.70A/C1-175[»]
B/D176-277[»]
1NMEX-ray1.60A29-174[»]
B186-277[»]
1NMQX-ray2.40A/B29-277[»]
1NMSX-ray1.70A/B29-277[»]
1PAUX-ray2.50A29-175[»]
B176-277[»]
1QX3X-ray1.90A29-277[»]
1RE1X-ray2.50A29-175[»]
B176-277[»]
1RHJX-ray2.20A/C29-175[»]
B/D176-277[»]
1RHKX-ray2.50A29-175[»]
B176-277[»]
1RHMX-ray2.50A/C29-175[»]
B/D176-277[»]
1RHQX-ray3.00A/D29-175[»]
B/E176-277[»]
1RHRX-ray3.00A29-175[»]
B176-277[»]
1RHUX-ray2.51A29-175[»]
B176-277[»]
2C1EX-ray1.77A29-175[»]
B176-277[»]
2C2KX-ray1.87A29-175[»]
B176-277[»]
2C2MX-ray1.94A29-175[»]
B176-277[»]
2C2OX-ray2.45A29-175[»]
B176-277[»]
2CDRX-ray1.70A29-175[»]
B176-277[»]
2CJXX-ray1.70A29-175[»]
B176-277[»]
2CJYX-ray1.67A29-175[»]
B176-277[»]
2CNKX-ray1.75A29-175[»]
B176-277[»]
2CNLX-ray1.67A29-175[»]
B176-277[»]
2CNNX-ray1.70A29-175[»]
B176-277[»]
2CNOX-ray1.95A29-175[»]
B176-277[»]
2DKOX-ray1.06A29-174[»]
B175-277[»]
2H5IX-ray1.69A29-174[»]
B184-277[»]
2H5JX-ray2.00A/C29-174[»]
B/D184-277[»]
2H65X-ray2.30A/C29-174[»]
B/D184-277[»]
2J30X-ray1.40A29-277[»]
2J31X-ray1.50A29-277[»]
2J32X-ray1.30A29-277[»]
2J33X-ray2.00A29-277[»]
2XYGX-ray1.54A29-174[»]
B185-277[»]
2XYHX-ray1.89A29-174[»]
B185-277[»]
2XYPX-ray1.86A29-174[»]
B185-277[»]
2XZDX-ray2.10A/C27-175[»]
B/D176-277[»]
2XZTX-ray2.70A/C29-175[»]
B/D176-277[»]
2Y0BX-ray2.10A/C29-175[»]
B/D176-277[»]
3DEHX-ray2.50A/B/C/D29-277[»]
3DEIX-ray2.80A/B/C/D29-277[»]
3DEJX-ray2.60A/B/C/D29-277[»]
3DEKX-ray2.40A/B/C/D29-277[»]
3EDQX-ray1.61A/C29-175[»]
B/D176-277[»]
3GJQX-ray2.60A/C29-175[»]
B/D176-277[»]
3GJRX-ray2.20A/C29-175[»]
B/D176-277[»]
3GJSX-ray1.90A/C29-175[»]
B/D176-277[»]
3GJTX-ray2.20A/C29-175[»]
B/D176-277[»]
3H0EX-ray2.00A/B29-277[»]
3ITNX-ray1.63A29-277[»]
3KJFX-ray2.00A29-175[»]
B176-277[»]
3PCXX-ray1.50A29-277[»]
3PD0X-ray2.00A29-277[»]
3PD1X-ray1.62A29-277[»]
4DCJX-ray1.70A/D29-175[»]
B/E176-277[»]
4DCOX-ray1.70A/D29-175[»]
B/E176-277[»]
4DCPX-ray1.70A/D29-175[»]
B/E176-277[»]
4EHAX-ray1.70A/C1-277[»]
4EHDX-ray1.58A1-277[»]
4EHFX-ray1.66A1-277[»]
4EHHX-ray1.78A1-277[»]
4EHKX-ray1.67A/C1-277[»]
4EHLX-ray1.80A/C1-277[»]
4EHNX-ray1.69A1-277[»]
4JJEX-ray1.48A29-277[»]
4JQYX-ray2.50A/B34-277[»]
4JQZX-ray2.89A/B34-277[»]
4JR0X-ray1.80A/B34-277[»]
4PRYX-ray1.70A1-277[»]
4PS0X-ray1.63A/B1-277[»]
4QTXX-ray1.97A1-277[»]
4QTYX-ray1.60A29-277[»]
4QU0X-ray1.95A1-277[»]
4QU5X-ray1.91A1-277[»]
4QU8X-ray1.72A1-277[»]
4QU9X-ray1.56A1-277[»]
4QUAX-ray1.89A1-277[»]
4QUBX-ray1.69A1-277[»]
4QUDX-ray2.00A/B1-277[»]
4QUEX-ray1.84A/C1-277[»]
4QUGX-ray1.92A/C1-277[»]
4QUHX-ray1.76A/C1-277[»]
4QUIX-ray1.76A/B1-277[»]
4QUJX-ray1.50A1-277[»]
4QULX-ray1.90A/C1-277[»]
5I9BX-ray1.80A1-277[»]
5I9TX-ray1.95A/C1-277[»]
5IABX-ray1.79A/C1-277[»]
5IAEX-ray1.55A/C1-277[»]
5IAGX-ray1.98A1-277[»]
5IAJX-ray1.58A1-277[»]
5IAKX-ray1.82A1-277[»]
5IANX-ray2.70A1-277[»]
5IARX-ray1.76A1-277[»]
5IASX-ray1.54A1-277[»]
5IBCX-ray1.66A1-277[»]
5IBPX-ray1.38A1-277[»]
5IBRX-ray1.74A/C1-277[»]
5IC4X-ray2.65A/C/E/G1-175[»]
B/D/F/H176-276[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P42574

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

More...SMRi		P42574

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P42574

<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

<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		ENSGT00940000153232

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000231878

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG050802

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P42574

KEGG Orthology (KO)

More...KOi		K02187

Identification of Orthologs from Complete Genome Data

More...OMAi		SAFHAKK

Database of Orthologous Groups

More...OrthoDBi		984395at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P42574

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
IPR015471 Casp3/7
IPR029030 Caspase-like_dom_sf
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:SF31 PTHR10454:SF31, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P42574-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MENTENSVDS KSIKNLEPKI IHGSESMDSG ISLDNSYKMD YPEMGLCIII 
        60         70         80         90        100
NNKNFHKSTG MTSRSGTDVD AANLRETFRN LKYEVRNKND LTREEIVELM 
       110        120        130        140        150
RDVSKEDHSK RSSFVCVLLS HGEEGIIFGT NGPVDLKKIT NFFRGDRCRS 
       160        170        180        190        200
LTGKPKLFII QACRGTELDC GIETDSGVDD DMACHKIPVE ADFLYAYSTA 
       210        220        230        240        250
PGYYSWRNSK DGSWFIQSLC AMLKQYADKL EFMHILTRVN RKVATEFESF 
       260        270 
SFDATFHAKK QIPCIVSMLT KELYFYH
Length:277
Mass (Da):31,608
Last modified:October 11, 2005 - v2
<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:i2F35CD3BCF7FF64A
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A8MVM1A8MVM1_HUMAN
Caspase-3
CASP3
182Annotation score:

Annotation score:1 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>
C9JXR7C9JXR7_HUMAN
Caspase-3
CASP3
117Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti31 – 36ISLDNS → MSWDTG in CAC88866 (PubMed:15003516).Curated6

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_04861622H → R. Corresponds to variant dbSNP:rs35578277Ensembl.1
Natural variantiVAR_001401190E → D3 PublicationsCorresponds to variant dbSNP:rs1049210Ensembl.1

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
U13737 mRNA Translation: AAA65015.1
U13738 mRNA Translation: AAB60355.1
U26943 mRNA Translation: AAA74929.1
AJ413269 mRNA Translation: CAC88866.1
AK291337 mRNA Translation: BAF84026.1
AY219866 Genomic DNA Translation: AAO25654.1
CH471056 Genomic DNA Translation: EAX04673.1
CH471056 Genomic DNA Translation: EAX04674.1
CH471056 Genomic DNA Translation: EAX04675.1
BC016926 mRNA Translation: AAH16926.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS3836.1

Protein sequence database of the Protein Information Resource

More...PIRi		A55315

NCBI Reference Sequences

More...RefSeqi		NP_004337.2, NM_004346.3
NP_116786.1, NM_032991.2
XP_011530603.1, XM_011532301.1

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.141125

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000308394; ENSP00000311032; ENSG00000164305
ENST00000523916; ENSP00000428929; ENSG00000164305

Database of genes from NCBI RefSeq genomes

More...GeneIDi		836

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:836

UCSC genome browser

More...UCSCi		uc003iwh.3 human

Keywords - Coding sequence diversityi

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

<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:
EMBLi
GenBanki
DDBJi
Links Updated
U13737 mRNA Translation: AAA65015.1
U13738 mRNA Translation: AAB60355.1
U26943 mRNA Translation: AAA74929.1
AJ413269 mRNA Translation: CAC88866.1
AK291337 mRNA Translation: BAF84026.1
AY219866 Genomic DNA Translation: AAO25654.1
CH471056 Genomic DNA Translation: EAX04673.1
CH471056 Genomic DNA Translation: EAX04674.1
CH471056 Genomic DNA Translation: EAX04675.1
BC016926 mRNA Translation: AAH16926.1
CCDSiCCDS3836.1
PIRiA55315
RefSeqiNP_004337.2, NM_004346.3
NP_116786.1, NM_032991.2
XP_011530603.1, XM_011532301.1
UniGeneiHs.141125

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CP3X-ray2.30A/B1-277[»]
1GFWX-ray2.80A29-175[»]
B181-277[»]
1I3OX-ray2.70A/C1-175[»]
B/D176-277[»]
1NMEX-ray1.60A29-174[»]
B186-277[»]
1NMQX-ray2.40A/B29-277[»]
1NMSX-ray1.70A/B29-277[»]
1PAUX-ray2.50A29-175[»]
B176-277[»]
1QX3X-ray1.90A29-277[»]
1RE1X-ray2.50A29-175[»]
B176-277[»]
1RHJX-ray2.20A/C29-175[»]
B/D176-277[»]
1RHKX-ray2.50A29-175[»]
B176-277[»]
1RHMX-ray2.50A/C29-175[»]
B/D176-277[»]
1RHQX-ray3.00A/D29-175[»]
B/E176-277[»]
1RHRX-ray3.00A29-175[»]
B176-277[»]
1RHUX-ray2.51A29-175[»]
B176-277[»]
2C1EX-ray1.77A29-175[»]
B176-277[»]
2C2KX-ray1.87A29-175[»]
B176-277[»]
2C2MX-ray1.94A29-175[»]
B176-277[»]
2C2OX-ray2.45A29-175[»]
B176-277[»]
2CDRX-ray1.70A29-175[»]
B176-277[»]
2CJXX-ray1.70A29-175[»]
B176-277[»]
2CJYX-ray1.67A29-175[»]
B176-277[»]
2CNKX-ray1.75A29-175[»]
B176-277[»]
2CNLX-ray1.67A29-175[»]
B176-277[»]
2CNNX-ray1.70A29-175[»]
B176-277[»]
2CNOX-ray1.95A29-175[»]
B176-277[»]
2DKOX-ray1.06A29-174[»]
B175-277[»]
2H5IX-ray1.69A29-174[»]
B184-277[»]
2H5JX-ray2.00A/C29-174[»]
B/D184-277[»]
2H65X-ray2.30A/C29-174[»]
B/D184-277[»]
2J30X-ray1.40A29-277[»]
2J31X-ray1.50A29-277[»]
2J32X-ray1.30A29-277[»]
2J33X-ray2.00A29-277[»]
2XYGX-ray1.54A29-174[»]
B185-277[»]
2XYHX-ray1.89A29-174[»]
B185-277[»]
2XYPX-ray1.86A29-174[»]
B185-277[»]
2XZDX-ray2.10A/C27-175[»]
B/D176-277[»]
2XZTX-ray2.70A/C29-175[»]
B/D176-277[»]
2Y0BX-ray2.10A/C29-175[»]
B/D176-277[»]
3DEHX-ray2.50A/B/C/D29-277[»]
3DEIX-ray2.80A/B/C/D29-277[»]
3DEJX-ray2.60A/B/C/D29-277[»]
3DEKX-ray2.40A/B/C/D29-277[»]
3EDQX-ray1.61A/C29-175[»]
B/D176-277[»]
3GJQX-ray2.60A/C29-175[»]
B/D176-277[»]
3GJRX-ray2.20A/C29-175[»]
B/D176-277[»]
3GJSX-ray1.90A/C29-175[»]
B/D176-277[»]
3GJTX-ray2.20A/C29-175[»]
B/D176-277[»]
3H0EX-ray2.00A/B29-277[»]
3ITNX-ray1.63A29-277[»]
3KJFX-ray2.00A29-175[»]
B176-277[»]
3PCXX-ray1.50A29-277[»]
3PD0X-ray2.00A29-277[»]
3PD1X-ray1.62A29-277[»]
4DCJX-ray1.70A/D29-175[»]
B/E176-277[»]
4DCOX-ray1.70A/D29-175[»]
B/E176-277[»]
4DCPX-ray1.70A/D29-175[»]
B/E176-277[»]
4EHAX-ray1.70A/C1-277[»]
4EHDX-ray1.58A1-277[»]
4EHFX-ray1.66A1-277[»]
4EHHX-ray1.78A1-277[»]
4EHKX-ray1.67A/C1-277[»]
4EHLX-ray1.80A/C1-277[»]
4EHNX-ray1.69A1-277[»]
4JJEX-ray1.48A29-277[»]
4JQYX-ray2.50A/B34-277[»]
4JQZX-ray2.89A/B34-277[»]
4JR0X-ray1.80A/B34-277[»]
4PRYX-ray1.70A1-277[»]
4PS0X-ray1.63A/B1-277[»]
4QTXX-ray1.97A1-277[»]
4QTYX-ray1.60A29-277[»]
4QU0X-ray1.95A1-277[»]
4QU5X-ray1.91A1-277[»]
4QU8X-ray1.72A1-277[»]
4QU9X-ray1.56A1-277[»]
4QUAX-ray1.89A1-277[»]
4QUBX-ray1.69A1-277[»]
4QUDX-ray2.00A/B1-277[»]
4QUEX-ray1.84A/C1-277[»]
4QUGX-ray1.92A/C1-277[»]
4QUHX-ray1.76A/C1-277[»]
4QUIX-ray1.76A/B1-277[»]
4QUJX-ray1.50A1-277[»]
4QULX-ray1.90A/C1-277[»]
5I9BX-ray1.80A1-277[»]
5I9TX-ray1.95A/C1-277[»]
5IABX-ray1.79A/C1-277[»]
5IAEX-ray1.55A/C1-277[»]
5IAGX-ray1.98A1-277[»]
5IAJX-ray1.58A1-277[»]
5IAKX-ray1.82A1-277[»]
5IANX-ray2.70A1-277[»]
5IARX-ray1.76A1-277[»]
5IASX-ray1.54A1-277[»]
5IBCX-ray1.66A1-277[»]
5IBPX-ray1.38A1-277[»]
5IBRX-ray1.74A/C1-277[»]
5IC4X-ray2.65A/C/E/G1-175[»]
B/D/F/H176-276[»]
ProteinModelPortaliP42574
SMRiP42574
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107286, 102 interactors
DIPiDIP-268N
ELMiP42574
IntActiP42574, 54 interactors
MINTiP42574
STRINGi9606.ENSP00000311032

Chemistry databases

BindingDBiP42574
ChEMBLiCHEMBL2334
DrugBankiDB06862 2-HYDROXY-5-(2-MERCAPTO-ETHYLSULFAMOYL)-BENZOIC ACID
DB08251 4-[5-(2-CARBOXY-1-FORMYL-ETHYLCARBAMOYL)-PYRIDIN-3-YL]-BENZOIC ACID
DB03124 5-[4-(1-Carboxymethyl-2-Oxo-Propylcarbamoyl)-Benzylsulfamoyl]-2-Hydroxy-Benzoic Acid
DB08229 [N-(3-DIBENZYLCARBAMOYL-OXIRANECARBONYL)-HYDRAZINO]-ACETIC ACID
DB05408 IDN-6556
DB07696 methyl (3S)-3-[(tert-butoxycarbonyl)amino]-4-oxopentanoate
DB01017 Minocycline
GuidetoPHARMACOLOGYi1619

Protein family/group databases

MEROPSiC14.003

PTM databases

iPTMnetiP42574
PhosphoSitePlusiP42574

Polymorphism and mutation databases

BioMutaiCASP3
DMDMi77416852

2D gel databases

OGPiP42574

Proteomic databases

EPDiP42574
jPOSTiP42574
MaxQBiP42574
PaxDbiP42574
PeptideAtlasiP42574
PRIDEiP42574
ProteomicsDBi55518

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		836
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000308394; ENSP00000311032; ENSG00000164305
ENST00000523916; ENSP00000428929; ENSG00000164305
GeneIDi836
KEGGihsa:836
UCSCiuc003iwh.3 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		836
DisGeNETi836
EuPathDBiHostDB:ENSG00000164305.17

GeneCards: human genes, protein and diseases

More...GeneCardsi		CASP3
HGNCiHGNC:1504 CASP3
HPAiCAB000091
CAB008381
HPA002643
MIMi600636 gene
neXtProtiNX_P42574
OpenTargetsiENSG00000164305
PharmGKBiPA26087

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3573 Eukaryota
ENOG410ZQIE LUCA
GeneTreeiENSGT00940000153232
HOGENOMiHOG000231878
HOVERGENiHBG050802
InParanoidiP42574
KOiK02187
OMAiSAFHAKK
OrthoDBi984395at2759
PhylomeDBiP42574
TreeFamiTF102023

Enzyme and pathway databases

BRENDAi3.4.22.56 2681
ReactomeiR-HSA-111459 Activation of caspases through apoptosome-mediated cleavage
R-HSA-111463 SMAC binds to IAPs
R-HSA-111464 SMAC-mediated dissociation of IAP:caspase complexes
R-HSA-111465 Apoptotic cleavage of cellular proteins
R-HSA-1474228 Degradation of the extracellular matrix
R-HSA-2028269 Signaling by Hippo
R-HSA-205025 NADE modulates death signalling
R-HSA-211227 Activation of DNA fragmentation factor
R-HSA-211736 Stimulation of the cell death response by PAK-2p34
R-HSA-264870 Caspase-mediated cleavage of cytoskeletal proteins
R-HSA-351906 Apoptotic cleavage of cell adhesion proteins
R-HSA-418889 Caspase activation via Dependence Receptors in the absence of ligand
R-HSA-449836 Other interleukin signaling
SABIO-RKiP42574
SIGNORiP42574

Miscellaneous databases

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

More...ChiTaRSi		CASP3 human
EvolutionaryTraceiP42574

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Caspase_3

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		836
PMAP-CutDBiP42574

Protein Ontology

More...PROi		PR:P42574

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000164305 Expressed in 194 organ(s), highest expression level in jejunal mucosa
CleanExiHS_CASP3
ExpressionAtlasiP42574 baseline and differential
GenevisibleiP42574 HS

Family and domain databases

CDDicd00032 CASc, 1 hit
InterProiView protein in InterPro
IPR015471 Casp3/7
IPR029030 Caspase-like_dom_sf
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:SF31 PTHR10454:SF31, 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

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 nameiCASP3_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>AccessioniPrimary (citable) accession number: P42574
Secondary accession number(s): A8K5M2
, D3DP53, Q96AN1, Q96KP2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: October 11, 2005
Last modified: January 16, 2019
This is version 218 of the entry and version 2 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
DisclaimerAny 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again