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Protein

Insulin-like receptor

Gene

daf-2

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

Functioni

Insulin receptor-like tyrosine kinase which regulates metabolism, controls longevity and prevents developmental arrest at the dauer stage (PubMed:9252323, PubMed:9790527, PubMed:24332851). Binding of INS family members may either stimulate, or antagonize, association of the receptor with downstream mediators such as pdk-1 and age-1 (PubMed:11274053). Required for germline progenitor proliferation during larval development (PubMed:22278922). Required for the response to environmental stimuli such as food, pheromone, and temperature. Negatively regulates resistance to UV and oxidative stress (PubMed:24332851). Role in immune function and pathogen resistance (PubMed:18782349). Negatively regulates autophagy (PubMed:22560223).7 Publications

Catalytic activityi

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

Cofactori

Mg2+Curated

Enzyme regulationi

Autophosphorylation activates the kinase activity (By similarity). Interaction with shc-1 may inhibits its activity (PubMed:18832074).By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1282 – 12821ATPPROSITE-ProRule annotationBy similarity
Active sitei1388 – 13881Proton acceptorPROSITE-ProRule annotationBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi1252 – 12609ATPPROSITE-ProRule annotationBy similarity

GO - Molecular functioni

  • ATP binding Source: WormBase
  • insulin-activated receptor activity Source: WormBase
  • metal ion binding Source: UniProtKB-KW
  • peptide hormone binding Source: WormBase
  • protein kinase binding Source: WormBase
  • PTB domain binding Source: WormBase
  • SH2 domain binding Source: WormBase

GO - Biological processi

  • carbohydrate metabolic process Source: UniProtKB-KW
  • dauer entry Source: UniProtKB
  • dauer exit Source: WormBase
  • dauer larval development Source: WormBase
  • determination of adult lifespan Source: WormBase
  • innate immune response Source: UniProtKB-KW
  • insulin receptor signaling pathway Source: WormBase
  • larval feeding behavior Source: UniProtKB
  • negative regulation of transcription factor import into nucleus Source: WormBase
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of multicellular organism growth Source: WormBase
  • protein autophosphorylation Source: WormBase
  • regulation of autophagosome assembly Source: BHF-UCL
  • regulation of dauer larval development Source: UniProtKB
  • regulation of development, heterochronic Source: WormBase
  • regulation of eating behavior Source: UniProtKB
  • regulation of response to reactive oxygen species Source: WormBase
  • reproduction Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

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

Keywords - Biological processi

Carbohydrate metabolism, Immunity, Innate immunity

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiR-CEL-77387. Insulin receptor recycling.
SignaLinkiQ968Y9.

Names & Taxonomyi

Protein namesi
Recommended name:
Insulin-like receptorBy similarity (EC:2.7.10.1)
Short name:
IRBy similarity
Alternative name(s):
Abnormal dauer formation protein 21 Publication
Cleaved into the following 2 chains:
Insulin-like receptor subunit alphaBy similarity
Insulin-like receptor subunit betaBy similarity
Gene namesi
Name:daf-2
ORF Names:Y55D5A.5
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiY55D5A.5a; CE27499; WBGene00000898; daf-2.
Y55D5A.5b; CE42198; WBGene00000898; daf-2.

Subcellular locationi

  • Membrane By similarity; Single-pass type I membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini970 – 1183214ExtracellularSequence analysisAdd
BLAST
Transmembranei1184 – 120421HelicalSequence analysisAdd
BLAST
Topological domaini1205 – 1846642CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • axon Source: WormBase
  • cytoplasm Source: WormBase
  • cytoplasmic vesicle Source: WormBase
  • neuronal cell body Source: WormBase
  • nonmotile primary cilium Source: WormBase
  • spanning component of plasma membrane Source: WormBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Disruption phenotypei

Accumulation of fat, pigmented intestine, increased lifespan, increased dauer formation and increased resistance to pathogens. Severe loss of function mutants display recessive early embryonic lethality (PubMed:9252323, PubMed:9790527, PubMed:11274053, PubMed:18782349, PubMed:18245374). RNAi-mediated knockdown in germline, hypodermis, intestine or in muscles causes increased lifespan (PubMed:24332851). RNAi-mediated knockdown in adults causes an increase in lgg-1 positive autophagic vesicles (PubMed:22560223).7 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi146 – 1461C → Y: Embronically lethal. 1 Publication
Mutagenesisi401 – 4011C → Y: Dauer formation; when associated with L-470. 1 Publication
Mutagenesisi469 – 4691C → S: Dauer formation above 20 degrees Celsius. 1 Publication
Mutagenesisi470 – 4701P → L: Dauer formation; when associated with Y-401. 1 Publication
Mutagenesisi573 – 5731S → L: Dauer formation above 25 degrees Celsius. 1 Publication
Mutagenesisi580 – 5801A → T: Dauer formation above 26 degrees Celsius. 1 Publication
Mutagenesisi648 – 6481D → N: Dauer formation above 25 degrees Celsius. 1 Publication
Mutagenesisi1374 – 13741D → N: Dauer formation above 20 degrees Celsius. 1 Publication
Mutagenesisi1434 – 14341P → L in e1391; dauer formation above 20 degrees Celsius and increased lifespan. 2 Publications
Mutagenesisi1465 – 14651P → S in e1370; extended lifespan. Accumulates fat and undergoes dauer formation above 25 degrees Celsius. Pigmented intestine and increased resistance to bacterial pathogens, UV, high temperature and paraquat treatment. Reduced number of germline progenitors during larval development. 7 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 966Insulin-like receptor subunit alphaSequence analysisPRO_0000386619
Signal peptidei1 – ?Sequence analysis
Chaini970 – 1846877Insulin-like receptor subunit betaSequence analysisPRO_0000386620Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi113 – 1131N-linked (GlcNAc...)Sequence analysis
Glycosylationi180 – 1801N-linked (GlcNAc...)Sequence analysis
Glycosylationi364 – 3641N-linked (GlcNAc...)1 Publication
Disulfide bondi371 ↔ 386By similarity
Disulfide bondi393 ↔ 401By similarity
Disulfide bondi397 ↔ 410By similarity
Disulfide bondi413 ↔ 422By similarity
Disulfide bondi426 ↔ 438By similarity
Glycosylationi453 – 4531N-linked (GlcNAc...)1 Publication
Disulfide bondi469 ↔ 483By similarity
Disulfide bondi486 ↔ 490By similarity
Glycosylationi518 – 5181N-linked (GlcNAc...)Sequence analysis
Disulfide bondi615 ↔ 646By similarity
Glycosylationi652 – 6521N-linked (GlcNAc...)Sequence analysis
Glycosylationi671 – 6711N-linked (GlcNAc...)Sequence analysis
Glycosylationi696 – 6961N-linked (GlcNAc...)1 Publication
Disulfide bondi706 – 706InterchainBy similarity
Glycosylationi1017 – 10171N-linked (GlcNAc...)1 Publication
Glycosylationi1047 – 10471N-linked (GlcNAc...)Sequence analysis
Glycosylationi1078 – 10781N-linked (GlcNAc...)1 Publication
Glycosylationi1087 – 10871N-linked (GlcNAc...)Sequence analysis
Glycosylationi1093 – 10931N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ968Y9.
PaxDbiQ968Y9.

Interactioni

Subunit structurei

Tetramer of 2 alpha and 2 beta chains linked by disulfide bonds. The alpha chains contribute to the formation of the ligand-binding domain, while the beta chains carry the kinase domain (By similarity). Interacts (via cytoplasmic domain) with shc-1 (PID domain) (PubMed:18832074).By similarity1 Publication

GO - Molecular functioni

  • protein kinase binding Source: WormBase
  • PTB domain binding Source: WormBase
  • SH2 domain binding Source: WormBase

Protein-protein interaction databases

BioGridi40655. 164 interactions.
STRINGi6239.Y55D5A.5a.

Structurei

3D structure databases

ProteinModelPortaliQ968Y9.
SMRiQ968Y9. Positions 180-917, 1026-1596.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini775 – 86995Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini969 – 106799Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini1077 – 1179103Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini1246 – 1528283Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.PROSITE-ProRule annotation
Contains 3 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4258. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000151241.
InParanoidiQ968Y9.
KOiK04527.
OMAiVINIRNG.
OrthoDBiEOG73RB9N.
PhylomeDBiQ968Y9.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
3.80.20.20. 3 hits.
InterProiIPR003961. FN3_dom.
IPR006211. Furin-like_Cys-rich_dom.
IPR009030. Growth_fac_rcpt_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR000719. Prot_kinase_dom.
IPR000494. Rcpt_L-dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00060. FN3. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 3 hits.
SSF52058. SSF52058. 3 hits.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS50853. FN3. 3 hits.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform a2 Publications (identifier: Q968Y9-1) [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
MTRMNIVRCR RRHKILENLE EENLGPSCSS TTSTTAATEA LGTTTEDMRL
60 70 80 90 100
KQQRSSSRAT EHDIVDGNHH DDEHITMRRL RLVKNSRTRR RTTPDSSMDC
110 120 130 140 150
YEENPPSQKT SINYSWISKK SSMTSLMLLL LFAFVQPCAS IVEKRCGPID
160 170 180 190 200
IRNRPWDIKP QWSKLGDPNE KDLAGQRMVN CTVVEGSLTI SFVLKHKTKA
210 220 230 240 250
QEEMHRSLQP RYSQDEFITF PHLREITGTL LVFETEGLVD LRKIFPNLRV
260 270 280 290 300
IGGRSLIQHY ALIIYRNPDL EIGLDKLSVI RNGGVRIIDN RKLCYTKTID
310 320 330 340 350
WKHLITSSIN DVVVDNAAEY AVTETGLMCP RGACEEDKGE SKCHYLEEKN
360 370 380 390 400
QEQGVERVQS CWSNTTCQKS CAYDRLLPTK EIGPGCDANG DRCHDQCVGG
410 420 430 440 450
CERVNDATAC HACKNVYHKG KCIEKCDAHL YLLLQRRCVT REQCLQLNPV
460 470 480 490 500
LSNKTVPIKA TAGLCSDKCP DGYQINPDDH RECRKCVGKC EIVCEINHVI
510 520 530 540 550
DTFPKAQAIR LCNIIDGNLT IEIRGKQDSG MASELKDIFA NIHTITGYLL
560 570 580 590 600
VRQSSPFISL NMFRNLRRIE AKSLFRNLYA ITVFENPNLK KLFDSTTDLT
610 620 630 640 650
LDRGTVSIAN NKMLCFKYIK QLMSKLNIPL DPIDQSEGTN GEKAICEDMA
660 670 680 690 700
INVSITAVNA DSVFFSWPSF NITDIDQRKF LGYELFFKEV PRIDENMTIE
710 720 730 740 750
EDRSACVDSW QSVFKQYYET SNGEPTPDIF MDIGPRERIR PNTLYAYYVA
760 770 780 790 800
TQMVLHAGAK NGVSKIGFVR TSYYTPDPPT LALAQVDSDA IHITWEAPLQ
810 820 830 840 850
PNGDLTHYTI MWRENEVSPY EEAEKFCTDA STPANRQHTK DPKETIVADK
860 870 880 890 900
PVDIPSSRTV APTLLTMMGH EDQQKTCAAT PGCCSCSAIE ESSEQNKKKR
910 920 930 940 950
PDPMSAIESS AFENKLLDEV LMPRDTMRVR RSIEDANRVS EELEKAENLG
960 970 980 990 1000
KAPKTLGGKK PLIHISKKKP SSSSTTSTPA PTIASMYALT RKPTTVPGTR
1010 1020 1030 1040 1050
IRLYEIYEPL PGSWAINVSA LALDNSYVIR NLKHYTLYAI SLSACQNMTV
1060 1070 1080 1090 1100
PGASCSISHR AGALKRTKHI TDIDKVLNET IEWRFMNNSQ QVNVTWDPPT
1110 1120 1130 1140 1150
EVNGGIFGYV VKLKSKVDGS IVMTRCVGAK RGYSTRNQGV LFQNLADGRY
1160 1170 1180 1190 1200
FVSVTATSVH GAGPEAESSD PIVVMTPGFF TVEIILGMLL VFLILMSIAG
1210 1220 1230 1240 1250
CIIYYYIQVR YGKKVKALSD FMQLNPEYCV DNKYNADDWE LRQDDVVLGQ
1260 1270 1280 1290 1300
QCGEGSFGKV YLGTGNNVVS LMGDRFGPCA IKINVDDPAS TENLNYLMEA
1310 1320 1330 1340 1350
NIMKNFKTNF IVKLYGVIST VQPAMVVMEM MDLGNLRDYL RSKREDEVFN
1360 1370 1380 1390 1400
ETDCNFFDII PRDKFHEWAA QICDGMAYLE SLKFCHRDLA ARNCMINRDE
1410 1420 1430 1440 1450
TVKIGDFGMA RDLFYHDYYK PSGKRMMPVR WMSPESLKDG KFDSKSDVWS
1460 1470 1480 1490 1500
FGVVLYEMVT LGAQPYIGLS NDEVLNYIGM ARKVIKKPEC CENYWYKVMK
1510 1520 1530 1540 1550
MCWRYSPRDR PTFLQLVHLL AAEASPEFRD LSFVLTDNQM ILDDSEALDL
1560 1570 1580 1590 1600
DDIDDTDMND QVVEVAPDVE NVEVQSDSER RNTDSIPLKQ FKTIPPINAT
1610 1620 1630 1640 1650
TSHSTISIDE TPMKAKQREG SLDEEYALMN HSGGPSDAEV RTYAGDGDYV
1660 1670 1680 1690 1700
ERDVRENDVP TRRNTGASTS SYTGGGPYCL TNRGGSNERG AGFGEAVRLT
1710 1720 1730 1740 1750
DGVGSGHLND DDYVEKEISS MDTRRSTGAS SSSYGVPQTN WSGNRGATYY
1760 1770 1780 1790 1800
TSKAQQAATA AAAAAAALQQ QQNGGRGDRL TQLPGTGHLQ STRGGQDGDY
1810 1820 1830 1840
IETEPKNYRN NGSPSRNGNS RDIFNGRSAF GENEHLIEDN EHHPLV
Length:1,846
Mass (Da):207,124
Last modified:November 3, 2009 - v2
Checksum:i230B28322FF0F126
GO
Isoform b1 Publication (identifier: Q968Y9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     925-1020: DTMRVRRSIE...PGSWAINVSA → CDIKNDPVGC...HDLMMSVMHD
     1021-1846: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:1,020
Mass (Da):115,345
Checksum:i0CAECAF111DF3E2A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti838 – 8381H → R in AAC47715 (PubMed:9252323).Curated
Sequence conflicti1313 – 13131K → Q in AAC47715 (PubMed:9252323).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei925 – 102096DTMRV…INVSA → CDIKNDPVGCAMLLLPPEID DSDVGDDDEEPGGGSEQQQR ILRNSEILKRQKRQILGRSL GGIHGIRSIGRKEYEQFADM ILYGNLHDLMMSVMHD in isoform b. 1 PublicationVSP_053157Add
BLAST
Alternative sequencei1021 – 1846826Missing in isoform b. 1 PublicationVSP_053158Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF012437 mRNA. Translation: AAC47715.1.
FO081525 Genomic DNA. Translation: CCD72201.2.
FO081525 Genomic DNA. Translation: CCD72203.2.
PIRiT42047.
RefSeqiNP_497650.4. NM_065249.4. [Q968Y9-1]
UniGeneiCel.8775.

Genome annotation databases

EnsemblMetazoaiY55D5A.5a; Y55D5A.5a; WBGene00000898. [Q968Y9-1]
GeneIDi175410.
KEGGicel:CELE_Y55D5A.5.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF012437 mRNA. Translation: AAC47715.1.
FO081525 Genomic DNA. Translation: CCD72201.2.
FO081525 Genomic DNA. Translation: CCD72203.2.
PIRiT42047.
RefSeqiNP_497650.4. NM_065249.4. [Q968Y9-1]
UniGeneiCel.8775.

3D structure databases

ProteinModelPortaliQ968Y9.
SMRiQ968Y9. Positions 180-917, 1026-1596.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi40655. 164 interactions.
STRINGi6239.Y55D5A.5a.

Proteomic databases

EPDiQ968Y9.
PaxDbiQ968Y9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiY55D5A.5a; Y55D5A.5a; WBGene00000898. [Q968Y9-1]
GeneIDi175410.
KEGGicel:CELE_Y55D5A.5.

Organism-specific databases

CTDi175410.
WormBaseiY55D5A.5a; CE27499; WBGene00000898; daf-2.
Y55D5A.5b; CE42198; WBGene00000898; daf-2.

Phylogenomic databases

eggNOGiKOG4258. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118818.
HOGENOMiHOG000151241.
InParanoidiQ968Y9.
KOiK04527.
OMAiVINIRNG.
OrthoDBiEOG73RB9N.
PhylomeDBiQ968Y9.

Enzyme and pathway databases

ReactomeiR-CEL-77387. Insulin receptor recycling.
SignaLinkiQ968Y9.

Miscellaneous databases

NextBioi888038.
PROiQ968Y9.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
3.80.20.20. 3 hits.
InterProiIPR003961. FN3_dom.
IPR006211. Furin-like_Cys-rich_dom.
IPR009030. Growth_fac_rcpt_.
IPR013783. Ig-like_fold.
IPR011009. Kinase-like_dom.
IPR032675. L_dom-like.
IPR000719. Prot_kinase_dom.
IPR000494. Rcpt_L-dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PRINTSiPR00109. TYRKINASE.
SMARTiSM00060. FN3. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 3 hits.
SSF52058. SSF52058. 3 hits.
SSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 1 hit.
PROSITEiPS50853. FN3. 3 hits.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "daf-2, an insulin receptor-like gene that regulates longevity and diapause in Caenorhabditis elegans."
    Kimura K.D., Tissenbaum H.A., Liu Y., Ruvkun G.
    Science 277:942-946(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-401; CYS-469; PRO-470; SER-573; ASP-648; ASP-1374; PRO-1434 AND PRO-1465.
    Strain: Bristol N2Imported.
  2. "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.
  3. "Cell nonautonomy of C. elegans daf-2 function in the regulation of diapause and life span."
    Apfeld J., Kenyon C.
    Cell 95:199-210(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF PRO-1465.
  4. "Regulation of DAF-2 receptor signaling by human insulin and ins-1, a member of the unusually large and diverse C. elegans insulin gene family."
    Pierce S.B., Costa M., Wisotzkey R., Devadhar S., Homburger S.A., Buchman A.R., Ferguson K.C., Heller J., Platt D.M., Pasquinelli A.A., Liu L.X., Doberstein S.K., Ruvkun G.
    Genes Dev. 15:672-686(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ALA-580 AND PRO-1465.
  5. "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins."
    Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T.
    Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-364; ASN-453; ASN-696; ASN-1017 AND ASN-1078, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Bristol N2.
  6. "The DAF-2 insulin-like signaling pathway independently regulates aging and immunity in C. elegans."
    Evans E.A., Chen W.C., Tan M.-W.
    Aging Cell 7:879-893(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF PRO-1465.
  7. "SHC-1/p52Shc targets the insulin/IGF-1 and JNK signaling pathways to modulate life span and stress response in C. elegans."
    Neumann-Haefelin E., Qi W., Finkbeiner E., Walz G., Baumeister R., Hertweck M.
    Genes Dev. 22:2721-2735(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH SHC-1.
  8. "Clustering of genetically defined allele classes in the Caenorhabditis elegans DAF-2 insulin/IGF-1 receptor."
    Patel D.S., Garza-Garcia A., Nanji M., McElwee J.J., Ackerman D., Driscoll P.C., Gems D.
    Genetics 178:931-946(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-146 AND PRO-1465.
  9. "TOR signaling and rapamycin influence longevity by regulating SKN-1/Nrf and DAF-16/FoxO."
    Robida-Stubbs S., Glover-Cutter K., Lamming D.W., Mizunuma M., Narasimhan S.D., Neumann-Haefelin E., Sabatini D.M., Blackwell T.K.
    Cell Metab. 15:713-724(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  10. "S6K links cell fate, cell cycle and nutrient response in C. elegans germline stem/progenitor cells."
    Korta D.Z., Tuck S., Hubbard E.J.
    Development 139:859-870(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF PRO-1465.
  11. "Germline signaling mediates the synergistically prolonged longevity produced by double mutations in daf-2 and rsks-1 in C. elegans."
    Chen D., Li P.W., Goldstein B.A., Cai W., Thomas E.L., Chen F., Hubbard A.E., Melov S., Kapahi P.
    Cell Rep. 5:1600-1610(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF PRO-1434 AND PRO-1465.

Entry informationi

Entry nameiINSR_CAEEL
AccessioniPrimary (citable) accession number: Q968Y9
Secondary accession number(s): B5QS63, O16131
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: November 3, 2009
Last modified: April 13, 2016
This is version 129 of the entry and version 2 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

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 one 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.