INSR_DROME - dbPTM
INSR_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID INSR_DROME
UniProt AC P09208
Protein Name Insulin-like receptor
Gene Name InR
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 2144
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Has a ligand-stimulated tyrosine-protein kinase activity. Required for cell survival. Regulates body size and organ size by altering cell number and cell size in a cell-autonomous manner. Involved in the development of the embryonic nervous system, and is necessary for axon guidance and targeting in the visual system. Also plays a role in life-span determination..
Protein Sequence MFNMPRGVTKSKSKRGKIKMENDMAAAATTTACTLGHICVLCRQEMLLDTCCCRQAVEAVDSPASSEEAYSSSNSSSCQASSEISAEEVWFLSHDDIVLCRRPKFDEVETTGKKRDVKCSGHQCSNECDDGSTKNNRQQRENFNIFSNCHNILRTLQSLLLLMFNCGIFNKRRRRQHQQQHHHHYQHHHQQHHQQHHQRQQANVSYTKFLLLLQTLAAATTRLSLSPKNYKQQQQLQHNQQLPRATPQQKQQEKDRHKCFHYKHNYSYSPGISLLLFILLANTLAIQAVVLPAHQQHLLHNDIADGLDKTALSVSGTQSRWTRSESNPTMRLSQNVKPCKSMDIRNMVSHFNQLENCTVIEGFLLIDLINDASPLNRSFPKLTEVTDYIIIYRVTGLHSLSKIFPNLSVIRGNKLFDGYALVVYSNFDLMDLGLHKLRSITRGGVRIEKNHKLCYDRTIDWLEILAENETQLVVLTENGKEKECRLSKCPGEIRIEEGHDTTAIEGELNASCQLHNNRRLCWNSKLCQTKCPEKCRNNCIDEHTCCSQDCLGGCVIDKNGNESCISCRNVSFNNICMDSCPKGYYQFDSRCVTANECITLTKFETNSVYSGIPYNGQCITHCPTGYQKSENKRMCEPCPGGKCDKECSSGLIDSLERAREFHGCTIITGTEPLTISIKRESGAHVMDELKYGLAAVHKIQSSLMVHLTYGLKSLKFFQSLTEISGDPPMDADKYALYVLDNRDLDELWGPNQTVFIRKGGVFFHFNPKLCVSTINQLLPMLASKPKFFEKSDVGADSNGNRGSCGTAVLNVTLQSVGANSAMLNVTTKVEIGEPQKPSNATIVFKDPRAFIGFVFYHMIDPYGNSTKSSDDPCDDRWKVSSPEKSGVMVLSNLIPYTNYSYYVRTMAISSELTNAESDVKNFRTNPGRPSKVTEVVATAISDSKINVTWSYLDKPYGVLTRYFIKAKLINRPTRNNNRDYCTEPLVKAMENDLPATTPTKKISDPLAGDCKCVEGSKKTSSQEYDDRKVQAGMEFENALQNFIFVPNIRKSKNGSSDKSDGAEGAALDSNAIPNGGATNPSRRRRDVALEPELDDVEGSVLLRHVRSITDDTDAFFEKDDENTYKDEEDLSSNKQFYEVFAKELPPNQTHFVFEKLRHFTRYAIFVVACREEIPSEKLRDTSFKKSLCSDYDTVFQTTKRKKFADIVMDLKVDLEHANNTESPVRVRWTPPVDPNGEIVTYEVAYKLQKPDQVEEKKCIPAADFNQTAGYLIKLNEGLYSFRVRANSIAGYGDFTEVEHIKVEPPPSYAKVFFWLLGIGLAFLIVSLFGYVCYLHKRKVPSNDLHMNTEVNPFYASMQYIPDDWEVLRENIIQLAPLGQGSFGMVYEGILKSFPPNGVDRECAIKTVNENATDRERTNFLSEASVMKEFDTYHVVRLLGVCSRGQPALVVMELMKKGDLKSYLRAHRPEERDEAMMTYLNRIGVTGNVQPPTYGRIYQMAIEIADGMAYLAAKKFVHRDLAARNCMVADDLTVKIGDFGMTRDIYETDYYRKGTKGLLPVRWMPPESLRDGVYSSASDVFSFGVVLWEMATLAAQPYQGLSNEQVLRYVIDGGVMERPENCPDFLHKLMQRCWHHRSSARPSFLDIIAYLEPQCPNSQFKEVSFYHSEAGLQHREKERKERNQLDAFAAVPLDQDLQDREQQEDATTPLRMGDYQQNSSLDQPPESPIAMVDDQGSHLPFSLPSGFIASSTPDGQTVMATAFQNIPAAQGDISATYVVPDADALDGDRGYEIYDPSPKCAELPTSRSGSTGGGKLSGEQHLLPRKGRQPTIMSSSMPDDVIGGSSLQPSTASAGSSNASSHTGRPSLKKTVADSVRNKANFINRHLFNHKRTGSNASHKSNASNAPSTSSNTNLTSHPVAMGNLGTIESGGSGSAGSYTGTPRFYTPSATPGGGSGMAISDNPNYRLLDESIASEQATILTTSSPNPNYEMMHPPTSLVSTNPNYMPMNETPVQMAGVTISHNPNYQPMQAPLNARQSQSSSDEDNEQEEDDEDEDDDVDDEHVEHIKMERMPLSRPRQRALPSKTQPPRSRSVSQTRKSPTNPNSGIGATGAGNRSNLLKENWLRPASTPRPPPPNGFIGREA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
74N-linked_GlycosylationEEAYSSSNSSSCQAS
HHHHHCCCCCCCCCC		48.10-
120PhosphorylationKKRDVKCSGHQCSNE
CCCCCCCCCCCCCCC		33.3222817900
125PhosphorylationKCSGHQCSNECDDGS
CCCCCCCCCCCCCCC		29.1522817900
133PhosphorylationNECDDGSTKNNRQQR
CCCCCCCCCCHHHHH		43.2322817900
203N-linked_GlycosylationHHQRQQANVSYTKFL
HHHHHHHHHHHHHHH		20.94-
265N-linked_GlycosylationKCFHYKHNYSYSPGI
HHHHHHCCCCCCCHH		24.24-
356N-linked_GlycosylationSHFNQLENCTVIEGF
HHHHHHCCCEEEECC		35.04-
376N-linked_GlycosylationINDASPLNRSFPKLT
HCCCCCCCCCCCCCH		40.72-
406N-linked_GlycosylationSLSKIFPNLSVIRGN
HHHHHCCCCEEEECC		33.91-
468N-linked_GlycosylationWLEILAENETQLVVL
HHHHHHCCCEEEEEE		52.59-
509N-linked_GlycosylationTAIEGELNASCQLHN
CCEECEECCEEEECC		26.04-
561N-linked_GlycosylationCVIDKNGNESCISCR
EEECCCCCCCCEECC		47.61-
569N-linked_GlycosylationESCISCRNVSFNNIC
CCCEECCCEEECCEE		37.80-
751N-linked_GlycosylationLDELWGPNQTVFIRK
HHHHCCCCCEEEEEE		46.33-
810N-linked_GlycosylationSCGTAVLNVTLQSVG
CCCCEEEEEEEEECC		20.37-
824N-linked_GlycosylationGANSAMLNVTTKVEI
CCCCCEEEEEEEEEC		18.9219349973
839N-linked_GlycosylationGEPQKPSNATIVFKD
CCCCCCCCCEEEECC		50.0219349973
864N-linked_GlycosylationHMIDPYGNSTKSSDD
EECCCCCCCCCCCCC		40.4319349973
898N-linked_GlycosylationSNLIPYTNYSYYVRT
CCCCCCCCCEEHHHH		20.2219349973
946N-linked_GlycosylationAISDSKINVTWSYLD
HHCCCCEEEEEECCC		28.98-
1053N-linked_GlycosylationPNIRKSKNGSSDKSD
CCCCCCCCCCCCCCC		63.77-
1109PhosphorylationLRHVRSITDDTDAFF
HHHHHCCCCCCCHHC		29.1222817900
1147N-linked_GlycosylationFAKELPPNQTHFVFE
HHHHCCCCCCCCHHH		58.4019349973
1218N-linked_GlycosylationKVDLEHANNTESPVR
EEEHHHCCCCCCCEE		58.8419349973
1219N-linked_GlycosylationVDLEHANNTESPVRV
EEHHHCCCCCCCEEE		46.1119349973
1265N-linked_GlycosylationCIPAADFNQTAGYLI
CCCHHHHCCCCCEEE		38.55-
1354PhosphorylationNTEVNPFYASMQYIP
CCCCCHHHHHCCCCC		10.06-
1545PhosphorylationFGMTRDIYETDYYRK
CCCCCCEEECCCCCC		19.6427626673
1549PhosphorylationRDIYETDYYRKGTKG
CCEEECCCCCCCCCC		16.7627626673
1550PhosphorylationDIYETDYYRKGTKGL
CEEECCCCCCCCCCC		14.5227626673
1816PhosphorylationSTGGGKLSGEQHLLP
CCCCCCCCCCCCCCC		43.7119429919
2097PhosphorylationRSRSVSQTRKSPTNP
CCCCCCCCCCCCCCC		32.3425749252
2100PhosphorylationSVSQTRKSPTNPNSG
CCCCCCCCCCCCCCC		33.4019429919
2102PhosphorylationSQTRKSPTNPNSGIG
CCCCCCCCCCCCCCC		71.1019429919
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of INSR_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of INSR_DROME !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of INSR_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
INSR_DROMEInRphysical
12702880
NOTCH_DROMENgenetic
23895933
HEP_DROMEhepgenetic
15820683
BUN1_DROMEbungenetic
26323255
BUN2_DROMEbungenetic
26323255
SESN_DROMESesngenetic
20203043
PDPK1_DROMEPdk1genetic
11752451
PTP61_DROMEPtp61Fgenetic
24752400
PTP61_DROMEPtp61Fgenetic
21707536
PTP61_DROMEPtp61Fgenetic
23339871
IMPL2_DROMEImpL2genetic
18412985
FNG_DROMEfnggenetic
23895933
FOXO_DROMEfoxogenetic
12908874
FOXO_DROMEfoxogenetic
21443682
FOXO_DROMEfoxogenetic
24690889
RL8_DROMERpL8genetic
18957936
RL36_DROMERpL36physical
27626673
RSSA_DROMEstaphysical
22028469
DYL1_DROMEctpphysical
22028469
DYL1_DROMEctpphysical
27626673
RS28_DROMERpS28bphysical
22028469
RLA1_DROMERpLP1physical
27626673
RL15_DROMERpL15physical
22028469
RL15_DROMERpL15physical
27626673
RS13_DROMERpS13physical
27626673
1433Z_DROME14-3-3zetaphysical
22028469
RS23_DROMERpS23physical
22028469
Y3800_DROMECG3800physical
22028469
HSP83_DROMEHsp83physical
22028469
FLNA_DROMEcherphysical
22028469
ROA1_DROMEHrb98DEphysical
27626673
RS7_DROMERpS7physical
27626673
RL10_DROMERpL10physical
22028469
IRS1_DROMEchicophysical
22028469
IRS1_DROMEchicophysical
26839216
IRS1_DROMEchicophysical
27626673
IRS1_DROMEchicophysical
23590848
IRS1_DROMEchicophysical
10801879
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of INSR_DROME

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-824; ASN-839; ASN-864;ASN-898; ASN-1147; ASN-1218 AND ASN-1219, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1816, AND MASSSPECTROMETRY.

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