Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 182 (02 Dec 2020)
Sequence version 1 (01 Nov 1997)
Previous versions | rss
Add a publicationFeedback
Protein

Myoblast growth factor receptor egl-15

Gene

egl-15

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

Receptor tyrosine kinase required for larval development (PubMed:7585964). May phosphorylate adapter protein soc-1 which in turn may result in the recruitment and/or activation of phosphatase ptp-2 (PubMed:11689700). May activate the Ras/MAPK kinase signaling pathway which includes sem-5, sos-1, let-60/Ras, lin-45/Raf, mek-2 and mpk-1 (PubMed:11689700). Acts in the hypodermis to regulate axon growth and fluid homeostasis (PubMed:12835392, PubMed:7585964). Activates protein degradation in muscles (PubMed:14517244). Probably following interaction with ligand let-756, regulates negatively membrane protrusion from body wall muscles during larval development (PubMed:16495308). Plays a role in nicotinic acetylcholine receptor (nAChR)-mediated sensitivity to nicotine (PubMed:15990870). Regulates synaptic levels of nAChR subunit lev-1 in the nerve cord (PubMed:15990870).6 Publications
Affects the maintenance of axon position without affecting axon growth. Interaction with egl-17 is required for the guidance of sex myoblast migration during gonad development.1 Publication
Interaction with let-756 appears to play a role in maintaining body morphology at higher temperatures.1 Publication
Interaction with let-756 appears to play a role in maintaining body morphology at higher temperatures.1 Publication
Interaction with let-756 appears to play a role in maintaining body morphology at higher temperatures.1 Publication
Interaction with let-756 appears to play a role in maintaining body morphology at higher temperatures.1 Publication

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

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+Curated

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei672ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei797Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi646 – 654ATPPROSITE-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, Magnesium, Metal-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-109704, PI3K Cascade
R-CEL-1257604, PIP3 activates AKT signaling
R-CEL-1307965, betaKlotho-mediated ligand binding
R-CEL-190322, FGFR4 ligand binding and activation
R-CEL-190370, FGFR1b ligand binding and activation
R-CEL-190371, FGFR3b ligand binding and activation
R-CEL-190372, FGFR3c ligand binding and activation
R-CEL-190373, FGFR1c ligand binding and activation
R-CEL-190374, FGFR1c and Klotho ligand binding and activation
R-CEL-190375, FGFR2c ligand binding and activation
R-CEL-190377, FGFR2b ligand binding and activation
R-CEL-445144, Signal transduction by L1
R-CEL-5654219, Phospholipase C-mediated cascade: FGFR1
R-CEL-5654221, Phospholipase C-mediated cascade, FGFR2
R-CEL-5654227, Phospholipase C-mediated cascade, FGFR3
R-CEL-5654228, Phospholipase C-mediated cascade, FGFR4
R-CEL-5654688, SHC-mediated cascade:FGFR1
R-CEL-5654689, PI-3K cascade:FGFR1
R-CEL-5654693, FRS-mediated FGFR1 signaling
R-CEL-5654695, PI-3K cascade:FGFR2
R-CEL-5654699, SHC-mediated cascade:FGFR2
R-CEL-5654704, SHC-mediated cascade:FGFR3
R-CEL-5654710, PI-3K cascade:FGFR3
R-CEL-5654712, FRS-mediated FGFR4 signaling
R-CEL-5654719, SHC-mediated cascade:FGFR4
R-CEL-5654720, PI-3K cascade:FGFR4
R-CEL-5654726, Negative regulation of FGFR1 signaling
R-CEL-5654733, Negative regulation of FGFR4 signaling
R-CEL-5673001, RAF/MAP kinase cascade
R-CEL-6811558, PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling

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

More...
SignaLinki
Q10656

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Myoblast growth factor receptor egl-15 (EC:2.7.10.1)
Alternative name(s):
Egg-laying defective protein 15
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:egl-15
ORF Names:F58A3.2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiCaenorhabditis elegans
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri6239 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditinaRhabditomorphaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001940 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

Organism-specific databases

WormBase

More...
WormBasei
F58A3.2a ; CE28238 ; WBGene00001184 ; egl-15
F58A3.2b ; CE35726 ; WBGene00001184 ; egl-15
F58A3.2c ; CE50149 ; WBGene00001184 ; egl-15
F58A3.2d ; CE50303 ; WBGene00001184 ; egl-15
F58A3.2e ; CE50247 ; WBGene00001184 ; egl-15

<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%5Flocation%5Fsection">'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 domaini20 – 525ExtracellularSequence analysisAdd BLAST506
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Transmembranei526 – 549HelicalSequence analysisAdd BLAST24
Topological domaini550 – 1040CytoplasmicSequence analysisAdd BLAST491

Keywords - Cellular componenti

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

Early arrest in larval development. Impaired guided migration of sex myoblasts (PubMed:7585964). RNAi-mediated knockdown causes ectopic membrane extension from body wall muscles (PubMed:16495308).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi680E → K in n1775; loss of activity. 1 Publication1
Mutagenesisi714P → L in n1783; loss of activity. Ectopic membrane extension in body wall muscles. 2 Publications1

<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 – 19Sequence analysisAdd BLAST19
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001679620 – 1040Myoblast growth factor receptor egl-15Add BLAST1021

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bondi55 ↔ 109PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Glycosylationi121N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi280N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi299N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi314 ↔ 367PROSITE-ProRule annotation
Glycosylationi401N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi407N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi414 ↔ 485PROSITE-ProRule annotation
Glycosylationi433N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi440N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi449N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi474N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi497N-linked (GlcNAc...) asparagineSequence analysis1
<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 residuei828Phosphotyrosine; by autocatalysisBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Activity is regulated by the phosphatase clr-1, however it is not known whether clr-1 acts directly on egl-15.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

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

More...
PaxDbi
Q10656

PeptideAtlas

More...
PeptideAtlasi
Q10656

PRoteomics IDEntifications database

More...
PRIDEi
Q10656

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q10656

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
WBGene00001184, Expressed in multi-cellular organism and 4 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q10656, 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)

More...
BioGRIDi
46202, 148 interactors

Protein interaction database and analysis system

More...
IntActi
Q10656, 1 interactor

STRING: functional protein association networks

More...
STRINGi
6239.F58A3.2c

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

3D structure databases

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

More...
SMRi
Q10656

Database of comparative protein structure models

More...
ModBasei
Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">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>Domaini33 – 125Ig-like C2-type 1Add BLAST93
Domaini287 – 383Ig-like C2-type 2Add BLAST97
Domaini391 – 501Ig-like C2-type 3Add BLAST111
Domaini640 – 931Protein kinasePROSITE-ProRule annotationAdd BLAST292

<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. Fibroblast growth factor receptor subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0200, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000167157

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q10656

Database of Orthologous Groups

More...
OrthoDBi
220433at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q10656

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 3 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR007110, Ig-like_dom
IPR036179, Ig-like_dom_sf
IPR013783, Ig-like_fold
IPR013098, Ig_I-set
IPR003599, Ig_sub
IPR003598, Ig_sub2
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
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
PF07679, I-set, 3 hits
PF07714, PK_Tyr_Ser-Thr, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00109, TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00409, IG, 3 hits
SM00408, IGc2, 3 hits
SM00219, TyrKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48726, SSF48726, 3 hits
SSF56112, SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50835, IG_LIKE, 3 hits
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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (5+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 5 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

Isoform a (identifier: Q10656-1) [UniParc]FASTAAdd to basket

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
MSYFLASCLG VGLLSTVSCS LQGLTSHYRE NIPRFKHVAN ERYEVFLGDE
60 70 80 90 100
IKFDCQTAAS KISAFVEWYR NDKLLKNDQI DKDKIRKDNN RMMLHLKNID
110 120 130 140 150
VSDQGLWSCR VHNAYGQISR NFTVEVIDFC DYFLFPDIHH LNIPMECVCL
160 170 180 190 200
WKYNKEAKRS DVNYAAVTGE VCSKYASRMI NRARKPLPMI PCFGDHCKEF
210 220 230 240 250
DTTPVSDFGL PGKPEDDPLV KRVVLKKDDV IVPVHDSEES PSESRTEFIN
260 270 280 290 300
ADEKENKEDE EEDYSVSQPV APDAGLTELN ITAEEPPYFK SNDNIVLFNE
310 320 330 340 350
THALPAGRTL KLNCRAKGYP EPQIIWYKNG KMLKKSSARS GGYEFKFNRW
360 370 380 390 400
SLEVEDAVVA DSGEFHCEAL NKVGSAKKYF HVIIVNRMRR PPIIVPNILA
410 420 430 440 450
NQSVNINDTA TFHCKVVSDL LPHIIWVRIN KINGSYSYYN NSAEEYMFNY
460 470 480 490 500
TEMDTFDKAH VHHVGDESTL TIFNVSLDDQ GIYACLSGNS LGMSMANATL
510 520 530 540 550
TVNEFMAIHL LTGDEPKIDR WTTSDYIFTT ILLFLLLAAT LFGILFMVCK
560 570 580 590 600
QTLHKKGFMD DTVGLVARKK RVVVSKRPMN EDNENSDDEP SPYQIQIIET
610 620 630 640 650
PITKKEAARK QRKRMNSENT VLSEYEVDSD PVWEVERSKL SLVHMLGEGA
660 670 680 690 700
FGEVWKATYK ETENNEIAVA VKKLKMSAHE KELIDLVSEM ETFKVIGEHE
710 720 730 740 750
NVLRLIGCCT GAGPLYVVVE LCKHGNLRDF LRAHRPKEEK AKKSSQELTD
760 770 780 790 800
YLEPRKASDK DDIELIPNLT QRHLVQFAWQ VAQGMNFLAS KKIIHRDLAA
810 820 830 840 850
RNVLVGDGHV LKISDFGLSR DVHCNDYYRK RGNGRLPIKW MALEALDSNV
860 870 880 890 900
YTVESDVWSY GVLLWEIMTL GGTPYPTIAM PELYANLKEG YRMEPPHLCP
910 920 930 940 950
QEVYHLMCSC WREKLEERPS FKTIVDYLDW MLTMTNETIE GSQEFNDQFF
960 970 980 990 1000
SERSTASGPV SPMESFQKKR KHRPLSAPVN LPSEPQHTIC DDYESNFSVE
1010 1020 1030 1040
PPNDPNHLYC NDNMLKNHII TPETSQRIPS NNNSMSKPEF
Length:1,040
Mass (Da):118,956
Last modified:November 1, 1997 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8CA227195DDBCD69
GO
Isoform b (identifier: Q10656-2) [UniParc]FASTAAdd to basket
Also known as: EGL-15(5A)

The sequence of this isoform differs from the canonical sequence as follows:
     129-245: FCDYFLFPDI...DSEESPSESR → PLKLFDWLTE...RLRQINHALG

Show »
Length:988
Mass (Da):113,327
Checksum:iA7365D218C082E49
GO
Isoform c (identifier: Q10656-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     829-829: R → RL
     984-984: E → EVDQN
     1027-1040: RIPSNNNSMSKPEF → LYIHKVLNEP...NPLPTKETIV

Show »
Length:1,158
Mass (Da):132,425
Checksum:i2159D2E7C6564685
GO
Isoform d (identifier: Q10656-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     829-829: R → RL
     984-984: E → EVDQN
     1027-1040: RIPSNNNSMSKPEF → LYIHKVLNEP...DDEKHHYYYS

Show »
Length:1,096
Mass (Da):125,172
Checksum:iC76B0B8A20852F80
GO
Isoform e (identifier: Q10656-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     829-829: R → RL
     984-984: E → EVDQN
     1027-1040: RIPSNNNSMSKPEF → LYIHKVLNEPIGNGSNSPVL

Show »
Length:1,051
Mass (Da):120,070
Checksum:iA9616D4CAEA14AEE
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 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0K3AVM0A0A0K3AVM0_CAEEL
Receptor protein-tyrosine kinase
egl-15 CELE_F58A3.2, F58A3.2
1,153Annotation 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>
A0A0K3ATB0A0A0K3ATB0_CAEEL
Receptor protein-tyrosine kinase
egl-15 CELE_F58A3.2, F58A3.2
1,046Annotation 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>
A0A0K3AYK2A0A0K3AYK2_CAEEL
Receptor protein-tyrosine kinase
egl-15 CELE_F58A3.2, F58A3.2
1,091Annotation 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>
A0A0K3AYL0A0A0K3AYL0_CAEEL
Receptor protein-tyrosine kinase
egl-15 CELE_F58A3.2, F58A3.2
1,101Annotation 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>
A0A0K3ASS4A0A0K3ASS4_CAEEL
Receptor protein-tyrosine kinase
egl-15 CELE_F58A3.2, F58A3.2
994Annotation 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>
A0A0K3ATB5A0A0K3ATB5_CAEEL
Receptor protein-tyrosine kinase
egl-15 CELE_F58A3.2, F58A3.2
1,039Annotation 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>

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 conflicti551Q → G in AAP44084 (PubMed:12835392).Curated1

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_019861129 – 245FCDYF…PSESR → PLKLFDWLTEHRVFDISHLL PKLLPPAEMRRVKSQLGGWE KMNNEQKIVRARHILRLRQI NHALG in isoform b. 1 PublicationAdd BLAST117
Alternative sequenceiVSP_002991829R → RL in isoform c, isoform d and isoform e. 1 Publication1
Alternative sequenceiVSP_002992984E → EVDQN in isoform c, isoform d and isoform e. 1 Publication1
Alternative sequenceiVSP_0029941027 – 1040RIPSN…SKPEF → LYIHKVLNEPIGNGYVRQDK LARAVSGVANQSLDSALGSP AWPSYDRPSNKASCLDQTHQ YYNTTSKIQYLHFTFDDPDC MTRSRDSAIFEESYHPNYIQ SHPLYSKIIIKKNMTPRNPL PTKETIV in isoform c. 1 PublicationAdd BLAST14
Alternative sequenceiVSP_0198621027 – 1040RIPSN…SKPEF → LYIHKVLNEPIGNGYVRQDK LARAVSGVANQSLDSALGSP AWPSYDRPSNKASCLDDEKH HYYYS in isoform d. 1 PublicationAdd BLAST14
Alternative sequenceiVSP_0198631027 – 1040RIPSN…SKPEF → LYIHKVLNEPIGNGSNSPVL in isoform e. 1 PublicationAdd BLAST14

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
U39761 mRNA Translation: AAC46934.1
AY268435 mRNA Translation: AAP31029.1
AY268436 mRNA Translation: AAP31030.1
AY288941 mRNA Translation: AAP44084.1
AY288942 mRNA Translation: AAP44085.1
AY292532 mRNA Translation: AAP74805.1
Z81017 Genomic DNA Translation: CAB02673.2
Z81017 Genomic DNA Translation: CAC70094.2
Z81017 Genomic DNA Translation: CAC70095.2
Z81017 Genomic DNA Translation: CAD44136.1
Z81017 Genomic DNA Translation: CAE47468.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A57638
T22889

NCBI Reference Sequences

More...
RefSeqi
NP_001024723.1, NM_001029552.2
NP_001024724.3, NM_001029553.5
NP_001024725.2, NM_001029554.4
NP_001024726.2, NM_001029555.4
NP_509842.2, NM_077441.6

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
F58A3.2a.1; F58A3.2a.1; WBGene00001184 [Q10656-1]
F58A3.2a.2; F58A3.2a.2; WBGene00001184 [Q10656-1]
F58A3.2a.3; F58A3.2a.3; WBGene00001184 [Q10656-1]
F58A3.2a.4; F58A3.2a.4; WBGene00001184 [Q10656-1]
F58A3.2a.5; F58A3.2a.5; WBGene00001184 [Q10656-1]
F58A3.2a.6; F58A3.2a.6; WBGene00001184 [Q10656-1]
F58A3.2b.1; F58A3.2b.1; WBGene00001184 [Q10656-2]
F58A3.2b.2; F58A3.2b.2; WBGene00001184 [Q10656-2]
F58A3.2b.3; F58A3.2b.3; WBGene00001184 [Q10656-2]
F58A3.2b.4; F58A3.2b.4; WBGene00001184 [Q10656-2]
F58A3.2b.5; F58A3.2b.5; WBGene00001184 [Q10656-2]
F58A3.2b.6; F58A3.2b.6; WBGene00001184 [Q10656-2]
F58A3.2c.1; F58A3.2c.1; WBGene00001184
F58A3.2d.1; F58A3.2d.1; WBGene00001184
F58A3.2e.1; F58A3.2e.1; WBGene00001184

UCSC genome browser

More...
UCSCi
F58A3.2e, c. elegans [Q10656-1]

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
U39761 mRNA Translation: AAC46934.1
AY268435 mRNA Translation: AAP31029.1
AY268436 mRNA Translation: AAP31030.1
AY288941 mRNA Translation: AAP44084.1
AY288942 mRNA Translation: AAP44085.1
AY292532 mRNA Translation: AAP74805.1
Z81017 Genomic DNA Translation: CAB02673.2
Z81017 Genomic DNA Translation: CAC70094.2
Z81017 Genomic DNA Translation: CAC70095.2
Z81017 Genomic DNA Translation: CAD44136.1
Z81017 Genomic DNA Translation: CAE47468.1
PIRiA57638
T22889
RefSeqiNP_001024723.1, NM_001029552.2
NP_001024724.3, NM_001029553.5
NP_001024725.2, NM_001029554.4
NP_001024726.2, NM_001029555.4
NP_509842.2, NM_077441.6

3D structure databases

SMRiQ10656
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi46202, 148 interactors
IntActiQ10656, 1 interactor
STRINGi6239.F58A3.2c

PTM databases

iPTMnetiQ10656

Proteomic databases

PaxDbiQ10656
PeptideAtlasiQ10656
PRIDEiQ10656

Genome annotation databases

EnsemblMetazoaiF58A3.2a.1; F58A3.2a.1; WBGene00001184 [Q10656-1]
F58A3.2a.2; F58A3.2a.2; WBGene00001184 [Q10656-1]
F58A3.2a.3; F58A3.2a.3; WBGene00001184 [Q10656-1]
F58A3.2a.4; F58A3.2a.4; WBGene00001184 [Q10656-1]
F58A3.2a.5; F58A3.2a.5; WBGene00001184 [Q10656-1]
F58A3.2a.6; F58A3.2a.6; WBGene00001184 [Q10656-1]
F58A3.2b.1; F58A3.2b.1; WBGene00001184 [Q10656-2]
F58A3.2b.2; F58A3.2b.2; WBGene00001184 [Q10656-2]
F58A3.2b.3; F58A3.2b.3; WBGene00001184 [Q10656-2]
F58A3.2b.4; F58A3.2b.4; WBGene00001184 [Q10656-2]
F58A3.2b.5; F58A3.2b.5; WBGene00001184 [Q10656-2]
F58A3.2b.6; F58A3.2b.6; WBGene00001184 [Q10656-2]
F58A3.2c.1; F58A3.2c.1; WBGene00001184
F58A3.2d.1; F58A3.2d.1; WBGene00001184
F58A3.2e.1; F58A3.2e.1; WBGene00001184
UCSCiF58A3.2e, c. elegans [Q10656-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
181291
WormBaseiF58A3.2a ; CE28238 ; WBGene00001184 ; egl-15
F58A3.2b ; CE35726 ; WBGene00001184 ; egl-15
F58A3.2c ; CE50149 ; WBGene00001184 ; egl-15
F58A3.2d ; CE50303 ; WBGene00001184 ; egl-15
F58A3.2e ; CE50247 ; WBGene00001184 ; egl-15

Phylogenomic databases

eggNOGiKOG0200, Eukaryota
GeneTreeiENSGT00940000167157
InParanoidiQ10656
OrthoDBi220433at2759
PhylomeDBiQ10656

Enzyme and pathway databases

BRENDAi2.7.10.1, 1045
ReactomeiR-CEL-109704, PI3K Cascade
R-CEL-1257604, PIP3 activates AKT signaling
R-CEL-1307965, betaKlotho-mediated ligand binding
R-CEL-190322, FGFR4 ligand binding and activation
R-CEL-190370, FGFR1b ligand binding and activation
R-CEL-190371, FGFR3b ligand binding and activation
R-CEL-190372, FGFR3c ligand binding and activation
R-CEL-190373, FGFR1c ligand binding and activation
R-CEL-190374, FGFR1c and Klotho ligand binding and activation
R-CEL-190375, FGFR2c ligand binding and activation
R-CEL-190377, FGFR2b ligand binding and activation
R-CEL-445144, Signal transduction by L1
R-CEL-5654219, Phospholipase C-mediated cascade: FGFR1
R-CEL-5654221, Phospholipase C-mediated cascade, FGFR2
R-CEL-5654227, Phospholipase C-mediated cascade, FGFR3
R-CEL-5654228, Phospholipase C-mediated cascade, FGFR4
R-CEL-5654688, SHC-mediated cascade:FGFR1
R-CEL-5654689, PI-3K cascade:FGFR1
R-CEL-5654693, FRS-mediated FGFR1 signaling
R-CEL-5654695, PI-3K cascade:FGFR2
R-CEL-5654699, SHC-mediated cascade:FGFR2
R-CEL-5654704, SHC-mediated cascade:FGFR3
R-CEL-5654710, PI-3K cascade:FGFR3
R-CEL-5654712, FRS-mediated FGFR4 signaling
R-CEL-5654719, SHC-mediated cascade:FGFR4
R-CEL-5654720, PI-3K cascade:FGFR4
R-CEL-5654726, Negative regulation of FGFR1 signaling
R-CEL-5654733, Negative regulation of FGFR4 signaling
R-CEL-5673001, RAF/MAP kinase cascade
R-CEL-6811558, PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
SignaLinkiQ10656

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q10656

Gene expression databases

BgeeiWBGene00001184, Expressed in multi-cellular organism and 4 other tissues
ExpressionAtlasiQ10656, baseline and differential

Family and domain databases

Gene3Di2.60.40.10, 3 hits
InterProiView protein in InterPro
IPR007110, Ig-like_dom
IPR036179, Ig-like_dom_sf
IPR013783, Ig-like_fold
IPR013098, Ig_I-set
IPR003599, Ig_sub
IPR003598, Ig_sub2
IPR011009, Kinase-like_dom_sf
IPR000719, Prot_kinase_dom
IPR017441, Protein_kinase_ATP_BS
IPR001245, Ser-Thr/Tyr_kinase_cat_dom
IPR008266, Tyr_kinase_AS
IPR020635, Tyr_kinase_cat_dom
PfamiView protein in Pfam
PF07679, I-set, 3 hits
PF07714, PK_Tyr_Ser-Thr, 1 hit
PRINTSiPR00109, TYRKINASE
SMARTiView protein in SMART
SM00409, IG, 3 hits
SM00408, IGc2, 3 hits
SM00219, TyrKc, 1 hit
SUPFAMiSSF48726, SSF48726, 3 hits
SSF56112, SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50835, IG_LIKE, 3 hits
PS00107, PROTEIN_KINASE_ATP, 1 hit
PS50011, PROTEIN_KINASE_DOM, 1 hit
PS00109, PROTEIN_KINASE_TYR, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiEGL15_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: Q10656
Secondary accession number(s): Q7JL68
, Q7YZM7, Q7YZM8, Q7YZN0, Q7YZN1, Q7Z025, Q8MQ14, Q93804, Q95QE0, Q95QE1
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: December 2, 2020
This is version 182 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry 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

Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families
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