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Protein

Myoblast growth factor receptor egl-15

Gene

egl-15

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Activation leads to the phosphorylation of SOC-1 on Tyr-408 triggering PTP-2 recruitment and/or activation. Activates the SEM-5/SOS-1/RAS/MAPK pathway (PubMed:11689700). Acts in the hypodermis to regulate axon growth (PubMed:12835392). Activates protein degradation in muscles (PubMed:14517244). Plays a role in fluid homeostasis by acting in the hypodermis and also has a role in larval development (PubMed:7585964). Isoform b has no effect on axon growth but affects the maintenance of axon position. Isoform b interaction with egl-17 is required for the guidance of sex myoblast migration during gonad development (PubMed:12835392). Isoforms a, c, d and e interaction with let-756 appears to play a role in maintaining body morphology at higher temperatures (PubMed:12835392).4 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Cofactori

Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei672 – 6721ATPPROSITE-ProRule annotation
Active sitei797 – 7971Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi646 – 6549ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • cell migration Source: WormBase
  • digestive tract morphogenesis Source: WormBase
  • fibroblast growth factor receptor signaling pathway Source: WormBase
  • muscle organ development Source: WormBase
  • nematode larval development Source: WormBase
  • oviposition Source: WormBase
  • protein phosphorylation Source: WormBase
  • regulation of cell projection organization Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 1045.
ReactomeiREACT_276818. PI3K Cascade.
REACT_279166. PIP3 activates AKT signaling.
REACT_281505. NCAM signaling for neurite out-growth.
REACT_283773. FGFR3b ligand binding and activation.
REACT_293065. FGFR1b ligand binding and activation.
REACT_294720. FGFR2b ligand binding and activation.
REACT_304028. Signal transduction by L1.
REACT_307540. FGFR3c ligand binding and activation.
REACT_333894. FGFR1c ligand binding and activation.
REACT_344035. FGFR2c ligand binding and activation.
REACT_344187. FGFR4 ligand binding and activation.
REACT_357181. SHC-mediated cascade:FGFR2.
REACT_357529. Negative regulation of FGFR2 signaling.
REACT_358113. Phospholipase C-mediated cascade, FGFR2.
REACT_359513. SHC-mediated cascade:FGFR1.
REACT_359955. FRS-mediated FGFR1 signaling.
REACT_360021. Negative regulation of FGFR3 signaling.
REACT_360255. PI-3K cascade:FGFR3.
REACT_360528. PI-3K cascade:FGFR1.
REACT_360607. Phospholipase C-mediated cascade, FGFR4.
REACT_360622. PI-3K cascade:FGFR4.
REACT_360734. Negative regulation of FGFR1 signaling.
REACT_361013. Negative regulation of FGFR4 signaling.
REACT_361068. FRS-mediated FGFR2 signaling.
REACT_361142. Phospholipase C-mediated cascade: FGFR1.
REACT_361163. SHC-mediated cascade:FGFR4.
REACT_361184. Phospholipase C-mediated cascade, FGFR3.
REACT_361511. PI-3K cascade:FGFR2.
REACT_361868. SHC-mediated cascade:FGFR3.
REACT_362258. FRS-mediated FGFR3 signaling.
REACT_362611. FRS2-mediated FGFR4 signaling.
SignaLinkiQ10656.

Names & Taxonomyi

Protein namesi
Recommended name:
Myoblast growth factor receptor egl-15 (EC:2.7.10.1)
Alternative name(s):
Egg-laying defective protein 15
Gene namesi
Name:egl-15
ORF Names:F58A3.2
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940 Componenti: Chromosome X

Organism-specific databases

WormBaseiF58A3.2a; CE28238; WBGene00001184; egl-15.
F58A3.2b; CE35726; WBGene00001184; egl-15.
F58A3.2c; CE41325; WBGene00001184; egl-15.
F58A3.2d; CE31549; WBGene00001184; egl-15.
F58A3.2e; CE35727; WBGene00001184; egl-15.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 525506ExtracellularSequence AnalysisAdd
BLAST
Transmembranei526 – 54924HelicalSequence AnalysisAdd
BLAST
Topological domaini550 – 1040491CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cell Source: WormBase
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Disruption phenotypei

Early arrest in larval development. Impaired guided migration of sex myoblasts.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi680 – 6801E → K in N1775; loss of activity. 1 Publication
Mutagenesisi714 – 7141P → L in N1783; loss of activity. 1 Publication
Mutagenesisi930 – 9301W → * in N1477ts; loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 10401021Myoblast growth factor receptor egl-15PRO_0000016796Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi55 ↔ 109PROSITE-ProRule annotation
Glycosylationi121 – 1211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi280 – 2801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi299 – 2991N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi314 ↔ 367PROSITE-ProRule annotation
Glycosylationi401 – 4011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi407 – 4071N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi414 ↔ 485PROSITE-ProRule annotation
Glycosylationi433 – 4331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi440 – 4401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi449 – 4491N-linked (GlcNAc...)Sequence Analysis
Glycosylationi474 – 4741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi497 – 4971N-linked (GlcNAc...)Sequence Analysis
Modified residuei828 – 8281Phosphotyrosine; by autocatalysisBy similarity

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

PaxDbiQ10656.
PRIDEiQ10656.

Expressioni

Developmental stagei

Expressed in the hypodermal membrane during the larval stage.1 Publication

Interactioni

Protein-protein interaction databases

BioGridi46202. 148 interactions.
IntActiQ10656. 1 interaction.
STRINGi6239.F58A3.2c.

Structurei

3D structure databases

ProteinModelPortaliQ10656.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 12593Ig-like C2-type 1Add
BLAST
Domaini287 – 38397Ig-like C2-type 2Add
BLAST
Domaini391 – 501111Ig-like C2-type 3Add
BLAST
Domaini640 – 931292Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118923.
InParanoidiQ10656.
OMAiVELCKHG.
PhylomeDBiQ10656.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
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.
[Graphical view]
PfamiPF07679. I-set. 3 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00409. IG. 1 hit.
SM00408. IGc2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50835. IG_LIKE. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

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

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti551 – 5511Q → G in AAP44084 (PubMed:12835392).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei129 – 245117FCDYF…PSESR → PLKLFDWLTEHRVFDISHLL PKLLPPAEMRRVKSQLGGWE KMNNEQKIVRARHILRLRQI NHALG in isoform b. 1 PublicationVSP_019861Add
BLAST
Alternative sequencei829 – 8291R → RL in isoform c, isoform d and isoform e. 1 PublicationVSP_002991
Alternative sequencei984 – 9841E → EVDQN in isoform c, isoform d and isoform e. 1 PublicationVSP_002992
Alternative sequencei1027 – 104014RIPSN…SKPEF → LYIHKVLNEPIGNGYVRQDK LARAVSGVANQSLDSALGSP AWPSYDRPSNKASCLDQTHQ YYNTTSKIQYLHFTFDDPDC MTRSRDSAIFEESYHPNYIQ SHPLYSKIIIKKNMTPRNPL PTKETIV in isoform c. 1 PublicationVSP_002994Add
BLAST
Alternative sequencei1027 – 104014RIPSN…SKPEF → LYIHKVLNEPIGNGYVRQDK LARAVSGVANQSLDSALGSP AWPSYDRPSNKASCLDDEKH HYYYS in isoform d. 1 PublicationVSP_019862Add
BLAST
Alternative sequencei1027 – 104014RIPSN…SKPEF → LYIHKVLNEPIGNGSNSPVL in isoform e. 1 PublicationVSP_019863Add
BLAST

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. [Q10656-2]
NP_001024724.2. NM_001029553.4. [Q10656-3]
NP_001024725.1. NM_001029554.3. [Q10656-4]
NP_001024726.1. NM_001029555.3. [Q10656-5]
NP_509842.2. NM_077441.6. [Q10656-1]
UniGeneiCel.17140.

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]
GeneIDi181291.
KEGGicel:CELE_F58A3.2.
UCSCiF58A3.2e. c. elegans. [Q10656-1]

Keywords - Coding sequence diversityi

Alternative splicing

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. [Q10656-2]
NP_001024724.2. NM_001029553.4. [Q10656-3]
NP_001024725.1. NM_001029554.3. [Q10656-4]
NP_001024726.1. NM_001029555.3. [Q10656-5]
NP_509842.2. NM_077441.6. [Q10656-1]
UniGeneiCel.17140.

3D structure databases

ProteinModelPortaliQ10656.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi46202. 148 interactions.
IntActiQ10656. 1 interaction.
STRINGi6239.F58A3.2c.

Proteomic databases

PaxDbiQ10656.
PRIDEiQ10656.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]
GeneIDi181291.
KEGGicel:CELE_F58A3.2.
UCSCiF58A3.2e. c. elegans. [Q10656-1]

Organism-specific databases

CTDi181291.
WormBaseiF58A3.2a; CE28238; WBGene00001184; egl-15.
F58A3.2b; CE35726; WBGene00001184; egl-15.
F58A3.2c; CE41325; WBGene00001184; egl-15.
F58A3.2d; CE31549; WBGene00001184; egl-15.
F58A3.2e; CE35727; WBGene00001184; egl-15.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118923.
InParanoidiQ10656.
OMAiVELCKHG.
PhylomeDBiQ10656.

Enzyme and pathway databases

BRENDAi2.7.10.1. 1045.
ReactomeiREACT_276818. PI3K Cascade.
REACT_279166. PIP3 activates AKT signaling.
REACT_281505. NCAM signaling for neurite out-growth.
REACT_283773. FGFR3b ligand binding and activation.
REACT_293065. FGFR1b ligand binding and activation.
REACT_294720. FGFR2b ligand binding and activation.
REACT_304028. Signal transduction by L1.
REACT_307540. FGFR3c ligand binding and activation.
REACT_333894. FGFR1c ligand binding and activation.
REACT_344035. FGFR2c ligand binding and activation.
REACT_344187. FGFR4 ligand binding and activation.
REACT_357181. SHC-mediated cascade:FGFR2.
REACT_357529. Negative regulation of FGFR2 signaling.
REACT_358113. Phospholipase C-mediated cascade, FGFR2.
REACT_359513. SHC-mediated cascade:FGFR1.
REACT_359955. FRS-mediated FGFR1 signaling.
REACT_360021. Negative regulation of FGFR3 signaling.
REACT_360255. PI-3K cascade:FGFR3.
REACT_360528. PI-3K cascade:FGFR1.
REACT_360607. Phospholipase C-mediated cascade, FGFR4.
REACT_360622. PI-3K cascade:FGFR4.
REACT_360734. Negative regulation of FGFR1 signaling.
REACT_361013. Negative regulation of FGFR4 signaling.
REACT_361068. FRS-mediated FGFR2 signaling.
REACT_361142. Phospholipase C-mediated cascade: FGFR1.
REACT_361163. SHC-mediated cascade:FGFR4.
REACT_361184. Phospholipase C-mediated cascade, FGFR3.
REACT_361511. PI-3K cascade:FGFR2.
REACT_361868. SHC-mediated cascade:FGFR3.
REACT_362258. FRS-mediated FGFR3 signaling.
REACT_362611. FRS2-mediated FGFR4 signaling.
SignaLinkiQ10656.

Miscellaneous databases

NextBioi913304.
PROiQ10656.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
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.
[Graphical view]
PfamiPF07679. I-set. 3 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00409. IG. 1 hit.
SM00408. IGc2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS50835. IG_LIKE. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An FGF receptor signaling pathway is required for the normal cell migrations of the sex myoblasts in C. elegans hermaphrodites."
    Devore D.L., Horvitz H.R., Stern M.J.
    Cell 83:611-620(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLU-680; PRO-714 AND TRP-930.
    Strain: Bristol N2.
  2. "Alternative splicing affecting a novel domain in the C. elegans EGL-15 FGF receptor confers functional specificity."
    Goodman S.J., Branda C.S., Robinson M.K., Burdine R.D., Stern M.J.
    Development 130:3757-3766(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), NUCLEOTIDE SEQUENCE [MRNA] OF 932-1040 (ISOFORMS A; C; D AND E), FUNCTION.
  3. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING.
    Strain: Bristol N2.
  4. "clr-1 encodes a receptor tyrosine phosphatase that negatively regulates an FGF receptor signaling pathway in Caenorhabditis elegans."
    Kokel M., Borland C.Z., DeLong L., Horvitz H.R., Stern M.J.
    Genes Dev. 12:1425-1437(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEPHOSPHORYLATION BY CLR-1.
    Strain: Bristol N2.
  5. "The Caenorhabditis elegans EGL-15 signaling pathway implicates a DOS-like multisubstrate adaptor protein in fibroblast growth factor signal transduction."
    Schutzman J.L., Borland C.Z., Newman J.C., Robinson M.K., Kokel M., Stern M.J.
    Mol. Cell. Biol. 21:8104-8116(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE.
  6. "Activated EGL-15 FGF receptor promotes protein degradation in muscles of Caenorhabditis elegans."
    Szewczyk N.J., Jacobson L.A.
    EMBO J. 22:5058-5067(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiEGL15_CAEEL
AccessioniPrimary (citable) accession number: Q10656
Secondary accession number(s): Q7JL68
, Q7YZM7, Q7YZM8, Q7YZN0, Q7YZN1, Q7Z025, Q8MQ14, Q93804, Q95QE0, Q95QE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 22, 2015
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.