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Entry version 193 (16 Oct 2019)
Sequence version 3 (25 Jul 2006)
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Protein

Receptor tyrosine-protein kinase let-23

Gene

let-23

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

Tyrosine-protein kinase receptor which, upon binding ligand lin-3, activates 2 signaling cascades: the let-60/Ras and MAP kinase signaling pathway and the let-60-independent phospholipase C-mediated Ca2+ signaling pathway. Each pathway regulates distinct functions. By activating let-60/Ras, regulates larval development, induction of vulva cell precursors during vulva development, male spicule formation and posterior development of the epidermis (PubMed:2071015, PubMed:8313880, PubMed:9491893, PubMed:20230814). Probably by activating phospholipase plc-3 and inositol 1,4,5-trisphosphate receptor itr-1 signaling cascade downstream of ligand lin-3, plays a role in ovulation by promoting ovulatory gonadal sheath cell contractions (PubMed:9491893, PubMed:15194811). Probably by regulating neuronal transmission in ALA neurons, mediates, independently of let-60/Ras, the decrease in pharyngeal pumping and locomotion during the quiescent state that precedes each larval molt, downstream of lin-3 and upstream of plc-3 (PubMed:17891142).6 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

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 sitei919ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1010Proton acceptorPROSITE-ProRule annotation1

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 bindingi891 – 899ATPPROSITE-ProRule annotation9

<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

Molecular functionDevelopmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.10.1 1045

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-CEL-1227986 Signaling by ERBB2
R-CEL-1250196 SHC1 events in ERBB2 signaling
R-CEL-1251985 Nuclear signaling by ERBB4
R-CEL-1253288 Downregulation of ERBB4 signaling
R-CEL-1257604 PIP3 activates AKT signaling
R-CEL-177929 Signaling by EGFR
R-CEL-179812 GRB2 events in EGFR signaling
R-CEL-180292 GAB1 signalosome
R-CEL-180336 SHC1 events in EGFR signaling
R-CEL-182971 EGFR downregulation
R-CEL-1963642 PI3K events in ERBB2 signaling
R-CEL-212718 EGFR interacts with phospholipase C-gamma
R-CEL-2179392 EGFR Transactivation by Gastrin
R-CEL-416572 Sema4D induced cell migration and growth-cone collapse
R-CEL-5673001 RAF/MAP kinase cascade
R-CEL-6785631 ERBB2 Regulates Cell Motility
R-CEL-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-CEL-8847993 ERBB2 Activates PTK6 Signaling
R-CEL-8856825 Cargo recognition for clathrin-mediated endocytosis
R-CEL-8856828 Clathrin-mediated endocytosis
R-CEL-8863795 Downregulation of ERBB2 signaling
R-CEL-9009391 Extra-nuclear estrogen signaling

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
P24348

<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:
Receptor tyrosine-protein kinase let-23 (EC:2.7.10.1)
Alternative name(s):
Lethal protein 23
<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:let-23Imported
Synonyms:kin-7Imported
ORF Names:ZK1067.1Imported
<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 II

Organism-specific databases

WormBase

More...
WormBasei
ZK1067.1a ; CE03840 ; WBGene00002299 ; let-23

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini21 – 818ExtracellularSequence analysisAdd BLAST798
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei819 – 839HelicalSequence analysisAdd BLAST21
Topological domaini840 – 1323CytoplasmicSequence analysisAdd BLAST484

Keywords - Cellular componenti

Cell membrane, Membrane

<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

Larval lethality, lack of vulva formation, infertility and lack of male spicule formation (PubMed:2071015). RNAi-mediated knockdown causes sterility, a small decrease in the peak rate of sheath cell contractions and a delay in the onset of ovulatory contractions (PubMed:15194811). Restores normal pharyngeal pumping rate in 30 percent of animals overexpressing lin-3 (PubMed:17891142).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>Mutagenesisi364C → Y in sa62; multivulva phenotype. RNAi-mediated knockdown of let-765 suppresses the multivulva phenotype. 1 Publication1
Mutagenesisi368C → Y in sy10; severe larval lethality, lack of vulva induction, infertile and lack of male spicule formation. Impaired ovulation characterized by a delay in the initiation of ovulatory sheath cell contractions and prolonged ovulatory contractions. 3 Publications1
Mutagenesisi469G → R in mn216; larval lethality. 1 Publication1
Mutagenesisi700C → W in mn23; larval lethality. 1 Publication1
Mutagenesisi753C → Y in SY11. 1 Publication1
Mutagenesisi1065T → I in sy16; larval lethality and lack of vulva induction. Viability, vulva induction but not fertility are restored in a let-60 (n1046gf) mutant background. Viability is not restored in a lfe-1 (sy290) or lfe-2 (sy326) mutant background. Fertility is restored in a let-60 (n1046gf) and lfe-1 (sy290) mutant background. 2 Publications1
Mutagenesisi1074G → E in SY7. 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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 20Sequence analysisAdd BLAST20
<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_000001667721 – 1323Receptor tyrosine-protein kinase let-23Add BLAST1303

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi91N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi169N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi220 ↔ 228By similarity
Disulfide bondi224 ↔ 236By similarity
Disulfide bondi244 ↔ 251By similarity
Disulfide bondi248 ↔ 262By similarity
Glycosylationi255N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi263 ↔ 271By similarity
Disulfide bondi267 ↔ 279By similarity
Disulfide bondi282 ↔ 291By similarity
Disulfide bondi295 ↔ 322By similarity
Disulfide bondi326 ↔ 337By similarity
Disulfide bondi341 ↔ 356By similarity
Disulfide bondi359 ↔ 364By similarity
Glycosylationi376N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi520 ↔ 529By similarity
Disulfide bondi524 ↔ 537By similarity
Disulfide bondi540 ↔ 549By similarity
Disulfide bondi553 ↔ 567By similarity
Glycosylationi561N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi570 ↔ 577By similarity
Disulfide bondi574 ↔ 585By similarity
Disulfide bondi588 ↔ 604By similarity
Disulfide bondi608 ↔ 620By similarity
Disulfide bondi623 ↔ 632By similarity
Disulfide bondi627 ↔ 644By similarity
Disulfide bondi647 ↔ 660Sequence analysis
Glycosylationi655N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi670 ↔ 693Sequence analysis
Disulfide bondi696 ↔ 703Sequence analysis
Disulfide bondi700 ↔ 715Sequence analysis
Disulfide bondi717 ↔ 731Sequence analysis
Disulfide bondi735 ↔ 750Sequence analysis
Glycosylationi746N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi753 ↔ 763Sequence analysis
Disulfide bondi757 ↔ 771Sequence analysis
Disulfide bondi774 ↔ 787Sequence analysis
Glycosylationi776N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi791 ↔ 805Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

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

More...
PaxDbi
P24348

PRoteomics IDEntifications database

More...
PRIDEi
P24348

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P24348

<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

Expressed in vulval precursor cells (at protein level) (PubMed:10359617). Expressed in ALA neurons, 2 ventral head neurons, a single neuron in the tail, pharyngeal-intestinal valve and posterior arcade epithelial cells (PubMed:17891142).2 Publications

<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

Expressed during L2 and L3 larval stages.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
WBGene00002299 Expressed in 4 organ(s), highest expression level in adult organism

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P24348 baseline and differential

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
39787, 105 interactors

Database of interacting proteins

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DIPi
DIP-1014N

Protein interaction database and analysis system

More...
IntActi
P24348, 2 interactors

Molecular INTeraction database

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MINTi
P24348

STRING: functional protein association networks

More...
STRINGi
6239.ZK1067.1c

<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

11323
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
P24348

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_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>Domaini885 – 1152Protein kinasePROSITE-ProRule annotationAdd BLAST268

<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 protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1025 Eukaryota
ENOG410XNSR LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000168382

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000016236

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P24348

Database for complete collections of gene phylogenies

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PhylomeDBi
P24348

Family and domain databases

Conserved Domains Database

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CDDi
cd00064 FU, 5 hits

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.80.20.20, 2 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR006211 Furin-like_Cys-rich_dom
IPR006212 Furin_repeat
IPR032778 GF_recep_IV
IPR009030 Growth_fac_rcpt_cys_sf
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR000494 Rcpt_L-dom
IPR036941 Rcpt_L-dom_sf
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00757 Furin-like, 1 hit
PF14843 GF_recep_IV, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PF01030 Recep_L_domain, 2 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00261 FU, 7 hits
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56112 SSF56112, 1 hit
SSF57184 SSF57184, 3 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 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>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 3 potential isoforms that are computationally mapped.Show allAlign All

P24348-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRYPPSIGSI LLIIPIFLTF FGNSNAQLWK RCVSPQDCLC SGTTNGISRY
60 70 80 90 100
GTGNILEDLE TMYRGCRRVY GNLEITWIEA NEIKKWREST NSTVDPKNED
110 120 130 140 150
SPLKSINFFD NLEEIRGSLI IYRANIQKIS FPRLRVIYGD EVFHDNALYI
160 170 180 190 200
HKNDKVHEVV MRELRVIRNG SVTIQDNPKM CYIGDKIDWK ELLYDPDVQK
210 220 230 240 250
VETTNSHQHC YQNGKSMAKC HESCNDKCWG SGDNDCQRVY RSVCPKSCSQ
260 270 280 290 300
CFYSNSTSSY ECCDSACLGG CTGHGPKNCI ACSKYELDGI CIETCPSRKI
310 320 330 340 350
FNHKTGRLVF NPDGRYQNGN HCVKECPPEL LIENDVCVRH CSDGHHYDAT
360 370 380 390 400
KDVRECEKCR SSSCPKICTV DGHLTNETLK NLEGCEQIDG HLIIEHAFTY
410 420 430 440 450
EQLKVLETVK IVSEYITIVQ QNFYDLKFLK NLQIIEGRKL HNVRWALAIY
460 470 480 490 500
QCDDLEELSL NSLKLIKTGA VLIMKNHRLC YVSKIDWSSI ITSKGKDNKP
510 520 530 540 550
SLAIAENRDS KLCETEQRVC DKNCNKRGCW GKEPEDCLEC KTWKSVGTCV
560 570 580 590 600
EKCDTKGFLR NQTSMKCERC SPECETCNGL GELDCLTCRH KTLYNSDFGN
610 620 630 640 650
RMECVHDCPV SHFPTQKNVC EKCHPTCYDN GCTGPDSNLG YGGCKQCKYA
660 670 680 690 700
VKYENDTIFC LQSSGMNNVC VENDLPNYYI STYDTEGVIE THCEKCSISC
710 720 730 740 750
KTCSSAGRNV VQNKCVCKHV EYQPNPSERI CMDQCPVNSF MVPDTNNTVC
760 770 780 790 800
KKCHHECDQN YHCANGQSTG CQKCKNFTVF KGDIAQCVSE CPKNLPFSNP
810 820 830 840 850
ANGECLDYDI ASRQRKTRMV IIGSVLFGFA VMFLFILLVY WRCQRIGKKL
860 870 880 890 900
KIAEMVDMPE LTPIDASVRP NMSRICLIPS SELQTKLDKK LGAGAFGTVF
910 920 930 940 950
AGIYYPKRAK NVKIPVAIKV FQTDQSQTDE MLEEATNMFR LRHDNLLKII
960 970 980 990 1000
GFCMHDDGLK IVTIYRPLGN LQNFLKLHKE NLGAREQVLY CYQIASGMQY
1010 1020 1030 1040 1050
LEKQRVVHRD LATRNVLVKK FNHVEITDFG LSKILKHDAD SITIKSGKVA
1060 1070 1080 1090 1100
IKWLAIEIFS KHCYTHASDV WAFGVTCWEI ITFGQSPYQG MSTDSIHNFL
1110 1120 1130 1140 1150
KDGNRLSQPP NCSQDLYQEL LRCWMADPKS RPGFEILYER FKEFCKVPQL
1160 1170 1180 1190 1200
FLENSNKISE SDLSAEERFQ TERIREMFDG NIDPQMYFDQ GSLPSMPSSP
1210 1220 1230 1240 1250
TSMATFTIPH GDLMNRMQSV NSSRYKTEPF DYGSTAQEDN SYLIPKTKEV
1260 1270 1280 1290 1300
QQSAVLYTAV TNEDGQTELS PSNGDYYNQP NTPSSSSGYY NEPHLKTKKP
1310 1320
ETSEEAEAVQ YENEEVSQKE TCL
Length:1,323
Mass (Da):150,511
Last modified:July 25, 2006 - v3
<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:i6B0307EE53EEFA99
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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B5BM27B5BM27_CAEEL
Receptor protein-tyrosine kinase
let-23 CELE_ZK1067.1, ZK1067.1
1,328Annotation score:

Annotation score:4 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>
B5BM28B5BM28_CAEEL
Receptor protein-tyrosine kinase
let-23 CELE_ZK1067.1, ZK1067.1
1,262Annotation score:

Annotation score:4 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>
A0A0K3AX35A0A0K3AX35_CAEEL
Receptor protein-tyrosine kinase
let-23 CELE_ZK1067.1, ZK1067.1
1,335Annotation score:

Annotation score:2 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>

<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

The sequence BAA09729 differs from that shown. Reason: Erroneous gene model prediction.Curated

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 conflicti1179D → H in CAA40919 (PubMed:1979659).Curated1

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

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DDBJi
Links Updated
X57767 mRNA Translation: CAA40919.1
D63426 Genomic DNA Translation: BAA09729.1 Sequence problems.
BX284602 Genomic DNA Translation: CAA93882.3

Protein sequence database of the Protein Information Resource

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PIRi
E88257
S70712

NCBI Reference Sequences

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RefSeqi
NP_495962.2, NM_063561.4

Genome annotation databases

Ensembl metazoan genome annotation project

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EnsemblMetazoai
ZK1067.1a.1; ZK1067.1a.1; WBGene00002299

Database of genes from NCBI RefSeq genomes

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GeneIDi
174462

UCSC genome browser

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UCSCi
ZK1067.1 c. elegans

<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
X57767 mRNA Translation: CAA40919.1
D63426 Genomic DNA Translation: BAA09729.1 Sequence problems.
BX284602 Genomic DNA Translation: CAA93882.3
PIRiE88257
S70712
RefSeqiNP_495962.2, NM_063561.4

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
5WNOX-ray2.39A866-1191[»]
SMRiP24348
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi39787, 105 interactors
DIPiDIP-1014N
IntActiP24348, 2 interactors
MINTiP24348
STRINGi6239.ZK1067.1c

PTM databases

iPTMnetiP24348

Proteomic databases

PaxDbiP24348
PRIDEiP24348

Genome annotation databases

EnsemblMetazoaiZK1067.1a.1; ZK1067.1a.1; WBGene00002299
GeneIDi174462
UCSCiZK1067.1 c. elegans

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
174462
WormBaseiZK1067.1a ; CE03840 ; WBGene00002299 ; let-23

Phylogenomic databases

eggNOGiKOG1025 Eukaryota
ENOG410XNSR LUCA
GeneTreeiENSGT00940000168382
HOGENOMiHOG000016236
InParanoidiP24348
PhylomeDBiP24348

Enzyme and pathway databases

BRENDAi2.7.10.1 1045
ReactomeiR-CEL-1227986 Signaling by ERBB2
R-CEL-1250196 SHC1 events in ERBB2 signaling
R-CEL-1251985 Nuclear signaling by ERBB4
R-CEL-1253288 Downregulation of ERBB4 signaling
R-CEL-1257604 PIP3 activates AKT signaling
R-CEL-177929 Signaling by EGFR
R-CEL-179812 GRB2 events in EGFR signaling
R-CEL-180292 GAB1 signalosome
R-CEL-180336 SHC1 events in EGFR signaling
R-CEL-182971 EGFR downregulation
R-CEL-1963642 PI3K events in ERBB2 signaling
R-CEL-212718 EGFR interacts with phospholipase C-gamma
R-CEL-2179392 EGFR Transactivation by Gastrin
R-CEL-416572 Sema4D induced cell migration and growth-cone collapse
R-CEL-5673001 RAF/MAP kinase cascade
R-CEL-6785631 ERBB2 Regulates Cell Motility
R-CEL-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-CEL-8847993 ERBB2 Activates PTK6 Signaling
R-CEL-8856825 Cargo recognition for clathrin-mediated endocytosis
R-CEL-8856828 Clathrin-mediated endocytosis
R-CEL-8863795 Downregulation of ERBB2 signaling
R-CEL-9009391 Extra-nuclear estrogen signaling
SignaLinkiP24348

Miscellaneous databases

Protein Ontology

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PROi
PR:P24348

Gene expression databases

BgeeiWBGene00002299 Expressed in 4 organ(s), highest expression level in adult organism
ExpressionAtlasiP24348 baseline and differential

Family and domain databases

CDDicd00064 FU, 5 hits
Gene3Di3.80.20.20, 2 hits
InterProiView protein in InterPro
IPR006211 Furin-like_Cys-rich_dom
IPR006212 Furin_repeat
IPR032778 GF_recep_IV
IPR009030 Growth_fac_rcpt_cys_sf
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR000494 Rcpt_L-dom
IPR036941 Rcpt_L-dom_sf
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
PfamiView protein in Pfam
PF00757 Furin-like, 1 hit
PF14843 GF_recep_IV, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PF01030 Recep_L_domain, 2 hits
PRINTSiPR00109 TYRKINASE
SMARTiView protein in SMART
SM00261 FU, 7 hits
SM00219 TyrKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
SSF57184 SSF57184, 3 hits
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLET23_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: P24348
<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: March 1, 1992
Last sequence update: July 25, 2006
Last modified: October 16, 2019
This is version 193 of the entry and version 3 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. SIMILARITY comments
    Index of protein domains and families
  2. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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