HUMAN:INS

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	INS
Protein Name(s)	Insulin Insulin B chain Insulin A chain
External Links
UniProt	P01308
EMBL	V00565 M10039 J00265 X70508 L15440 AY899304 AY138590 BT006808 CH471158 BC005255 AJ009655
CCDS	CCDS7729.1
PIR	A93222
RefSeq	NP_000198.1 NP_001172026.1 NP_001172027.1 NP_001278826.1
UniGene	Hs.272259
PDB	1A7F 1AI0 1AIY 1B9E 1BEN 1EFE 1EV3 1EV6 1EVR 1FU2 1FUB 1G7A 1G7B 1GUJ 1HIQ 1HIS 1HIT 1HLS 1HTV 1HUI 1IOG 1IOH 1J73 1JCA 1JCO 1JK8 1K3M 1KMF 1LKQ 1LPH 1MHI 1MHJ 1MSO 1OS3 1OS4 1Q4V 1QIY 1QIZ 1QJ0 1RWE 1SF1 1SJT 1SJU 1T0C 1T1K 1T1P 1T1Q 1TRZ 1TYL 1TYM 1UZ9 1VKT 1W8P 1XDA 1XGL 1XW7 1ZEG 1ZEH 1ZNJ 2AIY 2C8Q 2C8R 2CEU 2G54 2G56 2H67 2HH4 2HHO 2HIU 2JMN 2JUM 2JUU 2JUV 2JV1 2JZQ 2K91 2K9R 2KJJ 2KJU 2KQP 2KQQ 2KXK 2L1Y 2L1Z 2LGB 2LWZ 2M1D 2M1E 2M2M 2M2N 2M2O 2M2P 2MLI 2MPG 2MPI 2MVC 2MVD 2OLY 2OLZ 2OM0 2OM1 2OMG 2OMH 2OMI 2OMQ 2QIU 2R34 2R35 2R36 2RN5 2VJZ 2VK0 2W44 2WBY 2WC0 2WRU 2WRV 2WRW 2WRX 2WS0 2WS1 2WS4 2WS6 2WS7 3AIY 3BXQ 3E7Y 3E7Z 3EXX 3FQ9 3HYD 3I3Z 3I40 3ILG 3INC 3IR0 3JSD 3KQ6 3P2X 3P33 3Q6E 3ROV 3TT8 3U4N 3UTQ 3UTS 3UTT 3V19 3V1G 3W11 3W12 3W13 3W7Y 3W7Z 3W80 3ZI3 3ZQR 3ZS2 3ZU1 4AIY 4AJX 4AJZ 4AK0 4AKJ 4CXL 4CXN 4CY7 4EFX 4EWW 4EWX 4EWZ 4EX0 4EX1 4EXX 4EY1 4EY9 4EYD 4EYN 4EYP 4F0N 4F0O 4F1A 4F1B 4F1C 4F1D 4F1F 4F1G 4F4T 4F4V 4F51 4F8F 4FG3 4FKA 4GBC 4GBI 4GBK 4GBL 4GBN 4IUZ 4IYD 4IYF 4NIB 4OGA 4P65 4Q5Z 4RXW 4UNE 4UNG 4UNH 4XC4 5AIY
PDBsum	1A7F 1AI0 1AIY 1B9E 1BEN 1EFE 1EV3 1EV6 1EVR 1FU2 1FUB 1G7A 1G7B 1GUJ 1HIQ 1HIS 1HIT 1HLS 1HTV 1HUI 1IOG 1IOH 1J73 1JCA 1JCO 1JK8 1K3M 1KMF 1LKQ 1LPH 1MHI 1MHJ 1MSO 1OS3 1OS4 1Q4V 1QIY 1QIZ 1QJ0 1RWE 1SF1 1SJT 1SJU 1T0C 1T1K 1T1P 1T1Q 1TRZ 1TYL 1TYM 1UZ9 1VKT 1W8P 1XDA 1XGL 1XW7 1ZEG 1ZEH 1ZNJ 2AIY 2C8Q 2C8R 2CEU 2G54 2G56 2H67 2HH4 2HHO 2HIU 2JMN 2JUM 2JUU 2JUV 2JV1 2JZQ 2K91 2K9R 2KJJ 2KJU 2KQP 2KQQ 2KXK 2L1Y 2L1Z 2LGB 2LWZ 2M1D 2M1E 2M2M 2M2N 2M2O 2M2P 2MLI 2MPG 2MPI 2MVC 2MVD 2OLY 2OLZ 2OM0 2OM1 2OMG 2OMH 2OMI 2OMQ 2QIU 2R34 2R35 2R36 2RN5 2VJZ 2VK0 2W44 2WBY 2WC0 2WRU 2WRV 2WRW 2WRX 2WS0 2WS1 2WS4 2WS6 2WS7 3AIY 3BXQ 3E7Y 3E7Z 3EXX 3FQ9 3HYD 3I3Z 3I40 3ILG 3INC 3IR0 3JSD 3KQ6 3P2X 3P33 3Q6E 3ROV 3TT8 3U4N 3UTQ 3UTS 3UTT 3V19 3V1G 3W11 3W12 3W13 3W7Y 3W7Z 3W80 3ZI3 3ZQR 3ZS2 3ZU1 4AIY 4AJX 4AJZ 4AK0 4AKJ 4CXL 4CXN 4CY7 4EFX 4EWW 4EWX 4EWZ 4EX0 4EX1 4EXX 4EY1 4EY9 4EYD 4EYN 4EYP 4F0N 4F0O 4F1A 4F1B 4F1C 4F1D 4F1F 4F1G 4F4T 4F4V 4F51 4F8F 4FG3 4FKA 4GBC 4GBI 4GBK 4GBL 4GBN 4IUZ 4IYD 4IYF 4NIB 4OGA 4P65 4Q5Z 4RXW 4UNE 4UNG 4UNH 4XC4 5AIY
ProteinModelPortal	P01308
SMR	P01308
BioGrid	109842
DIP	DIP-6024N
IntAct	P01308
MINT	MINT-106847
STRING	9606.ENSP00000250971
ChEMBL	CHEMBL5881
Allergome	2121
PhosphoSite	P01308
BioMuta	INS
DMDM	124617
PaxDb	P01308
PeptideAtlas	P01308
PRIDE	P01308
DNASU	3630
Ensembl	ENST00000250971 ENST00000381330 ENST00000397262
GeneID	3630
KEGG	hsa:3630
UCSC	uc001lvn.2
CTD	3630
GeneCards	GC11M002181
GeneReviews	INS
HGNC	HGNC:6081
HPA	CAB000048 CAB012098 CAB053843 HPA004932
MIM	125852 176730 606176 613370 616214
neXtProt	NX_P01308
Orphanet	552 99885
PharmGKB	PA201
eggNOG	NOG45999
GeneTree	ENSGT00390000015440
HOGENOM	HOG000261669
HOVERGEN	HBG006137
InParanoid	P01308
KO	K04526
OMA	GFFYSPK
PhylomeDB	P01308
TreeFam	TF332820
BioCyc	MetaCyc:MONOMER-16190
Reactome	REACT_1109 REACT_13819 REACT_15550 REACT_1661 REACT_18325 REACT_19189 REACT_498 REACT_508 REACT_570
SignaLink	P01308
EvolutionaryTrace	P01308
GeneWiki	Insulin
GenomeRNAi	3630
NextBio	14203
PMAP-CutDB	P01308
PRO	PR:P01308
Proteomes	UP000005640
Bgee	P01308
ExpressionAtlas	P01308
Genevisible	P01308
GO	GO:0005788 GO:0031904 GO:0005576 GO:0005615 GO:0005796 GO:0034774 GO:0005179 GO:0042802 GO:0005158 GO:0005159 GO:0002020 GO:0032148 GO:0006953 GO:0046631 GO:0007267 GO:0044267 GO:0031018 GO:0006112 GO:0055089 GO:0007186 GO:0042593 GO:0006006 GO:0015758 GO:0008286 GO:0000165 GO:0002674 GO:0045922 GO:2000252 GO:0045721 GO:0045818 GO:0050995 GO:0033861 GO:1902176 GO:0042177 GO:0032460 GO:0050709 GO:0045861 GO:0060266 GO:0045908 GO:0090336 GO:0045597 GO:0030307 GO:0030335 GO:0008284 GO:0032270 GO:0050715 GO:0045740 GO:0046326 GO:0045725 GO:0045821 GO:0046628 GO:0046889 GO:0043410 GO:0045840 GO:0051092 GO:0045429 GO:0051000 GO:0090277 GO:0050731 GO:0014068 GO:0031954 GO:0051897 GO:1900182 GO:0060267 GO:0045909 GO:0006521 GO:0050796 GO:0032880 GO:0050708 GO:0006355 GO:0022898 GO:0044281 GO:0042060
Gene3D	1.10.100.10
InterPro	IPR004825 IPR016179 IPR022353 IPR022352
Pfam	PF00049
PRINTS	PR00277 PR00276
SMART	SM00078
SUPFAM	SSF56994
PROSITE	PS00262

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0005813	centrosome		ECO:0000314			C		Source: HPA	Missing: reference
involved_in	GO:0010750	positive regulation of nitric oxide mediated signal transduction	PMID:15792832^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046628	positive regulation of insulin receptor signaling pathway	PMID:14615391^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046326	positive regulation of glucose import	PMID:14615391^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	happens_during:(GO:0071731)\|happens_during:(GO:0032868)	Seeded From UniProt	complete
involved_in	GO:0046326	positive regulation of glucose import	PMID:15792832^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	happens_during:(GO:0071731)\|happens_during:(GO:0032868)	Seeded From UniProt	complete
involved_in	GO:1902952	positive regulation of dendritic spine maintenance	PMID:19188609^[3]	ECO:0000316	genetic interaction evidence used in manual assertion	ComplexPortal:CPX-1134	P	occurs_in:(CL:0002608)	Seeded From UniProt	complete
involved_in	GO:1903427	negative regulation of reactive oxygen species biosynthetic process	PMID:19188609^[3]	ECO:0000316	genetic interaction evidence used in manual assertion	ComplexPortal:CPX-1134	P	occurs_in:(CL:0002608) part_of:(GO:1990535)	Seeded From UniProt	complete
involved_in	GO:1990535	neuron projection maintenance	PMID:19188609^[3]	ECO:0000316	genetic interaction evidence used in manual assertion	ComplexPortal:CPX-1134,UniProtKB:P15127	P	occurs_in:(CL:0002608)	Seeded From UniProt	complete
involved_in	GO:1903076	regulation of protein localization to plasma membrane	PMID:19188609^[3]	ECO:0000316	genetic interaction evidence used in manual assertion	ComplexPortal:CPX-1134	P	occurs_in:(CL:0002608) has_target_start_location:(GO:0032590) transports_or_maintains_localization_of:(UniProtKB:P06213) has_target_end_location:(GO:0032809)	Seeded From UniProt	complete
involved_in	GO:0010628	positive regulation of gene expression	PMID:25403480^[4]	ECO:0000316	genetic interaction evidence used in manual assertion	RNAcentral:URS00004AD914_9606,RNAcentral:URS00004BCD9C_9606	P	regulates_expression_of:(ENSEMBL:ENSG00000171105) occurs_in:(CL:0000737)	Seeded From UniProt	complete
involved_in	GO:0043410	positive regulation of MAPK cascade	PMID:20455999^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	part_of:(GO:0008286)	Seeded From UniProt	complete
involved_in	GO:0008286	insulin receptor signaling pathway	PMID:20455999^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1900182	positive regulation of protein localization to nucleus	PMID:20455999^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	part_of:(GO:0008286)	Seeded From UniProt	complete
involved_in	GO:0050995	negative regulation of lipid catabolic process	PMID:24675707^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:2000252	negative regulation of feeding behavior	PMID:17957153^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1902176	negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway	PMID:16604263^[8]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0060267	positive regulation of respiratory burst	PMID:9092559^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0060266	negative regulation of respiratory burst involved in inflammatory response	PMID:11443198^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0055089	fatty acid homeostasis	PMID:1184755^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051897	positive regulation of protein kinase B signaling	PMID:11500939^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051092	positive regulation of NF-kappaB transcription factor activity	PMID:19727662^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050995	negative regulation of lipid catabolic process	PMID:11742412^[14]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050709	negative regulation of protein secretion	PMID:14739855^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046889	positive regulation of lipid biosynthetic process	PMID:11742412^[14]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046628	positive regulation of insulin receptor signaling pathway	PMID:7688386^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046326	positive regulation of glucose import	PMID:14615391^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045922	negative regulation of fatty acid metabolic process	PMID:1184755^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045861	negative regulation of proteolysis	PMID:3553851^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045840	positive regulation of mitotic nuclear division	PMID:11500939^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045821	positive regulation of glycolytic process	PMID:381941^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045821	positive regulation of glycolytic process	PMID:7688386^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
	GO:0097017	renal protein absorption	PMID:23022543^[19]	ECO:0000314			P		Figure 4B	complete CACAO 5990
	GO:0097017	renal protein absorption	PMID:23022543^[19]	ECO:0000314			P		Figure 4C	complete CACAO 5991
involved_in	GO:0045818	negative regulation of glycogen catabolic process	PMID:381941^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
	GO:0003985	acetyl-CoA C-acetyltransferase activity	PMID:23564383^[20]	ECO:0000314			F		Figure 5 shows that insulin stimulates ACAT1 activity and expression.	complete CACAO 7646
involved_in	GO:0008284	positive regulation of cell population proliferation	PMID:7688386^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045725	positive regulation of glycogen biosynthetic process	PMID:17925406^[21]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045721	negative regulation of gluconeogenesis	PMID:11742412^[14]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045597	positive regulation of cell differentiation	PMID:11742412^[14]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043410	positive regulation of MAPK cascade	PMID:11500939^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042593	glucose homeostasis	PMID:381941^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042060	wound healing	PMID:9498508^[22]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0033861	negative regulation of NAD(P)H oxidase activity	PMID:11443198^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032880	regulation of protein localization	PMID:14615391^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032270	positive regulation of cellular protein metabolic process	PMID:3553851^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032148	activation of protein kinase B activity	PMID:8702995^[23]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031954	positive regulation of protein autophosphorylation	PMID:3518947^[24]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P01315	P		Seeded From UniProt	complete
involved_in	GO:0030335	positive regulation of cell migration	PMID:12138094^[25]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P01315	P		Seeded From UniProt	complete
involved_in	GO:0030307	positive regulation of cell growth	PMID:11742412^[14]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0022898	regulation of transmembrane transporter activity	PMID:14615391^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0014068	positive regulation of phosphatidylinositol 3-kinase signaling	PMID:7688386^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0008284	positive regulation of cell population proliferation	PMID:17925406^[21]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007186	G protein-coupled receptor signaling pathway	PMID:9092559^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006953	acute-phase response	PMID:14739855^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006521	regulation of cellular amino acid metabolic process	PMID:3553851^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	PMID:12881524^[26]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:9667398^[27]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005179	hormone activity	PMID:381941^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005179	hormone activity	PMID:9667398^[27]	ECO:0000305	curator inference used in manual assertion	GO:0005158	F		Seeded From UniProt	complete
enables	GO:0005159	insulin-like growth factor receptor binding	PMID:8452530^[28]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P08069	F		Seeded From UniProt	complete
enables	GO:0005158	insulin receptor binding	PMID:8452530^[28]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P06213	F		Seeded From UniProt	complete
enables	GO:0005158	insulin receptor binding	PMID:9667398^[27]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0002674	negative regulation of acute inflammatory response	PMID:11443198^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051000	positive regulation of nitric-oxide synthase activity	PMID:12135947^[29]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050715	positive regulation of cytokine secretion	PMID:15473891^[30]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050708	regulation of protein secretion	PMID:15591776^[31]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046631	alpha-beta T cell activation	PMID:10604997^[32]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0097755	positive regulation of blood vessel diameter	PMID:14744991^[33]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0097756	negative regulation of blood vessel diameter	PMID:12946932^[34]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045840	positive regulation of mitotic nuclear division	PMID:10644978^[35]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010750	positive regulation of nitric oxide mediated signal transduction	PMID:14615391^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042177	negative regulation of protein catabolic process	PMID:15185208^[36]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032460	negative regulation of protein oligomerization	PMID:9830016^[37]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P05067)	Seeded From UniProt	complete
involved_in	GO:0046628	positive regulation of insulin receptor signaling pathway	PMID:15792832^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007267	cell-cell signaling	PMID:7556975^[38]	ECO:0000305	curator inference used in manual assertion	GO:0005158	P		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	PMID:7556975^[38]	ECO:0000305	curator inference used in manual assertion	GO:0005158	C		Seeded From UniProt	complete
enables	GO:0005179	hormone activity	PMID:14986111^[39]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005158	insulin receptor binding	PMID:7556975^[38]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0002020	protease binding	PMID:20082125^[40]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P14735	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23510797^[41]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P01308	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23416304^[42]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P01308	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23106816^[43]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P01308	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20738396^[44]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P01308	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:17472440^[45]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P01308	F		Seeded From UniProt	complete
involved_in	GO:0010469	regulation of signaling receptor activity	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0005179	P		Seeded From UniProt	complete
involved_in	GO:0010469	regulation of signaling receptor activity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0005179	P		Seeded From UniProt	complete
involved_in	GO:0010469	regulation of signaling receptor activity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0005179	P		Seeded From UniProt	complete
involved_in	GO:0010469	regulation of signaling receptor activity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0005179	P		Seeded From UniProt	complete
involved_in	GO:0010469	regulation of signaling receptor activity	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0005179	P		Seeded From UniProt	complete
enables	GO:0005179	hormone activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004825 InterPro:IPR016179 InterPro:IPR022352	F		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004825 InterPro:IPR016179	C		Seeded From UniProt	complete
involved_in	GO:1900273	positive regulation of long-term synaptic potentiation	PMID:19188609^[3]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	occurs_in:(UBERON:0002421)	Seeded From UniProt	complete
involved_in	GO:0050890	cognition	PMID:19188609^[3]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0048167	regulation of synaptic plasticity	PMID:19188609^[3]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0090336	positive regulation of brown fat cell differentiation	PMID:11387233^[46]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0090277	positive regulation of peptide hormone secretion	PMID:11387233^[46]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	has_input:(UniProtKB:P41159)	Seeded From UniProt	complete
involved_in	GO:0044267	cellular protein metabolic process	Reactome:R-HSA-392499	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0034774	secretory granule lumen	Reactome:R-NUL-9023186 Reactome:R-NUL-9023180 Reactome:R-NUL-9023166 Reactome:R-NUL-9023165 Reactome:R-HSA-265153	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0033116	endoplasmic reticulum-Golgi intermediate compartment membrane	Reactome:R-HSA-6807877 Reactome:R-HSA-6807875	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0031904	endosome lumen	Reactome:R-HSA-74730 Reactome:R-HSA-74726 Reactome:R-HSA-74718	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030133	transport vesicle	Reactome:R-HSA-6809006 Reactome:R-HSA-6809003 Reactome:R-HSA-6807877	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0008286	insulin receptor signaling pathway	Reactome:R-HSA-74752	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006888	endoplasmic reticulum to Golgi vesicle-mediated transport	Reactome:R-HSA-199977	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005796	Golgi lumen	Reactome:R-HSA-265153 Reactome:R-HSA-265010 Reactome:R-HSA-264976	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005788	endoplasmic reticulum lumen	Reactome:R-HSA-265010 Reactome:R-HSA-264997	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-977136 Reactome:R-HSA-976734 Reactome:R-HSA-74743 Reactome:R-HSA-74742 Reactome:R-HSA-74740 Reactome:R-HSA-74718 Reactome:R-HSA-74716 Reactome:R-HSA-74715 Reactome:R-HSA-74712 Reactome:R-HSA-74711 Reactome:R-HSA-74707 Reactome:R-HSA-110011	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0000139	Golgi membrane	Reactome:R-HSA-6809011 Reactome:R-HSA-6809010 Reactome:R-HSA-6809006	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0964 UniProtKB-SubCell:SL-0243	C		Seeded From UniProt	complete
involved_in	GO:0006006	glucose metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0313	P		Seeded From UniProt	complete
enables	GO:0005179	hormone activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0372	F		Seeded From UniProt	complete
involved_in	GO:0005975	carbohydrate metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0119	P		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 Acevedo, CG et al. (2005) Insulin and nitric oxide stimulates glucose transport in human placenta. Life Sci. 76 2643-53 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Bergandi, L et al. (2003) Insulin stimulates glucose transport via nitric oxide/cyclic GMP pathway in human vascular smooth muscle cells. Arterioscler. Thromb. Vasc. Biol. 23 2215-21 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 ^3.6 De Felice, FG et al. (2009) Protection of synapses against Alzheimer's-linked toxins: insulin signaling prevents the pathogenic binding of Abeta oligomers. Proc. Natl. Acad. Sci. U.S.A. 106 1971-6 PubMed GONUTS page
↑ Bork-Jensen, J et al. (2015) Glucose tolerance is associated with differential expression of microRNAs in skeletal muscle: results from studies of twins with and without type 2 diabetes. Diabetologia 58 363-73 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 Kwon, H et al. (2011) A novel domain of caveolin-2 that controls nuclear targeting: regulation of insulin-specific ERK activation and nuclear translocation by caveolin-2. J. Cell. Mol. Med. 15 888-908 PubMed GONUTS page
↑ Reverchon, M et al. (2014) Resistin in dairy cows: plasma concentrations during early lactation, expression and potential role in adipose tissue. PLoS ONE 9 e93198 PubMed GONUTS page
↑ James, RJ et al. (2007) Milk intake and feeding behavior in the first week of life and its relationship to cord blood ghrelin, leptin, and insulin concentrations. Pediatr. Res. 62 695-9 PubMed GONUTS page
↑ Yu, XR et al. (2006) Neuroprotection of insulin against oxidative stress-induced apoptosis in cultured retinal neurons: involvement of phosphoinositide 3-kinase/Akt signal pathway. Acta Biochim. Biophys. Sin. (Shanghai) 38 241-8 PubMed GONUTS page
↑ ^9.0 ^9.1 Krieger-Brauer, HI et al. (1997) Insulin-induced activation of NADPH-dependent H2O2 generation in human adipocyte plasma membranes is mediated by Galphai2. J. Biol. Chem. 272 10135-43 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 Dandona, P et al. (2001) Insulin inhibits intranuclear nuclear factor kappaB and stimulates IkappaB in mononuclear cells in obese subjects: evidence for an anti-inflammatory effect? J. Clin. Endocrinol. Metab. 86 3257-65 PubMed GONUTS page
↑ ^11.0 ^11.1 Schade, DS & Eaton, RP (1975) Glucagon regulation of plasma ketone body concentration in human diabetes. J. Clin. Invest. 56 1340-4 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 Scalia, P et al. (2001) Regulation of the Akt/Glycogen synthase kinase-3 axis by insulin-like growth factor-II via activation of the human insulin receptor isoform-A. J. Cell. Biochem. 82 610-8 PubMed GONUTS page
↑ Romacho, T et al. (2009) Extracellular PBEF/NAMPT/visfatin activates pro-inflammatory signalling in human vascular smooth muscle cells through nicotinamide phosphoribosyltransferase activity. Diabetologia 52 2455-63 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 ^14.3 ^14.4 Saltiel, AR & Kahn, CR (2001) Insulin signalling and the regulation of glucose and lipid metabolism. Nature 414 799-806 PubMed GONUTS page
↑ ^15.0 ^15.1 Wu, X et al. (2004) Insulin decreases hepatic acute phase protein levels in severely burned children. Surgery 135 196-202 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 ^16.3 Freund, GG et al. (1993) Insulin and IGF-1 increase mitogenesis and glucose metabolism in the multiple myeloma cell line, RPMI 8226. J. Immunol. 151 1811-20 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 Nair, KS et al. (1987) Effect of intravenous insulin treatment on in vivo whole body leucine kinetics and oxygen consumption in insulin-deprived type I diabetic patients. Metab. Clin. Exp. 36 491-5 PubMed GONUTS page
↑ ^18.0 ^18.1 ^18.2 ^18.3 Tager, H et al. (1979) A structurally abnormal insulin causing human diabetes. Nature 281 122-5 PubMed GONUTS page
↑ ^19.0 ^19.1 Nault, L et al. (2013) Human insulin adsorption kinetics, conformational changes and amyloidal aggregate formation on hydrophobic surfaces. Acta Biomater 9 5070-9 PubMed GONUTS page
↑ Ge, J et al. (2013) Insulin induces human acyl-coenzyme A: cholesterol acyltransferase1 gene expression via MAP kinases and CCAAT/enhancer-binding protein α. J. Cell. Biochem. 114 2188-98 PubMed GONUTS page
↑ ^21.0 ^21.1 Jensen, M et al. (2007) Activation of the insulin receptor by insulin and a synthetic peptide leads to divergent metabolic and mitogenic signaling and responses. J. Biol. Chem. 282 35179-86 PubMed GONUTS page
↑ Pierre, EJ et al. (1998) Effects of insulin on wound healing. J Trauma 44 342-5 PubMed GONUTS page
↑ Kohn, AD et al. (1996) Akt, a pleckstrin homology domain containing kinase, is activated primarily by phosphorylation. J. Biol. Chem. 271 21920-6 PubMed GONUTS page
↑ Ellis, L et al. (1986) Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose. Cell 45 721-32 PubMed GONUTS page
↑ Pandini, G et al. (2002) Insulin/insulin-like growth factor I hybrid receptors have different biological characteristics depending on the insulin receptor isoform involved. J. Biol. Chem. 277 39684-95 PubMed GONUTS page
↑ Pandini, G et al. (2003) Differential gene expression induced by insulin and insulin-like growth factor-II through the insulin receptor isoform A. J. Biol. Chem. 278 42178-89 PubMed GONUTS page
↑ ^27.0 ^27.1 ^27.2 Collinet, M et al. (1998) Familial hyperproinsulinaemia due to a mutation substituting histidine for arginine at position 65 in proinsulin: identification of the mutation by restriction enzyme mapping. Eur. J. Pediatr. 157 456-60 PubMed GONUTS page
↑ ^28.0 ^28.1 Soos, MA et al. (1993) Purified hybrid insulin/insulin-like growth factor-I receptors bind insulin-like growth factor-I, but not insulin, with high affinity. Biochem. J. 290 ( Pt 2) 419-26 PubMed GONUTS page
↑ Federici, M et al. (2002) Insulin-dependent activation of endothelial nitric oxide synthase is impaired by O-linked glycosylation modification of signaling proteins in human coronary endothelial cells. Circulation 106 466-72 PubMed GONUTS page
↑ Doronzo, G et al. (2004) Insulin activates vascular endothelial growth factor in vascular smooth muscle cells: influence of nitric oxide and of insulin resistance. Eur. J. Clin. Invest. 34 664-73 PubMed GONUTS page
↑ Allister, EM et al. () Insulin decreases the secretion of apoB-100 from hepatic HepG2 cells but does not decrease the secretion of apoB-48 from intestinal CaCo-2 cells. J. Biomed. Sci. 11 789-98 PubMed GONUTS page
↑ Ma, H et al. (2000) Bovine and human insulin activate CD8+-autoreactive CTL expressing both type 1 and type 2 cytokines in C57BL/6 mice. J. Immunol. 164 86-92 PubMed GONUTS page
↑ Randriamboavonjy, V et al. (2004) Insulin induces the release of vasodilator compounds from platelets by a nitric oxide-G kinase-VAMP-3-dependent pathway. J. Exp. Med. 199 347-56 PubMed GONUTS page
↑ Campia, U et al. (2004) Insulin impairs endothelium-dependent vasodilation independent of insulin sensitivity or lipid profile. Am. J. Physiol. Heart Circ. Physiol. 286 H76-82 PubMed GONUTS page
↑ Riedel, H et al. (2000) PSM, a mediator of PDGF-BB-, IGF-I-, and insulin-stimulated mitogenesis. Oncogene 19 39-50 PubMed GONUTS page
↑ Agus, MS et al. (2004) Intravenous insulin decreases protein breakdown in infants on extracorporeal membrane oxygenation. J. Pediatr. Surg. 39 839-44; discussion 839-44 PubMed GONUTS page
↑ Qiu, WQ et al. (1998) Insulin-degrading enzyme regulates extracellular levels of amyloid beta-protein by degradation. J. Biol. Chem. 273 32730-8 PubMed GONUTS page
↑ ^38.0 ^38.1 ^38.2 Kotzke, G et al. (1995) Binding of human, porcine and bovine insulin to insulin receptors from human brain, muscle and adipocytes and to expressed recombinant alternatively spliced insulin receptor isoforms. Diabetologia 38 757-63 PubMed GONUTS page
↑ Chakraborty, S et al. (2004) Impaired binding of insulin to erythrocyte membrane receptor and the activation of nitric oxide synthase by the hormone in human breast cancer. J. Cancer Res. Clin. Oncol. 130 294-300 PubMed GONUTS page
↑ Zhang, WJ et al. (2010) In vitro degradation of insulin-like peptide 3 by insulin-degrading enzyme. Protein J. 29 93-8 PubMed GONUTS page
↑ Nault, L et al. (2013) Peptides that form β-sheets on hydrophobic surfaces accelerate surface-induced insulin amyloidal aggregation. FEBS Lett. 587 1281-6 PubMed GONUTS page
↑ Babenko, V & Dzwolak, W (2013) Amino acid sequence determinants in self-assembly of insulin chiral amyloid superstructures: role of C-terminus of B-chain in association of fibrils. FEBS Lett. 587 625-30 PubMed GONUTS page
↑ Landreh, M et al. (2012) Insulin solubility transitions by pH-dependent interactions with proinsulin C-peptide. FEBS J. 279 4589-97 PubMed GONUTS page
↑ Lind, J et al. (2010) Structural features of proinsulin C-peptide oligomeric and amyloid states. FEBS J. 277 3759-68 PubMed GONUTS page
↑ Vestergaard, B et al. (2007) A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils. PLoS Biol. 5 e134 PubMed GONUTS page
↑ ^46.0 ^46.1 Buyse, M et al. (2001) Insulin and glucocorticoids differentially regulate leptin transcription and secretion in brown adipocytes. FASEB J. 15 1357-66 PubMed GONUTS page

[PMID:15792832-1] 1.0 ^1.1 ^1.2 Acevedo, CG et al. (2005) Insulin and nitric oxide stimulates glucose transport in human placenta. Life Sci. 76 2643-53 PubMed GONUTS page

[PMID:14615391-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Bergandi, L et al. (2003) Insulin stimulates glucose transport via nitric oxide/cyclic GMP pathway in human vascular smooth muscle cells. Arterioscler. Thromb. Vasc. Biol. 23 2215-21 PubMed GONUTS page

[PMID:19188609-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 ^3.6 De Felice, FG et al. (2009) Protection of synapses against Alzheimer's-linked toxins: insulin signaling prevents the pathogenic binding of Abeta oligomers. Proc. Natl. Acad. Sci. U.S.A. 106 1971-6 PubMed GONUTS page

[PMID:25403480-4] Bork-Jensen, J et al. (2015) Glucose tolerance is associated with differential expression of microRNAs in skeletal muscle: results from studies of twins with and without type 2 diabetes. Diabetologia 58 363-73 PubMed GONUTS page

[PMID:20455999-5] 5.0 ^5.1 ^5.2 Kwon, H et al. (2011) A novel domain of caveolin-2 that controls nuclear targeting: regulation of insulin-specific ERK activation and nuclear translocation by caveolin-2. J. Cell. Mol. Med. 15 888-908 PubMed GONUTS page

[PMID:24675707-6] Reverchon, M et al. (2014) Resistin in dairy cows: plasma concentrations during early lactation, expression and potential role in adipose tissue. PLoS ONE 9 e93198 PubMed GONUTS page

[PMID:17957153-7] James, RJ et al. (2007) Milk intake and feeding behavior in the first week of life and its relationship to cord blood ghrelin, leptin, and insulin concentrations. Pediatr. Res. 62 695-9 PubMed GONUTS page

[PMID:16604263-8] Yu, XR et al. (2006) Neuroprotection of insulin against oxidative stress-induced apoptosis in cultured retinal neurons: involvement of phosphoinositide 3-kinase/Akt signal pathway. Acta Biochim. Biophys. Sin. (Shanghai) 38 241-8 PubMed GONUTS page

[PMID:9092559-9] 9.0 ^9.1 Krieger-Brauer, HI et al. (1997) Insulin-induced activation of NADPH-dependent H2O2 generation in human adipocyte plasma membranes is mediated by Galphai2. J. Biol. Chem. 272 10135-43 PubMed GONUTS page

[PMID:11443198-10] 10.0 ^10.1 ^10.2 Dandona, P et al. (2001) Insulin inhibits intranuclear nuclear factor kappaB and stimulates IkappaB in mononuclear cells in obese subjects: evidence for an anti-inflammatory effect? J. Clin. Endocrinol. Metab. 86 3257-65 PubMed GONUTS page

[PMID:1184755-11] 11.0 ^11.1 Schade, DS & Eaton, RP (1975) Glucagon regulation of plasma ketone body concentration in human diabetes. J. Clin. Invest. 56 1340-4 PubMed GONUTS page

[PMID:11500939-12] 12.0 ^12.1 ^12.2 Scalia, P et al. (2001) Regulation of the Akt/Glycogen synthase kinase-3 axis by insulin-like growth factor-II via activation of the human insulin receptor isoform-A. J. Cell. Biochem. 82 610-8 PubMed GONUTS page

[PMID:19727662-13] Romacho, T et al. (2009) Extracellular PBEF/NAMPT/visfatin activates pro-inflammatory signalling in human vascular smooth muscle cells through nicotinamide phosphoribosyltransferase activity. Diabetologia 52 2455-63 PubMed GONUTS page

[PMID:11742412-14] 14.0 ^14.1 ^14.2 ^14.3 ^14.4 Saltiel, AR & Kahn, CR (2001) Insulin signalling and the regulation of glucose and lipid metabolism. Nature 414 799-806 PubMed GONUTS page

[PMID:14739855-15] 15.0 ^15.1 Wu, X et al. (2004) Insulin decreases hepatic acute phase protein levels in severely burned children. Surgery 135 196-202 PubMed GONUTS page

[PMID:7688386-16] 16.0 ^16.1 ^16.2 ^16.3 Freund, GG et al. (1993) Insulin and IGF-1 increase mitogenesis and glucose metabolism in the multiple myeloma cell line, RPMI 8226. J. Immunol. 151 1811-20 PubMed GONUTS page

[PMID:3553851-17] 17.0 ^17.1 ^17.2 Nair, KS et al. (1987) Effect of intravenous insulin treatment on in vivo whole body leucine kinetics and oxygen consumption in insulin-deprived type I diabetic patients. Metab. Clin. Exp. 36 491-5 PubMed GONUTS page

[PMID:381941-18] 18.0 ^18.1 ^18.2 ^18.3 Tager, H et al. (1979) A structurally abnormal insulin causing human diabetes. Nature 281 122-5 PubMed GONUTS page

[PMID:23022543-19] 19.0 ^19.1 Nault, L et al. (2013) Human insulin adsorption kinetics, conformational changes and amyloidal aggregate formation on hydrophobic surfaces. Acta Biomater 9 5070-9 PubMed GONUTS page

[PMID:23564383-20] Ge, J et al. (2013) Insulin induces human acyl-coenzyme A: cholesterol acyltransferase1 gene expression via MAP kinases and CCAAT/enhancer-binding protein α. J. Cell. Biochem. 114 2188-98 PubMed GONUTS page

[PMID:17925406-21] 21.0 ^21.1 Jensen, M et al. (2007) Activation of the insulin receptor by insulin and a synthetic peptide leads to divergent metabolic and mitogenic signaling and responses. J. Biol. Chem. 282 35179-86 PubMed GONUTS page

[PMID:9498508-22] Pierre, EJ et al. (1998) Effects of insulin on wound healing. J Trauma 44 342-5 PubMed GONUTS page

[PMID:8702995-23] Kohn, AD et al. (1996) Akt, a pleckstrin homology domain containing kinase, is activated primarily by phosphorylation. J. Biol. Chem. 271 21920-6 PubMed GONUTS page

[PMID:3518947-24] Ellis, L et al. (1986) Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose. Cell 45 721-32 PubMed GONUTS page

[PMID:12138094-25] Pandini, G et al. (2002) Insulin/insulin-like growth factor I hybrid receptors have different biological characteristics depending on the insulin receptor isoform involved. J. Biol. Chem. 277 39684-95 PubMed GONUTS page

[PMID:12881524-26] Pandini, G et al. (2003) Differential gene expression induced by insulin and insulin-like growth factor-II through the insulin receptor isoform A. J. Biol. Chem. 278 42178-89 PubMed GONUTS page

[PMID:9667398-27] 27.0 ^27.1 ^27.2 Collinet, M et al. (1998) Familial hyperproinsulinaemia due to a mutation substituting histidine for arginine at position 65 in proinsulin: identification of the mutation by restriction enzyme mapping. Eur. J. Pediatr. 157 456-60 PubMed GONUTS page

[PMID:8452530-28] 28.0 ^28.1 Soos, MA et al. (1993) Purified hybrid insulin/insulin-like growth factor-I receptors bind insulin-like growth factor-I, but not insulin, with high affinity. Biochem. J. 290 ( Pt 2) 419-26 PubMed GONUTS page

[PMID:12135947-29] Federici, M et al. (2002) Insulin-dependent activation of endothelial nitric oxide synthase is impaired by O-linked glycosylation modification of signaling proteins in human coronary endothelial cells. Circulation 106 466-72 PubMed GONUTS page

[PMID:15473891-30] Doronzo, G et al. (2004) Insulin activates vascular endothelial growth factor in vascular smooth muscle cells: influence of nitric oxide and of insulin resistance. Eur. J. Clin. Invest. 34 664-73 PubMed GONUTS page

[PMID:15591776-31] Allister, EM et al. () Insulin decreases the secretion of apoB-100 from hepatic HepG2 cells but does not decrease the secretion of apoB-48 from intestinal CaCo-2 cells. J. Biomed. Sci. 11 789-98 PubMed GONUTS page

[PMID:10604997-32] Ma, H et al. (2000) Bovine and human insulin activate CD8+-autoreactive CTL expressing both type 1 and type 2 cytokines in C57BL/6 mice. J. Immunol. 164 86-92 PubMed GONUTS page

[PMID:14744991-33] Randriamboavonjy, V et al. (2004) Insulin induces the release of vasodilator compounds from platelets by a nitric oxide-G kinase-VAMP-3-dependent pathway. J. Exp. Med. 199 347-56 PubMed GONUTS page

[PMID:12946932-34] Campia, U et al. (2004) Insulin impairs endothelium-dependent vasodilation independent of insulin sensitivity or lipid profile. Am. J. Physiol. Heart Circ. Physiol. 286 H76-82 PubMed GONUTS page

[PMID:10644978-35] Riedel, H et al. (2000) PSM, a mediator of PDGF-BB-, IGF-I-, and insulin-stimulated mitogenesis. Oncogene 19 39-50 PubMed GONUTS page

[PMID:15185208-36] Agus, MS et al. (2004) Intravenous insulin decreases protein breakdown in infants on extracorporeal membrane oxygenation. J. Pediatr. Surg. 39 839-44; discussion 839-44 PubMed GONUTS page

[PMID:9830016-37] Qiu, WQ et al. (1998) Insulin-degrading enzyme regulates extracellular levels of amyloid beta-protein by degradation. J. Biol. Chem. 273 32730-8 PubMed GONUTS page

[PMID:7556975-38] 38.0 ^38.1 ^38.2 Kotzke, G et al. (1995) Binding of human, porcine and bovine insulin to insulin receptors from human brain, muscle and adipocytes and to expressed recombinant alternatively spliced insulin receptor isoforms. Diabetologia 38 757-63 PubMed GONUTS page

[PMID:14986111-39] Chakraborty, S et al. (2004) Impaired binding of insulin to erythrocyte membrane receptor and the activation of nitric oxide synthase by the hormone in human breast cancer. J. Cancer Res. Clin. Oncol. 130 294-300 PubMed GONUTS page

[PMID:20082125-40] Zhang, WJ et al. (2010) In vitro degradation of insulin-like peptide 3 by insulin-degrading enzyme. Protein J. 29 93-8 PubMed GONUTS page

[PMID:23510797-41] Nault, L et al. (2013) Peptides that form β-sheets on hydrophobic surfaces accelerate surface-induced insulin amyloidal aggregation. FEBS Lett. 587 1281-6 PubMed GONUTS page

[PMID:23416304-42] Babenko, V & Dzwolak, W (2013) Amino acid sequence determinants in self-assembly of insulin chiral amyloid superstructures: role of C-terminus of B-chain in association of fibrils. FEBS Lett. 587 625-30 PubMed GONUTS page

[PMID:23106816-43] Landreh, M et al. (2012) Insulin solubility transitions by pH-dependent interactions with proinsulin C-peptide. FEBS J. 279 4589-97 PubMed GONUTS page

[PMID:20738396-44] Lind, J et al. (2010) Structural features of proinsulin C-peptide oligomeric and amyloid states. FEBS J. 277 3759-68 PubMed GONUTS page

[PMID:17472440-45] Vestergaard, B et al. (2007) A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils. PLoS Biol. 5 e134 PubMed GONUTS page

[PMID:11387233-46] 46.0 ^46.1 Buyse, M et al. (2001) Insulin and glucocorticoids differentially regulate leptin transcription and secretion in brown adipocytes. FASEB J. 15 1357-66 PubMed GONUTS page

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