INS

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

hormone activity
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- "A structurally abnormal insulin causing human diabetes."
  Tager H., Given B., Baldwin D., Mako M., Markese J., Rubenstein A., Olefsky J., Kobayashi M., Kolterman O., Poucher R.
  Nature 281:122-125(1979) [PubMed] [Europe PMC] [Abstract]
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
- "A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils."
  Vestergaard B., Groenning M., Roessle M., Kastrup J.S., van de Weert M., Flink J.M., Frokjaer S., Gajhede M., Svergun D.I.
  PLoS Biol. 5:e134-e134(2007) [PubMed] [Europe PMC] [Abstract]
- "Structural features of proinsulin C-peptide oligomeric and amyloid states."
  Lind J., Lindahl E., Peralvarez-Marin A., Holmlund A., Jornvall H., Maler L.
  FEBS J. 277:3759-3768(2010) [PubMed] [Europe PMC] [Abstract]
- "SERF protein is a direct modifier of amyloid fiber assembly."
  Falsone S.F., Meyer N.H., Schrank E., Leitinger G., Pham C.L., Fodero-Tavoletti M.T., Holmberg M., Dulle M., Scicluna B., Gesslbauer B., Rueckert H.M., Wagner G.E., Merle D.A., Nollen E.A., Kungl A.J., Hill A.F., Cappai R., Zangger K.
  Cell Rep. 2:358-371(2012) [PubMed] [Europe PMC] [Abstract]
- "Insulin solubility transitions by pH-dependent interactions with proinsulin C-peptide."
  Landreh M., Alvelius G., Willander H., Stukenborg J.B., Soder O., Johansson J., Jornvall H.
  FEBS J. 279:4589-4597(2012) [PubMed] [Europe PMC] [Abstract]
- "Amino acid sequence determinants in self-assembly of insulin chiral amyloid superstructures: role of C-terminus of B-chain in association of fibrils."
  Babenko V., Dzwolak W.
  FEBS Lett. 587:625-630(2013) [PubMed] [Europe PMC] [Abstract]
- "Peptides that form beta-sheets on hydrophobic surfaces accelerate surface-induced insulin amyloidal aggregation."
  Nault L., Vendrely C., Brechet Y., Bruckert F., Weidenhaupt M.
  FEBS Lett. 587:1281-1286(2013) [PubMed] [Europe PMC] [Abstract]
insulin-like growth factor receptor binding
Source: BHF-UCL
Inferred from physical interactionⁱ
- "Purified hybrid insulin/insulin-like growth factor-I receptors bind insulin-like growth factor-I, but not insulin, with high affinity."
  Soos M.A., Field C.E., Siddle K.
  Biochem. J. 290:419-426(1993) [PubMed] [Europe PMC] [Abstract]
insulin receptor binding
Source: UniProtKB
Inferred from direct assayⁱ
- "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."
  Kotzke G., Schutt M., Missler U., Moller D.E., Fehm H.L., Klein H.H.
  Diabetologia 38:757-763(1995) [PubMed] [Europe PMC] [Abstract]
protease binding
Source: UniProtKB
Inferred from physical interactionⁱ
- "In vitro degradation of insulin-like peptide 3 by insulin-degrading enzyme."
  Zhang W.J., Luo X., Guo Z.Y.
  Protein J. 29:93-98(2010) [PubMed] [Europe PMC] [Abstract]

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

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-9615017 FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes 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

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.

Related information in OMIM

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.

Related information in OMIM

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.

Related information in OMIM

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.

Related information in OMIM

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_063729	46	R → Q in MODY10; reduces binding affinity to INSR; reduces biological activity; reduces folding properties. 3 PublicationsCorresponds to variant dbSNP:rs121908260EnsemblClinVar.	1

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

Miscellaneous databases

Pharosⁱ	P01308 Tbio

Pharosⁱ

P01308 Tbio

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 DB01593 Zinc DB14487 Zinc acetate DB14533 Zinc chloride

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

EPDⁱ	P01308
jPOSTⁱ	P01308
MassIVEⁱ	P01308
PaxDbⁱ	P01308
PeptideAtlas More...PeptideAtlasⁱ	P01308
PRIDEⁱ	P01308
ProteomicsDBⁱ	51374 [P01308-1]

PTM databases

CarbonylDBⁱ	P01308
iPTMnetⁱ	P01308
PhosphoSitePlusⁱ	P01308

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000254647 Expressed in type B pancreatic cell and 71 other tissues
ExpressionAtlasⁱ	P01308 baseline and differential
Genevisibleⁱ	P01308 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	ENSG00000254647 Tissue enriched (pancreas)

HPAⁱ

ENSG00000254647 Tissue enriched (pancreas)

Interactionⁱ

Subunit structureⁱ

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

1 Publication

Binary interactionsⁱ

With	#Exp.	IntAct
itself	19	EBI-7090529,EBI-7090529
ADAMTSL4 - isoform 3 [Q6UY14-3]	3	EBI-7090529,EBI-10173507
CYSRT1 [A8MQ03]	3	EBI-7090529,EBI-3867333
IDE - isoform 1 [P14735-1]	3	EBI-7090529,EBI-15607031
INSR - isoform Short [P06213-2]	3	EBI-7090529,EBI-9984921
KRTAP1-1 [Q07627]	3	EBI-7090529,EBI-11959885
NOTCH2NLC [P0DPK4]	3	EBI-7090529,EBI-22310682

With	#Exp.	IntAct
HSPA8 [P11142]	2	EBI-20765227,EBI-351896

Show more details

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	109842, 16 interactors
Database of interacting proteins More...DIPⁱ	DIP-6024N
IntActⁱ	P01308, 17 interactors
Molecular INTeraction database More...MINTⁱ	P01308
STRINGⁱ	9606.ENSP00000380432

Miscellaneous databases

RNActⁱ	P01308 protein

RNActⁱ

P01308 protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

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

Show more details

3D structure databases

SMRⁱ	P01308
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

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
InParanoidⁱ	P01308
KEGG Orthology (KO) More...KOⁱ	K04526
OMAⁱ	APPQHLC
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
PANTHERⁱ	PTHR11454 PTHR11454, 1 hit
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

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show all Align All

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

This isoform has been chosen as the canonicalⁱ sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        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

GO

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.

Length:200

Mass (Da):21,537

GO

Computationally mapped potential isoform sequencesⁱ

There are 2 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

A6XGL2	A6XGL2_HUMAN	Insulin Insulin	INS	98	Annotation score:
C9JNR5	C9JNR5_HUMAN	Insulin Insulin	INS	92	Annotation score:

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]

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

Protein	Similar proteins		Species	Score	Length	Source
P01308	Insulin		GORGO		110	UniRef100_P01308
Insulin		HUMAN		110
Insulin (Fragment)		HUMAN		94

Protein	Similar proteins		Species	Score	Length	Source
P01308	Insulin		GORGO		110	UniRef90_P01308
Insulin		PONPY		110
Insulin		MACFA		110
Insulin		HUMAN		110
Insulin		TUPCH		110
+16

Protein	Similar proteins		Species	Score	Length	Source
P01308	Insulin		GORGO		110	UniRef50_P01308
Insulin		MACFA		110
Insulin		PONPY		110
Insulin		RODSP		108
Insulin	)	BOVIN		105
+194

Cross-referencesⁱ

Web resourcesⁱ

Insulin at Eli Lilly

Clinical information on Eli Lilly insulin products

Protein Spotlight

Protein of the 20th century - Issue 9 of April 2001

Wikipedia

Insulin entry

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
CCDSⁱ	CCDS7729.1 [P01308-1]
PIRⁱ	A93222 IPHU
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]

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	[»]
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	[»]
5WOB	X-ray	3.95	a/b/c/d/e/f/g/h	90-109	[»]
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	[»]
6CK2	X-ray	2.25	A/C	90-110	[»]
			B/D	25-54	[»]
6GNQ	X-ray	2.20	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	[»]
6GV0	X-ray	1.26	B/D	25-54	[»]
			G/I	90-110	[»]
6H3M	X-ray	1.82	A/C/E/G/I/K/N/R	90-110	[»]
			B/D/F/H/J/L/P/Q	25-54	[»]
6HN5	electron microscopy	3.20	A	90-110	[»]
			B	25-54	[»]
6P4Z	X-ray	1.80	A/C	90-110	[»]
			B/D	25-54	[»]
6S34	X-ray	1.35	A	90-110	[»]
			B	25-54	[»]
6SOF	electron microscopy	4.30	E/G/I/K	90-110	[»]
			F/H/J/L	25-54	[»]
6TYH	X-ray	1.60	A/C/E/G/I/K	90-110	[»]
			B/D/F/H/J/L	25-54	[»]
SMRⁱ	P01308
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	109842, 16 interactors
DIPⁱ	DIP-6024N
IntActⁱ	P01308, 17 interactors
MINTⁱ	P01308
STRINGⁱ	9606.ENSP00000380432

Chemistry databases

ChEMBLⁱ	CHEMBL5881
DrugBankⁱ	DB01776 M-Cresol DB08231 Myristic acid DB01593 Zinc DB14487 Zinc acetate DB14533 Zinc chloride

Protein family/group databases

Allergomeⁱ	2121 Hom s Insulin

Allergomeⁱ

2121 Hom s Insulin

PTM databases

CarbonylDBⁱ	P01308
iPTMnetⁱ	P01308
PhosphoSitePlusⁱ	P01308

Polymorphism and mutation databases

BioMutaⁱ	INS
DMDMⁱ	124617

Proteomic databases

EPDⁱ	P01308
jPOSTⁱ	P01308
MassIVEⁱ	P01308
PaxDbⁱ	P01308
PeptideAtlasⁱ	P01308
PRIDEⁱ	P01308
ProteomicsDBⁱ	51374 [P01308-1]

Protocols and materials databases

ABCDⁱ	P01308
Antibodypediaⁱ	56056 3340 antibodies
The DNASU plasmid repository More...DNASUⁱ	3630

Genome annotation databases

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

Organism-specific databases

CTDⁱ	3630
DisGeNETⁱ	3630
GeneCardsⁱ	INS
GeneReviewsⁱ	INS
HGNCⁱ	HGNC:6081 INS
HPAⁱ	ENSG00000254647 Tissue enriched (pancreas)
MalaCardsⁱ	INS
MIMⁱ	125852 phenotype 176730 gene 606176 phenotype 613370 phenotype 616214 phenotype
neXtProtⁱ	NX_P01308
OpenTargetsⁱ	ENSG00000254647
Orphanetⁱ	552 MODY 99885 Permanent neonatal diabetes mellitus
PharmGKBⁱ	PA201
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	ENOG410J0XC Eukaryota ENOG4111VJB LUCA
GeneTreeⁱ	ENSGT00390000015440
InParanoidⁱ	P01308
KOⁱ	K04526
OMAⁱ	APPQHLC
PhylomeDBⁱ	P01308
TreeFamⁱ	TF332820

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-9615017 FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes R-HSA-977225 Amyloid fiber formation
SignaLinkⁱ	P01308
SIGNORⁱ	P01308

Miscellaneous databases

EvolutionaryTraceⁱ	P01308
GeneWikiⁱ	Insulin
GenomeRNAiⁱ	3630
Pharosⁱ	P01308 Tbio
Protein Ontology More...PROⁱ	PR:P01308
RNActⁱ	P01308 protein
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000254647 Expressed in type B pancreatic cell and 71 other tissues
ExpressionAtlasⁱ	P01308 baseline and differential
Genevisibleⁱ	P01308 HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR004825 Insulin IPR016179 Insulin-like IPR036438 Insulin-like_sf IPR022353 Insulin_CS IPR022352 Insulin_family
PANTHERⁱ	PTHR11454 PTHR11454, 1 hit
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
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	INS_HUMAN
Accessionⁱ	P01308Primary (citable) accession number: P01308 Secondary accession number(s): Q5EEX2
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
	Last sequence update:	July 21, 1986
	Last modified:	April 22, 2020
	This is version 254 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Direct protein sequencing, Pharmaceutical, Reference proteome

Documents

Human chromosome 11
Human chromosome 11: entries, gene names and cross-references to MIM
SIMILARITY comments
Index of protein domains and families
Protein Spotlight
Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

UniProtKB

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Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P01308 (INS_HUMAN)

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Insulin

Select a section on the left to see content.

<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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

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

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted

Endoplasmic reticulum

Endosome

Extracellular region or secreted

Golgi apparatus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Keywords - Diseasei

Organism-specific databases

Miscellaneous databases

Protein family/group databases

Chemistry databases

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

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

P01308

P01308 (PRO_0000015820)

GO - Molecular functioni

Protein-protein interaction databases

Miscellaneous 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

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<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

Keywords - Domaini

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

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ