dbPTM

IRS1_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IRS1_DROME
UniProt AC	Q9XTN2
Protein Name	Insulin receptor substrate 1
Gene Name	chico
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	968
Subcellular Localization
Protein Description	Activates phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit (By similarity). May mediate the control of various cellular processes by insulin-like peptides. When phosphorylated by the insulin receptor binds specifically to various cellular proteins containing SH2 domains. Involved in control of cell proliferation, cell size, and body and organ growth throughout development. Also has a role in a signaling pathway controlling the physiological response required to endure periods of low nutrient conditions. Insulin/insulin-like growth factor (IGF) signaling pathway has a role in regulating aging and is necessary in the ovary for vitellogenic maturation..
Protein Sequence	MASISDDGMALSGYLKKLKTMKKKFFVLYEETSTSAARLEYYDTEKKFLQRAEPKRVIYLKNCFNINRRLDTKHRFVIVLSSRDGGFGIVLENENDLRKWLDKLLVLQRNIANSNGTAHSPYDHVWQVVIQKKGISEKVGITGTYHCCLTSKSLTFVCIGPEKTPNGEDRVASIEILLTTIRRCGHASPQCIFYVELGRQSVLGSGDLWMETDNAAIATNMHNTILSAMSAKTESNTNLINVYQNRPDLSHEPMRKRSSSANEASKPINVNVIQNSQNSLELRSCSSPHNYGFGRERCDSLPTRNGTLSESSNQTYFGSNHGLRSNTISGIRPHSTNKHSNSPTFTMPLRCSESEESSISVDESDDNGSFSHYRLNTRSSETAIPEENIDDFASAELFSKVTEQNVSDENYIPMNPVNPTDAIHEKEKADMQRLEDASLHFNFPEHASEKLAKDFDLDSDNQCCRPIRAYSIGNKVEHLKFNKRLGHLNDTGQNPNRVRAYSVGSKSKIPRCDLQRVVLVEDNKHEFTANRSQSSITKEGTSYGSSANRQKKSTSAPLLSLKNQINSDRMSDLMEIDFSQATNLEKQKFIKNNEIPKYIENVFPKAPRTDSSSLTLHATSQKDIFNGTKLNNTAITSEDGYLEMKPVGNGYTPSSNCLPMKVEKLKLSDYQTAPPLTATAAPVHDLNKISTYNISAEKWREQPSRSEEKKSNSPLNDNTFSSKPTNVESTSKSHDVHSANQIDCEKVCAQSSDKLNNHLADKIVENNNLDIGGHEEKKLVHSISSEDYTQIKDKSNDFTKFNEAGYKILQIKSDSSLISSKLYQKGIHKDNLERSQRLTESVNTIPDNATATAVSSSSLTKFNINSAKPAAAADSRSTGTDPSTPQNILQIKDLNFPSRSSSRISQPELHYASLDLPHCSGQNPAKYLKRGSRESPPVSACPEDGNTYAKIDFDQSDSSSSSSNIFNT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MASISDDGMA -----CCCCCHHHHH	22.71	19429919
5	Phosphorylation	---MASISDDGMALS ---CCCCCHHHHHHH	27.44	19429919
235	Phosphorylation	AMSAKTESNTNLINV HHHCCCCCCCCCEEE	54.94	21082442
259	Phosphorylation	EPMRKRSSSANEASK CCCCCCCCCCCCCCC	37.19	21082442
260	Phosphorylation	PMRKRSSSANEASKP CCCCCCCCCCCCCCC	36.04	21082442
286	Phosphorylation	SLELRSCSSPHNYGF CEEEECCCCCCCCCC	48.42	22817900
287	Phosphorylation	LELRSCSSPHNYGFG EEEECCCCCCCCCCC	34.21	22817900
291	Phosphorylation	SCSSPHNYGFGRERC CCCCCCCCCCCHHHC	15.70	18281928
300	Phosphorylation	FGRERCDSLPTRNGT CCHHHCCCCCCCCCC	39.61	29892262
316	Phosphorylation	SESSNQTYFGSNHGL CCCCCCEECCCCCCC	9.00	18281928
319	Phosphorylation	SNQTYFGSNHGLRSN CCCEECCCCCCCCCC	18.76	22817900
327	Phosphorylation	NHGLRSNTISGIRPH CCCCCCCCCCCCCCC	20.12	21082442
336	Phosphorylation	SGIRPHSTNKHSNSP CCCCCCCCCCCCCCC	45.30	21082442
340	Phosphorylation	PHSTNKHSNSPTFTM CCCCCCCCCCCCEEE	40.38	19429919
342	Phosphorylation	STNKHSNSPTFTMPL CCCCCCCCCCEEEEE	28.47	19429919
344	Phosphorylation	NKHSNSPTFTMPLRC CCCCCCCCEEEEEEC	31.40	19429919
382	Phosphorylation	LNTRSSETAIPEENI EECCCCCCCCCCCCH	31.66	29892262
411	Phosphorylation	QNVSDENYIPMNPVN CCCCCCCCCCCCCCC	12.35	-
438	Phosphorylation	MQRLEDASLHFNFPE HHHHHHHCHHCCCCH	34.40	21082442
470	Phosphorylation	CCRPIRAYSIGNKVE CCCEEEEEECCCEEE	7.32	29892262
471	Phosphorylation	CRPIRAYSIGNKVEH CCEEEEEECCCEEEE	24.04	25749252
501	Phosphorylation	NPNRVRAYSVGSKSK CCCCEEEEEECCCCC	8.04	22817900
502	Phosphorylation	PNRVRAYSVGSKSKI CCCEEEEEECCCCCC	21.01	27626673
505	Phosphorylation	VRAYSVGSKSKIPRC EEEEEECCCCCCCCC	31.44	22817900
532	Phosphorylation	HEFTANRSQSSITKE CEEECCCCCCCCCCC	33.93	29892262
553	Phosphorylation	SANRQKKSTSAPLLS CCCCCCCCCCCCHHH	34.33	19429919
554	Phosphorylation	ANRQKKSTSAPLLSL CCCCCCCCCCCHHHH	37.48	19429919
555	Phosphorylation	NRQKKSTSAPLLSLK CCCCCCCCCCHHHHH	34.67	19429919
560	Phosphorylation	STSAPLLSLKNQINS CCCCCHHHHHHCCCC	45.01	22817900
609	Phosphorylation	VFPKAPRTDSSSLTL HCCCCCCCCCCCEEE	38.89	19429919
611	Phosphorylation	PKAPRTDSSSLTLHA CCCCCCCCCCEEEEE	22.63	19429919
612	Phosphorylation	KAPRTDSSSLTLHAT CCCCCCCCCEEEEEC	31.98	19429919
613	Phosphorylation	APRTDSSSLTLHATS CCCCCCCCEEEEECC	29.35	19429919
619	Phosphorylation	SSLTLHATSQKDIFN CCEEEEECCHHHCCC	22.42	19429919
620	Phosphorylation	SLTLHATSQKDIFNG CEEEEECCHHHCCCC	35.70	19429919
641	Phosphorylation	AITSEDGYLEMKPVG EEECCCCEEEEEECC	16.29	19429919
668	Phosphorylation	KVEKLKLSDYQTAPP EEEEECCCCCCCCCC	32.46	19429919
670	Phosphorylation	EKLKLSDYQTAPPLT EEECCCCCCCCCCCC	12.37	19429919
672	Phosphorylation	LKLSDYQTAPPLTAT ECCCCCCCCCCCCCC	34.60	19429919
677	Phosphorylation	YQTAPPLTATAAPVH CCCCCCCCCCCCCCC	27.95	19429919
692	Phosphorylation	DLNKISTYNISAEKW CCCCCCCCCCCHHHH	12.05	21082442
713	Phosphorylation	SEEKKSNSPLNDNTF CCCCCCCCCCCCCCC	37.54	27794539
782	Phosphorylation	EEKKLVHSISSEDYT CHHHHHEECCCCCCH	19.38	19429919
784	Phosphorylation	KKLVHSISSEDYTQI HHHHEECCCCCCHHH	30.59	19429919
785	Phosphorylation	KLVHSISSEDYTQIK HHHEECCCCCCHHHC	32.58	19429919
795	Phosphorylation	YTQIKDKSNDFTKFN CHHHCCCCCCCHHHH	52.33	22817900
806	Phosphorylation	TKFNEAGYKILQIKS HHHHHHCCEEEEECC	11.25	27626673
813	Phosphorylation	YKILQIKSDSSLISS CEEEEECCCCHHHHH	44.33	22817900
815	Phosphorylation	ILQIKSDSSLISSKL EEEECCCCHHHHHHH	33.85	29892262
823	Phosphorylation	SLISSKLYQKGIHKD HHHHHHHHHCCCCHH	16.35	18281928
839	Phosphorylation	LERSQRLTESVNTIP HHHHHHHHHHHCCCC	28.53	21082442
883	Phosphorylation	RSTGTDPSTPQNILQ CCCCCCCCCCCCEEE	56.37	29892262
884	Phosphorylation	STGTDPSTPQNILQI CCCCCCCCCCCEEEE	33.99	22817900
898	Phosphorylation	IKDLNFPSRSSSRIS ECCCCCCCCCCCCCC	40.43	19429919
900	Phosphorylation	DLNFPSRSSSRISQP CCCCCCCCCCCCCCC	36.68	19429919
901	Phosphorylation	LNFPSRSSSRISQPE CCCCCCCCCCCCCCC	23.64	19429919
902	Phosphorylation	NFPSRSSSRISQPEL CCCCCCCCCCCCCCE	34.57	19429919
905	Phosphorylation	SRSSSRISQPELHYA CCCCCCCCCCCEEEE	38.27	19429919
911	Phosphorylation	ISQPELHYASLDLPH CCCCCEEEEECCCCC	15.54	22817900
932	Phosphorylation	AKYLKRGSRESPPVS HHHHHCCCCCCCCCC	36.59	19429919
935	Phosphorylation	LKRGSRESPPVSACP HHCCCCCCCCCCCCC	33.13	19429919
948	Phosphorylation	CPEDGNTYAKIDFDQ CCCCCCEEEEEECCC	15.19	-
956	Phosphorylation	AKIDFDQSDSSSSSS EEEECCCCCCCCCCC	41.11	19429919
958	Phosphorylation	IDFDQSDSSSSSSNI EECCCCCCCCCCCCC	37.05	19429919
959	Phosphorylation	DFDQSDSSSSSSNIF ECCCCCCCCCCCCCC	38.95	19429919
960	Phosphorylation	FDQSDSSSSSSNIFN CCCCCCCCCCCCCCC	37.89	19429919
961	Phosphorylation	DQSDSSSSSSNIFNT CCCCCCCCCCCCCCC	39.47	19429919
962	Phosphorylation	QSDSSSSSSNIFNT- CCCCCCCCCCCCCC-	29.38	19429919
963	Phosphorylation	SDSSSSSSNIFNT-- CCCCCCCCCCCCC--	35.57	19429919
968	Phosphorylation	SSSNIFNT------- CCCCCCCC-------	29.28	19429919

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
411	Y	Phosphorylation	Kinase	INSR	P09208	Uniprot
911	Y	Phosphorylation	Kinase	INSR	P09208	Uniprot
948	Y	Phosphorylation	Kinase	INSR	P09208	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IRS1_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 IRS1_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
1433Z_DROME	14-3-3zeta	physical	17956857
1433E_DROME	14-3-3epsilon	physical	17956857
INSR_DROME	InR	physical	17956857
CHMP5_DROME	CG6259	physical	22036573
FLOT1_DROME	Flo1	physical	22036573
FLOT2_DROME	Flo2	physical	22036573
CYA1_DROME	rut	genetic	27048332
RAS1_DROME	Ras85D	genetic	26119340
FOXO_DROME	foxo	genetic	12908874
INSR_DROME	InR	genetic	10399915
2AAA_DROME	Pp2A-29B	physical	27626673
PGAM5_DROME	Pgam5	physical	22068330
RL7A_DROME	RpL7A	physical	27626673
RL17_DROME	RpL17	physical	27626673
HSP7C_DROME	Hsc70-3	physical	27626673
RS26_DROME	RpS26	physical	27626673
1433Z_DROME	14-3-3zeta	physical	22068330
1433Z_DROME	14-3-3zeta	physical	26839216
1433Z_DROME	14-3-3zeta	physical	27626673
RBP9X_DROME	RanBPM	physical	27626673
RL18_DROME	RpL18	physical	27626673
RL14_DROME	RpL14	physical	27626673
1433E_DROME	14-3-3epsilon	physical	22068330
1433E_DROME	14-3-3epsilon	physical	26839216
1433E_DROME	14-3-3epsilon	physical	27626673
INSR_DROME	InR	physical	22068330
INSR_DROME	InR	physical	27626673
RL4_DROME	RpL4	physical	27626673
RS15A_DROME	RpS15Aa	physical	27626673
2ABA_DROME	tws	physical	27626673

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of IRS1_DROME

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-286; SER-287; SER-342;SER-555; SER-932 AND SER-935, AND MASS SPECTROMETRY.	18327897 [Abstract]