[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1038/284026a0; PubMed=6243748 [NCBI, ExPASy, EBI, Israel, Japan] Bell G.I., Pictet R.L., Rutter W.J., Cordell B., Tischer E., Goodman H.M.; "Sequence of the human insulin gene."; Nature 284:26-32(1980).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=6248962 [NCBI, ExPASy, EBI, Israel, Japan] Ullrich A., Dull T.J., Gray A., Brosius J., Sures I.; "Genetic variation in the human insulin gene."; Science 209:612-615(1980).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1038/282525a0; PubMed=503234 [NCBI, ExPASy, EBI, Israel, Japan] Bell G.I., Swain W.F., Pictet R.L., Cordell B., Goodman H.M., Rutter W.J.; "Nucleotide sequence of a cDNA clone encoding human preproinsulin."; Nature 282:525-527(1979).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=6927840 [NCBI, ExPASy, EBI, Israel, Japan] Sures I., Goeddel D.V., Gray A., Ullrich A.; "Nucleotide sequence of human preproinsulin complementary DNA."; Science 208:57-59(1980).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1038/ng0793-305; PubMed=8358440 [NCBI, ExPASy, EBI, Israel, Japan] Lucassen A.M., Julier C., Beressi J.-P., Boitard C., Froguel P., Lathrop M., Bell J.I.; "Susceptibility to insulin dependent diabetes mellitus maps to a 4.1 kb segment of DNA spanning the insulin gene and associated VNTR."; Nat. Genet. 4:305-310(1993).
[6]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/S0140-6736(04)15438-X; PubMed=15070567 [NCBI, ExPASy, EBI, Israel, Japan] Minn A.H., Kayton M., Lorang D., Hoffmann S.C., Harlan D.M., Libutti S.K., Shalev A.; "Insulinomas and expression of an insulin splice variant."; Lancet 363:363-367(2004).
[7]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1101/gr.948003; PubMed=12952878 [NCBI, ExPASy, EBI, Israel, Japan] Stead J.D.H., Hurles M.E., Jeffreys A.J.; "Global haplotype diversity in the human insulin gene region."; Genome Res. 13:2101-2111(2003).
[8]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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.; "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[9]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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., 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.
[10]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Pancreas; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[11]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59. TISSUE=Blood; Fajardy I.I., Weill J.J., Stuckens C.C., Danze P.M.P.; "Description of a novel RFLP diallelic polymorphism (-127 BsgI C/G) within the 5' region of insulin gene."; Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[12]	PROTEIN SEQUENCE OF 25-54 AND 90-110. PubMed=14426955 [NCBI, ExPASy, EBI, Israel, Japan] Nicol D.S.H.W., Smith L.F.; "Amino-acid sequence of human insulin."; Nature 187:483-485(1960).
[13]	PROTEIN SEQUENCE OF 57-87. PubMed=5101771 [NCBI, ExPASy, EBI, Israel, Japan] Oyer P.E., Cho S., Peterson J.D., Steiner D.F.; "Studies on human proinsulin. Isolation and amino acid sequence of the human pancreatic C-peptide."; J. Biol. Chem. 246:1375-1386(1971).
[14]	PROTEIN SEQUENCE OF 57-87. PubMed=5560404 [NCBI, ExPASy, EBI, Israel, Japan] Ko A., Smyth D.G., Markussen J., Sundby F.; "The amino acid sequence of the C-peptide of human proinsulin."; Eur. J. Biochem. 20:190-199(1971).
[15]	SYNTHESIS. DOI=10.1002/hlca.19740570839; PubMed=4443293 [NCBI, ExPASy, EBI, Israel, Japan] Sieber P., Kamber B., Hartmann A., Joehl A., Riniker B., Rittel W.; "Total synthesis of human insulin under directed formation of the disulfide bonds."; Helv. Chim. Acta 57:2617-2621(1974).
[16]	SYNTHESIS OF 57-87. PubMed=4803504 [NCBI, ExPASy, EBI, Israel, Japan] Naithani V.K.; "Studies on polypeptides, IV. The synthesis of C-peptide of human proinsulin."; Hoppe-Seyler's Z. Physiol. Chem. 354:659-672(1973).
[17]	SYNTHESIS OF 65-69 AND 70-73. PubMed=4698555 [NCBI, ExPASy, EBI, Israel, Japan] Geiger R., Volk A.; "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."; Chem. Ber. 106:199-205(1973).
[18]	SYNTHESIS OF 84-87. PubMed=4698553 [NCBI, ExPASy, EBI, Israel, Japan] Geiger R., Jaeger G., Keonig W., Treuth G.; "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."; Chem. Ber. 106:188-192(1973).
[19]	VARIANT LOS ANGELES SER-48. PubMed=6312455 [NCBI, ExPASy, EBI, Israel, Japan] Haneda M., Chan S.J., Kwok S.C.M., Rubenstein A.H., Steiner D.F.; "Studies on mutant human insulin genes: identification and sequence analysis of a gene encoding [SerB24]insulin."; Proc. Natl. Acad. Sci. U.S.A. 80:6366-6370(1983).
[20]	VARIANTS LOS ANGELES SER-48 AND CHICAGO LEU-49. PubMed=6424111 [NCBI, ExPASy, EBI, Israel, Japan] Shoelson S., Fickova M., Haneda M., Nahum A., Musso G., Kaiser E.T., Rubenstein A.H., Tager H.; "Identification of a mutant human insulin predicted to contain a serine-for-phenylalanine substitution."; Proc. Natl. Acad. Sci. U.S.A. 80:7390-7394(1983).
[21]	VARIANT PROVIDENCE ASP-34. PubMed=3470784 [NCBI, ExPASy, EBI, Israel, Japan] Chan S.J., Seino S., Gruppuso P.A., Schwartz R., Steiner D.F.; "A mutation in the B chain coding region is associated with impaired proinsulin conversion in a family with hyperproinsulinemia."; Proc. Natl. Acad. Sci. U.S.A. 84:2194-2197(1987).
[22]	VARIANT WAKAYAMA LEU-92. PubMed=3537011 [NCBI, ExPASy, EBI, Israel, Japan] Sakura H., Iwamoto Y., Sakamoto Y., Kuzuya T., Hirata H.; "Structurally abnormal insulin in a diabetic patient. Characterization of the mutant insulin A3 (Val-->Leu) isolated from the pancreas."; J. Clin. Invest. 78:1666-1672(1986).
[23]	VARIANT HIS-89. PubMed=2196279 [NCBI, ExPASy, EBI, Israel, Japan] Barbetti F., Raben N., Kadowaki T., Cama A., Accili D., Gabbay K.H., Merenich J.A., Taylor S.I., Roth J.; "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."; J. Clin. Endocrinol. Metab. 71:164-169(1990).
[24]	VARIANT HIS-89. PubMed=4019786 [NCBI, ExPASy, EBI, Israel, Japan] Shibasaki Y., Kawakami T., Kanazawa Y., Akanuma Y., Takaku F.; "Posttranslational cleavage of proinsulin is blocked by a point mutation in familial hyperproinsulinemia."; J. Clin. Invest. 76:378-380(1985).
[25]	VARIANT KYOTO LEU-89. PubMed=1601997 [NCBI, ExPASy, EBI, Israel, Japan] Yano H., Kitano N., Morimoto M., Polonsky K.S., Imura H., Seino Y.; "A novel point mutation in the human insulin gene giving rise to hyperproinsulinemia (proinsulin Kyoto)."; J. Clin. Invest. 89:1902-1907(1992).
[26]	STRUCTURE BY NMR. DOI=10.1021/bi00498a018; PubMed=2271664 [NCBI, ExPASy, EBI, Israel, Japan] Hua Q.-X., Weiss M.A.; "Toward the solution structure of human insulin: sequential 2D 1H NMR assignment of a des-pentapeptide analogue and comparison with crystal structure."; Biochemistry 29:10545-10555(1990).
[27]	STRUCTURE BY NMR. DOI=10.1021/bi00236a025; PubMed=2036420 [NCBI, ExPASy, EBI, Israel, Japan] Hua Q.-X., Weiss M.A.; "Comparative 2D NMR studies of human insulin and des-pentapeptide insulin: sequential resonance assignment and implications for protein dynamics and receptor recognition."; Biochemistry 30:5505-5515(1991).
[28]	STRUCTURE BY NMR. DOI=10.1016/0167-4838(91)90098-K; PubMed=1646635 [NCBI, ExPASy, EBI, Israel, Japan] Hua Q.-X., Weiss M.A.; "Two-dimensional NMR studies of Des-(B26-B30)-insulin: sequence-specific resonance assignments and effects of solvent composition."; Biochim. Biophys. Acta 1078:101-110(1991).
[29]	STRUCTURE BY NMR. DOI=10.1016/0022-2836(92)90527-Q; PubMed=1433291 [NCBI, ExPASy, EBI, Israel, Japan] Joergensen A.M.M., Kristensen S.M., Led J.J., Balschmidt P.; "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."; J. Mol. Biol. 227:1146-1163(1992).
[30]	STRUCTURE BY NMR OF VARIANT LOS-ANGELES SER-48. PubMed=8421693 [NCBI, ExPASy, EBI, Israel, Japan] Hua Q.-X., Shoelson S.E., Inouye K., Weiss M.A.; "Paradoxical structure and function in a mutant human insulin associated with diabetes mellitus."; Proc. Natl. Acad. Sci. U.S.A. 90:582-586(1993).
[31]	STRUCTURE BY NMR. DOI=10.1021/bi9631069; PubMed=9235985 [NCBI, ExPASy, EBI, Israel, Japan] Chang X., Joergensen A.M., Bardrum P., Led J.J.; "Solution structures of the R6 human insulin hexamer."; Biochemistry 36:9409-9422(1997).

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: Heterodimer of a B chain and an A chain linked by two disulfide bonds.
SUBCELLULAR LOCATION: Secreted.
DISEASE: Defects in INS are the cause of familial hyperproinsulinemia [MIM:176730].
PHARMACEUTICAL: 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.
SIMILARITY: Belongs to the insulin family.
SEQUENCE CAUTION:
- Sequence=AAA59179.1; Type=Erroneous gene model prediction;
WEB RESOURCE: Name=Insulin at Eli Lilly; Note=Clinical information on Eli Lilly insulin products; URL="http://www.lillyDiabetes.com/Products/PatientInfo.cfm";.
WEB RESOURCE: Name=Protein Spotlight; Note=Protein of the 20th century - Issue 9 of April 2001; URL="http://www.expasy.org/spotlight/back_issues/sptlt009.shtml";.
WEB RESOURCE: Name=Wikipedia; Note=Insulin entry; URL="http://en.wikipedia.org/wiki/Insulin";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

V00565; CAA23828.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M10039; AAA59173.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J00265; AAA59172.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X70508; CAA49913.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L15440; AAA59179.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY899304; AAW83741.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY138590; AAN39451.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006808; AAP35454.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471158; EAX02488.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005255; AAH05255.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ009655; CAA08766.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A93222; IPHU.

NP_000198.1; -.

3D structure databases

PDB

1A7F; NMR; -; A=90-110, B=25-53.	[ExPASy / RCSB / EBI]
1AI0; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.	[ExPASy / RCSB / EBI]
1AIY; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.	[ExPASy / RCSB / EBI]
1B9E; X-ray; 2.50 A; A/C=90-110, B/D=25-54.	[ExPASy / RCSB / EBI]
1BEN; X-ray; 1.40 A; A/C=90-110, B/D=25-54.	[ExPASy / RCSB / EBI]
1EFE; NMR; -; A=25-60.	[ExPASy / RCSB / EBI]
1EV3; X-ray; 1.78 A; A/C=90-110, B/D=25-54.	[ExPASy / RCSB / EBI]
1EV6; X-ray; 1.90 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.	[ExPASy / RCSB / EBI]
1EVR; X-ray; 1.90 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.	[ExPASy / RCSB / EBI]
1FU2; X-ray; 3.24 A; A/C/E/G=90-110, B/D/F/H=25-54.	[ExPASy / RCSB / EBI]
1FUB; X-ray; 3.09 A; A/C=90-110, B/D=25-54.	[ExPASy / RCSB / EBI]
1G7A; X-ray; 1.20 A; A/C/E/G=90-110, B/D/F/H=25-54.	[ExPASy / RCSB / EBI]
1G7B; X-ray; 1.30 A; A/C/E/G=90-110, B/D/F/H=25-54.	[ExPASy / RCSB / EBI]
1GUJ; X-ray; 1.62 A; A/C=90-110, B/D=25-54.	[ExPASy / RCSB / EBI]
1HIQ; NMR; -; A=90-110, B=25-54.	[ExPASy / RCSB / EBI]
1HIS; NMR; -; A=90-110, B=25-49.	[ExPASy / RCSB / EBI]
1HIT; NMR; -; A=90-110, B=25-54.	[ExPASy / RCSB / EBI]
1HLS; NMR; -; A=90-110, B=25-54.	[ExPASy / RCSB / EBI]
1HTV; X-ray; 1.90 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-51.	[ExPASy / RCSB / EBI]
1HUI; NMR; -; A=90-110, B=26-53.	[ExPASy / RCSB / EBI]
1IOG; NMR; -; A=90-110, B=26-53.	[ExPASy / RCSB / EBI]
1IOH; NMR; -; A=90-110, B=26-53.	[ExPASy / RCSB / EBI]
1J73; X-ray; 2.00 A; A/C=90-110, B/D=25-54.	[ExPASy / RCSB / EBI]
1JCA; X-ray; 2.50 A; A/C=90-110, B/D=25-54.	[ExPASy / RCSB / EBI]
1JCO; NMR; -; A=90-110, B=25-54.	[ExPASy / RCSB / EBI]
1K3M; NMR; -; A=90-110, B=25-54.	[ExPASy / RCSB / EBI]
1KMF; NMR; -; A=90-110, B=25-54.	[ExPASy / RCSB / EBI]
1LKQ; NMR; -; A=90-110, B=25-54.	[ExPASy / RCSB / EBI]
1LPH; X-ray; 2.30 A; A/C=90-110, B/D=25-54.	[ExPASy / RCSB / EBI]
1MHI; NMR; -; A=90-110, B=25-54.	[ExPASy / RCSB / EBI]
1MHJ; NMR; -; A=90-110, B=25-48.	[ExPASy / RCSB / EBI]
1MSO; X-ray; 1.00 A; A/C=90-110, B/D=25-54.	[ExPASy / RCSB / EBI]
1OS3; X-ray; 1.95 A; A/C=90-110, B/D=25-54.	[ExPASy / RCSB / EBI]
1OS4; X-ray; 2.25 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.	[ExPASy / RCSB / EBI]
1QIY; X-ray; 2.30 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.	[ExPASy / RCSB / EBI]
1QIZ; X-ray; 2.00 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.	[ExPASy / RCSB / EBI]
1QJ0; X-ray; 2.40 A; A/C=90-110, B/D=25-54.	[ExPASy / RCSB / EBI]
1RWE; X-ray; 1.80 A; A/C=90-110, B/D=25-54.	[ExPASy / RCSB / EBI]
1SF1; NMR; -; A=90-110, B=25-54.	[ExPASy / RCSB / EBI]
1SJT; NMR; -; A=90-110, B=25-53.	[ExPASy / RCSB / EBI]
1SJU; NMR; -; A=25-53.	[ExPASy / RCSB / EBI]
1T0C; NMR; -; A=57-87.	[ExPASy / RCSB / EBI]
1T1K; NMR; -; A=90-110, B=25-54.	[ExPASy / RCSB / EBI]
1T1P; NMR; -; A=90-110, B=25-54.	[ExPASy / RCSB / EBI]
1T1Q; NMR; -; A=90-110, B=25-54.	[ExPASy / RCSB / EBI]
1TRZ; X-ray; 1.60 A; A/C=90-110, B/D=25-54.	[ExPASy / RCSB / EBI]
1TYL; X-ray; 1.90 A; A/C=90-110, B/D=25-54.	[ExPASy / RCSB / EBI]
1TYM; X-ray; 1.90 A; A/C=90-110, B/D=25-54.	[ExPASy / RCSB / EBI]
1UZ9; X-ray; 1.60 A; A=90-110, B=25-53.	[ExPASy / RCSB / EBI]
1VKT; NMR; -; A=90-110, B=25-54.	[ExPASy / RCSB / EBI]
1W8P; X-ray; 2.08 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.	[ExPASy / RCSB / EBI]
1XDA; X-ray; 1.80 A; A/C/E/G=90-110, B/D/F/H=25-53.	[ExPASy / RCSB / EBI]
1XGL; NMR; -; A=90-110, B=25-54.	[ExPASy / RCSB / EBI]
1XW7; X-ray; 2.30 A; A/C=90-110, B/D=25-54.	[ExPASy / RCSB / EBI]
1ZEG; X-ray; 1.60 A; A/C=90-110, B/D=25-54.	[ExPASy / RCSB / EBI]
1ZEH; X-ray; 1.50 A; A/C=90-110, B/D=25-54.	[ExPASy / RCSB / EBI]
1ZNJ; X-ray; 2.00 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.	[ExPASy / RCSB / EBI]
2AIY; NMR; -; B/D/F/H/J/L=25-54.	[ExPASy / RCSB / EBI]
2C8Q; X-ray; 1.95 A; A=90-110, B=25-53.	[ExPASy / RCSB / EBI]
2C8R; X-ray; 1.50 A; A=90-110, B=25-53.	[ExPASy / RCSB / EBI]
2CEU; X-ray; 1.80 A; A/C=90-110, B/D=25-49.	[ExPASy / RCSB / EBI]
2H67; NMR; -; A=90-110, B=25-54.	[ExPASy / RCSB / EBI]
2HH4; NMR; -; A=90-110.	[ExPASy / RCSB / EBI]
2HHO; NMR; -; A=90-110, B=25-54.	[ExPASy / RCSB / EBI]
2HIU; NMR; -; A=90-110, B=25-54.	[ExPASy / RCSB / EBI]
2JMN; NMR; -; A=90-110, B=25-54.	[ExPASy / RCSB / EBI]
2OMG; X-ray; 1.52 A; A/C/E=90-110, F=25-54.	[ExPASy / RCSB / EBI]
2OMH; X-ray; 1.36 A; A/C/E=90-110, B/F=25-54.	[ExPASy / RCSB / EBI]
2OMI; X-ray; 2.24 A; A/C/E/G/I/K=90-110, B/F/J=25-54.	[ExPASy / RCSB / EBI]
3AIY; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.	[ExPASy / RCSB / EBI]
4AIY; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.	[ExPASy / RCSB / EBI]
5AIY; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1A7F; -.
1AI0; -.
1AIY; -.
1B9E; -.
1BEN; -.
1EFE; -.
1EV3; -.
1EV6; -.
1EVR; -.
1FU2; -.
1FUB; -.
1G7A; -.
1G7B; -.
1GUJ; -.
1HIQ; -.
1HIS; -.
1HIT; -.
1HLS; -.
1HTV; -.
1HUI; -.
1IOG; -.
1IOH; -.
1J73; -.
1JCA; -.
1JCO; -.
1K3M; -.
1KMF; -.
1LKQ; -.
1LPH; -.
1MHI; -.
1MHJ; -.
1MSO; -.
1OS3; -.
1OS4; -.
1QIY; -.
1QIZ; -.
1QJ0; -.
1RWE; -.
1SF1; -.
1SJT; -.
1SJU; -.
1T0C; -.
1T1K; -.
1T1P; -.
1T1Q; -.
1TRZ; -.
1TYL; -.
1TYM; -.
1UZ9; -.
1VKT; -.
1W8P; -.
1XDA; -.
1XGL; -.
1XW7; -.
1ZEG; -.
1ZEH; -.
1ZNJ; -.
2AIY; -.
2C8Q; -.
2C8R; -.
2CEU; -.
2H67; -.
2HH4; -.
2HHO; -.
2HIU; -.
2JMN; -.
2OMG; -.
2OMH; -.
2OMI; -.
3AIY; -.
4AIY; -.
5AIY; -.

SMR

P01308; 25-84.

ModBase

P01308.

Protein-protein interaction databases

DIP

DIP:6024N; -.

Enzyme and pathway databases

Reactome

REACT_1355; Insulin degradation.
REACT_498; Signaling by insulin receptor.
REACT_508; Signal attenuation.

Organism-specific databases

HGNC:6081; INS.

INS; Homo sapiens.

INS.

CAB000048; -.

176730; gene+phenotype. [NCBI / EBI]

PharmGKB

PA201; -.

GeneCards

P01308.

Gene expression databases

ArrayExpress

P01308; -.

CleanEx

HS_INS; -.

GermOnline

ENSG00000129965; Homo sapiens.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred by curator from UniProtKB).
GO:0005179;	Molecular function: hormone activity (non-traceable author statement from UniProtKB).
GO:0005158;	Molecular function: insulin receptor binding (inferred from direct assay from UniProtKB).
GO:0005520;	Molecular function: insulin-like growth factor binding (inferred from physical interaction from UniProtKB).
GO:0006953;	Biological process: acute-phase response (non-traceable author statement from UniProtKB).
GO:0046631;	Biological process: alpha-beta T cell activation (inferred from direct assay from UniProtKB).
GO:0008219;	Biological process: cell death (non-traceable author statement from UniProtKB).
GO:0007166;	Biological process: cell surface receptor linked signal transduction (traceable author statement from ProtInc).
GO:0007267;	Biological process: cell-cell signaling (inferred by curator from UniProtKB).
GO:0006091;	Biological process: generation of precursor metabolites and energy (traceable author statement from ProtInc).
GO:0006006;	Biological process: glucose metabolic process (traceable author statement from ProtInc).
GO:0015758;	Biological process: glucose transport (inferred from direct assay from UniProtKB).
GO:0042177;	Biological process: negative regulation of protein catabolic process (inferred from direct assay from UniProtKB).
GO:0045908;	Biological process: negative regulation of vasodilation (non-traceable author statement from UniProtKB).
GO:0050715;	Biological process: positive regulation of cytokine secretion (inferred from direct assay from UniProtKB).
GO:0045429;	Biological process: positive regulation of nitric oxide biosynthetic process (non-traceable author statement from UniProtKB).
GO:0051000;	Biological process: positive regulation of nitric-oxide synthase activity (non-traceable author statement from UniProtKB).
GO:0045909;	Biological process: positive regulation of vasodilation (non-traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR004825; Ins/IGF/relaxin.
IPR003234; Insulin-related_peptide.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.100.10; Ins/IGF/relaxin; 1.

Pfam

PF00049; Insulin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00276; INSULINA.
PR00277; INSULINB.

ProDom

PD015667; Mollusc_ins; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00078; IlGF; 1.
SMART graphical view of domain structure.

PS00262; INSULIN; 1.

Proteomic databases

P01308; -.

Genome annotation databases

Ensembl

ENSG00000129965; Homo sapiens. [Contig view]

GeneID

3630; -.

KEGG

hsa:3630; -.

Other

P01308; -.

INS; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Carbohydrate metabolism; Cleavage on pair of basic residues; Diabetes mellitus; Direct protein sequencing; Disease mutation; Glucose metabolism; Hormone; Pharmaceutical; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 24`	`24`
`PEPTIDE`	`25 54`	`30`	`Insulin B chain.`	`PRO_0000015819`
`PROPEP`	`57 87`	`31`	`C peptide.`	`PRO_0000015820`
`PEPTIDE`	`90 110`	`21`	`Insulin A chain.`	`PRO_0000015821`
`DISULFID`	`31 96`		`Interchain (between B and A chains).`
`DISULFID`	`43 109`		`Interchain (between B and A chains).`
`DISULFID`	`95 100`
`VARIANT`	`34 34`	`1`	`H -> D (in familial hyperproinsulinemia; Providence).`	`VAR_003971 [3D]`
`VARIANT`	`48 48`	`1`	`F -> S (associated with diabetes mellitus type-II; Los-Angeles).`	`VAR_003972 [3D]`
`VARIANT`	`49 49`	`1`	`F -> L (in Chicago).`	`VAR_003973 [3D]`
`VARIANT`	`89 89`	`1`	`R -> H (in familial hyperproinsulinemia; impairs posttranslational cleavage).`	`VAR_003974`
`VARIANT`	`89 89`	`1`	`R -> L (in familial hyperproinsulinemia; Kyoto).`	`VAR_003975`
`VARIANT`	`92 92`	`1`	`V -> L (in Wakayama).`	`VAR_003976`
`HELIX`	`33 43`	`11`
`HELIX`	`44 46`	`3`
`STRAND`	`48 50`	`3`
`TURN`	`61 66`	`6`
`STRAND`	`74 76`	`3`
`HELIX`	`79 81`	`3`
`TURN`	`84 86`	`3`
`HELIX`	`91 95`	`5`
`HELIX`	`102 105`	`4`
`HELIX`	`106 108`	`3`

Sequence information

Length: 110 AA [This is the length of the unprocessed precursor]

Molecular weight: 11981 Da [This is the MW of the unprocessed precursor]

CRC64: C2C3B23B85E520E5 [This is a checksum on the sequence]

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

        70         80         90        100        110 
LQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC SLYQLENYCN

P01308 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools

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