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UniProtKB/Swiss-Prot entry P01308

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name INS_HUMAN
Primary accession number P01308
Secondary accession number Q5EEX2
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 120)
Name and origin of the protein
Protein name Insulin [Precursor]
Synonyms None
Contains Insulin B chain
Insulin A chain
Gene name
Name: INS
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[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
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]
PIR A93222; IPHU.
RefSeq NP_000198.1; -.
UniGene Hs.654579
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]
2JV1; NMR; -; A=90-110, B=25-54.[ExPASy / RCSB / EBI]
2JZQ; NMR; -; A=25-54, A=90-110.[ExPASy / RCSB / EBI]
2OLY; X-ray; 1.70 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.[ExPASy / RCSB / EBI]
2OLZ; X-ray; 1.70 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.[ExPASy / RCSB / EBI]
2OM0; X-ray; 2.05 A; 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.[ExPASy / RCSB / EBI]
2OM1; X-ray; 1.97 A; 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.[ExPASy / RCSB / EBI]
2OMG; X-ray; 1.52 A; A/C/E=90-110, B/D/F=25-54.[ExPASy / RCSB / EBI]
2OMH; X-ray; 1.36 A; A/C/E=90-110, B/D/F=25-54.[ExPASy / RCSB / EBI]
2OMI; X-ray; 2.24 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.[ExPASy / RCSB / EBI]
2QIU; X-ray; 2.00 A; A/C=89-110, B/D=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; -.
2JV1; -.
2JZQ; -.
2OLY; -.
2OLZ; -.
2OM0; -.
2OM1; -.
2OMG; -.
2OMH; -.
2OMI; -.
2QIU; -.
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 HGNC:6081; INS.
GeneLynx INS; Homo sapiens.
GenAtlas INS.
HPA CAB000048; -.
CAB012098; -.
HPA004932; -.
MIM 176730; gene+phenotype. [NCBI / EBI]
PharmGKB PA201; -.
GeneCards P01308.
Gene expression databases
ArrayExpress P01308; -.
GermOnline ENSG00000129965; Homo sapiens.
Ontologies
GO
GO:0005615; Cellular component: extracellular space (inferred from direct assay 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:0005159; Molecular function: insulin-like growth factor receptor binding (inferred from physical interaction from UniProtKB).
GO:0006953; Biological process: acute-phase response (inferred from direct assay 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:0007267; Biological process: cell-cell signaling (inferred by curator from UniProtKB).
GO:0055089; Biological process: fatty acid homeostasis (inferred from mutant phenotype from UniProtKB).
GO:0007186; Biological process: G-protein coupled receptor protein signaling pathway (inferred from direct assay from UniProtKB).
GO:0042593; Biological process: glucose homeostasis (inferred from mutant phenotype from UniProtKB).
GO:0002674; Biological process: negative regulation of acute inflammatory response (inferred from direct assay from UniProtKB).
GO:0045922; Biological process: negative regulation of fatty acid metabolic process (inferred from mutant phenotype from UniProtKB).
GO:0045818; Biological process: negative regulation of glycogen catabolic process (inferred from mutant phenotype from UniProtKB).
GO:0033861; Biological process: negative regulation of NAD(P)H oxidase activity (inferred from direct assay from UniProtKB).
GO:0042177; Biological process: negative regulation of protein catabolic process (inferred from direct assay from UniProtKB).
GO:0050709; Biological process: negative regulation of protein secretion (inferred from direct assay from UniProtKB).
GO:0045861; Biological process: negative regulation of proteolysis (inferred from mutant phenotype from UniProtKB).
GO:0045908; Biological process: negative regulation of vasodilation (non-traceable author statement from UniProtKB).
GO:0014065; Biological process: phosphoinositide 3-kinase cascade (inferred from direct assay from UniProtKB).
GO:0032270; Biological process: positive regulation of cellular protein metabolic process (inferred from mutant phenotype from UniProtKB).
GO:0050715; Biological process: positive regulation of cytokine secretion (inferred from direct assay from UniProtKB).
GO:0045740; Biological process: positive regulation of DNA replication (inferred from direct assay from UniProtKB).
GO:0046326; Biological process: positive regulation of glucose import (inferred from direct assay from UniProtKB).
GO:0045821; Biological process: positive regulation of glycolysis (inferred from direct assay from UniProtKB).
GO:0046628; Biological process: positive regulation of insulin receptor signaling pathway (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).
GO:0006521; Biological process: regulation of amino acid metabolic process (inferred from mutant phenotype from UniProtKB).
GO:0032583; Biological process: regulation of gene-specific transcription (non-traceable author statement from UniProtKB).
GO:0032880; Biological process: regulation of protein localization (inferred from direct assay from UniProtKB).
GO:0022898; Biological process: regulation of transmembrane transporter activity (inferred from direct assay from UniProtKB).
GO:0045730; Biological process: respiratory burst (inferred from direct assay from UniProtKB).
GO:0042060; Biological process: wound healing (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR004825; Ins/IGF/relaxin.
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.
PROSITE PS00262; INSULIN; 1.
BLOCKS P01308.
Proteomic databases
PeptideAtlas P01308; -.
Genome annotation databases
Ensembl ENSG00000129965; Homo sapiens. [Contig view]
GeneID 3630; -.
KEGG hsa:3630; -.
Phylogenomic databases
HOGENOM P01308; -.
HOVERGEN P01308; -.
Other
LinkHub P01308; -.
SOURCE INS; Homo sapiens.
ProtoNet P01308.
UniRef 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
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   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 &n