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P01308 (INS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 194. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Insulin

Cleaved into the following 2 chains:

  1. Insulin B chain
  2. Insulin A chain
Gene names
Name:INS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length110 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Heterodimer of a B chain and an A chain linked by two disulfide bonds.

Subcellular location

Secreted.

Involvement in disease

Hyperproinsulinemia, familial (FHPRI) [MIM:176730]: An autosomal dominant condition characterized by elevated levels of serum proinsulin-like material.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21 Ref.23 Ref.24 Ref.25

Diabetes mellitus, insulin-dependent, 2 (IDDM2) [MIM:125852]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.34

Diabetes mellitus, permanent neonatal (PNDM) [MIM:606176]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.32 Ref.33

Maturity-onset diabetes of the young 10 (MODY10) [MIM:613370]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.33 Ref.34 Ref.35

Pharmaceutical use

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.

Sequence similarities

Belongs to the insulin family.

Sequence caution

The sequence AAA59179.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Glucose metabolism
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDiabetes mellitus
Disease mutation
   DomainSignal
   Molecular functionHormone
   PTMCleavage on pair of basic residues
Disulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Pharmaceutical
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 9092559. Source: BHF-UCL

MAPK cascade

Inferred from direct assay PubMed 11278339. Source: BHF-UCL

activation of protein kinase B activity

Inferred from direct assay PubMed 8702995. Source: BHF-UCL

acute-phase response

Inferred from direct assay PubMed 14739855. Source: BHF-UCL

alpha-beta T cell activation

Inferred from direct assay PubMed 10604997. Source: UniProtKB

cell-cell signaling

Inferred by curator PubMed 7556975. Source: UniProtKB

cellular protein metabolic process

Traceable author statement. Source: Reactome

endocrine pancreas development

Traceable author statement. Source: Reactome

energy reserve metabolic process

Traceable author statement. Source: Reactome

fatty acid homeostasis

Inferred from mutant phenotype PubMed 1184755. Source: BHF-UCL

glucose homeostasis

Inferred from mutant phenotype PubMed 381941. Source: BHF-UCL

glucose metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

glucose transport

Inferred from direct assay PubMed 14615391PubMed 15792832. Source: UniProtKB

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

negative regulation of NAD(P)H oxidase activity

Inferred from direct assay PubMed 11443198. Source: BHF-UCL

negative regulation of acute inflammatory response

Inferred from direct assay PubMed 11443198. Source: BHF-UCL

negative regulation of fatty acid metabolic process

Inferred from mutant phenotype PubMed 1184755. Source: BHF-UCL

negative regulation of feeding behavior

Inferred from direct assay PubMed 17957153. Source: DFLAT

negative regulation of gluconeogenesis

Non-traceable author statement PubMed 11742412. Source: BHF-UCL

negative regulation of glycogen catabolic process

Inferred from mutant phenotype PubMed 381941. Source: BHF-UCL

negative regulation of intrinsic apoptotic signaling pathway in response to oxidative stress

Non-traceable author statement PubMed 16604263. Source: BHF-UCL

negative regulation of lipid catabolic process

Non-traceable author statement PubMed 11742412. Source: BHF-UCL

negative regulation of protein catabolic process

Inferred from direct assay PubMed 15185208. Source: UniProtKB

negative regulation of protein oligomerization

Inferred from direct assay PubMed 9830016. Source: UniProtKB

negative regulation of protein secretion

Inferred from direct assay PubMed 14739855. Source: BHF-UCL

negative regulation of proteolysis

Inferred from mutant phenotype PubMed 3553851. Source: BHF-UCL

negative regulation of respiratory burst involved in inflammatory response

Inferred from direct assay PubMed 11443198. Source: BHF-UCL

negative regulation of vasodilation

Non-traceable author statement PubMed 12946932. Source: UniProtKB

positive regulation of DNA replication

Inferred from direct assay PubMed 7688386. Source: BHF-UCL

positive regulation of MAPK cascade

Inferred from direct assay PubMed 11500939. Source: BHF-UCL

positive regulation of NF-kappaB transcription factor activity

Inferred from direct assay PubMed 19727662. Source: BHF-UCL

positive regulation of brown fat cell differentiation

Traceable author statement PubMed 11387233. Source: BHF-UCL

positive regulation of cell differentiation

Non-traceable author statement PubMed 11742412. Source: BHF-UCL

positive regulation of cell growth

Non-traceable author statement PubMed 11742412. Source: BHF-UCL

positive regulation of cell migration

Inferred from sequence or structural similarity PubMed 12138094. Source: BHF-UCL

positive regulation of cell proliferation

Inferred from direct assay PubMed 17925406. Source: BHF-UCL

positive regulation of cellular protein metabolic process

Inferred from mutant phenotype PubMed 3553851. Source: BHF-UCL

positive regulation of cytokine secretion

Inferred from direct assay PubMed 15473891. Source: UniProtKB

positive regulation of glucose import

Inferred from direct assay PubMed 14615391. Source: BHF-UCL

positive regulation of glycogen biosynthetic process

Inferred from direct assay PubMed 17925406. Source: BHF-UCL

positive regulation of glycolytic process

Inferred from direct assay PubMed 7688386. Source: BHF-UCL

positive regulation of insulin receptor signaling pathway

Inferred from direct assay PubMed 7688386. Source: BHF-UCL

positive regulation of lipid biosynthetic process

Non-traceable author statement PubMed 11742412. Source: BHF-UCL

positive regulation of mitosis

Inferred from direct assay PubMed 10644978. Source: UniProtKB

positive regulation of nitric oxide biosynthetic process

Non-traceable author statement PubMed 14615391. Source: UniProtKB

positive regulation of nitric-oxide synthase activity

Non-traceable author statement PubMed 12135947. Source: UniProtKB

positive regulation of peptide hormone secretion

Traceable author statement PubMed 11387233. Source: BHF-UCL

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 11278339. Source: BHF-UCL

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from direct assay PubMed 7688386. Source: BHF-UCL

positive regulation of protein autophosphorylation

Inferred from sequence or structural similarity PubMed 3518947. Source: BHF-UCL

positive regulation of protein kinase B signaling

Inferred from direct assay PubMed 11500939. Source: BHF-UCL

positive regulation of respiratory burst

Inferred from direct assay PubMed 9092559. Source: BHF-UCL

positive regulation of vasodilation

Non-traceable author statement PubMed 14744991. Source: UniProtKB

regulation of cellular amino acid metabolic process

Inferred from mutant phenotype PubMed 3553851. Source: BHF-UCL

regulation of insulin secretion

Traceable author statement. Source: Reactome

regulation of protein localization

Inferred from direct assay PubMed 14615391. Source: BHF-UCL

regulation of protein secretion

Inferred from direct assay PubMed 15591776. Source: UniProtKB

regulation of transcription, DNA-templated

Non-traceable author statement PubMed 12881524. Source: BHF-UCL

regulation of transmembrane transporter activity

Inferred from direct assay PubMed 14615391. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

wound healing

Inferred from direct assay PubMed 9498508. Source: BHF-UCL

   Cellular_componentGolgi lumen

Traceable author statement. Source: Reactome

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

endosome lumen

Traceable author statement. Source: Reactome

extracellular region

Inferred by curator PubMed 7556975. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 9667398. Source: BHF-UCL

secretory granule lumen

Traceable author statement. Source: Reactome

   Molecular_functionhormone activity

Non-traceable author statement PubMed 14986111. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 20738396PubMed 23106816PubMed 23416304PubMed 23510797. Source: IntAct

insulin receptor binding

Inferred from direct assay PubMed 7556975. Source: UniProtKB

insulin-like growth factor receptor binding

Inferred from physical interaction PubMed 8452530. Source: BHF-UCL

protease binding

Inferred from physical interaction PubMed 20082125. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 9773776. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself16EBI-7090529,EBI-7090529

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P01308-1)

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.
Isoform 2 (identifier: F8WCM5-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.12
Peptide25 – 5430Insulin B chain Ref.12
PRO_0000015819
Propeptide57 – 8731C peptide Ref.13 Ref.14
PRO_0000015820
Peptide90 – 11021Insulin A chain
PRO_0000015821

Amino acid modifications

Disulfide bond31 ↔ 96Interchain (between B and A chains)
Disulfide bond43 ↔ 109Interchain (between B and A chains)
Disulfide bond95 ↔ 100 Ref.13

Natural variations

Natural variant61R → C in MODY10. Ref.33
Corresponds to variant rs121908278 [ dbSNP | Ensembl ].
VAR_063721
Natural variant61R → H in MODY10. Ref.35
Corresponds to variant rs121908259 [ dbSNP | Ensembl ].
VAR_063722
Natural variant241A → D in PNDM. Ref.32 Ref.33
Corresponds to variant rs80356663 [ dbSNP | Ensembl ].
VAR_063723
Natural variant291H → D in PNDM. Ref.33
Corresponds to variant rs121908272 [ dbSNP | Ensembl ].
VAR_063724
Natural variant321G → R in PNDM. Ref.32 Ref.33
Corresponds to variant rs80356664 [ dbSNP | Ensembl ].
VAR_063725
Natural variant321G → S in PNDM. Ref.32 Ref.33
Corresponds to variant rs80356664 [ dbSNP | Ensembl ].
VAR_063726
Natural variant341H → D in FHPRI; Providence. Ref.21
VAR_003971
Natural variant351L → P in PNDM. Ref.33
Corresponds to variant rs121908273 [ dbSNP | Ensembl ].
VAR_063727
Natural variant431C → G in PNDM. Ref.32 Ref.33
Corresponds to variant rs80356666 [ dbSNP | Ensembl ].
VAR_063728
Natural variant461R → Q in MODY10. Ref.34 Ref.35
Corresponds to variant rs121908260 [ dbSNP | Ensembl ].
VAR_063729
Natural variant471G → V in PNDM. Ref.32 Ref.33
Corresponds to variant rs80356667 [ dbSNP | Ensembl ].
VAR_063730
Natural variant481F → C in PNDM. Ref.32 Ref.33
Corresponds to variant rs80356668 [ dbSNP | Ensembl ].
VAR_063731
Natural variant481F → S Associated with diabetes mellitus type-II; Los-Angeles. Ref.19 Ref.20 Ref.30
VAR_003972
Natural variant491F → L in Chicago. Ref.20
VAR_003973
Natural variant551R → C in IDDM2. Ref.34
Corresponds to variant rs121908261 [ dbSNP | Ensembl ].
VAR_063732
Natural variant681L → M. Ref.33
Corresponds to variant rs121908279 [ dbSNP | Ensembl ].
VAR_063733
Natural variant841G → R in PNDM; uncertain pathological significance. Ref.33
Corresponds to variant rs121908274 [ dbSNP | Ensembl ].
VAR_063734
Natural variant891R → C in PNDM. Ref.32 Ref.33
Corresponds to variant rs80356669 [ dbSNP | Ensembl ].
VAR_063735
Natural variant891R → H in FHPRI; impairs posttranslational cleavage. Ref.23 Ref.24
Corresponds to variant rs28933985 [ dbSNP | Ensembl ].
VAR_003974
Natural variant891R → L in FHPRI; Kyoto. Ref.25
VAR_003975
Natural variant901G → C in PNDM. Ref.32 Ref.33
Corresponds to variant rs80356670 [ dbSNP | Ensembl ].
VAR_063736
Natural variant921V → L in Wakayama. Ref.22
VAR_003976
Natural variant961C → S in PNDM. Ref.33
Corresponds to variant rs80356671 [ dbSNP | Ensembl ].
VAR_063737
Natural variant961C → Y in PNDM. Ref.32 Ref.33
Corresponds to variant rs80356671 [ dbSNP | Ensembl ].
VAR_063738
Natural variant1011S → C in PNDM. Ref.33
Corresponds to variant rs121908276 [ dbSNP | Ensembl ].
VAR_063739
Natural variant1031Y → C in PNDM. Ref.33
Corresponds to variant rs121908277 [ dbSNP | Ensembl ].
VAR_063740
Natural variant1081Y → C in PNDM. Ref.32 Ref.33
Corresponds to variant rs80356672 [ dbSNP | Ensembl ].
VAR_063741

Secondary structure

..................... 110
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: C2C3B23B85E520E5

FASTA11011,981
        10         20         30         40         50         60 
MALWMRLLPL LALLALWGPD PAAAFVNQHL CGSHLVEALY LVCGERGFFY TPKTRREAED 

        70         80         90        100        110 
LQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC SLYQLENYCN 

« Hide

Isoform 2 (INS-IGF2) [UniParc].

See F8WCM5.

References

« Hide 'large scale' references
[1]"Sequence of the human insulin gene."
Bell G.I., Pictet R.L., Rutter W.J., Cordell B., Tischer E., Goodman H.M.
Nature 284:26-32(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Genetic variation in the human insulin gene."
Ullrich A., Dull T.J., Gray A., Brosius J., Sures I.
Science 209:612-615(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Nucleotide sequence of a cDNA clone encoding human preproinsulin."
Bell G.I., Swain W.F., Pictet R.L., Cordell B., Goodman H.M., Rutter W.J.
Nature 282:525-527(1979) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Nucleotide sequence of human preproinsulin complementary DNA."
Sures I., Goeddel D.V., Gray A., Ullrich A.
Science 208:57-59(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Susceptibility to insulin dependent diabetes mellitus maps to a 4.1 kb segment of DNA spanning the insulin gene and associated VNTR."
Lucassen A.M., Julier C., Beressi J.-P., Boitard C., Froguel P., Lathrop M., Bell J.I.
Nat. Genet. 4:305-310(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Insulinomas and expression of an insulin splice variant."
Minn A.H., Kayton M., Lorang D., Hoffmann S.C., Harlan D.M., Libutti S.K., Shalev A.
Lancet 363:363-367(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[7]"Global haplotype diversity in the human insulin gene region."
Stead J.D.H., Hurles M.E., Jeffreys A.J.
Genome Res. 13:2101-2111(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pancreas.
[11]"Description of a novel RFLP diallelic polymorphism (-127 BsgI C/G) within the 5' region of insulin gene."
Fajardy I.I., Weill J.J., Stuckens C.C., Danze P.M.P.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59.
Tissue: Blood.
[12]"Amino-acid sequence of human insulin."
Nicol D.S.H.W., Smith L.F.
Nature 187:483-485(1960) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-54 AND 90-110.
[13]"Studies on human proinsulin. Isolation and amino acid sequence of the human pancreatic C-peptide."
Oyer P.E., Cho S., Peterson J.D., Steiner D.F.
J. Biol. Chem. 246:1375-1386(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 57-87.
[14]"The amino acid sequence of the C-peptide of human proinsulin."
Ko A., Smyth D.G., Markussen J., Sundby F.
Eur. J. Biochem. 20:190-199(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 57-87.
[15]"Total synthesis of human insulin under directed formation of the disulfide bonds."
Sieber P., Kamber B., Hartmann A., Joehl A., Riniker B., Rittel W.
Helv. Chim. Acta 57:2617-2621(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: SYNTHESIS.
[16]"Studies on polypeptides, IV. The synthesis of C-peptide of human proinsulin."
Naithani V.K.
Hoppe-Seyler's Z. Physiol. Chem. 354:659-672(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: SYNTHESIS OF 57-87.
[17]"Synthesis of peptides with the properties of human proinsulin C peptides (hC peptide). 3. Synthesis of the sequences 14-17 and 9-13 of human proinsulin C peptides."
Geiger R., Volk A.
Chem. Ber. 106:199-205(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: SYNTHESIS OF 65-69 AND 70-73.
[18]"Synthesis of peptides with the properties of human proinsulin C peptides (hC peptide). I. Scheme for the synthesis and preparation of the sequence 28-31 of human proinsulin C peptide."
Geiger R., Jaeger G., Keonig W., Treuth G.
Chem. Ber. 106:188-192(1973) [PubMed] [Europe PMC] [Abstract]
Cited for: SYNTHESIS OF 84-87.
[19]"Studies on mutant human insulin genes: identification and sequence analysis of a gene encoding [SerB24]insulin."
Haneda M., Chan S.J., Kwok S.C.M., Rubenstein A.H., Steiner D.F.
Proc. Natl. Acad. Sci. U.S.A. 80:6366-6370(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LOS ANGELES SER-48.
[20]"Identification of a mutant human insulin predicted to contain a serine-for-phenylalanine substitution."
Shoelson S., Fickova M., Haneda M., Nahum A., Musso G., Kaiser E.T., Rubenstein A.H., Tager H.
Proc. Natl. Acad. Sci. U.S.A. 80:7390-7394(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LOS ANGELES SER-48 AND CHICAGO LEU-49.
[21]"A mutation in the B chain coding region is associated with impaired proinsulin conversion in a family with hyperproinsulinemia."
Chan S.J., Seino S., Gruppuso P.A., Schwartz R., Steiner D.F.
Proc. Natl. Acad. Sci. U.S.A. 84:2194-2197(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FHPRI ASP-34.
[22]"Structurally abnormal insulin in a diabetic patient. Characterization of the mutant insulin A3 (Val-->Leu) isolated from the pancreas."
Sakura H., Iwamoto Y., Sakamoto Y., Kuzuya T., Hirata H.
J. Clin. Invest. 78:1666-1672(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT WAKAYAMA LEU-92.
[23]"Two unrelated patients with familial hyperproinsulinemia due to a mutation substituting histidine for arginine at position 65 in the proinsulin molecule: identification of the mutation by direct sequencing of genomic deoxyribonucleic acid amplified by polymerase chain reaction."
Barbetti F., Raben N., Kadowaki T., Cama A., Accili D., Gabbay K.H., Merenich J.A., Taylor S.I., Roth J.
J. Clin. Endocrinol. Metab. 71:164-169(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FHPRI HIS-89.
[24]"Posttranslational cleavage of proinsulin is blocked by a point mutation in familial hyperproinsulinemia."
Shibasaki Y., Kawakami T., Kanazawa Y., Akanuma Y., Takaku F.
J. Clin. Invest. 76:378-380(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FHPRI HIS-89.
[25]"A novel point mutation in the human insulin gene giving rise to hyperproinsulinemia (proinsulin Kyoto)."
Yano H., Kitano N., Morimoto M., Polonsky K.S., Imura H., Seino Y.
J. Clin. Invest. 89:1902-1907(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FHPRI LEU-89.
[26]"Toward the solution structure of human insulin: sequential 2D 1H NMR assignment of a des-pentapeptide analogue and comparison with crystal structure."
Hua Q.-X., Weiss M.A.
Biochemistry 29:10545-10555(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[27]"Comparative 2D NMR studies of human insulin and des-pentapeptide insulin: sequential resonance assignment and implications for protein dynamics and receptor recognition."
Hua Q.-X., Weiss M.A.
Biochemistry 30:5505-5515(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[28]"Two-dimensional NMR studies of Des-(B26-B30)-insulin: sequence-specific resonance assignments and effects of solvent composition."
Hua Q.-X., Weiss M.A.
Biochim. Biophys. Acta 1078:101-110(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[29]"Three-dimensional solution structure of an insulin dimer. A study of the B9(Asp) mutant of human insulin using nuclear magnetic resonance, distance geometry and restrained molecular dynamics."
Joergensen A.M.M., Kristensen S.M., Led J.J., Balschmidt P.
J. Mol. Biol. 227:1146-1163(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[30]"Paradoxical structure and function in a mutant human insulin associated with diabetes mellitus."
Hua Q.-X., Shoelson S.E., Inouye K., Weiss M.A.
Proc. Natl. Acad. Sci. U.S.A. 90:582-586(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF VARIANT LOS-ANGELES SER-48.
[31]"Solution structures of the R6 human insulin hexamer."
Chang X., Joergensen A.M., Bardrum P., Led J.J.
Biochemistry 36:9409-9422(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[32]"Insulin gene mutations as a cause of permanent neonatal diabetes."
Stoy J., Edghill E.L., Flanagan S.E., Ye H., Paz V.P., Pluzhnikov A., Below J.E., Hayes M.G., Cox N.J., Lipkind G.M., Lipton R.B., Greeley S.A., Patch A.M., Ellard S., Steiner D.F., Hattersley A.T., Philipson L.H., Bell G.I.
Proc. Natl. Acad. Sci. U.S.A. 104:15040-15044(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PNDM ASP-24; ARG-32; SER-32; GLY-43; VAL-47; CYS-48; CYS-89; CYS-90; TYR-96 AND CYS-108.
[33]"Insulin mutation screening in 1,044 patients with diabetes: mutations in the INS gene are a common cause of neonatal diabetes but a rare cause of diabetes diagnosed in childhood or adulthood."
Edghill E.L., Flanagan S.E., Patch A.M., Boustred C., Parrish A., Shields B., Shepherd M.H., Hussain K., Kapoor R.R., Malecki M., MacDonald M.J., Stoy J., Steiner D.F., Philipson L.H., Bell G.I., Hattersley A.T., Ellard S.
Diabetes 57:1034-1042(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PNDM ASP-24; ASP-29; ARG-32; SER-32; PRO-35; GLY-43; VAL-47; CYS-48; ARG-84; CYS-89; CYS-90; SER-96; TYR-96; CYS-101; CYS-103 AND CYS-108, VARIANT MODY10 CYS-6, VARIANT MET-68.
[34]"Mutations in the insulin gene can cause MODY and autoantibody-negative type 1 diabetes."
Molven A., Ringdal M., Nordbo A.M., Raeder H., Stoy J., Lipkind G.M., Steiner D.F., Philipson L.H., Bergmann I., Aarskog D., Undlien D.E., Joner G., Sovik O., Bell G.I., Njolstad P.R.
Diabetes 57:1131-1135(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MODY10 GLN-46, VARIANT IDDM2 CYS-55.
[35]"Further evidence that mutations in INS can be a rare cause of Maturity-Onset Diabetes of the Young (MODY)."
Boesgaard T.W., Pruhova S., Andersson E.A., Cinek O., Obermannova B., Lauenborg J., Damm P., Bergholdt R., Pociot F., Pisinger C., Barbetti F., Lebl J., Pedersen O., Hansen T.
BMC Med. Genet. 11:42-42(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MODY10 HIS-6 AND GLN-46.
+Additional computationally mapped references.

Web resources

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS7729.1. [P01308-1]
PIRIPHU. A93222.
RefSeqNP_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.
UniGeneHs.272259.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A7FNMR-A90-110[»]
B25-53[»]
1AI0NMR-A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
1AIYNMR-A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
1B9EX-ray2.50A/C90-110[»]
B/D25-54[»]
1BENX-ray1.40A/C90-110[»]
B/D25-54[»]
1EFENMR-A25-54[»]
A90-110[»]
1EV3X-ray1.78A/C90-110[»]
B/D25-54[»]
1EV6X-ray1.90A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
1EVRX-ray1.90A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
1FU2X-ray3.24A/C/E/G90-110[»]
B/D/F/H25-54[»]
1FUBX-ray3.09A/C90-110[»]
B/D25-54[»]
1G7AX-ray1.20A/C/E/G90-110[»]
B/D/F/H25-54[»]
1G7BX-ray1.30A/C/E/G90-110[»]
B/D/F/H25-54[»]
1GUJX-ray1.62A/C90-110[»]
B/D25-54[»]
1HIQNMR-A90-110[»]
B25-54[»]
1HISNMR-A90-110[»]
B25-49[»]
1HITNMR-A90-110[»]
B25-54[»]
1HLSNMR-A90-110[»]
B25-54[»]
1HTVX-ray1.90A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-51[»]
1HUINMR-A90-110[»]
B26-53[»]
1IOGNMR-A90-110[»]
B25-53[»]
1IOHNMR-A90-110[»]
B25-53[»]
1J73X-ray2.00A/C90-110[»]
B/D25-54[»]
1JCAX-ray2.50A/C90-110[»]
B/D25-54[»]
1JCONMR-A90-110[»]
B25-54[»]
1JK8X-ray2.40C35-47[»]
1K3MNMR-A90-110[»]
B25-54[»]
1KMFNMR-A90-110[»]
B25-54[»]
1LKQNMR-A90-110[»]
B25-54[»]
1LPHX-ray2.30A/C90-110[»]
B/D25-54[»]
1MHINMR-A90-110[»]
B25-54[»]
1MHJNMR-A90-110[»]
B25-54[»]
1MSOX-ray1.00A/C90-110[»]
B/D25-54[»]
1OS3X-ray1.95A/C90-110[»]
B/D25-54[»]
1OS4X-ray2.25A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
1Q4VX-ray2.00A/C90-110[»]
B/D25-54[»]
1QIYX-ray2.30A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
1QIZX-ray2.00A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
1QJ0X-ray2.40A/C90-110[»]
B/D25-54[»]
1RWEX-ray1.80A/C90-110[»]
B/D25-54[»]
1SF1NMR-A90-110[»]
B25-54[»]
1SJTNMR-A90-110[»]
B25-51[»]
1SJUNMR-A25-110[»]
1T0CNMR-A57-87[»]
1T1KNMR-A90-110[»]
B25-54[»]
1T1PNMR-A90-110[»]
B25-54[»]
1T1QNMR-A90-110[»]
B25-54[»]
1TRZX-ray1.60A/C90-110[»]
B/D25-54[»]
1TYLX-ray1.90A/C90-110[»]
B/D25-54[»]
1TYMX-ray1.90A/C90-110[»]
B/D25-54[»]
1UZ9X-ray1.60A90-110[»]
B25-53[»]
1VKTNMR-A90-110[»]
B25-54[»]
1W8PX-ray2.08A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
1XDAX-ray1.80A/C/E/G90-110[»]
B/D/F/H25-53[»]
1XGLNMR-A90-110[»]
B25-54[»]
1XW7X-ray2.30A/C90-110[»]
B/D25-54[»]
1ZEGX-ray1.60A/C90-110[»]
B/D25-54[»]
1ZEHX-ray1.50A/C90-110[»]
B/D25-54[»]
1ZNJX-ray2.00A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
2AIYNMR-A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
2C8QX-ray1.95A90-110[»]
B25-53[»]
2C8RX-ray1.50A90-110[»]
B25-53[»]
2CEUX-ray1.80A/C90-110[»]
B/D25-49[»]
2G54X-ray2.25C/D25-54[»]
2G56X-ray2.20C/D25-54[»]
2H67NMR-A90-110[»]
B25-54[»]
2HH4NMR-A90-110[»]
B25-54[»]
2HHONMR-A90-110[»]
B25-54[»]
2HIUNMR-A90-110[»]
B25-54[»]
2JMNNMR-A90-110[»]
B25-54[»]
2JUMNMR-A90-110[»]
B25-54[»]
2JUUNMR-A90-110[»]
B25-54[»]
2JUVNMR-A90-110[»]
B25-54[»]
2JV1NMR-A90-110[»]
B25-54[»]
2JZQNMR-A25-54[»]
A90-110[»]
2K91NMR-A90-110[»]
B25-54[»]
2K9RNMR-A90-110[»]
B25-54[»]
2KJJNMR-A90-110[»]
B25-54[»]
2KJUNMR-A90-110[»]
B25-54[»]
2KQPNMR-A25-110[»]
2KQQNMR-A90-110[»]
B25-54[»]
2KXKNMR-A90-110[»]
B25-54[»]
2L1YNMR-A90-110[»]
B25-54[»]
2L1ZNMR-A90-110[»]
B25-54[»]
2LGBNMR-A90-110[»]
B25-55[»]
2LWZNMR-A25-54[»]
A89-110[»]
2M1DNMR-A90-110[»]
B25-54[»]
2M1ENMR-A90-110[»]
B25-54[»]
2M2MNMR-A90-110[»]
B25-54[»]
2M2NNMR-A90-110[»]
B25-54[»]
2M2ONMR-A90-110[»]
B25-54[»]
2M2PNMR-A90-110[»]
B25-54[»]
2OLYX-ray1.70A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
2OLZX-ray1.70A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
2OM0X-ray2.051/3/A/C/E/G/I/K/Q/S/U/X/a/c/e/g/i/k90-110[»]
2/4/B/D/F/H/J/L/R/T/V/Y/b/d/f/h/j/l25-54[»]
2OM1X-ray1.971/3/A/C/E/G/I/K/Q/S/U/X/a/c/e/g/i/k90-110[»]
2/4/B/D/F/H/J/L/R/T/V/Y/b/d/f/h/j/l25-54[»]
2OMGX-ray1.52A/C/E90-110[»]
B/D/F25-54[»]
2OMHX-ray1.36A/C/E90-110[»]
B/D/F25-54[»]
2OMIX-ray2.24A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
2QIUX-ray2.00A/C89-110[»]
B/D25-54[»]
2R34X-ray2.25A/C89-110[»]
B/D25-54[»]
2R35X-ray2.08A/C89-110[»]
B/D25-54[»]
2R36X-ray2.00A/C89-110[»]
B/D25-54[»]
2RN5NMR-A90-110[»]
B25-54[»]
2VJZX-ray1.80A/C90-110[»]
B/D25-54[»]
2VK0X-ray2.20A/C90-110[»]
B/D25-54[»]
2W44X-ray2.00A/C/E94-110[»]
B/D/F25-53[»]
2WBYX-ray2.60C/E90-109[»]
D/F25-43[»]
2WC0X-ray2.80C/E90-110[»]
D/F25-54[»]
2WRUX-ray1.57A90-110[»]
B25-50[»]
2WRVX-ray2.15A90-110[»]
B25-50[»]
2WRWX-ray2.41A90-110[»]
B25-50[»]
2WRXX-ray1.50A/C90-110[»]
B/D25-54[»]
2WS0X-ray2.10A90-110[»]
B25-54[»]
2WS1X-ray1.60A90-110[»]
B25-54[»]
2WS4X-ray1.90A90-110[»]
B25-50[»]
2WS6X-ray1.50A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
2WS7X-ray2.59A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-50[»]
3AIYNMR-A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
3BRRX-ray1.70A/C90-110[»]
B/D25-53[»]
3BXQX-ray1.30A/C90-110[»]
B/D25-54[»]
3E7YX-ray1.60A/C90-110[»]
B/D25-53[»]
3E7ZX-ray1.70A/C90-110[»]
B/D25-53[»]
3EXXX-ray1.35A/C90-110[»]
B/D25-54[»]
3FQ9X-ray1.35A/C91-110[»]
B/D25-54[»]
3HYDX-ray1.00A35-41[»]
3I3ZX-ray1.60A90-110[»]
B25-54[»]
3I40X-ray1.85A90-110[»]
B25-54[»]
3ILGX-ray1.90A/C90-110[»]
B/D25-54[»]
3INCX-ray1.85A/C90-110[»]
B/D25-54[»]
3IR0X-ray2.20A/C/E/G/I/K/M/O/R/T/V/X90-110[»]
B/D/F/H/J/L/N/P/S/U/W/Y25-54[»]
3JSDX-ray2.50A/C90-110[»]
B/D25-54[»]
3KQ6X-ray1.90A/C90-110[»]
B/D25-54[»]
3P2XX-ray2.00A/C90-110[»]
B/D25-54[»]
3P33X-ray2.30A/C/E/G90-110[»]
B/D/F/H25-54[»]
3Q6EX-ray2.05A/C90-110[»]
B/D25-54[»]
3ROVX-ray2.30A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
3TT8X-ray1.12A/C90-110[»]
B/D25-54[»]
3U4NX-ray1.98A90-110[»]
B25-53[»]
3UTQX-ray1.67C15-24[»]
3UTSX-ray2.71C/H15-24[»]
3UTTX-ray2.60C/H15-24[»]
3V19X-ray2.00A/C90-110[»]
B/D25-54[»]
3V1GX-ray2.20A/C90-110[»]
B/D25-54[»]
3W11X-ray3.90A90-110[»]
B25-54[»]
3W12X-ray4.30A90-110[»]
B25-50[»]
3W13X-ray4.30A90-110[»]
B25-50[»]
3W7YX-ray0.92A/C90-110[»]
B/D25-54[»]
3W7ZX-ray1.15A/C90-110[»]
B/D25-54[»]
3W80X-ray1.40A/C/E/G90-110[»]
B/D/F/H25-54[»]
3ZI3X-ray1.70A90-110[»]
B25-54[»]
3ZQRX-ray1.90A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
3ZS2X-ray1.97A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
3ZU1X-ray1.60A/C90-110[»]
B/D25-54[»]
4AIYNMR-A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
4AJXX-ray1.20A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-53[»]
4AJZX-ray1.80A/C90-110[»]
B/D25-53[»]
4AK0X-ray2.28A90-110[»]
B25-53[»]
4AKJX-ray2.01A/C90-110[»]
B/D25-53[»]
4EFXX-ray1.98A/C90-110[»]
B/D25-52[»]
4EWWX-ray2.30A/C90-110[»]
B/D25-54[»]
4EWXX-ray2.20A/C90-110[»]
B/D25-54[»]
4EWZX-ray1.79A/C90-110[»]
B/D25-54[»]
4EX0X-ray1.86A/C90-110[»]
B/D25-54[»]
4EX1X-ray1.66A/C90-110[»]
B/D25-54[»]
4EXXX-ray1.55A/C90-110[»]
B/D25-54[»]
4EY1X-ray1.47A/C90-110[»]
B/D25-54[»]
4EY9X-ray1.47A/C90-110[»]
B/D25-54[»]
4EYDX-ray1.47A/C90-110[»]
B/D25-54[»]
4EYNX-ray1.53A/C90-110[»]
B/D25-54[»]
4EYPX-ray1.59A/C90-110[»]
B/D25-54[»]
4F0NX-ray1.68A/C90-110[»]
B/D25-54[»]
4F0OX-ray1.67A/C90-110[»]
B/D25-54[»]
4F1AX-ray1.80A/C90-110[»]
B/D25-54[»]
4F1BX-ray1.59A/C90-110[»]
B/D25-54[»]
4F1CX-ray1.70A/C90-110[»]
B/D25-54[»]
4F1DX-ray1.64A/C90-110[»]
B/D25-54[»]
4F1FX-ray1.68A/C90-110[»]
B/D25-54[»]
4F1GX-ray1.64A/C90-110[»]
B/D25-54[»]
4F4TX-ray1.64A/C90-110[»]
B/D25-54[»]
4F4VX-ray1.64A/C90-110[»]
B/D25-54[»]
4F51X-ray1.64A/C90-110[»]
B/D25-54[»]
4F8FX-ray1.68A/C90-110[»]
B/D25-54[»]
4FG3X-ray2.00A/C90-110[»]
B/D25-54[»]
4FKAX-ray1.08A/C90-110[»]
B/D25-54[»]
4GBCX-ray1.78A/C90-110[»]
B/D25-54[»]
4GBIX-ray2.50A/C90-110[»]
B/D25-54[»]
4GBKX-ray2.40A/C90-110[»]
B/D25-54[»]
4GBLX-ray2.50A/C90-110[»]
B/D25-54[»]
4GBNX-ray1.87A/C90-110[»]
B/D25-54[»]
4IUZX-ray1.60A90-110[»]
B25-54[»]
4IYDX-ray1.66A90-109[»]
B25-53[»]
4IYFX-ray1.80A90-109[»]
B25-53[»]
5AIYNMR-A/C/E/G/I/K90-110[»]
B/D/F/H/J/L25-54[»]
ProteinModelPortalP01308.
SMRP01308. Positions 25-110.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109842. 10 interactions.
DIPDIP-6024N.
IntActP01308. 2 interactions.
MINTMINT-106847.
STRING9606.ENSP00000348986.

Chemistry

ChEMBLCHEMBL5881.

Protein family/group databases

Allergome2121. Hom s Insulin.

PTM databases

PhosphoSiteP01308.

Polymorphism databases

DMDM124617.

Proteomic databases

PaxDbP01308.
PeptideAtlasP01308.
PRIDEP01308.

Protocols and materials databases

DNASU3630.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000250971; ENSP00000250971; ENSG00000254647. [P01308-1]
ENST00000381330; ENSP00000370731; ENSG00000254647. [P01308-1]
ENST00000397262; ENSP00000380432; ENSG00000254647. [P01308-1]
GeneID3630.
KEGGhsa:3630.
UCSCuc001lvn.2. human. [P01308-1]

Organism-specific databases

CTD3630.
GeneCardsGC11M002181.
GeneReviewsINS.
HGNCHGNC:6081. INS.
HPACAB000048.
CAB012098.
CAB053843.
HPA004932.
MIM125852. phenotype.
176730. gene+phenotype.
606176. phenotype.
613370. phenotype.
neXtProtNX_P01308.
Orphanet552. MODY syndrome.
99885. Permanent neonatal diabetes mellitus.
PharmGKBPA201.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG45999.
HOGENOMHOG000261669.
HOVERGENHBG006137.
KOK04526.
OMAVEQCCHN.
PhylomeDBP01308.
TreeFamTF332820.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16190.
ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_17015. Metabolism of proteins.
SignaLinkP01308.

Gene expression databases

ArrayExpressP01308.
BgeeP01308.
GenevestigatorP01308.

Family and domain databases

Gene3D1.10.100.10. 2 hits.
InterProIPR004825. Insulin.
IPR016179. Insulin-like.
IPR022353. Insulin_CS.
IPR022352. Insulin_family.
[Graphical view]
PfamPF00049. Insulin. 1 hit.
[Graphical view]
PRINTSPR00277. INSULIN.
PR00276. INSULINFAMLY.
SMARTSM00078. IlGF. 1 hit.
[Graphical view]
SUPFAMSSF56994. SSF56994. 1 hit.
PROSITEPS00262. INSULIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP01308.
GeneWikiInsulin.
GenomeRNAi3630.
NextBio14203.
PMAP-CutDBP01308.
PROP01308.
SOURCESearch...

Entry information

Entry nameINS_HUMAN
AccessionPrimary (citable) accession number: P01308
Secondary accession number(s): Q5EEX2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 194 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM