dbPTM

IGF1R_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IGF1R_HUMAN
UniProt AC	P08069
Protein Name	Insulin-like growth factor 1 receptor
Gene Name	IGF1R
Organism	Homo sapiens (Human).
Sequence Length	1367
Subcellular Localization	Cell membrane Single-pass type I membrane protein .
Protein Description	Receptor tyrosine kinase which mediates actions of insulin-like growth factor 1 (IGF1). Binds IGF1 with high affinity and IGF2 and insulin (INS) with a lower affinity. The activated IGF1R is involved in cell growth and survival control. IGF1R is crucial for tumor transformation and survival of malignant cell. Ligand binding activates the receptor kinase, leading to receptor autophosphorylation, and tyrosines phosphorylation of multiple substrates, that function as signaling adapter proteins including, the insulin-receptor substrates (IRS1/2), Shc and 14-3-3 proteins. Phosphorylation of IRSs proteins lead to the activation of two main signaling pathways: the PI3K-AKT/PKB pathway and the Ras-MAPK pathway. The result of activating the MAPK pathway is increased cellular proliferation, whereas activating the PI3K pathway inhibits apoptosis and stimulates protein synthesis. Phosphorylated IRS1 can activate the 85 kDa regulatory subunit of PI3K (PIK3R1), leading to activation of several downstream substrates, including protein AKT/PKB. AKT phosphorylation, in turn, enhances protein synthesis through mTOR activation and triggers the antiapoptotic effects of IGFIR through phosphorylation and inactivation of BAD. In parallel to PI3K-driven signaling, recruitment of Grb2/SOS by phosphorylated IRS1 or Shc leads to recruitment of Ras and activation of the ras-MAPK pathway. In addition to these two main signaling pathways IGF1R signals also through the Janus kinase/signal transducer and activator of transcription pathway (JAK/STAT). Phosphorylation of JAK proteins can lead to phosphorylation/activation of signal transducers and activators of transcription (STAT) proteins. In particular activation of STAT3, may be essential for the transforming activity of IGF1R. The JAK/STAT pathway activates gene transcription and may be responsible for the transforming activity. JNK kinases can also be activated by the IGF1R. IGF1 exerts inhibiting activities on JNK activation via phosphorylation and inhibition of MAP3K5/ASK1, which is able to directly associate with the IGF1R.; When present in a hybrid receptor with INSR, binds IGF1. PubMed:12138094 shows that hybrid receptors composed of IGF1R and INSR isoform Long are activated with a high affinity by IGF1, with low affinity by IGF2 and not significantly activated by insulin, and that hybrid receptors composed of IGF1R and INSR isoform Short are activated by IGF1, IGF2 and insulin. In contrast, PubMed:16831875 shows that hybrid receptors composed of IGF1R and INSR isoform Long and hybrid receptors composed of IGF1R and INSR isoform Short have similar binding characteristics, both bind IGF1 and have a low affinity for insulin..
Protein Sequence	MKSGSGGGSPTSLWGLLFLSAALSLWPTSGEICGPGIDIRNDYQQLKRLENCTVIEGYLHILLISKAEDYRSYRFPKLTVITEYLLLFRVAGLESLGDLFPNLTVIRGWKLFYNYALVIFEMTNLKDIGLYNLRNITRGAIRIEKNADLCYLSTVDWSLILDAVSNNYIVGNKPPKECGDLCPGTMEEKPMCEKTTINNEYNYRCWTTNRCQKMCPSTCGKRACTENNECCHPECLGSCSAPDNDTACVACRHYYYAGVCVPACPPNTYRFEGWRCVDRDFCANILSAESSDSEGFVIHDGECMQECPSGFIRNGSQSMYCIPCEGPCPKVCEEEKKTKTIDSVTSAQMLQGCTIFKGNLLINIRRGNNIASELENFMGLIEVVTGYVKIRHSHALVSLSFLKNLRLILGEEQLEGNYSFYVLDNQNLQQLWDWDHRNLTIKAGKMYFAFNPKLCVSEIYRMEEVTGTKGRQSKGDINTRNNGERASCESDVLHFTSTTTSKNRIIITWHRYRPPDYRDLISFTVYYKEAPFKNVTEYDGQDACGSNSWNMVDVDLPPNKDVEPGILLHGLKPWTQYAVYVKAVTLTMVENDHIRGAKSEILYIRTNASVPSIPLDVLSASNSSSQLIVKWNPPSLPNGNLSYYIVRWQRQPQDGYLYRHNYCSKDKIPIRKYADGTIDIEEVTENPKTEVCGGEKGPCCACPKTEAEKQAEKEEAEYRKVFENFLHNSIFVPRPERKRRDVMQVANTTMSSRSRNTTAADTYNITDPEELETEYPFFESRVDNKERTVISNLRPFTLYRIDIHSCNHEAEKLGCSASNFVFARTMPAEGADDIPGPVTWEPRPENSIFLKWPEPENPNGLILMYEIKYGSQVEDQRECVSRQEYRKYGGAKLNRLNPGNYTARIQATSLSGNGSWTDPVFFYVQAKTGYENFIHLIIALPVAVLLIVGGLVIMLYVFHRKRNNSRLGNGVLYASVNPEYFSAADVYVPDEWEVAREKITMSRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMTRGDLKSYLRSLRPEMENNPVLAPPSLSKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGLSNEQVLRFVMEGGLLDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIISSIKEEMEPGFREVSFYYSEENKLPEPEELDLEPENMESVPLDPSASSSSLPLPDRHSGHKAENGPGPGVLVLRASFDERQPYAHMNGGRKNERALPLPQSSTC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MKSGSGGGSP -----CCCCCCCCCH	50.48	18187866
5	Phosphorylation	---MKSGSGGGSPTS ---CCCCCCCCCHHH	41.16	18187866
9	Phosphorylation	KSGSGGGSPTSLWGL CCCCCCCCHHHHHHH	28.42	22817900
11	Phosphorylation	GSGGGSPTSLWGLLF CCCCCCHHHHHHHHH	37.84	22817900
12	Phosphorylation	SGGGSPTSLWGLLFL CCCCCHHHHHHHHHH	26.05	22817900
28	Phosphorylation	AALSLWPTSGEICGP HHHHHCCCCCCCCCC	37.47	22817900
29	Phosphorylation	ALSLWPTSGEICGPG HHHHCCCCCCCCCCC	30.28	22817900
51	N-linked_Glycosylation	QQLKRLENCTVIEGY HHHHHHHCCEEEECE	31.20	9690478
102	N-linked_Glycosylation	SLGDLFPNLTVIRGW HHHHHCCCCEEEECC	40.80	UniProtKB CARBOHYD
113	Phosphorylation	IRGWKLFYNYALVIF EECCEEHHEEEEEEE	20.07	-
115	Phosphorylation	GWKLFYNYALVIFEM CCEEHHEEEEEEEEE	7.02	-
123	Phosphorylation	ALVIFEMTNLKDIGL EEEEEEECCCCCCEE	30.15	-
131	Phosphorylation	NLKDIGLYNLRNITR CCCCCEEEHHCCCCC	13.62	21406692
135	N-linked_Glycosylation	IGLYNLRNITRGAIR CEEEHHCCCCCCCEE	43.05	9690478
201	Phosphorylation	KTTINNEYNYRCWTT CCCCCCCEEEEEECC	21.44	30576142
203	Phosphorylation	TINNEYNYRCWTTNR CCCCCEEEEEECCCH	13.27	30576142
207	Phosphorylation	EYNYRCWTTNRCQKM CEEEEEECCCHHHHH	20.16	30576142
244	N-linked_Glycosylation	GSCSAPDNDTACVAC CCCCCCCCCCEEEEC	47.69	9690478
314	N-linked_Glycosylation	CPSGFIRNGSQSMYC CCCCEEECCCCCEEE	50.04	9690478
316	Phosphorylation	SGFIRNGSQSMYCIP CCEEECCCCCEEEEE	23.72	30631047
318	Phosphorylation	FIRNGSQSMYCIPCE EEECCCCCEEEEECC	17.26	30631047
320	Phosphorylation	RNGSQSMYCIPCEGP ECCCCCEEEEECCCC	7.77	30631047
345	Phosphorylation	TKTIDSVTSAQMLQG CCCCCHHCHHHHHCC	23.46	24260401
346	Phosphorylation	KTIDSVTSAQMLQGC CCCCHHCHHHHHCCC	17.85	24260401
354	Phosphorylation	AQMLQGCTIFKGNLL HHHHCCCEEEECCEE	35.95	24260401
372	Phosphorylation	RRGNNIASELENFMG ECCCCHHHHHHHHHH	38.63	21406692
385	Phosphorylation	MGLIEVVTGYVKIRH HHHHHHHHCCCEECC	28.15	21406692
387	Phosphorylation	LIEVVTGYVKIRHSH HHHHHHCCCEECCCC	6.82	21406692
400	Phosphorylation	SHALVSLSFLKNLRL CCCHHHHHHHHHCCH	22.49	24719451
417	N-linked_Glycosylation	GEEQLEGNYSFYVLD CHHHHCCCEEEEEEC	21.65	UniProtKB CARBOHYD
438	N-linked_Glycosylation	LWDWDHRNLTIKAGK HHCCCCCCEEEECCC	37.81	UniProtKB CARBOHYD
466	Phosphorylation	IYRMEEVTGTKGRQS HEEHHHHHCCCCCCC	42.27	20068231
468	Phosphorylation	RMEEVTGTKGRQSKG EHHHHHCCCCCCCCC	22.44	20068231
471	Methylation	EVTGTKGRQSKGDIN HHHCCCCCCCCCCCC	38.87	12018391
473	Phosphorylation	TGTKGRQSKGDINTR HCCCCCCCCCCCCCC	36.93	20068231
479	Phosphorylation	QSKGDINTRNNGERA CCCCCCCCCCCCCCC	34.80	27251275
480	Methylation	SKGDINTRNNGERAS CCCCCCCCCCCCCCC	30.08	12018405
487	Phosphorylation	RNNGERASCESDVLH CCCCCCCCEECCEEE	25.33	27251275
490	Phosphorylation	GERASCESDVLHFTS CCCCCEECCEEEEEE	37.03	27251275
496	Phosphorylation	ESDVLHFTSTTTSKN ECCEEEEEECCCCCC	17.89	27251275
497	Phosphorylation	SDVLHFTSTTTSKNR CCEEEEEECCCCCCE	23.86	27251275
498	Phosphorylation	DVLHFTSTTTSKNRI CEEEEEECCCCCCEE	30.91	27251275
499	Phosphorylation	VLHFTSTTTSKNRII EEEEEECCCCCCEEE	28.92	27251275
500	Phosphorylation	LHFTSTTTSKNRIII EEEEECCCCCCEEEE	37.48	27251275
501	Phosphorylation	HFTSTTTSKNRIIIT EEEECCCCCCEEEEE	26.33	27251275
534	N-linked_Glycosylation	YKEAPFKNVTEYDGQ EECCCCCCCEEECCC	46.45	UniProtKB CARBOHYD
577	Phosphorylation	GLKPWTQYAVYVKAV CCCCCCCEEEEEEEE	7.23	22817900
580	Phosphorylation	PWTQYAVYVKAVTLT CCCCEEEEEEEEEEE	6.51	22817900
606	Phosphorylation	SEILYIRTNASVPSI CEEEEEECCCCCCCC	26.10	22210691
607	N-linked_Glycosylation	EILYIRTNASVPSIP EEEEEECCCCCCCCC	21.99	UniProtKB CARBOHYD
609	Phosphorylation	LYIRTNASVPSIPLD EEEECCCCCCCCCCH	36.31	22210691
622	N-linked_Glycosylation	LDVLSASNSSSQLIV CHHHCCCCCCCCEEE	45.70	UniProtKB CARBOHYD
623	Phosphorylation	DVLSASNSSSQLIVK HHHCCCCCCCCEEEE	28.95	-
624	Phosphorylation	VLSASNSSSQLIVKW HHCCCCCCCCEEEEC	26.76	-
640	N-linked_Glycosylation	PPSLPNGNLSYYIVR CCCCCCCCEEEEEEE	32.24	UniProtKB CARBOHYD
672	Ubiquitination	KDKIPIRKYADGTID CCCCCCEECCCCCCC	45.57	-
684	O-linked_Glycosylation	TIDIEEVTENPKTEV CCCHHHHCCCCCCCC	33.07	OGP
747	N-linked_Glycosylation	RDVMQVANTTMSSRS CHHHHHHHHHCCCCC	36.91	UniProtKB CARBOHYD
748	Phosphorylation	DVMQVANTTMSSRSR HHHHHHHHHCCCCCC	17.71	23612710
749	Phosphorylation	VMQVANTTMSSRSRN HHHHHHHHCCCCCCC	18.18	23612710
751	Phosphorylation	QVANTTMSSRSRNTT HHHHHHCCCCCCCCC	22.10	23612710
752	Phosphorylation	VANTTMSSRSRNTTA HHHHHCCCCCCCCCC	24.37	23612710
756	N-linked_Glycosylation	TMSSRSRNTTAADTY HCCCCCCCCCCCCCC	42.92	UniProtKB CARBOHYD
764	N-linked_Glycosylation	TTAADTYNITDPEEL CCCCCCCCCCCHHHH	32.54	UniProtKB CARBOHYD
791	Phosphorylation	NKERTVISNLRPFTL CCCCEEEECCCCEEE	26.02	24719451
797	Phosphorylation	ISNLRPFTLYRIDIH EECCCCEEEEEEEEE	26.09	24719451
869	Phosphorylation	ILMYEIKYGSQVEDQ EEEEEEECCCCCCCH	27.89	21406692
871	Phosphorylation	MYEIKYGSQVEDQRE EEEEECCCCCCCHHH	28.15	21406692
900	N-linked_Glycosylation	LNRLNPGNYTARIQA CCCCCCCCCEEEEEE	32.04	UniProtKB CARBOHYD
913	N-linked_Glycosylation	QATSLSGNGSWTDPV EEEECCCCCCCCCCE	37.64	UniProtKB CARBOHYD
973	Phosphorylation	RLGNGVLYASVNPEY CCCCCEEEEECCHHH	8.40	8940173
975	Phosphorylation	GNGVLYASVNPEYFS CCCEEEEECCHHHCC	14.63	27259358
980	Phosphorylation	YASVNPEYFSAADVY EEECCHHHCCCCCEE	12.23	10786694
982	Phosphorylation	SVNPEYFSAADVYVP ECCHHHCCCCCEECC	22.96	11591350
1000	Phosphorylation	EVAREKITMSRELGQ HHHHHHHCCCCCCCC	21.84	24719451
1002	Phosphorylation	AREKITMSRELGQGS HHHHHCCCCCCCCCC	17.60	24719451
1009	Phosphorylation	SRELGQGSFGMVYEG CCCCCCCCCCHHEEE	15.67	21945579
1014	Phosphorylation	QGSFGMVYEGVAKGV CCCCCHHEEEHHHCC	9.70	21945579
1033	Ubiquitination	PETRVAIKTVNEAAS CCCEEEEEEHHHHHH	36.36	21890473
1055	Sumoylation	LNEASVMKEFNCHHV HHHHHHHHHCCCHHH	57.93	-
1055	Sumoylation	LNEASVMKEFNCHHV HHHHHHHHHCCCHHH	57.93	-
1088	Acetylation	LMTRGDLKSYLRSLR ECCCCCHHHHHHHHC	41.62	19608861
1130	Sumoylation	MAYLNANKFVHRDLA HHHHCCCHHHCHHHH	46.48	-
1130	Sumoylation	MAYLNANKFVHRDLA HHHHCCCHHHCHHHH	46.48	-
1150	Sumoylation	VAEDFTVKIGDFGMT EECCEEEEECCCCCC	37.60	-
1150	Sumoylation	VAEDFTVKIGDFGMT EECCEEEEECCCCCC	37.60	-
1157	Phosphorylation	KIGDFGMTRDIYETD EECCCCCCCEEEECC	26.10	21945579
1161	Phosphorylation	FGMTRDIYETDYYRK CCCCCEEEECCCCCC	19.64	21945579
1163	Phosphorylation	MTRDIYETDYYRKGG CCCEEEECCCCCCCC	16.60	21945579
1165	Phosphorylation	RDIYETDYYRKGGKG CEEEECCCCCCCCCC	16.76	22322096
1166	Phosphorylation	DIYETDYYRKGGKGL EEEECCCCCCCCCCC	14.52	21945579
1168	Ubiquitination	YETDYYRKGGKGLLP EECCCCCCCCCCCCC	56.76	21994939
1171	Ubiquitination	DYYRKGGKGLLPVRW CCCCCCCCCCCCEEE	55.86	-
1193	Phosphorylation	DGVFTTYSDVWSFGV CCCCCCHHHHHHHHH	24.48	-
1278	Phosphorylation	EPGFREVSFYYSEEN CCCCEEEEEEECCCC	11.63	22509025
1280	Phosphorylation	GFREVSFYYSEENKL CCEEEEEEECCCCCC	9.89	10786694
1281	Phosphorylation	FREVSFYYSEENKLP CEEEEEEECCCCCCC	13.95	10786694
1282	Phosphorylation	REVSFYYSEENKLPE EEEEEEECCCCCCCC	27.36	-
1308	Phosphorylation	ESVPLDPSASSSSLP CCCCCCCCCCCCCCC	40.21	18691976
1310	Phosphorylation	VPLDPSASSSSLPLP CCCCCCCCCCCCCCC	34.78	10786694
1311	Phosphorylation	PLDPSASSSSLPLPD CCCCCCCCCCCCCCC	24.54	10786694
1312	Phosphorylation	LDPSASSSSLPLPDR CCCCCCCCCCCCCCC	33.14	10786694
1313	Phosphorylation	DPSASSSSLPLPDRH CCCCCCCCCCCCCCC	35.63	10786694
1321	Phosphorylation	LPLPDRHSGHKAENG CCCCCCCCCCCCCCC	43.41	22509025
1339	Phosphorylation	GVLVLRASFDERQPY CEEEEEECCCCCCCC	27.14	21945579
1346	Phosphorylation	SFDERQPYAHMNGGR CCCCCCCCCCCCCCC	10.78	10786694
1354	Methylation	AHMNGGRKNERALPL CCCCCCCCCCCCCCC	67.45	-
1364	Phosphorylation	RALPLPQSSTC---- CCCCCCCCCCC----	26.19	30266825
1365	Phosphorylation	ALPLPQSSTC----- CCCCCCCCCC-----	28.66	30266825
1366	Phosphorylation	LPLPQSSTC------ CCCCCCCCC------	27.73	25463755

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
973	Y	Phosphorylation	Kinase	IGF1R	P08069	PhosphoELM
980	Y	Phosphorylation	Kinase	IGF1R	P08069	PSP
982	S	Phosphorylation	Kinase	IGF1R	P08069	PSP
1161	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
1161	Y	Phosphorylation	Kinase	IGF1R	P08069	PSP
1161	Y	Phosphorylation	Kinase	SRC	P12931	GPS
1165	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
1165	Y	Phosphorylation	Kinase	IGF1R	P08069	PSP
1165	Y	Phosphorylation	Kinase	SRC	P12931	GPS
1166	Y	Phosphorylation	Kinase	IGF1R	P08069	PSP
1166	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
1166	Y	Phosphorylation	Kinase	SRC	P12931	GPS
1278	S	Phosphorylation	Kinase	GRK2	P25098	PSP
1278	S	Phosphorylation	Kinase	GSK3-BETA	P49841	Uniprot
1280	Y	Phosphorylation	Kinase	IGF1R	P08069	PSP
1281	Y	Phosphorylation	Kinase	IGF1R	P08069	PSP
1321	S	Phosphorylation	Kinase	GRK6	P43250	PSP
1346	Y	Phosphorylation	Kinase	IGF1R	P08069	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:12821780
-	K	Ubiquitination	E3 ubiquitin ligase	NEDD4	P46934	PMID:18286479
-	K	Ubiquitination	E3 ubiquitin ligase	CBL	P22681	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
29	K	ubiquitylation	11694888
Polyubiquitinated at Lys-1168 and Lys-1171 through both 'Lys-48' and 'Lys-29' linkages, promoting receptor endocytosis and subsequent degradation by the proteasome.
48	K	ubiquitylation	11694888
Polyubiquitinated at Lys-1168 and Lys-1171 through both 'Lys-48' and 'Lys-29' linkages, promoting receptor endocytosis and subsequent degradation by the proteasome.
1168	K	ubiquitylation	21994939
Polyubiquitinated at Lys-1168 and Lys-1171 through both 'Lys-48' and 'Lys-29' linkages, promoting receptor endocytosis and subsequent degradation by the proteasome.
1171	K	ubiquitylation	21994939
Polyubiquitinated at Lys-1168 and Lys-1171 through both 'Lys-48' and 'Lys-29' linkages, promoting receptor endocytosis and subsequent degradation by the proteasome.
1278	S	Phosphorylation	-
Phosphorylation of Ser-1278 by GSK-3beta restrains kinase activity and promotes cell surface expression, it requires a priming phosphorylation at Ser-1282.
1282	S	Phosphorylation	-
Phosphorylation of Ser-1278 by GSK-3beta restrains kinase activity and promotes cell surface expression, it requires a priming phosphorylation at Ser-1282.

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 IGF1R_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IRS1_HUMAN	IRS1	physical	7559507
GRB10_HUMAN	GRB10	physical	12697834
NEDD4_HUMAN	NEDD4	physical	12697834
IGF1_HUMAN	IGF1	physical	1852007
EHD1_HUMAN	EHD1	physical	11423532
SNP29_HUMAN	SNAP29	physical	11423532
ARHGC_HUMAN	ARHGEF12	physical	11724822
P55G_HUMAN	PIK3R3	physical	9415396
IRS1_HUMAN	IRS1	physical	8776723
SHC1_HUMAN	SHC1	physical	8776723
GRB10_HUMAN	GRB10	physical	8776723
ESR1_HUMAN	ESR1	physical	16113100
SHC1_HUMAN	SHC1	physical	16113100
CSK_HUMAN	CSK	physical	10026153
FAK1_HUMAN	PTK2	physical	10082579
IRS1_HUMAN	IRS1	physical	10082579
PAXI_HUMAN	PXN	physical	10082579
PTN11_HUMAN	PTPN11	physical	10082579
PTN11_HUMAN	PTPN11	physical	7642582
RASA1_HUMAN	RASA1	physical	7642582
SOCS3_HUMAN	SOCS3	physical	11071852
PTN1_HUMAN	PTPN1	physical	8999839
RACK1_HUMAN	GNB2L1	physical	11884618
GRB10_HUMAN	GRB10	physical	8764099
SHC1_HUMAN	SHC1	physical	7559507
CBL_HUMAN	CBL	physical	18632619
MDM2_HUMAN	MDM2	physical	18632619
EEA1_HUMAN	EEA1	physical	18632619
MDM2_HUMAN	MDM2	physical	12821780
ARRB1_RAT	Arrb1	physical	12167719
EGFR_HUMAN	EGFR	physical	17307140
ERBB2_HUMAN	ERBB2	physical	17307140
CAMP_HUMAN	CAMP	physical	21685939
MDM2_HUMAN	MDM2	physical	19165858
ARRB2_HUMAN	ARRB2	physical	19165858
P53_HUMAN	TP53	physical	19165858
GRB10_HUMAN	GRB10	physical	19165858
NEDD4_HUMAN	NEDD4	physical	19165858
ARRB1_HUMAN	ARRB1	physical	15878855
ARRB2_HUMAN	ARRB2	physical	15878855
RACK1_HUMAN	GNB2L1	physical	20871634
A4_HUMAN	APP	physical	21832049
RUVB1_HUMAN	RUVBL1	physical	22939629
S23A3_HUMAN	SLC23A3	physical	20368287
S23A3_MOUSE	Slc23a3	physical	20368287
SHC1_HUMAN	SHC1	physical	14764897
ESR1_HUMAN	ESR1	physical	14764897
RL11_HUMAN	RPL11	physical	21988832
SHC1_HUMAN	SHC1	physical	24051437
ESR1_HUMAN	ESR1	physical	24051437
PHB2_HUMAN	PHB2	physical	24051437
CSEN_HUMAN	KCNIP3	physical	25416956
FPPS_HUMAN	FDPS	physical	26344197
BAP1_HUMAN	BAP1	physical	25640309
CP17A_HUMAN	CYP17A1	physical	25640309
HXC6_HUMAN	HOXC6	physical	25640309
I13R2_HUMAN	IL13RA2	physical	25640309
KLK5_HUMAN	KLK5	physical	25640309
LYPD3_HUMAN	LYPD3	physical	25640309
MTA3_HUMAN	MTA3	physical	25640309
ARY2_HUMAN	NAT2	physical	25640309
THRSP_HUMAN	THRSP	physical	25640309
TRI25_HUMAN	TRIM25	physical	25640309
VPS45_HUMAN	VPS45	physical	25640309
P85A_HUMAN	PIK3R1	physical	25241761
MDM2_HUMAN	MDM2	physical	25241761
P55G_HUMAN	PIK3R3	physical	25241761
CRKL_HUMAN	CRKL	physical	25241761
STAT3_HUMAN	STAT3	physical	25241761
SYVN1_HUMAN	SYVN1	physical	26536657
14331_MAIZE	grf1	physical	15248125
PPI1_ARATH	PPI1	physical	15248125
PRKDC_HUMAN	PRKDC	genetic	28319113
MTOR_HUMAN	MTOR	genetic	28319113
MDM2_HUMAN	MDM2	physical	28092675
PTPRR_HUMAN	PTPRR	physical	28065597
PTN6_HUMAN	PTPN6	physical	28065597
PTN7_HUMAN	PTPN7	physical	28065597
PTN11_HUMAN	PTPN11	physical	28065597
PTN12_HUMAN	PTPN12	physical	28065597
PPM1A_HUMAN	PPM1A	physical	28065597
PPM1F_HUMAN	PPM1F	physical	28065597
MPZL2_HUMAN	MPZL2	physical	28065597
SSH1_HUMAN	SSH1	physical	28065597
ILKAP_HUMAN	ILKAP	physical	28065597
DUS10_HUMAN	DUSP10	physical	28065597
DUS14_HUMAN	DUSP14	physical	28065597
DUS15_HUMAN	DUSP15	physical	28065597
DUS18_HUMAN	DUSP18	physical	28065597
DUS19_HUMAN	DUSP19	physical	28065597
DUS21_HUMAN	DUSP21	physical	28065597
DUS26_HUMAN	DUSP26	physical	28065597
DUPD1_HUMAN	DUPD1	physical	28065597
STYX_HUMAN	STYX	physical	28065597

Drug and Disease Associations

Kegg Disease
H00015	Malignant pleural mesothelioma
H00050	Synovial sarcoma
H01274	Growth delay due to insulin-like growth factor I resistance; IGF-I resistance
OMIM Disease
270450	Insulin-like growth factor 1 resistance (IGF1RES)
Kegg Drug
D03297	Mecasermin (genetical recombination) (JAN); Mecasermin (USAN/INN); Increlex (TN); Myotrophin (TN)
D04870	Mecasermin rinfabate (USAN/INN); Iplex (TN)
D09328	Cixutumumab (USAN)
D09345	Figitumumab (USAN)
D09746	Dalotuzumab (USAN)
D09908	Ganitumab (USAN/INN)
D09925	Linsitinib (USAN/INN)
D10056	Robatumumab (USAN/INN)
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of IGF1R_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Crystal structure of the first three domains of the type-1 insulin-like growth factor receptor."; Garrett T.P., McKern N.M., Lou M., Frenkel M.J., Bentley J.D.,Lovrecz G.O., Elleman T.C., Cosgrove L.J., Ward C.W.; Nature 394:395-399(1998). Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 31-492, DISULFIDE BONDS, ANDGLYCOSYLATION AT ASN-51; ASN-135; ASN-244 AND ASN-314.	9690478 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1165; SER-1339; SER-1365AND THR-1366, AND MASS SPECTROMETRY.	19369195 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1339, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1161; TYR-1165; SER-1339AND THR-1366, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Lead identification to generate 3-cyanoquinoline inhibitors ofinsulin-like growth factor receptor (IGF-1R) for potential use incancer treatment."; Miller L.M., Mayer S.C., Berger D.M., Boschelli D.H., Boschelli F.,Di L., Du X., Dutia M., Floyd M.B., Johnson M., Kenny C.H.,Krishnamurthy G., Moy F., Petusky S., Tkach D., Torres N., Wu B.,Xu W.; Bioorg. Med. Chem. Lett. 19:62-66(2009). Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 981-1286 IN COMPLEX WITH3-CYANOQUINOLINE INHIBITOR, CATALYTIC ACTIVITY, ENZYME REGULATION, ANDPHOSPHORYLATION AT TYR-1161; TYR-1165 AND TYR-1166.	19041240 [Abstract]
"Lead identification to generate isoquinolinedione inhibitors ofinsulin-like growth factor receptor (IGF-1R) for potential use incancer treatment."; Mayer S.C., Banker A.L., Boschelli F., Di L., Johnson M., Kenny C.H.,Krishnamurthy G., Kutterer K., Moy F., Petusky S., Ravi M., Tkach D.,Tsou H.R., Xu W.; Bioorg. Med. Chem. Lett. 18:3641-3645(2008). Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 981-1286, ANDPHOSPHORYLATION AT TYR-1161; TYR-1165 AND TYR-1166.	18501599 [Abstract]
"Structure and autoregulation of the insulin-like growth factor 1receptor kinase."; Favelyukis S., Till J.H., Hubbard S.R., Miller W.T.; Nat. Struct. Biol. 8:1058-1063(2001). Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 988-1286 IN COMPLEX WITHAMP-PCP AND PEPTIDE SUBSTRATE, CATALYTIC ACTIVITY, ACTIVE SITE, ENZYMEREGULATION, MASS SPECTROMETRY, AND PHOSPHORYLATION AT TYR-1161;TYR-1165 AND TYR-1166.	11694888 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1161; TYR-1165 ANDTYR-1166, AND MASS SPECTROMETRY.	18083107 [Abstract]

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