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Entry version 158 (08 May 2019)
Sequence version 2 (29 Mar 2005)
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Protein

Cell death protein 4

Gene

ced-4

Organism
Caenorhabditis elegans
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

Component of the egl-1, ced-9, ced-4 and ced-3 apoptotic signaling cascade required for the initiation of programmed cell death in cells fated to die during embryonic and postembryonic development (PubMed:3955651). During oogenesis, required for germline apoptosis downstream of ced-9 and upstream of ced-3 but independently of egl-1 (PubMed:9927601). May regulate germline apoptosis in response to DNA damage, probably downstream of let-60/ras and mpk-1 pathway (PubMed:21901106). Regulates CEP neuron apoptosis in response to high Al3+ levels (PubMed:23106139). During male tail morphogenesis, promotes apoptosis of the tail-spike cell upstream of ced-3 but independently of egl-1 and ced-9 (PubMed:17329362). May play a role in sex-specific cell apoptosis, probably by promoting ced-3-mediated cleavage of sex-determining protein fem-1 (PubMed:10764728). During larval development, required for the elimination of transient presynaptic components downstream of egl-1 and ced-9 and upstream of ced-3 apoptotic pathway (PubMed:26074078). Downstream of calreticulin crt-1 and upstream of ced-3 and independently of egl-1 and ced-9, plays a role in the initial steps of axonal regrowth following axotomy (PubMed:22629231). Together with ain-1, a component of the miRNA-induced-silencing complex (miRISC), and probably upstream of ced-3, regulates temporal cell fate patterning during larval development (PubMed:25432023). May play a role in resistance to S.typhimurium-mediated infection (PubMed:11226309).10 Publications
Isoform a: Plays a major role in programmed cell death (PubMed:1286611, PubMed:8706125). egl-1 binds to and directly inhibits the activity of ced-9, releasing the cell death activator ced-4 from a ced-9/ced-4 containing protein complex and allowing ced-4 to induce caspase ced-3 autoproteolytic cleavage and activation (PubMed:15383288, PubMed:16208361, PubMed:20434985, PubMed:24065769). Also forms a holoenzyme with processed ced-3 enhancing ced-3 activity (PubMed:20434985).7 Publications
Isoform b: Prevents programmed cell death.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei131ATP; via carbonyl oxygenCombined sources3 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi166Magnesium2 Publications1
Binding sitei171ATPCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi162 – 167ATPCombined sources3 Publications6

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

GO - Biological processi

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

Biological processApoptosis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

<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:
Cell death protein 4
<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:ced-4
ORF Names:C35D10.9
<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>OrganismiCaenorhabditis elegans
<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 identifieri6239 [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 lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditinaRhabditomorphaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
<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
  • UP000001940 <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 III

Organism-specific databases

WormBase

More...
WormBasei
C35D10.9a ; CE01203 ; WBGene00000418 ; ced-4
C35D10.9b ; CE38154 ; WBGene00000418 ; ced-4

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

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

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

Mutants exhibit a block in almost all programmed cell deaths that normally occur during development (PubMed:1286611). RNAi-mediated knockdown causes a defect in egg laying in a small proportion of animals (PubMed:25432023). Also causes a moderate increase in CEP neuron survival in response to high Al3+ levels (PubMed:23106139). In an ain-1 mutant background, enhances the proportion of animals arrested at the larval stage, with egg-laying defects and with a ruptured vulva (PubMed:25432023).3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Mutagenesisi252V → D: Loss of dimerization without affecting interaction with ced-9, loss of ced-3 activation and severe reduction in the number of cell corpses in embryos in a ced-1 mutant background; when associated with E-255 and E-256. 1 Publication1
Mutagenesisi255R → E: Severe reduction in the number of cell corpses in embryos in a ced-1 mutant background. Loss of dimerization without affecting interaction with ced-9, loss of ced-3 activation and severe reduction in the number of cell corpses in embryos in a ced-1 mutant background; when associated with E-252 and E-256. 1 Publication1
Mutagenesisi256M → E: Loss of dimerization without affecting interaction with ced-9, loss of ced-3 activation and severe reduction in the number of cell corpses in embryos in a ced-1 mutant background; when associated with E-252 and E-255. 1 Publication1
Mutagenesisi272 – 273DD → AA: Severe reduction in the number of cell corpses in embryos in a ced-1 mutant background. 1 Publication2
Mutagenesisi280I → N in n1948; no effect on the interaction with mac-1. 1 Publication1
Mutagenesisi416A → W: Reduced interaction with ced-3. 1 Publication1

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘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_00000894701 – 571Cell death protein 4Add BLAST571

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P30429

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

More...
PaxDbi
P30429

PeptideAtlas

More...
PeptideAtlasi
P30429

PRoteomics IDEntifications database

More...
PRIDEi
P30429

<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 the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Abundantly expressed during embryogenesis and to a lesser extent in larvae and adults (PubMed:1286611). Expression starts at the 100-cell stage and persists through embryogenesis (at protein level) (PubMed:9027313). Not expressed in larvae and adults (at protein level) (PubMed:9027313).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
WBGene00000418 Expressed in 5 organ(s), highest expression level in germ line (C elegans)

<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

Associates as an asymmetric homodimer with ced-9 (PubMed:16208361, PubMed:9027313, PubMed:15383288). Upon release from ced-9, forms an octamer, known as the apoptosome, and interacts with ced-3; the interaction results in ced-3 autoproteolytic cleavage and activation (PubMed:20434985, PubMed:24065769). The octamer (a tetramer of an asymmetric dimer) also interacts with two processed ced-3 to form a stable holoenzyme (PubMed:20434985).

Interacts with sex-determining protein fem-1 (PubMed:10764728). May form a complex composed of ced-3, ced-4 and mac-1 or of ced-9, ced-4 and mac-1 (PubMed:10101135). Within the complex, interacts with ced-4 (PubMed:10101135).

7 Publications

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
40877, 5 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1358 ced-3-ced-4-mac-1 complex
CPX-1359 ced-4-ced-9-mac-1 complex
CPX-1360 ced-3-ced-4 caspase complex
CPX-399 ced-9-ced-4 complex

Database of interacting proteins

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DIPi
DIP-1016N

Protein interaction database and analysis system

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IntActi
P30429, 7 interactors

STRING: functional protein association networks

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STRINGi
6239.C35D10.9b

<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

1571
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
P30429

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P30429

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 91CARDPROSITE-ProRule annotationAdd BLAST91
Domaini133 – 439NB-ARCSequence analysisAdd BLAST307

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG4658 Eukaryota
COG4886 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000111533

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P30429

KEGG Orthology (KO)

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KOi
K20105

Identification of Orthologs from Complete Genome Data

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OMAi
AIMESYK

Database of Orthologous Groups

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OrthoDBi
1576724at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P30429

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016854 Apop_reg_Ced-4
IPR001315 CARD
IPR011029 DEATH-like_dom_sf
IPR002182 NB-ARC
IPR027417 P-loop_NTPase
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00619 CARD, 1 hit
PF00931 NB-ARC, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF027202 Apop_reg_Ced-4, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00114 CARD, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF46785 SSF46785, 1 hit
SSF47986 SSF47986, 1 hit
SSF52540 SSF52540, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50209 CARD, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)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.

This entry describes 2 <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 basket
Isoform b (identifier: P30429-1) [UniParc]FASTAAdd to basket
Also known as: Long

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MLCEIECRAL STAHTRLIHD FEPRDALTYL EGKNIFTEDH SELISKMSTR
60 70 80 90 100
LERIANFLRI YRRQASELGP LIDFFNYNNQ SHLADFLEDY IDFAINEPDL
110 120 130 140 150
LRPVVIAPQF SRQMLDRKLL LGNVPKQMTC YIREYHVDRV IKKLDEMCDL
160 170 180 190 200
DSFFLFLHGR AGSGKSVIAS QALSKSDQLI GINYDSIVWL KDSGTAPKST
210 220 230 240 250
FDLFTDILLM LARVVSDTDD SHSITDFINR VLSRSEDDLL NFPSVEHVTS
260 270 280 290 300
VVLKRMICNA LIDRPNTLFV FDDVVQEETI RWAQELRLRC LVTTRDVEIS
310 320 330 340 350
NAASQTCEFI EVTSLEIDEC YDFLEAYGMP MPVGEKEEDV LNKTIELSSG
360 370 380 390 400
NPATLMMFFK SCEPKTFEKM AQLNNKLESR GLVGVECITP YSYKSLAMAL
410 420 430 440 450
QRCVEVLSDE DRSALAFAVV MPPGVDIPVK LWSCVIPVDI CSNEEEQLDD
460 470 480 490 500
EVADRLKRLS KRGALLSGKR MPVLTFKIDH IIHMFLKHVV DAQTIANGIS
510 520 530 540 550
ILEQRLLEIG NNNVSVPERH IPSHFQKFRR SSASEMYPKT TEETVIRPED
560 570
FPKFMQLHQK FYDSLKNFAC C
Note: Minor transcript.
Length:571
Mass (Da):65,336
Last modified:March 29, 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:i6BE9893946B79E6C
GO
Isoform a (identifier: P30429-2) [UniParc]FASTAAdd to basket
Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     212-234: ARVVSDTDDSHSITDFINRVLSR → K

Note: Major transcript.
Show »
Length:549
Mass (Da):62,878
Checksum:iDB2A7969BDA50AF8
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_013199212 – 234ARVVS…RVLSR → K in isoform a. CuratedAdd BLAST23

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X69016 Genomic DNA Translation: CAA48781.1
FO080789 Genomic DNA Translation: CCD66781.1
FO080789 Genomic DNA Translation: CCD66782.1

Protein sequence database of the Protein Information Resource

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PIRi
S72566

NCBI Reference Sequences

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RefSeqi
NP_001021202.1, NM_001026031.2 [P30429-2]
NP_001021203.1, NM_001026032.1 [P30429-1]

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
C35D10.9a.1; C35D10.9a.1; WBGene00000418 [P30429-2]
C35D10.9a.2; C35D10.9a.2; WBGene00000418 [P30429-2]
C35D10.9b.1; C35D10.9b.1; WBGene00000418 [P30429-1]
C35D10.9b.2; C35D10.9b.2; WBGene00000418 [P30429-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
175643

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
cel:CELE_C35D10.9

UCSC genome browser

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UCSCi
C35D10.9b c. elegans [P30429-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69016 Genomic DNA Translation: CAA48781.1
FO080789 Genomic DNA Translation: CCD66781.1
FO080789 Genomic DNA Translation: CCD66782.1
PIRiS72566
RefSeqiNP_001021202.1, NM_001026031.2 [P30429-2]
NP_001021203.1, NM_001026032.1 [P30429-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2A5YX-ray2.60B/C1-571[»]
3LQQX-ray3.53A/B1-571[»]
3LQRX-ray3.90A/B1-571[»]
4M9SX-ray3.21A/B/C/D1-571[»]
4M9XX-ray3.34A/B1-571[»]
4M9YX-ray4.20A/B1-571[»]
4M9ZX-ray3.40A/B/C/D1-571[»]
SMRiP30429
ModBaseiSearch...

Protein-protein interaction databases

BioGridi40877, 5 interactors
ComplexPortaliCPX-1358 ced-3-ced-4-mac-1 complex
CPX-1359 ced-4-ced-9-mac-1 complex
CPX-1360 ced-3-ced-4 caspase complex
CPX-399 ced-9-ced-4 complex
DIPiDIP-1016N
IntActiP30429, 7 interactors
STRINGi6239.C35D10.9b

Proteomic databases

EPDiP30429
PaxDbiP30429
PeptideAtlasiP30429
PRIDEiP30429

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiC35D10.9a.1; C35D10.9a.1; WBGene00000418 [P30429-2]
C35D10.9a.2; C35D10.9a.2; WBGene00000418 [P30429-2]
C35D10.9b.1; C35D10.9b.1; WBGene00000418 [P30429-1]
C35D10.9b.2; C35D10.9b.2; WBGene00000418 [P30429-1]
GeneIDi175643
KEGGicel:CELE_C35D10.9
UCSCiC35D10.9b c. elegans [P30429-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
175643
WormBaseiC35D10.9a ; CE01203 ; WBGene00000418 ; ced-4
C35D10.9b ; CE38154 ; WBGene00000418 ; ced-4

Phylogenomic databases

eggNOGiKOG4658 Eukaryota
COG4886 LUCA
HOGENOMiHOG000111533
InParanoidiP30429
KOiK20105
OMAiAIMESYK
OrthoDBi1576724at2759
PhylomeDBiP30429

Miscellaneous databases

EvolutionaryTraceiP30429

Protein Ontology

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PROi
PR:P30429

Gene expression databases

BgeeiWBGene00000418 Expressed in 5 organ(s), highest expression level in germ line (C elegans)

Family and domain databases

Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR016854 Apop_reg_Ced-4
IPR001315 CARD
IPR011029 DEATH-like_dom_sf
IPR002182 NB-ARC
IPR027417 P-loop_NTPase
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF00619 CARD, 1 hit
PF00931 NB-ARC, 1 hit
PIRSFiPIRSF027202 Apop_reg_Ced-4, 1 hit
SMARTiView protein in SMART
SM00114 CARD, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
SSF47986 SSF47986, 1 hit
SSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS50209 CARD, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCED4_CAEEL
<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: P30429
Secondary accession number(s): Q5BHI5
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: March 29, 2005
Last modified: May 8, 2019
This is version 158 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 programCaenorhabditis annotation project

<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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
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