UniProtKB - P01308 (INS_HUMAN)

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History
Entry version 237 (23 May 2018)
Sequence version 1 (21 Jul 1986)
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Protein

Insulin

Gene

INS

Organism

Homo sapiens (Human)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

activation of protein kinase B activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 8702995
acute-phase response
Source: BHF-UCL
Inferred from direct assayⁱ
- 14739855
alpha-beta T cell activation
Source: UniProtKB
Inferred from direct assayⁱ
- 10604997
cell-cell signaling
Source: UniProtKB
Inferred by curatorⁱ
- 7556975
cellular protein metabolic process Source: Reactome
cognition
Source: ARUK-UCL
Traceable author statementⁱ
- 19188609
ER to Golgi vesicle-mediated transport Source: Reactome
fatty acid homeostasis
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 1184755
glucose homeostasis
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 381941
glucose metabolic process Source: UniProtKB-KW
G-protein coupled receptor signaling pathway
Source: BHF-UCL
Inferred from direct assayⁱ
- 9092559
insulin receptor signaling pathway
Source: BHF-UCL
Inferred from direct assayⁱ
- 20455999
MAPK cascade
Source: BHF-UCL
Inferred from direct assayⁱ
- 11278339
negative regulation of acute inflammatory response
Source: BHF-UCL
Inferred from direct assayⁱ
- 11443198
negative regulation of blood vessel diameter
Source: UniProtKB
Non-traceable author statementⁱ
- 12946932
negative regulation of fatty acid metabolic process
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 1184755
negative regulation of feeding behavior
Source: DFLAT
Inferred from direct assayⁱ
- 17957153
negative regulation of gluconeogenesis
Source: BHF-UCL
Non-traceable author statementⁱ
- 11742412
negative regulation of glycogen catabolic process
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 381941
negative regulation of lipid catabolic process
Source: AgBase
Inferred from mutant phenotypeⁱ
- 24675707
negative regulation of NAD(P)H oxidase activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 11443198
negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
Source: BHF-UCL
Non-traceable author statementⁱ
- 16604263
negative regulation of protein catabolic process
Source: UniProtKB
Inferred from direct assayⁱ
- 15185208
negative regulation of protein oligomerization
Source: UniProtKB
Inferred from direct assayⁱ
- 9830016
negative regulation of protein secretion
Source: BHF-UCL
Inferred from direct assayⁱ
- 14739855
negative regulation of proteolysis
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 3553851
negative regulation of reactive oxygen species biosynthetic process
Source: ARUK-UCL
Inferred from genetic interactionⁱ
- 19188609
negative regulation of respiratory burst involved in inflammatory response
Source: BHF-UCL
Inferred from direct assayⁱ
- 11443198
neuron projection maintenance
Source: ARUK-UCL
Inferred from genetic interactionⁱ
- 19188609
positive regulation of blood vessel diameter
Source: UniProtKB
Non-traceable author statementⁱ
- 14744991
positive regulation of brown fat cell differentiation
Source: BHF-UCL
Traceable author statementⁱ
- 11387233
positive regulation of cell differentiation
Source: BHF-UCL
Non-traceable author statementⁱ
- 11742412
positive regulation of cell growth
Source: BHF-UCL
Non-traceable author statementⁱ
- 11742412
positive regulation of cell migration
Source: BHF-UCL
Inferred from sequence or structural similarityⁱ
- 12138094
positive regulation of cell proliferation
Source: BHF-UCL
Inferred from direct assayⁱ
- 17925406
- 7688386
positive regulation of cellular protein metabolic process
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 3553851
positive regulation of cytokine secretion
Source: UniProtKB
Inferred from direct assayⁱ
- 15473891
positive regulation of dendritic spine maintenance
Source: ARUK-UCL
Inferred from genetic interactionⁱ
- 19188609
positive regulation of gene expression
Source: BHF-UCL
Inferred from genetic interactionⁱ
- 25403480
positive regulation of glucose import
Source: UniProtKB
Inferred from direct assayⁱ
- 15792832
positive regulation of glucose import in response to insulin stimulus
Source: UniProtKB
Inferred from direct assayⁱ
- 15792832
positive regulation of glycogen biosynthetic process
Source: BHF-UCL
Inferred from direct assayⁱ
- 17925406
positive regulation of glycolytic process
Source: BHF-UCL
Inferred from direct assayⁱ
- 7688386
positive regulation of insulin receptor signaling pathway
Source: BHF-UCL
Inferred from direct assayⁱ
- 7688386
positive regulation of lipid biosynthetic process
Source: BHF-UCL
Non-traceable author statementⁱ
- 11742412
positive regulation of long-term synaptic potentiation
Source: ARUK-UCL
Traceable author statementⁱ
- 19188609
positive regulation of MAPK cascade
Source: BHF-UCL
Inferred from direct assayⁱ
- 20455999
- 11500939
positive regulation of mitotic nuclear division
Source: UniProtKB
Inferred from direct assayⁱ
- 10644978
positive regulation of NF-kappaB transcription factor activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 19727662
positive regulation of nitric oxide mediated signal transduction
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 14615391
positive regulation of nitric-oxide synthase activity
Source: UniProtKB
Non-traceable author statementⁱ
- 12135947
positive regulation of peptide hormone secretion
Source: BHF-UCL
Traceable author statementⁱ
- 11387233
positive regulation of peptidyl-tyrosine phosphorylation
Source: BHF-UCL
Inferred from direct assayⁱ
- 11278339
positive regulation of phosphatidylinositol 3-kinase signaling
Source: BHF-UCL
Inferred from direct assayⁱ
- 7688386
positive regulation of protein autophosphorylation
Source: BHF-UCL
Inferred from sequence or structural similarityⁱ
- 3518947
positive regulation of protein kinase B signaling
Source: BHF-UCL
Inferred from direct assayⁱ
- 11500939
positive regulation of protein localization to nucleus
Source: BHF-UCL
Inferred from direct assayⁱ
- 20455999
positive regulation of respiratory burst
Source: BHF-UCL
Inferred from direct assayⁱ
- 9092559
regulation of cellular amino acid metabolic process
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 3553851
regulation of protein localization
Source: BHF-UCL
Inferred from direct assayⁱ
- 14615391
regulation of protein localization to plasma membrane
Source: ARUK-UCL
Inferred from genetic interactionⁱ
- 19188609
regulation of protein secretion
Source: UniProtKB
Inferred from direct assayⁱ
- 15591776
regulation of synaptic plasticity
Source: ARUK-UCL
Traceable author statementⁱ
- 19188609
regulation of transcription, DNA-templated
Source: BHF-UCL
Non-traceable author statementⁱ
- 12881524
regulation of transmembrane transporter activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 14615391
wound healing
Source: BHF-UCL
Inferred from direct assayⁱ
- 9498508

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hormone
Biological process	Carbohydrate metabolism, Glucose metabolism

Enzyme and pathway databases

BioCycⁱ	MetaCyc:MONOMER-16190
Reactomeⁱ	R-HSA-210745 Regulation of gene expression in beta cells R-HSA-264876 Insulin processing R-HSA-422085 Synthesis, secretion, and deacylation of Ghrelin R-HSA-422356 Regulation of insulin secretion R-HSA-6807878 COPI-mediated anterograde transport R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling R-HSA-74713 IRS activation R-HSA-74749 Signal attenuation R-HSA-74751 Insulin receptor signalling cascade R-HSA-74752 Signaling by Insulin receptor R-HSA-77387 Insulin receptor recycling R-HSA-977225 Amyloid fiber formation
SignaLinkⁱ	P01308
SIGNORⁱ	P01308

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Insulin Cleaved into the following 2 chains: Insulin B chain Insulin A chain
Gene namesⁱ	Name:INS
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 11

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000254647.6
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:6081 INS
MIMⁱ	176730 gene
neXtProtⁱ	NX_P01308

Keywords - Cellular componentⁱ

Secreted

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Hyperproinsulinemia (HPRI)4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal dominant condition characterized by elevated levels of serum proinsulin-like material.

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_003971	34	H → D in HPRI; Providence. 1 PublicationCorresponds to variant dbSNP:rs121918101EnsemblClinVar.	1
Natural variantⁱVAR_003974	89	R → H in HPRI; impairs post-translational cleavage. 2 PublicationsCorresponds to variant dbSNP:rs28933985EnsemblClinVar.	1
Natural variantⁱVAR_003975	89	R → L in HPRI; Kyoto. 1 PublicationCorresponds to variant dbSNP:rs28933985EnsemblClinVar.	1

Diabetes mellitus, insulin-dependent, 2 (IDDM2)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA multifactorial disorder of glucose homeostasis that is characterized by susceptibility to ketoacidosis in the absence of insulin therapy. Clinical features are polydipsia, polyphagia and polyuria which result from hyperglycemia-induced osmotic diuresis and secondary thirst. These derangements result in long-term complications that affect the eyes, kidneys, nerves, and blood vessels.

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_063732	55	R → C in IDDM2. 1 PublicationCorresponds to variant dbSNP:rs121908261EnsemblClinVar.		1

Diabetes mellitus, permanent neonatal (PNDM)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA rare form of diabetes distinct from childhood-onset autoimmune diabetes mellitus type 1. It is characterized by insulin-requiring hyperglycemia that is diagnosed within the first months of life. Permanent neonatal diabetes requires lifelong therapy.

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_063723	24	A → D in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356663EnsemblClinVar.	1
Natural variantⁱVAR_063724	29	H → D in PNDM. 1 PublicationCorresponds to variant dbSNP:rs121908272EnsemblClinVar.	1
Natural variantⁱVAR_063725	32	G → R in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356664EnsemblClinVar.	1
Natural variantⁱVAR_063726	32	G → S in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356664EnsemblClinVar.	1
Natural variantⁱVAR_063727	35	L → P in PNDM. 1 PublicationCorresponds to variant dbSNP:rs121908273EnsemblClinVar.	1
Natural variantⁱVAR_063728	43	C → G in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356666EnsemblClinVar.	1
Natural variantⁱVAR_063730	47	G → V in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356667EnsemblClinVar.	1
Natural variantⁱVAR_063731	48	F → C in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356668EnsemblClinVar.	1
Natural variantⁱVAR_063734	84	G → R in PNDM; uncertain pathological significance. 1 PublicationCorresponds to variant dbSNP:rs121908274EnsemblClinVar.	1
Natural variantⁱVAR_063735	89	R → C in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356669EnsemblClinVar.	1
Natural variantⁱVAR_063736	90	G → C in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356670EnsemblClinVar.	1
Natural variantⁱVAR_063737	96	C → S in PNDM. 1 PublicationCorresponds to variant dbSNP:rs80356671EnsemblClinVar.	1
Natural variantⁱVAR_063738	96	C → Y in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356671EnsemblClinVar.	1
Natural variantⁱVAR_063739	101	S → C in PNDM. 1 PublicationCorresponds to variant dbSNP:rs121908276EnsemblClinVar.	1
Natural variantⁱVAR_063740	103	Y → C in PNDM. 1 PublicationCorresponds to variant dbSNP:rs121908277EnsemblClinVar.	1
Natural variantⁱVAR_063741	108	Y → C in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356672EnsemblClinVar.	1

Maturity-onset diabetes of the young 10 (MODY10)4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA form of diabetes that is characterized by an autosomal dominant mode of inheritance, onset in childhood or early adulthood (usually before 25 years of age), a primary defect in insulin secretion and frequent insulin-independence at the beginning of the disease.

Pharmaceutical useⁱ

Available under the names Humulin or Humalog (Eli Lilly) and Novolin (Novo Nordisk). Used in the treatment of diabetes. Humalog is an insulin analog with 52-Lys-Pro-53 instead of 52-Pro-Lys-53.

Keywords - Diseaseⁱ

Diabetes mellitus, Disease mutation

Organism-specific databases

DisGeNET More...DisGeNETⁱ	3630
GeneReviewsⁱ	INS
MalaCards human disease database More...MalaCardsⁱ	INS
MIMⁱ	125852 phenotype 606176 phenotype 613370 phenotype 616214 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000254647
Orphanetⁱ	552 MODY 99885 Permanent neonatal diabetes mellitus
PharmGKBⁱ	PA201

Protein family/group databases

Allergomeⁱ	2121 Hom s Insulin

Allergomeⁱ

2121 Hom s Insulin

Chemistry databases

ChEMBLⁱ	CHEMBL5881
Drug and drug target database More...DrugBankⁱ	DB01776 M-Cresol DB08231 MYRISTIC ACID

Polymorphism and mutation databases

BioMutaⁱ	INS
DMDMⁱ	124617

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Length
Signal peptideⁱ	1 – 24	1 PublicationAdd BLAST	24
PeptideⁱPRO_0000015819	25 – 54	Insulin B chainAdd BLAST	30
PropeptideⁱPRO_0000015820	57 – 87	C peptideAdd BLAST	31
PeptideⁱPRO_0000015821	90 – 110	Insulin A chainAdd BLAST	21

Amino acid modifications

Feature key	Position(s)	DescriptionActions
Disulfide bondⁱ	31 ↔ 96	Interchain (between B and A chains)Combined sources3 Publications
Disulfide bondⁱ	43 ↔ 109	Interchain (between B and A chains)Combined sources3 Publications
Disulfide bondⁱ	95 ↔ 100	Combined sources5 Publications

Keywords - PTMⁱ

Cleavage on pair of basic residues, Disulfide bond

Proteomic databases

PaxDbⁱ	P01308
PeptideAtlas More...PeptideAtlasⁱ	P01308
PRIDEⁱ	P01308

PTM databases

CarbonylDBⁱ	P01308
iPTMnetⁱ	P01308
PhosphoSitePlusⁱ	P01308

Miscellaneous databases

PMAP-CutDBⁱ	P01308

PMAP-CutDBⁱ

P01308

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000254647
ExpressionAtlasⁱ	P01308 baseline and differential
Genevisibleⁱ	P01308 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB000048 CAB012098 CAB053843 HPA004932

HPAⁱ

CAB000048
CAB012098
CAB053843
HPA004932

Interactionⁱ

Subunit structureⁱ

Heterodimer of a B chain and an A chain linked by two disulfide bonds (PubMed:25423173).1 Publication

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
itself		18	EBI-7090529,EBI-7090529
IDE	P14735-1	3	EBI-7090529,EBI-15607031
INSR	P06213-2	3	EBI-7090529,EBI-9984921
KRTAP1-1	Q07627	4	EBI-7090529,EBI-11959885

Show more details

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	109842, 13 interactors
Database of interacting proteins More...DIPⁱ	DIP-6024N
IntActⁱ	P01308, 11 interactors
Molecular INTeraction database More...MINTⁱ	P01308
STRINGⁱ	9606.ENSP00000250971

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	26 – 29	Combined sources	4
Helixⁱ	33 – 43	Combined sources	11
Helixⁱ	44 – 46	Combined sources	3
Beta strandⁱ	48 – 50	Combined sources	3
Beta strandⁱ	56 – 58	Combined sources	3
Turnⁱ	59 – 66	Combined sources	8
Beta strandⁱ	74 – 76	Combined sources	3
Helixⁱ	79 – 81	Combined sources	3
Turnⁱ	84 – 86	Combined sources	3
Helixⁱ	91 – 97	Combined sources	7
Beta strandⁱ	98 – 101	Combined sources	4
Helixⁱ	102 – 106	Combined sources	5
Turnⁱ	107 – 109	Combined sources	3

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1A7F	NMR	-	A	90-110	[»]
				B	25-53	[»]
	1AI0	NMR	-	A/C/E/G/I/K	90-110	[»]
				B/D/F/H/J/L	25-54	[»]
	1AIY	NMR	-	A/C/E/G/I/K	90-110	[»]
				B/D/F/H/J/L	25-54	[»]
	1B9E	X-ray	2.50	A/C	90-110	[»]
				B/D	25-54	[»]
	1BEN	X-ray	1.40	A/C	90-110	[»]
				B/D	25-54	[»]
	1EFE	NMR	-	A	25-54	[»]
				A	90-110	[»]
	1EV3	X-ray	1.78	A/C	90-110	[»]
				B/D	25-54	[»]
	1EV6	X-ray	1.90	A/C/E/G/I/K	90-110	[»]
				B/D/F/H/J/L	25-54	[»]
	1EVR	X-ray	1.90	A/C/E/G/I/K	90-110	[»]
				B/D/F/H/J/L	25-54	[»]
	1FU2	X-ray	3.24	A/C/E/G	90-110	[»]
				B/D/F/H	25-54	[»]
	1FUB	X-ray	3.09	A/C	90-110	[»]
				B/D	25-54	[»]
	1G7A	X-ray	1.20	A/C/E/G	90-110	[»]
				B/D/F/H	25-54	[»]
	1G7B	X-ray	1.30	A/C/E/G	90-110	[»]
				B/D/F/H	25-54	[»]
	1GUJ	X-ray	1.62	A/C	90-110	[»]
				B/D	25-54	[»]
	1HIQ	NMR	-	A	90-110	[»]
				B	25-54	[»]
	1HIS	NMR	-	A	90-110	[»]
				B	25-49	[»]
	1HIT	NMR	-	A	90-110	[»]
				B	25-54	[»]
	1HLS	NMR	-	A	90-110	[»]
				B	25-54	[»]
	1HTV	X-ray	1.90	A/C/E/G/I/K	90-110	[»]
				B/D/F/H/J/L	25-51	[»]
	1HUI	NMR	-	A	90-110	[»]
				B	26-53	[»]
	1IOG	NMR	-	A	90-110	[»]
				B	25-53	[»]
	1IOH	NMR	-	A	90-110	[»]
				B	25-53	[»]
	1J73	X-ray	2.00	A/C	90-110	[»]
				B/D	25-54	[»]
	1JCA	X-ray	2.50	A/C	90-110	[»]
				B/D	25-54	[»]
	1JCO	NMR	-	A	90-110	[»]
				B	25-54	[»]
	1JK8	X-ray	2.40	C	35-47	[»]
	1K3M	NMR	-	A	90-110	[»]
				B	25-54	[»]
	1KMF	NMR	-	A	90-110	[»]
				B	25-54	[»]
	1LKQ	NMR	-	A	90-110	[»]
				B	25-54	[»]
	1LPH	X-ray	2.30	A/C	90-110	[»]
				B/D	25-54	[»]
	1MHI	NMR	-	A	90-110	[»]
				B	25-54	[»]
	1MHJ	NMR	-	A	90-110	[»]
				B	25-54	[»]
1MSO	X-ray	1.00	A/C	90-110	[»]
			B/D	25-54	[»]
1OS3	X-ray	1.95	A/C	90-110	[»]
			B/D	25-54	[»]
1OS4	X-ray	2.25	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-54	[»]
1Q4V	X-ray	2.00	A/C	90-110	[»]
			B/D	25-54	[»]
1QIY	X-ray	2.30	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-54	[»]
1QIZ	X-ray	2.00	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-54	[»]
1QJ0	X-ray	2.40	A/C	90-110	[»]
			B/D	25-54	[»]
1RWE	X-ray	1.80	A/C	90-110	[»]
			B/D	25-54	[»]
1SF1	NMR	-	A	90-110	[»]
			B	25-54	[»]
1SJT	NMR	-	A	90-110	[»]
			B	25-51	[»]
1SJU	NMR	-	A	25-110	[»]
1T0C	NMR	-	A	57-87	[»]
1T1K	NMR	-	A	90-110	[»]
			B	25-54	[»]
1T1P	NMR	-	A	90-110	[»]
			B	25-54	[»]
1T1Q	NMR	-	A	90-110	[»]
			B	25-54	[»]
1TRZ	X-ray	1.60	A/C	90-110	[»]
			B/D	25-54	[»]
1TYL	X-ray	1.90	A/C	90-110	[»]
			B/D	25-54	[»]
1TYM	X-ray	1.90	A/C	90-110	[»]
			B/D	25-54	[»]
1UZ9	X-ray	1.60	A	90-110	[»]
			B	25-53	[»]
1VKT	NMR	-	A	90-110	[»]
			B	25-54	[»]
1W8P	X-ray	2.08	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-54	[»]
1XDA	X-ray	1.80	A/C/E/G	90-110	[»]
			B/D/F/H	25-53	[»]
1XGL	NMR	-	A	90-110	[»]
			B	25-54	[»]
1XW7	X-ray	2.30	A/C	90-110	[»]
			B/D	25-54	[»]
1ZEG	X-ray	1.60	A/C	90-110	[»]
			B/D	25-54	[»]
1ZEH	X-ray	1.50	A/C	90-110	[»]
			B/D	25-54	[»]
1ZNJ	X-ray	2.00	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-54	[»]
2AIY	NMR	-	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-54	[»]
2C8Q	X-ray	1.95	A	90-110	[»]
			B	25-53	[»]
2C8R	X-ray	1.50	A	90-110	[»]
			B	25-53	[»]
2CEU	X-ray	1.80	A/C	90-110	[»]
			B/D	25-49	[»]
2G54	X-ray	2.25	C/D	25-54	[»]
2G56	X-ray	2.20	C/D	25-54	[»]
2H67	NMR	-	A	90-110	[»]
			B	25-54	[»]
2HH4	NMR	-	A	90-110	[»]
			B	25-54	[»]
2HHO	NMR	-	A	90-110	[»]
			B	25-54	[»]
2HIU	NMR	-	A	90-110	[»]
			B	25-54	[»]
2JMN	NMR	-	A	90-110	[»]
			B	25-54	[»]
2JUM	NMR	-	A	90-110	[»]
			B	25-54	[»]
2JUU	NMR	-	A	90-110	[»]
			B	25-54	[»]
2JUV	NMR	-	A	90-110	[»]
			B	25-54	[»]
2JV1	NMR	-	A	90-110	[»]
			B	25-54	[»]
2JZQ	NMR	-	A	25-54	[»]
			A	90-110	[»]
2K91	NMR	-	A	90-110	[»]
			B	25-54	[»]
2K9R	NMR	-	A	90-110	[»]
			B	25-54	[»]
2KJJ	NMR	-	A	90-110	[»]
			B	25-54	[»]
2KJU	NMR	-	A	90-110	[»]
			B	25-54	[»]
2KQP	NMR	-	A	25-110	[»]
2KQQ	NMR	-	A	90-110	[»]
			B	25-54	[»]
2KXK	NMR	-	A	90-110	[»]
			B	25-54	[»]
2L1Y	NMR	-	A	90-110	[»]
			B	25-54	[»]
2L1Z	NMR	-	A	90-110	[»]
			B	25-54	[»]
2LGB	NMR	-	A	90-110	[»]
			B	25-55	[»]
2LWZ	NMR	-	A	25-54	[»]
			A	89-110	[»]
2M1D	NMR	-	A	90-110	[»]
			B	25-54	[»]
2M1E	NMR	-	A	90-110	[»]
			B	25-54	[»]
2M2M	NMR	-	A	90-110	[»]
			B	25-54	[»]
2M2N	NMR	-	A	90-110	[»]
			B	25-54	[»]
2M2O	NMR	-	A	90-110	[»]
			B	25-54	[»]
2M2P	NMR	-	A	90-110	[»]
			B	25-54	[»]
2MLI	NMR	-	A	90-110	[»]
			B	25-54	[»]
2MPG	NMR	-	A	90-110	[»]
			B	25-54	[»]
2MPI	NMR	-	A	90-110	[»]
			B	25-54	[»]
2MVC	NMR	-	A	90-110	[»]
			B	25-54	[»]
2MVD	NMR	-	A	90-110	[»]
			B	25-54	[»]
2N2V	NMR	-	A	90-110	[»]
			B	25-54	[»]
2N2W	NMR	-	A	90-110	[»]
			B	25-54	[»]
2N2X	NMR	-	A	90-110	[»]
			B	25-54	[»]
2OLY	X-ray	1.70	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-54	[»]
2OLZ	X-ray	1.70	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-54	[»]
2OM0	X-ray	2.05	1/3/A/C/E/G/I/K/Q/S/U/X/a/c/e/g/i/k	90-110	[»]
			2/4/B/D/F/H/J/L/R/T/V/Y/b/d/f/h/j/l	25-54	[»]
2OM1	X-ray	1.97	1/3/A/C/E/G/I/K/Q/S/U/X/a/c/e/g/i/k	90-110	[»]
			2/4/B/D/F/H/J/L/R/T/V/Y/b/d/f/h/j/l	25-54	[»]
2OMG	X-ray	1.52	A/C/E	90-110	[»]
			B/D/F	25-54	[»]
2OMH	X-ray	1.36	A/C/E	90-110	[»]
			B/D/F	25-54	[»]
2OMI	X-ray	2.24	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-54	[»]
2OMQ	X-ray	2.00	A/B/C/D	36-41	[»]
2QIU	X-ray	2.00	A/C	89-110	[»]
			B/D	25-54	[»]
2R34	X-ray	2.25	A/C	89-110	[»]
			B/D	25-54	[»]
2R35	X-ray	2.08	A/C	89-110	[»]
			B/D	25-54	[»]
2R36	X-ray	2.00	A/C	89-110	[»]
			B/D	25-54	[»]
2RN5	NMR	-	A	90-110	[»]
			B	25-54	[»]
2VJZ	X-ray	1.80	A/C	90-110	[»]
			B/D	25-54	[»]
2VK0	X-ray	2.20	A/C	90-110	[»]
			B/D	25-54	[»]
2W44	X-ray	2.00	A/C/E	94-110	[»]
			B/D/F	25-53	[»]
2WBY	X-ray	2.60	C/E	90-109	[»]
			D/F	25-43	[»]
2WC0	X-ray	2.80	C/E	90-110	[»]
			D/F	25-54	[»]
2WRU	X-ray	1.57	A	90-110	[»]
			B	25-50	[»]
2WRV	X-ray	2.15	A	90-110	[»]
			B	25-50	[»]
2WRW	X-ray	2.41	A	90-110	[»]
			B	25-50	[»]
2WRX	X-ray	1.50	A/C	90-110	[»]
			B/D	25-54	[»]
2WS0	X-ray	2.10	A	90-110	[»]
			B	25-54	[»]
2WS1	X-ray	1.60	A	90-110	[»]
			B	25-54	[»]
2WS4	X-ray	1.90	A	90-110	[»]
			B	25-50	[»]
2WS6	X-ray	1.50	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-54	[»]
2WS7	X-ray	2.59	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-50	[»]
3AIY	NMR	-	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-54	[»]
3BXQ	X-ray	1.30	A/C	90-110	[»]
			B/D	25-54	[»]
3E7Y	X-ray	1.60	A/C	90-110	[»]
			B/D	25-53	[»]
3E7Z	X-ray	1.70	A/C	90-110	[»]
			B/D	25-53	[»]
3EXX	X-ray	1.35	A/C	90-110	[»]
			B/D	25-54	[»]
3FQ9	X-ray	1.35	A/C	91-110	[»]
			B/D	25-54	[»]
3HYD	X-ray	1.00	A	35-41	[»]
3I3Z	X-ray	1.60	A	90-110	[»]
			B	25-54	[»]
3I40	X-ray	1.85	A	90-110	[»]
			B	25-54	[»]
3ILG	X-ray	1.90	A/C	90-110	[»]
			B/D	25-54	[»]
3INC	X-ray	1.85	A/C	90-110	[»]
			B/D	25-54	[»]
3IR0	X-ray	2.20	A/C/E/G/I/K/M/O/R/T/V/X	90-110	[»]
			B/D/F/H/J/L/N/P/S/U/W/Y	25-54	[»]
3JSD	X-ray	2.50	A/C	90-110	[»]
			B/D	25-54	[»]
3KQ6	X-ray	1.90	A/C	90-110	[»]
			B/D	25-54	[»]
3P2X	X-ray	2.00	A/C	90-110	[»]
			B/D	25-54	[»]
3P33	X-ray	2.30	A/C/E/G	90-110	[»]
			B/D/F/H	25-54	[»]
3Q6E	X-ray	2.05	A/C	90-110	[»]
			B/D	25-54	[»]
3ROV	X-ray	2.30	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-54	[»]
3TT8	X-ray	1.12	A/C	90-110	[»]
			B/D	25-54	[»]
3U4N	X-ray	1.98	A	90-110	[»]
			B	25-53	[»]
3UTQ	X-ray	1.67	C	15-24	[»]
3UTS	X-ray	2.71	C/H	15-24	[»]
3UTT	X-ray	2.60	C/H	15-24	[»]
3V19	X-ray	2.00	A/C	90-110	[»]
			B/D	25-54	[»]
3V1G	X-ray	2.20	A/C	90-110	[»]
			B/D	25-54	[»]
3W11	X-ray	3.90	A	90-110	[»]
			B	25-54	[»]
3W12	X-ray	4.30	A	90-110	[»]
			B	25-50	[»]
3W13	X-ray	4.30	A	90-110	[»]
			B	25-50	[»]
3W7Y	X-ray	0.92	A/C	90-110	[»]
			B/D	25-54	[»]
3W7Z	X-ray	1.15	A/C	90-110	[»]
			B/D	25-54	[»]
3W80	X-ray	1.40	A/C/E/G	90-110	[»]
			B/D/F/H	25-54	[»]
3ZI3	X-ray	1.70	A	90-110	[»]
			B	25-54	[»]
3ZQR	X-ray	1.90	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-54	[»]
3ZS2	X-ray	1.97	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-54	[»]
3ZU1	X-ray	1.60	A/C	90-110	[»]
			B/D	25-54	[»]
4AIY	NMR	-	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-54	[»]
4AJX	X-ray	1.20	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-53	[»]
4AJZ	X-ray	1.80	A/C	90-110	[»]
			B/D	25-53	[»]
4AK0	X-ray	2.28	A	90-110	[»]
			B	25-53	[»]
4AKJ	X-ray	2.01	A/C	90-110	[»]
			B/D	25-53	[»]
4CXL	X-ray	1.50	A	90-110	[»]
			B	25-54	[»]
4CXN	X-ray	1.70	A	90-110	[»]
			B	25-54	[»]
4CY7	X-ray	1.40	A/C	90-110	[»]
			B/D	25-54	[»]
4EFX	X-ray	1.98	A/C	90-110	[»]
			B/D	25-52	[»]
4EWW	X-ray	2.30	A/C	90-110	[»]
			B/D	25-54	[»]
4EWX	X-ray	2.20	A/C	90-110	[»]
			B/D	25-54	[»]
4EWZ	X-ray	1.79	A/C	90-110	[»]
			B/D	25-54	[»]
4EX0	X-ray	1.86	A/C	90-110	[»]
			B/D	25-54	[»]
4EX1	X-ray	1.66	A/C	90-110	[»]
			B/D	25-54	[»]
4EXX	X-ray	1.55	A/C	90-110	[»]
			B/D	25-54	[»]
4EY1	X-ray	1.47	A/C	90-110	[»]
			B/D	25-54	[»]
4EY9	X-ray	1.47	A/C	90-110	[»]
			B/D	25-54	[»]
4EYD	X-ray	1.47	A/C	90-110	[»]
			B/D	25-54	[»]
4EYN	X-ray	1.53	A/C	90-110	[»]
			B/D	25-54	[»]
4EYP	X-ray	1.59	A/C	90-110	[»]
			B/D	25-54	[»]
4F0N	X-ray	1.68	A/C	90-110	[»]
			B/D	25-54	[»]
4F0O	X-ray	1.67	A/C	90-110	[»]
			B/D	25-54	[»]
4F1A	X-ray	1.80	A/C	90-110	[»]
			B/D	25-54	[»]
4F1B	X-ray	1.59	A/C	90-110	[»]
			B/D	25-54	[»]
4F1C	X-ray	1.70	A/C	90-110	[»]
			B/D	25-54	[»]
4F1D	X-ray	1.64	A/C	90-110	[»]
			B/D	25-54	[»]
4F1F	X-ray	1.68	A/C	90-110	[»]
			B/D	25-54	[»]
4F1G	X-ray	1.64	A/C	90-110	[»]
			B/D	25-54	[»]
4F4T	X-ray	1.64	A/C	90-110	[»]
			B/D	25-54	[»]
4F4V	X-ray	1.64	A/C	90-110	[»]
			B/D	25-54	[»]
4F51	X-ray	1.64	A/C	90-110	[»]
			B/D	25-54	[»]
4F8F	X-ray	1.68	A/C	90-110	[»]
			B/D	25-54	[»]
4FG3	X-ray	2.00	A/C	90-110	[»]
			B/D	25-54	[»]
4FKA	X-ray	1.08	A/C	90-110	[»]
			B/D	25-54	[»]
4GBC	X-ray	1.78	A/C	90-110	[»]
			B/D	25-54	[»]
4GBI	X-ray	2.50	A/C	90-110	[»]
			B/D	25-54	[»]
4GBK	X-ray	2.40	A/C	90-110	[»]
			B/D	25-54	[»]
4GBL	X-ray	2.50	A/C	90-110	[»]
			B/D	25-54	[»]
4GBN	X-ray	1.87	A/C	90-110	[»]
			B/D	25-54	[»]
4IUZ	X-ray	1.60	A	90-110	[»]
			B	25-54	[»]
4IYD	X-ray	1.66	A	90-109	[»]
			B	25-53	[»]
4IYF	X-ray	1.80	A	90-109	[»]
			B	25-53	[»]
4NIB	X-ray	1.40	A	90-110	[»]
			B	25-54	[»]
4OGA	X-ray	3.50	A	90-110	[»]
			B	25-54	[»]
4P65	X-ray	1.50	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-54	[»]
4Q5Z	X-ray	3.93	a/b/c/d/e/f/g/h	90-109	[»]
			x	25-43	[»]
4RXW	X-ray	1.73	A/C	90-110	[»]
			B/D	25-54	[»]
4UNE	X-ray	1.59	A/C	90-110	[»]
			B/D	25-54	[»]
4UNG	X-ray	1.81	A/C	90-110	[»]
			B/D	25-54	[»]
4UNH	X-ray	2.75	A	90-110	[»]
			B	25-54	[»]
4WDI	X-ray	2.31	C/F	39-47	[»]
4XC4	X-ray	1.50	A/C	90-110	[»]
			B/D	25-54	[»]
4Y19	X-ray	2.50	C	75-90	[»]
4Y1A	X-ray	4.00	C	75-90	[»]
4Z76	X-ray	1.88	C/F	39-46	[»]
4Z77	X-ray	1.85	C/F	39-47	[»]
4Z78	X-ray	2.30	C/F/I	39-48	[»]
5AIY	NMR	-	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-54	[»]
5BOQ	X-ray	1.70	A/C/E/G	90-110	[»]
			B/D/F/H	25-54	[»]
5BPO	X-ray	1.90	A/C	90-110	[»]
			B/D	25-54	[»]
5BQQ	X-ray	1.54	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-50	[»]
5BTS	X-ray	1.77	A	90-110	[»]
			B	25-54	[»]
5C0D	X-ray	1.68	C	15-24	[»]
5CJO	X-ray	3.29	a	90-109	[»]
5CNY	X-ray	1.70	A/C	90-110	[»]
			B/D	25-54	[»]
5CO2	X-ray	1.70	A/C	90-110	[»]
			B/D	25-54	[»]
5CO6	X-ray	1.80	A/C	90-110	[»]
			B/D	25-54	[»]
5CO9	X-ray	1.92	A/C	90-110	[»]
			B/D	25-54	[»]
5E7W	X-ray	0.95	A/C	90-110	[»]
			B/D	25-54	[»]
5EMS	X-ray	2.30	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-52	[»]
5EN9	X-ray	1.50	A	90-110	[»]
			B	25-54	[»]
5ENA	X-ray	1.35	A	90-110	[»]
			B	25-54	[»]
5HPR	X-ray	1.33	A	90-110	[»]
			B	25-54	[»]
5HPU	X-ray	2.20	A/C	90-110	[»]
			B/D	25-54	[»]
5HQI	X-ray	0.97	A	90-110	[»]
			B	25-54	[»]
5HRQ	X-ray	1.28	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-54	[»]
5HYJ	X-ray	3.06	C/H	15-24	[»]
5MAM	X-ray	2.20	0/2/4/A/C/E/G/I/K/M/O/Q/S/U/W/Y	90-110	[»]
			1/3/5/B/D/F/H/J/L/N/P/R/T/V/X/Z	25-54	[»]
5MHD	NMR	-	A	90-110	[»]
			B	25-55	[»]
5MT3	X-ray	2.02	A/C/E/G/I/K/M/O/Q/S/U/W/Y/a/c/e	90-110	[»]
			B/D/F/H/J/L/N/P/R/T/V/X/Z/b/d/f	25-54	[»]
5MT9	X-ray	1.88	A/C/E/G/I/K/M/O/Q/S/U/W/Y/a/c/e	90-110	[»]
			B/D/F/H/J/L/N/P/R/T/V/X/Z/b/d/f	25-54	[»]
5MWQ	NMR	-	A	90-110	[»]
			B	25-56	[»]
5T7R	X-ray	1.55	A/C	90-110	[»]
			B/D	25-54	[»]
5UDP	X-ray	1.35	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-54	[»]
5UOZ	X-ray	1.17	A	90-110	[»]
			B	25-54	[»]
5UQA	X-ray	1.31	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-54	[»]
5URT	X-ray	1.18	A	90-110	[»]
			B	25-54	[»]
5URU	X-ray	2.41	A/C/E/G	90-110	[»]
			B/D/F/H	25-54	[»]
5USP	X-ray	1.17	A	90-110	[»]
			B	25-54	[»]
5USS	X-ray	2.06	A/C	90-110	[»]
			B/D	25-54	[»]
5USV	X-ray	1.30	A	90-110	[»]
			B	25-54	[»]
5UU2	X-ray	1.22	A	90-110	[»]
			B	25-54	[»]
5UU3	X-ray	2.25	A/C/E/G/I/K/M/O/Q/S/U/W	90-110	[»]
			B/D/F/H/J/L/N/P/R/T/V/X	25-54	[»]
5UU4	X-ray	1.97	A/C	90-110	[»]
			B/D	25-54	[»]
5VIZ	X-ray	1.70	A	90-109	[»]
			B	25-53	[»]
5WBT	NMR	-	A	25-54	[»]
			A	90-110	[»]
5WDM	X-ray	2.80	A/B/C/D/E/F	25-110	[»]
6B3Q	electron microscopy	3.70	a/b	1-110	[»]
6B70	electron microscopy	3.70	a/c	1-110	[»]
6BFC	electron microscopy	3.70	a/b	1-110	[»]
6CE7	electron microscopy	7.40	N	90-110	[»]
6CE9	electron microscopy	4.30	K/N	90-110	[»]
6CEB	electron microscopy	4.70	K/N	90-110	[»]
ProteinModelPortalⁱ	P01308
SMRⁱ	P01308
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P01308

EvolutionaryTraceⁱ

P01308

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the insulin family.Curated

Keywords - Domainⁱ

Signal

Phylogenomic databases

eggNOGⁱ	ENOG410J0XC Eukaryota ENOG4111VJB LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000015440
HOGENOMⁱ	HOG000261669
HOVERGENⁱ	HBG006137
InParanoidⁱ	P01308
KEGG Orthology (KO) More...KOⁱ	K04526
OMAⁱ	PQHLCGS
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0H56
PhylomeDBⁱ	P01308
TreeFamⁱ	TF332820

Family and domain databases

InterProⁱ	View protein in InterPro IPR004825 Insulin IPR016179 Insulin-like IPR036438 Insulin-like_sf IPR022353 Insulin_CS IPR022352 Insulin_family
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00049 Insulin, 1 hit
PRINTSⁱ	PR00277 INSULIN PR00276 INSULINFAMLY
SMARTⁱ	View protein in SMART SM00078 IlGF, 1 hit
SUPFAMⁱ	SSF56994 SSF56994, 1 hit
PROSITEⁱ	View protein in PROSITE PS00262 INSULIN, 1 hit

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. Align Add to basket Added to basket

Isoform 1 (identifier: P01308-1) [UniParc]FASTA Add 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.

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        10         20         30         40         50
MALWMRLLPL LALLALWGPD PAAAFVNQHL CGSHLVEALY LVCGERGFFY 
        60         70         80         90        100
TPKTRREAED LQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC 
       110
SLYQLENYCN

Length:110

Mass (Da):11,981

Last modified:July 21, 1986 - v1

Checksum:ⁱC2C3B23B85E520E5

Isoform 2 (identifier: F8WCM5-1) [UniParc]FASTA Add to basket

Also known as: INS-IGF2

The sequence of this isoform can be found in the external entry F8WCM5.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Based on a readthrough transcript which may produce an INS-IGF2 fusion protein.

Length:200

Mass (Da):21,537

Sequence cautionⁱ

The sequence AAA59179 differs from that shown. Reason: Erroneous gene model prediction.Curated

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_063721	6	R → C in MODY10. 1 PublicationCorresponds to variant dbSNP:rs121908278EnsemblClinVar.	1
Natural variantⁱVAR_063722	6	R → H in MODY10. 1 PublicationCorresponds to variant dbSNP:rs121908259EnsemblClinVar.	1
Natural variantⁱVAR_063723	24	A → D in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356663EnsemblClinVar.	1
Natural variantⁱVAR_063724	29	H → D in PNDM. 1 PublicationCorresponds to variant dbSNP:rs121908272EnsemblClinVar.	1
Natural variantⁱVAR_063725	32	G → R in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356664EnsemblClinVar.	1
Natural variantⁱVAR_063726	32	G → S in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356664EnsemblClinVar.	1
Natural variantⁱVAR_003971	34	H → D in HPRI; Providence. 1 PublicationCorresponds to variant dbSNP:rs121918101EnsemblClinVar.	1
Natural variantⁱVAR_063727	35	L → P in PNDM. 1 PublicationCorresponds to variant dbSNP:rs121908273EnsemblClinVar.	1
Natural variantⁱVAR_063728	43	C → G in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356666EnsemblClinVar.	1
Natural variantⁱVAR_063729	46	R → Q in MODY10; reduces binding affinity to INSR; reduces biological activity; reduces folding properties. 3 PublicationsCorresponds to variant dbSNP:rs121908260EnsemblClinVar.	1
Natural variantⁱVAR_063730	47	G → V in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356667EnsemblClinVar.	1
Natural variantⁱVAR_063731	48	F → C in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356668EnsemblClinVar.	1
Natural variantⁱVAR_003972	48	F → S Associated with diabetes mellitus type-II; Los-Angeles. 3 PublicationsCorresponds to variant dbSNP:rs80356668EnsemblClinVar.	1
Natural variantⁱVAR_003973	49	F → L in Chicago. 1 PublicationCorresponds to variant dbSNP:rs148685531EnsemblClinVar.	1
Natural variantⁱVAR_063732	55	R → C in IDDM2. 1 PublicationCorresponds to variant dbSNP:rs121908261EnsemblClinVar.	1
Natural variantⁱVAR_063733	68	L → M1 PublicationCorresponds to variant dbSNP:rs121908279EnsemblClinVar.	1
Natural variantⁱVAR_063734	84	G → R in PNDM; uncertain pathological significance. 1 PublicationCorresponds to variant dbSNP:rs121908274EnsemblClinVar.	1
Natural variantⁱVAR_063735	89	R → C in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356669EnsemblClinVar.	1
Natural variantⁱVAR_003974	89	R → H in HPRI; impairs post-translational cleavage. 2 PublicationsCorresponds to variant dbSNP:rs28933985EnsemblClinVar.	1
Natural variantⁱVAR_003975	89	R → L in HPRI; Kyoto. 1 PublicationCorresponds to variant dbSNP:rs28933985EnsemblClinVar.	1
Natural variantⁱVAR_063736	90	G → C in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356670EnsemblClinVar.	1
Natural variantⁱVAR_003976	92	V → L in Wakayama. 1 PublicationCorresponds to variant dbSNP:rs121918102EnsemblClinVar.	1
Natural variantⁱVAR_063737	96	C → S in PNDM. 1 PublicationCorresponds to variant dbSNP:rs80356671EnsemblClinVar.	1
Natural variantⁱVAR_063738	96	C → Y in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356671EnsemblClinVar.	1
Natural variantⁱVAR_063739	101	S → C in PNDM. 1 PublicationCorresponds to variant dbSNP:rs121908276EnsemblClinVar.	1
Natural variantⁱVAR_063740	103	Y → C in PNDM. 1 PublicationCorresponds to variant dbSNP:rs121908277EnsemblClinVar.	1
Natural variantⁱVAR_063741	108	Y → C in PNDM. 2 PublicationsCorresponds to variant dbSNP:rs80356672EnsemblClinVar.	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	V00565 Genomic DNA Translation: CAA23828.1 M10039 Genomic DNA Translation: AAA59173.1 J00265 Genomic DNA Translation: AAA59172.1 X70508 mRNA Translation: CAA49913.1 L15440 Genomic DNA Translation: AAA59179.1 Sequence problems. AY899304 mRNA Translation: AAW83741.1 AY138590 Genomic DNA Translation: AAN39451.1 BT006808 mRNA Translation: AAP35454.1 CH471158 Genomic DNA Translation: EAX02488.1 BC005255 mRNA Translation: AAH05255.1 AJ009655 Genomic DNA Translation: CAA08766.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS7729.1 [P01308-1]
PIRⁱ	A93222 IPHU
NCBI Reference Sequences More...RefSeqⁱ	NP_000198.1, NM_000207.2 [P01308-1] NP_001172026.1, NM_001185097.1 [P01308-1] NP_001172027.1, NM_001185098.1 [P01308-1] NP_001278826.1, NM_001291897.1 [P01308-1]
UniGeneⁱ	Hs.272259

Genome annotation databases

Ensemblⁱ	ENST00000250971; ENSP00000250971; ENSG00000254647 [P01308-1] ENST00000381330; ENSP00000370731; ENSG00000254647 [P01308-1] ENST00000397262; ENSP00000380432; ENSG00000254647 [P01308-1]
GeneIDⁱ	3630
KEGGⁱ	hsa:3630
UCSC genome browser More...UCSCⁱ	uc001lvn.3 human [P01308-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P01308 (INS_HUMAN)

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Insulin

INS

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

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Extracellular region or secreted

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Endosome

Extracellular region or secreted

Golgi apparatus

Other locations

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Organism-specific databases

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Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

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Amino acid modifications

Proteomic databases

PTM databases

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Gene expression databases

Organism-specific databases

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Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

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<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Natural variant

Sequence databases

Genome annotation databases

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Sequence databases

3D structure databases

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Functionⁱ

GO - Molecular functionⁱ

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Names & Taxonomyⁱ

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Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Web resourcesⁱ