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INS_HUMAN
ID   INS_HUMAN               Reviewed;         110 AA.
AC   P01308; Q5EEX2;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 265.
DE   RecName: Full=Insulin;
DE   Contains:
DE     RecName: Full=Insulin B chain;
DE   Contains:
DE     RecName: Full=Insulin A chain;
DE   Flags: Precursor;
GN   Name=INS;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6243748; DOI=10.1038/284026a0;
RA   Bell G.I., Pictet R.L., Rutter W.J., Cordell B., Tischer E., Goodman H.M.;
RT   "Sequence of the human insulin gene.";
RL   Nature 284:26-32(1980).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6248962; DOI=10.1126/science.6248962;
RA   Ullrich A., Dull T.J., Gray A., Brosius J., Sures I.;
RT   "Genetic variation in the human insulin gene.";
RL   Science 209:612-615(1980).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=503234; DOI=10.1038/282525a0;
RA   Bell G.I., Swain W.F., Pictet R.L., Cordell B., Goodman H.M., Rutter W.J.;
RT   "Nucleotide sequence of a cDNA clone encoding human preproinsulin.";
RL   Nature 282:525-527(1979).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6927840; DOI=10.1126/science.6927840;
RA   Sures I., Goeddel D.V., Gray A., Ullrich A.;
RT   "Nucleotide sequence of human preproinsulin complementary DNA.";
RL   Science 208:57-59(1980).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8358440; DOI=10.1038/ng0793-305;
RA   Lucassen A.M., Julier C., Beressi J.-P., Boitard C., Froguel P.,
RA   Lathrop M., Bell J.I.;
RT   "Susceptibility to insulin dependent diabetes mellitus maps to a 4.1 kb
RT   segment of DNA spanning the insulin gene and associated VNTR.";
RL   Nat. Genet. 4:305-310(1993).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15070567; DOI=10.1016/s0140-6736(04)15438-x;
RA   Minn A.H., Kayton M., Lorang D., Hoffmann S.C., Harlan D.M., Libutti S.K.,
RA   Shalev A.;
RT   "Insulinomas and expression of an insulin splice variant.";
RL   Lancet 363:363-367(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12952878; DOI=10.1101/gr.948003;
RA   Stead J.D.H., Hurles M.E., Jeffreys A.J.;
RT   "Global haplotype diversity in the human insulin gene region.";
RL   Genome Res. 13:2101-2111(2003).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59.
RC   TISSUE=Blood;
RA   Fajardy I.I., Weill J.J., Stuckens C.C., Danze P.M.P.;
RT   "Description of a novel RFLP diallelic polymorphism (-127 BsgI C/G) within
RT   the 5' region of insulin gene.";
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   PROTEIN SEQUENCE OF 25-54 AND 90-110.
RX   PubMed=14426955; DOI=10.1038/187483a0;
RA   Nicol D.S.H.W., Smith L.F.;
RT   "Amino-acid sequence of human insulin.";
RL   Nature 187:483-485(1960).
RN   [13]
RP   PROTEIN SEQUENCE OF 57-87.
RX   PubMed=5101771; DOI=10.1016/s0021-9258(19)76984-1;
RA   Oyer P.E., Cho S., Peterson J.D., Steiner D.F.;
RT   "Studies on human proinsulin. Isolation and amino acid sequence of the
RT   human pancreatic C-peptide.";
RL   J. Biol. Chem. 246:1375-1386(1971).
RN   [14]
RP   PROTEIN SEQUENCE OF 57-87.
RX   PubMed=5560404; DOI=10.1111/j.1432-1033.1971.tb01378.x;
RA   Ko A., Smyth D.G., Markussen J., Sundby F.;
RT   "The amino acid sequence of the C-peptide of human proinsulin.";
RL   Eur. J. Biochem. 20:190-199(1971).
RN   [15]
RP   SYNTHESIS.
RX   PubMed=4443293; DOI=10.1002/hlca.19740570839;
RA   Sieber P., Kamber B., Hartmann A., Joehl A., Riniker B., Rittel W.;
RT   "Total synthesis of human insulin under directed formation of the disulfide
RT   bonds.";
RL   Helv. Chim. Acta 57:2617-2621(1974).
RN   [16]
RP   SYNTHESIS OF 57-87.
RX   PubMed=4803504; DOI=10.1515/bchm2.1973.354.1.659;
RA   Naithani V.K.;
RT   "Studies on polypeptides, IV. The synthesis of C-peptide of human
RT   proinsulin.";
RL   Hoppe-Seyler's Z. Physiol. Chem. 354:659-672(1973).
RN   [17]
RP   SYNTHESIS OF 65-69 AND 70-73.
RX   PubMed=4698555; DOI=10.1002/cber.19731060124;
RA   Geiger R., Volk A.;
RT   "Synthesis of peptides with the properties of human proinsulin C peptides
RT   (hC peptide). 3. Synthesis of the sequences 14-17 and 9-13 of human
RT   proinsulin C peptides.";
RL   Chem. Ber. 106:199-205(1973).
RN   [18]
RP   SYNTHESIS OF 84-87.
RX   PubMed=4698553; DOI=10.1002/cber.19731060122;
RA   Geiger R., Jaeger G., Keonig W., Treuth G.;
RT   "Synthesis of peptides with the properties of human proinsulin C peptides
RT   (hC peptide). I. Scheme for the synthesis and preparation of the sequence
RT   28-31 of human proinsulin C peptide.";
RL   Chem. Ber. 106:188-192(1973).
RN   [19]
RP   VARIANT LOS ANGELES SER-48.
RX   PubMed=6312455; DOI=10.1073/pnas.80.20.6366;
RA   Haneda M., Chan S.J., Kwok S.C.M., Rubenstein A.H., Steiner D.F.;
RT   "Studies on mutant human insulin genes: identification and sequence
RT   analysis of a gene encoding [SerB24]insulin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:6366-6370(1983).
RN   [20]
RP   VARIANTS LOS ANGELES SER-48 AND CHICAGO LEU-49.
RX   PubMed=6424111; DOI=10.1073/pnas.80.24.7390;
RA   Shoelson S., Fickova M., Haneda M., Nahum A., Musso G., Kaiser E.T.,
RA   Rubenstein A.H., Tager H.;
RT   "Identification of a mutant human insulin predicted to contain a serine-
RT   for-phenylalanine substitution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:7390-7394(1983).
RN   [21]
RP   VARIANT HPRI ASP-34.
RX   PubMed=3470784; DOI=10.1073/pnas.84.8.2194;
RA   Chan S.J., Seino S., Gruppuso P.A., Schwartz R., Steiner D.F.;
RT   "A mutation in the B chain coding region is associated with impaired
RT   proinsulin conversion in a family with hyperproinsulinemia.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:2194-2197(1987).
RN   [22]
RP   VARIANT WAKAYAMA LEU-92.
RX   PubMed=3537011; DOI=10.1172/jci112760;
RA   Sakura H., Iwamoto Y., Sakamoto Y., Kuzuya T., Hirata H.;
RT   "Structurally abnormal insulin in a diabetic patient. Characterization of
RT   the mutant insulin A3 (Val-->Leu) isolated from the pancreas.";
RL   J. Clin. Invest. 78:1666-1672(1986).
RN   [23]
RP   VARIANT HPRI HIS-89.
RX   PubMed=2196279; DOI=10.1210/jcem-71-1-164;
RA   Barbetti F., Raben N., Kadowaki T., Cama A., Accili D., Gabbay K.H.,
RA   Merenich J.A., Taylor S.I., Roth J.;
RT   "Two unrelated patients with familial hyperproinsulinemia due to a mutation
RT   substituting histidine for arginine at position 65 in the proinsulin
RT   molecule: identification of the mutation by direct sequencing of genomic
RT   deoxyribonucleic acid amplified by polymerase chain reaction.";
RL   J. Clin. Endocrinol. Metab. 71:164-169(1990).
RN   [24]
RP   VARIANT HPRI HIS-89.
RX   PubMed=4019786; DOI=10.1172/jci111973;
RA   Shibasaki Y., Kawakami T., Kanazawa Y., Akanuma Y., Takaku F.;
RT   "Posttranslational cleavage of proinsulin is blocked by a point mutation in
RT   familial hyperproinsulinemia.";
RL   J. Clin. Invest. 76:378-380(1985).
RN   [25]
RP   VARIANT HPRI LEU-89.
RX   PubMed=1601997; DOI=10.1172/jci115795;
RA   Yano H., Kitano N., Morimoto M., Polonsky K.S., Imura H., Seino Y.;
RT   "A novel point mutation in the human insulin gene giving rise to
RT   hyperproinsulinemia (proinsulin Kyoto).";
RL   J. Clin. Invest. 89:1902-1907(1992).
RN   [26]
RP   STRUCTURE BY NMR.
RX   PubMed=2271664; DOI=10.1021/bi00498a018;
RA   Hua Q.-X., Weiss M.A.;
RT   "Toward the solution structure of human insulin: sequential 2D 1H NMR
RT   assignment of a des-pentapeptide analogue and comparison with crystal
RT   structure.";
RL   Biochemistry 29:10545-10555(1990).
RN   [27]
RP   STRUCTURE BY NMR.
RX   PubMed=2036420; DOI=10.1021/bi00236a025;
RA   Hua Q.-X., Weiss M.A.;
RT   "Comparative 2D NMR studies of human insulin and des-pentapeptide insulin:
RT   sequential resonance assignment and implications for protein dynamics and
RT   receptor recognition.";
RL   Biochemistry 30:5505-5515(1991).
RN   [28]
RP   STRUCTURE BY NMR.
RX   PubMed=1646635; DOI=10.1016/0167-4838(91)90098-k;
RA   Hua Q.-X., Weiss M.A.;
RT   "Two-dimensional NMR studies of Des-(B26-B30)-insulin: sequence-specific
RT   resonance assignments and effects of solvent composition.";
RL   Biochim. Biophys. Acta 1078:101-110(1991).
RN   [29]
RP   STRUCTURE BY NMR OF 90-110 AND 25-54, AND DISULFIDE BONDS.
RX   PubMed=1433291; DOI=10.1016/0022-2836(92)90527-q;
RA   Joergensen A.M.M., Kristensen S.M., Led J.J., Balschmidt P.;
RT   "Three-dimensional solution structure of an insulin dimer. A study of the
RT   B9(Asp) mutant of human insulin using nuclear magnetic resonance, distance
RT   geometry and restrained molecular dynamics.";
RL   J. Mol. Biol. 227:1146-1163(1992).
RN   [30]
RP   STRUCTURE BY NMR OF 90-110 AND 25-54 OF VARIANT LOS-ANGELES SER-48, AND
RP   DISULFIDE BONDS.
RX   PubMed=8421693; DOI=10.1073/pnas.90.2.582;
RA   Hua Q.-X., Shoelson S.E., Inouye K., Weiss M.A.;
RT   "Paradoxical structure and function in a mutant human insulin associated
RT   with diabetes mellitus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:582-586(1993).
RN   [31]
RP   STRUCTURE BY NMR OF 90-110 AND 25-54, AND DISULFIDE BONDS.
RX   PubMed=9235985; DOI=10.1021/bi9631069;
RA   Chang X., Joergensen A.M., Bardrum P., Led J.J.;
RT   "Solution structures of the R6 human insulin hexamer.";
RL   Biochemistry 36:9409-9422(1997).
RN   [32]
RP   VARIANTS PNDM4 ASP-24; ARG-32; SER-32; GLY-43; VAL-47; CYS-48; CYS-89;
RP   CYS-90; TYR-96 AND CYS-108.
RX   PubMed=17855560; DOI=10.1073/pnas.0707291104;
RA   Stoy J., Edghill E.L., Flanagan S.E., Ye H., Paz V.P., Pluzhnikov A.,
RA   Below J.E., Hayes M.G., Cox N.J., Lipkind G.M., Lipton R.B., Greeley S.A.,
RA   Patch A.M., Ellard S., Steiner D.F., Hattersley A.T., Philipson L.H.,
RA   Bell G.I.;
RT   "Insulin gene mutations as a cause of permanent neonatal diabetes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:15040-15044(2007).
RN   [33]
RP   VARIANTS PNDM4 ASP-24; ASP-29; ARG-32; SER-32; PRO-35; GLY-43; VAL-47;
RP   CYS-48; ARG-84; CYS-89; CYS-90; SER-96; TYR-96; CYS-101; CYS-103 AND
RP   CYS-108, VARIANT MODY10 CYS-6, AND VARIANT MET-68.
RX   PubMed=18162506; DOI=10.2337/db07-1405;
RA   Edghill E.L., Flanagan S.E., Patch A.M., Boustred C., Parrish A.,
RA   Shields B., Shepherd M.H., Hussain K., Kapoor R.R., Malecki M.,
RA   MacDonald M.J., Stoy J., Steiner D.F., Philipson L.H., Bell G.I.,
RA   Hattersley A.T., Ellard S.;
RT   "Insulin mutation screening in 1,044 patients with diabetes: mutations in
RT   the INS gene are a common cause of neonatal diabetes but a rare cause of
RT   diabetes diagnosed in childhood or adulthood.";
RL   Diabetes 57:1034-1042(2008).
RN   [34]
RP   VARIANT MODY10 GLN-46, AND VARIANT IDDM2 CYS-55.
RX   PubMed=18192540; DOI=10.2337/db07-1467;
RA   Molven A., Ringdal M., Nordbo A.M., Raeder H., Stoy J., Lipkind G.M.,
RA   Steiner D.F., Philipson L.H., Bergmann I., Aarskog D., Undlien D.E.,
RA   Joner G., Sovik O., Bell G.I., Njolstad P.R.;
RT   "Mutations in the insulin gene can cause MODY and autoantibody-negative
RT   type 1 diabetes.";
RL   Diabetes 57:1131-1135(2008).
RN   [35]
RP   VARIANTS MODY10 HIS-6 AND GLN-46.
RX   PubMed=20226046; DOI=10.1186/1471-2350-11-42;
RA   Boesgaard T.W., Pruhova S., Andersson E.A., Cinek O., Obermannova B.,
RA   Lauenborg J., Damm P., Bergholdt R., Pociot F., Pisinger C., Barbetti F.,
RA   Lebl J., Pedersen O., Hansen T.;
RT   "Further evidence that mutations in INS can be a rare cause of Maturity-
RT   Onset Diabetes of the Young (MODY).";
RL   BMC Med. Genet. 11:42-42(2010).
RN   [36]
RP   VARIANT MODY10 GLN-46, CHARACTERIZATION OF VARIANT MODY10 GLN-46, STRUCTURE
RP   BY NMR OF 90-110 AND 25-54, DISULFIDE BONDS OF VARIANT MODY10 GLN-46, AND
RP   SUBUNIT.
RX   PubMed=25423173; DOI=10.1371/journal.pone.0112883;
RA   Krizkova K., Veverka V., Maletinska L., Hexnerova R., Brzozowski A.M.,
RA   Jiracek J., Zakova L.;
RT   "Structural and functional study of the GlnB22-insulin mutant responsible
RT   for maturity-onset diabetes of the young.";
RL   PLoS ONE 9:E112883-E112883(2014).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It increases
CC       cell permeability to monosaccharides, amino acids and fatty acids. It
CC       accelerates glycolysis, the pentose phosphate cycle, and glycogen
CC       synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds (PubMed:25423173). {ECO:0000269|PubMed:25423173}.
CC   -!- INTERACTION:
CC       P01308; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-7090529, EBI-10173507;
CC       P01308; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-7090529, EBI-3867333;
CC       P01308; P14735-1: IDE; NbExp=3; IntAct=EBI-7090529, EBI-15607031;
CC       P01308; P01308: INS; NbExp=19; IntAct=EBI-7090529, EBI-7090529;
CC       P01308; P06213-2: INSR; NbExp=6; IntAct=EBI-7090529, EBI-9984921;
CC       P01308; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-7090529, EBI-11959885;
CC       P01308; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-7090529, EBI-11749135;
CC       P01308; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-7090529, EBI-22310682;
CC       PRO_0000015820; P11142: HSPA8; NbExp=2; IntAct=EBI-20765227, EBI-351896;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P01308-1; Sequence=Displayed;
CC       Name=2; Synonyms=INS-IGF2;
CC         IsoId=F8WCM5-1; Sequence=External;
CC   -!- DISEASE: Hyperproinsulinemia (HPRI) [MIM:616214]: An autosomal dominant
CC       condition characterized by elevated levels of serum proinsulin-like
CC       material. {ECO:0000269|PubMed:1601997, ECO:0000269|PubMed:2196279,
CC       ECO:0000269|PubMed:3470784, ECO:0000269|PubMed:4019786}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Diabetes mellitus, insulin-dependent, 2 (IDDM2) [MIM:125852]:
CC       A multifactorial disorder of glucose homeostasis that is characterized
CC       by susceptibility to ketoacidosis in the absence of insulin therapy.
CC       Clinical features are polydipsia, polyphagia and polyuria which result
CC       from hyperglycemia-induced osmotic diuresis and secondary thirst. These
CC       derangements result in long-term complications that affect the eyes,
CC       kidneys, nerves, and blood vessels. {ECO:0000269|PubMed:18192540}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- DISEASE: Diabetes mellitus, permanent neonatal, 4 (PNDM4) [MIM:618858]:
CC       A form of permanent neonatal diabetes mellitus, a type of diabetes
CC       characterized by onset of persistent hyperglycemia within the first six
CC       months of life. Initial clinical manifestations include intrauterine
CC       growth retardation, hyperglycemia, glycosuria, osmotic polyuria, severe
CC       dehydration, and failure to thrive. PNDM4 transmission pattern is
CC       consistent with autosomal dominant or autosomal recessive inheritance.
CC       {ECO:0000269|PubMed:17855560, ECO:0000269|PubMed:18162506}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Maturity-onset diabetes of the young 10 (MODY10) [MIM:613370]:
CC       A form of diabetes that is characterized by an autosomal dominant mode
CC       of inheritance, onset in childhood or early adulthood (usually before
CC       25 years of age), a primary defect in insulin secretion and frequent
CC       insulin-independence at the beginning of the disease.
CC       {ECO:0000269|PubMed:18162506, ECO:0000269|PubMed:18192540,
CC       ECO:0000269|PubMed:20226046, ECO:0000269|PubMed:25423173}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- PHARMACEUTICAL: Available under the names Humulin or Humalog (Eli
CC       Lilly) and Novolin (Novo Nordisk). Used in the treatment of diabetes.
CC       Humalog is an insulin analog with 52-Lys-Pro-53 instead of 52-Pro-Lys-
CC       53.
CC   -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA59179.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Insulin at Eli Lilly; Note=Clinical information on
CC       Eli Lilly insulin products;
CC       URL="https://www.lillydiabetes.com/assets/pdf/pp-ld-us-1198-types_of_treatments.pdf";
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Protein of the 20th century
CC       - Issue 9 of April 2001;
CC       URL="https://web.expasy.org/spotlight/back_issues/009";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Insulin entry;
CC       URL="https://en.wikipedia.org/wiki/Insulin";
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DR   EMBL; V00565; CAA23828.1; -; Genomic_DNA.
DR   EMBL; M10039; AAA59173.1; -; Genomic_DNA.
DR   EMBL; J00265; AAA59172.1; -; Genomic_DNA.
DR   EMBL; X70508; CAA49913.1; -; mRNA.
DR   EMBL; L15440; AAA59179.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AY899304; AAW83741.1; -; mRNA.
DR   EMBL; AY138590; AAN39451.1; -; Genomic_DNA.
DR   EMBL; BT006808; AAP35454.1; -; mRNA.
DR   EMBL; CH471158; EAX02488.1; -; Genomic_DNA.
DR   EMBL; BC005255; AAH05255.1; -; mRNA.
DR   EMBL; AJ009655; CAA08766.1; -; Genomic_DNA.
DR   CCDS; CCDS7729.1; -. [P01308-1]
DR   PIR; A93222; IPHU.
DR   RefSeq; NP_000198.1; NM_000207.2. [P01308-1]
DR   RefSeq; NP_001172026.1; NM_001185097.1. [P01308-1]
DR   RefSeq; NP_001172027.1; NM_001185098.1. [P01308-1]
DR   RefSeq; NP_001278826.1; NM_001291897.1. [P01308-1]
DR   PDB; 1A7F; NMR; -; A=90-110, B=25-53.
DR   PDB; 1AI0; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 1AIY; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 1B9E; X-ray; 2.50 A; A/C=90-110, B/D=25-54.
DR   PDB; 1BEN; X-ray; 1.40 A; A/C=90-110, B/D=25-54.
DR   PDB; 1EFE; NMR; -; A=25-54, A=90-110.
DR   PDB; 1EV3; X-ray; 1.78 A; A/C=90-110, B/D=25-54.
DR   PDB; 1EV6; X-ray; 1.90 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 1EVR; X-ray; 1.90 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 1FU2; X-ray; 3.24 A; A/C/E/G=90-110, B/D/F/H=25-54.
DR   PDB; 1FUB; X-ray; 3.09 A; A/C=90-110, B/D=25-54.
DR   PDB; 1G7A; X-ray; 1.20 A; A/C/E/G=90-110, B/D/F/H=25-54.
DR   PDB; 1G7B; X-ray; 1.30 A; A/C/E/G=90-110, B/D/F/H=25-54.
DR   PDB; 1GUJ; X-ray; 1.62 A; A/C=90-110, B/D=25-54.
DR   PDB; 1HIQ; NMR; -; A=90-110, B=25-54.
DR   PDB; 1HIS; NMR; -; A=90-110, B=25-49.
DR   PDB; 1HIT; NMR; -; A=90-110, B=25-54.
DR   PDB; 1HLS; NMR; -; A=90-110, B=25-54.
DR   PDB; 1HTV; X-ray; 1.90 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-51.
DR   PDB; 1HUI; NMR; -; A=90-110, B=26-53.
DR   PDB; 1IOG; NMR; -; A=90-110, B=25-53.
DR   PDB; 1IOH; NMR; -; A=90-110, B=25-53.
DR   PDB; 1J73; X-ray; 2.00 A; A/C=90-110, B/D=25-54.
DR   PDB; 1JCA; X-ray; 2.50 A; A/C=90-110, B/D=25-54.
DR   PDB; 1JCO; NMR; -; A=90-110, B=25-54.
DR   PDB; 1JK8; X-ray; 2.40 A; C=35-47.
DR   PDB; 1K3M; NMR; -; A=90-110, B=25-54.
DR   PDB; 1KMF; NMR; -; A=90-110, B=25-54.
DR   PDB; 1LKQ; NMR; -; A=90-110, B=25-54.
DR   PDB; 1LPH; X-ray; 2.30 A; A/C=90-110, B/D=25-54.
DR   PDB; 1MHI; NMR; -; A=90-110, B=25-54.
DR   PDB; 1MHJ; NMR; -; A=90-110, B=25-54.
DR   PDB; 1MSO; X-ray; 1.00 A; A/C=90-110, B/D=25-54.
DR   PDB; 1OS3; X-ray; 1.95 A; A/C=90-110, B/D=25-54.
DR   PDB; 1OS4; X-ray; 2.25 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 1Q4V; X-ray; 2.00 A; A/C=90-110, B/D=25-54.
DR   PDB; 1QIY; X-ray; 2.30 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 1QIZ; X-ray; 2.00 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 1QJ0; X-ray; 2.40 A; A/C=90-110, B/D=25-54.
DR   PDB; 1RWE; X-ray; 1.80 A; A/C=90-110, B/D=25-54.
DR   PDB; 1SF1; NMR; -; A=90-110, B=25-54.
DR   PDB; 1SJT; NMR; -; A=90-110, B=25-51.
DR   PDB; 1SJU; NMR; -; A=25-110.
DR   PDB; 1T0C; NMR; -; A=57-87.
DR   PDB; 1T1K; NMR; -; A=90-110, B=25-54.
DR   PDB; 1T1P; NMR; -; A=90-110, B=25-54.
DR   PDB; 1T1Q; NMR; -; A=90-110, B=25-54.
DR   PDB; 1TRZ; X-ray; 1.60 A; A/C=90-110, B/D=25-54.
DR   PDB; 1TYL; X-ray; 1.90 A; A/C=90-110, B/D=25-54.
DR   PDB; 1TYM; X-ray; 1.90 A; A/C=90-110, B/D=25-54.
DR   PDB; 1UZ9; X-ray; 1.60 A; A=90-110, B=25-53.
DR   PDB; 1VKT; NMR; -; A=90-110, B=25-54.
DR   PDB; 1W8P; X-ray; 2.08 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 1XDA; X-ray; 1.80 A; A/C/E/G=90-110, B/D/F/H=25-53.
DR   PDB; 1XGL; NMR; -; A=90-110, B=25-54.
DR   PDB; 1XW7; X-ray; 2.30 A; A/C=90-110, B/D=25-54.
DR   PDB; 1ZEG; X-ray; 1.60 A; A/C=90-110, B/D=25-54.
DR   PDB; 1ZEH; X-ray; 1.50 A; A/C=90-110, B/D=25-54.
DR   PDB; 1ZNJ; X-ray; 2.00 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 2AIY; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 2C8Q; X-ray; 1.95 A; A=90-110, B=25-53.
DR   PDB; 2C8R; X-ray; 1.50 A; A=90-110, B=25-53.
DR   PDB; 2CEU; X-ray; 1.80 A; A/C=90-110, B/D=25-49.
DR   PDB; 2G54; X-ray; 2.25 A; C/D=25-54.
DR   PDB; 2G56; X-ray; 2.20 A; C/D=25-54.
DR   PDB; 2H67; NMR; -; A=90-110, B=25-54.
DR   PDB; 2HH4; NMR; -; A=90-110, B=25-54.
DR   PDB; 2HHO; NMR; -; A=90-110, B=25-54.
DR   PDB; 2HIU; NMR; -; A=90-110, B=25-54.
DR   PDB; 2JMN; NMR; -; A=90-110, B=25-54.
DR   PDB; 2JUM; NMR; -; A=90-110, B=25-54.
DR   PDB; 2JUU; NMR; -; A=90-110, B=25-54.
DR   PDB; 2JUV; NMR; -; A=90-110, B=25-54.
DR   PDB; 2JV1; NMR; -; A=90-110, B=25-54.
DR   PDB; 2JZQ; NMR; -; A=25-54, A=90-110.
DR   PDB; 2K91; NMR; -; A=90-110, B=25-54.
DR   PDB; 2K9R; NMR; -; A=90-110, B=25-54.
DR   PDB; 2KJJ; NMR; -; A=90-110, B=25-54.
DR   PDB; 2KJU; NMR; -; A=90-110, B=25-54.
DR   PDB; 2KQP; NMR; -; A=25-110.
DR   PDB; 2KQQ; NMR; -; A=90-110, B=25-54.
DR   PDB; 2KXK; NMR; -; A=90-110, B=25-54.
DR   PDB; 2L1Y; NMR; -; A=90-110, B=25-54.
DR   PDB; 2L1Z; NMR; -; A=90-110, B=25-54.
DR   PDB; 2LGB; NMR; -; A=90-110, B=25-55.
DR   PDB; 2LWZ; NMR; -; A=25-54, A=89-110.
DR   PDB; 2M1D; NMR; -; A=90-110, B=25-54.
DR   PDB; 2M1E; NMR; -; A=90-110, B=25-54.
DR   PDB; 2M2M; NMR; -; A=90-110, B=25-54.
DR   PDB; 2M2N; NMR; -; A=90-110, B=25-54.
DR   PDB; 2M2O; NMR; -; A=90-110, B=25-54.
DR   PDB; 2M2P; NMR; -; A=90-110, B=25-54.
DR   PDB; 2MLI; NMR; -; A=90-110, B=25-54.
DR   PDB; 2MPG; NMR; -; A=90-110, B=25-54.
DR   PDB; 2MPI; NMR; -; A=90-110, B=25-54.
DR   PDB; 2MVC; NMR; -; A=90-110, B=25-54.
DR   PDB; 2MVD; NMR; -; A=90-110, B=25-54.
DR   PDB; 2N2V; NMR; -; A=90-110, B=25-54.
DR   PDB; 2N2W; NMR; -; A=90-110, B=25-54.
DR   PDB; 2N2X; NMR; -; A=90-110, B=25-54.
DR   PDB; 2OLY; X-ray; 1.70 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 2OLZ; X-ray; 1.70 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 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.
DR   PDB; 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.
DR   PDB; 2OMG; X-ray; 1.52 A; A/C/E=90-110, B/D/F=25-54.
DR   PDB; 2OMH; X-ray; 1.36 A; A/C/E=90-110, B/D/F=25-54.
DR   PDB; 2OMI; X-ray; 2.24 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 2OMQ; X-ray; 2.00 A; A/B/C/D=36-41.
DR   PDB; 2QIU; X-ray; 2.00 A; A/C=89-110, B/D=25-54.
DR   PDB; 2R34; X-ray; 2.25 A; A/C=89-110, B/D=25-54.
DR   PDB; 2R35; X-ray; 2.08 A; A/C=89-110, B/D=25-54.
DR   PDB; 2R36; X-ray; 2.00 A; A/C=89-110, B/D=25-54.
DR   PDB; 2RN5; NMR; -; A=90-110, B=25-54.
DR   PDB; 2VJZ; X-ray; 1.80 A; A/C=90-110, B/D=25-54.
DR   PDB; 2VK0; X-ray; 2.20 A; A/C=90-110, B/D=25-54.
DR   PDB; 2W44; X-ray; 2.00 A; A/C/E=94-110, B/D/F=25-53.
DR   PDB; 2WBY; X-ray; 2.60 A; C/E=90-109, D/F=25-43.
DR   PDB; 2WC0; X-ray; 2.80 A; C/E=90-110, D/F=25-54.
DR   PDB; 2WRU; X-ray; 1.57 A; A=90-110, B=25-50.
DR   PDB; 2WRV; X-ray; 2.15 A; A=90-110, B=25-50.
DR   PDB; 2WRW; X-ray; 2.41 A; A=90-110, B=25-50.
DR   PDB; 2WRX; X-ray; 1.50 A; A/C=90-110, B/D=25-54.
DR   PDB; 2WS0; X-ray; 2.10 A; A=90-110, B=25-54.
DR   PDB; 2WS1; X-ray; 1.60 A; A=90-110, B=25-54.
DR   PDB; 2WS4; X-ray; 1.90 A; A=90-110, B=25-50.
DR   PDB; 2WS6; X-ray; 1.50 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 2WS7; X-ray; 2.59 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-50.
DR   PDB; 3AIY; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 3BXQ; X-ray; 1.30 A; A/C=90-110, B/D=25-54.
DR   PDB; 3E7Y; X-ray; 1.60 A; A/C=90-110, B/D=25-53.
DR   PDB; 3E7Z; X-ray; 1.70 A; A/C=90-110, B/D=25-53.
DR   PDB; 3EXX; X-ray; 1.35 A; A/C=90-110, B/D=25-54.
DR   PDB; 3FQ9; X-ray; 1.35 A; A/C=91-110, B/D=25-54.
DR   PDB; 3HYD; X-ray; 1.00 A; A=35-41.
DR   PDB; 3I3Z; X-ray; 1.60 A; A=90-110, B=25-54.
DR   PDB; 3I40; X-ray; 1.85 A; A=90-110, B=25-54.
DR   PDB; 3ILG; X-ray; 1.90 A; A/C=90-110, B/D=25-54.
DR   PDB; 3INC; X-ray; 1.85 A; A/C=90-110, B/D=25-54.
DR   PDB; 3IR0; X-ray; 2.20 A; 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.
DR   PDB; 3JSD; X-ray; 2.50 A; A/C=90-110, B/D=25-54.
DR   PDB; 3KQ6; X-ray; 1.90 A; A/C=90-110, B/D=25-54.
DR   PDB; 3P2X; X-ray; 2.00 A; A/C=90-110, B/D=25-54.
DR   PDB; 3P33; X-ray; 2.30 A; A/C/E/G=90-110, B/D/F/H=25-54.
DR   PDB; 3Q6E; X-ray; 2.05 A; A/C=90-110, B/D=25-54.
DR   PDB; 3ROV; X-ray; 2.30 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 3TT8; X-ray; 1.12 A; A/C=90-110, B/D=25-54.
DR   PDB; 3U4N; X-ray; 1.98 A; A=90-110, B=25-53.
DR   PDB; 3UTQ; X-ray; 1.67 A; C=15-24.
DR   PDB; 3UTS; X-ray; 2.71 A; C/H=15-24.
DR   PDB; 3UTT; X-ray; 2.60 A; C/H=15-24.
DR   PDB; 3V19; X-ray; 2.00 A; A/C=90-110, B/D=25-54.
DR   PDB; 3V1G; X-ray; 2.20 A; A/C=90-110, B/D=25-54.
DR   PDB; 3W11; X-ray; 3.90 A; A=90-110, B=25-54.
DR   PDB; 3W12; X-ray; 4.30 A; A=90-110, B=25-50.
DR   PDB; 3W13; X-ray; 4.30 A; A=90-110, B=25-50.
DR   PDB; 3W7Y; X-ray; 0.92 A; A/C=90-110, B/D=25-54.
DR   PDB; 3W7Z; X-ray; 1.15 A; A/C=90-110, B/D=25-54.
DR   PDB; 3W80; X-ray; 1.40 A; A/C/E/G=90-110, B/D/F/H=25-54.
DR   PDB; 3ZI3; X-ray; 1.70 A; A=90-110, B=25-54.
DR   PDB; 3ZQR; X-ray; 1.90 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 3ZS2; X-ray; 1.97 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 3ZU1; X-ray; 1.60 A; A/C=90-110, B/D=25-54.
DR   PDB; 4AIY; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 4AJX; X-ray; 1.20 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-53.
DR   PDB; 4AJZ; X-ray; 1.80 A; A/C=90-110, B/D=25-53.
DR   PDB; 4AK0; X-ray; 2.28 A; A=90-110, B=25-53.
DR   PDB; 4AKJ; X-ray; 2.01 A; A/C=90-110, B/D=25-53.
DR   PDB; 4CXL; X-ray; 1.50 A; A=90-110, B=25-54.
DR   PDB; 4CXN; X-ray; 1.70 A; A=90-110, B=25-54.
DR   PDB; 4CY7; X-ray; 1.40 A; A/C=90-110, B/D=25-54.
DR   PDB; 4EFX; X-ray; 1.98 A; A/C=90-110, B/D=25-52.
DR   PDB; 4EWW; X-ray; 2.30 A; A/C=90-110, B/D=25-54.
DR   PDB; 4EWX; X-ray; 2.20 A; A/C=90-110, B/D=25-54.
DR   PDB; 4EWZ; X-ray; 1.79 A; A/C=90-110, B/D=25-54.
DR   PDB; 4EX0; X-ray; 1.86 A; A/C=90-110, B/D=25-54.
DR   PDB; 4EX1; X-ray; 1.66 A; A/C=90-110, B/D=25-54.
DR   PDB; 4EXX; X-ray; 1.55 A; A/C=90-110, B/D=25-54.
DR   PDB; 4EY1; X-ray; 1.47 A; A/C=90-110, B/D=25-54.
DR   PDB; 4EY9; X-ray; 1.47 A; A/C=90-110, B/D=25-54.
DR   PDB; 4EYD; X-ray; 1.47 A; A/C=90-110, B/D=25-54.
DR   PDB; 4EYN; X-ray; 1.53 A; A/C=90-110, B/D=25-54.
DR   PDB; 4EYP; X-ray; 1.59 A; A/C=90-110, B/D=25-54.
DR   PDB; 4F0N; X-ray; 1.68 A; A/C=90-110, B/D=25-54.
DR   PDB; 4F0O; X-ray; 1.67 A; A/C=90-110, B/D=25-54.
DR   PDB; 4F1A; X-ray; 1.80 A; A/C=90-110, B/D=25-54.
DR   PDB; 4F1B; X-ray; 1.59 A; A/C=90-110, B/D=25-54.
DR   PDB; 4F1C; X-ray; 1.70 A; A/C=90-110, B/D=25-54.
DR   PDB; 4F1D; X-ray; 1.64 A; A/C=90-110, B/D=25-54.
DR   PDB; 4F1F; X-ray; 1.68 A; A/C=90-110, B/D=25-54.
DR   PDB; 4F1G; X-ray; 1.64 A; A/C=90-110, B/D=25-54.
DR   PDB; 4F4T; X-ray; 1.64 A; A/C=90-110, B/D=25-54.
DR   PDB; 4F4V; X-ray; 1.64 A; A/C=90-110, B/D=25-54.
DR   PDB; 4F51; X-ray; 1.64 A; A/C=90-110, B/D=25-54.
DR   PDB; 4F8F; X-ray; 1.68 A; A/C=90-110, B/D=25-54.
DR   PDB; 4FG3; X-ray; 2.00 A; A/C=90-110, B/D=25-54.
DR   PDB; 4FKA; X-ray; 1.08 A; A/C=90-110, B/D=25-54.
DR   PDB; 4GBC; X-ray; 1.78 A; A/C=90-110, B/D=25-54.
DR   PDB; 4GBI; X-ray; 2.50 A; A/C=90-110, B/D=25-54.
DR   PDB; 4GBK; X-ray; 2.40 A; A/C=90-110, B/D=25-54.
DR   PDB; 4GBL; X-ray; 2.50 A; A/C=90-110, B/D=25-54.
DR   PDB; 4GBN; X-ray; 1.87 A; A/C=90-110, B/D=25-54.
DR   PDB; 4IUZ; X-ray; 1.60 A; A=90-110, B=25-54.
DR   PDB; 4IYD; X-ray; 1.66 A; A=90-109, B=25-53.
DR   PDB; 4IYF; X-ray; 1.80 A; A=90-109, B=25-53.
DR   PDB; 4NIB; X-ray; 1.40 A; A=90-110, B=25-54.
DR   PDB; 4OGA; X-ray; 3.50 A; A=90-110, B=25-54.
DR   PDB; 4P65; X-ray; 1.50 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 4RXW; X-ray; 1.73 A; A/C=90-110, B/D=25-54.
DR   PDB; 4UNE; X-ray; 1.59 A; A/C=90-110, B/D=25-54.
DR   PDB; 4UNG; X-ray; 1.81 A; A/C=90-110, B/D=25-54.
DR   PDB; 4UNH; X-ray; 2.75 A; A=90-110, B=25-54.
DR   PDB; 4WDI; X-ray; 2.31 A; C/F=39-47.
DR   PDB; 4XC4; X-ray; 1.50 A; A/C=90-110, B/D=25-54.
DR   PDB; 4Y19; X-ray; 2.50 A; C=75-90.
DR   PDB; 4Y1A; X-ray; 4.00 A; C=75-90.
DR   PDB; 4Z76; X-ray; 1.88 A; C/F=39-46.
DR   PDB; 4Z77; X-ray; 1.85 A; C/F=39-47.
DR   PDB; 4Z78; X-ray; 2.30 A; C/F/I=39-48.
DR   PDB; 5AIY; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 5BOQ; X-ray; 1.70 A; A/C/E/G=90-110, B/D/F/H=25-54.
DR   PDB; 5BPO; X-ray; 1.90 A; A/C=90-110, B/D=25-54.
DR   PDB; 5BQQ; X-ray; 1.54 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-50.
DR   PDB; 5BTS; X-ray; 1.77 A; A=90-110, B=25-54.
DR   PDB; 5C0D; X-ray; 1.68 A; C=15-24.
DR   PDB; 5CJO; X-ray; 3.29 A; a=90-109.
DR   PDB; 5CNY; X-ray; 1.70 A; A/C=90-110, B/D=25-54.
DR   PDB; 5CO2; X-ray; 1.70 A; A/C=90-110, B/D=25-54.
DR   PDB; 5CO6; X-ray; 1.80 A; A/C=90-110, B/D=25-54.
DR   PDB; 5CO9; X-ray; 1.92 A; A/C=90-110, B/D=25-54.
DR   PDB; 5E7W; X-ray; 0.95 A; A/C=90-110, B/D=25-54.
DR   PDB; 5EMS; X-ray; 2.30 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-52.
DR   PDB; 5EN9; X-ray; 1.50 A; A=90-110, B=25-54.
DR   PDB; 5ENA; X-ray; 1.35 A; A=90-110, B=25-54.
DR   PDB; 5HPR; X-ray; 1.33 A; A=90-110, B=25-54.
DR   PDB; 5HPU; X-ray; 2.20 A; A/C=90-110, B/D=25-54.
DR   PDB; 5HQI; X-ray; 0.97 A; A=90-110, B=25-54.
DR   PDB; 5HRQ; X-ray; 1.28 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 5HYJ; X-ray; 3.06 A; C/H=15-24.
DR   PDB; 5MAM; X-ray; 2.20 A; 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.
DR   PDB; 5MHD; NMR; -; A=90-110, B=25-55.
DR   PDB; 5MT3; X-ray; 2.02 A; 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.
DR   PDB; 5MT9; X-ray; 1.88 A; 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.
DR   PDB; 5MWQ; NMR; -; A=90-110, B=25-56.
DR   PDB; 5T7R; X-ray; 1.55 A; A/C=90-110, B/D=25-54.
DR   PDB; 5UDP; X-ray; 1.35 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 5UOZ; X-ray; 1.17 A; A=90-110, B=25-54.
DR   PDB; 5UQA; X-ray; 1.31 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 5URT; X-ray; 1.18 A; A=90-110, B=25-54.
DR   PDB; 5URU; X-ray; 2.41 A; A/C/E/G=90-110, B/D/F/H=25-54.
DR   PDB; 5USP; X-ray; 1.17 A; A=90-110, B=25-54.
DR   PDB; 5USS; X-ray; 2.06 A; A/C=90-110, B/D=25-54.
DR   PDB; 5USV; X-ray; 1.30 A; A=90-110, B=25-54.
DR   PDB; 5UU2; X-ray; 1.22 A; A=90-110, B=25-54.
DR   PDB; 5UU3; X-ray; 2.25 A; 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.
DR   PDB; 5UU4; X-ray; 1.97 A; A/C=90-110, B/D=25-54.
DR   PDB; 5VIZ; X-ray; 1.70 A; A=90-109, B=25-53.
DR   PDB; 5WBT; NMR; -; A=25-54, A=90-110.
DR   PDB; 5WDM; X-ray; 2.80 A; A/B/C/D/E/F=25-110.
DR   PDB; 5WOB; X-ray; 3.95 A; a/b/c/d/e/f/g/h=90-109.
DR   PDB; 6B3Q; EM; 3.70 A; a/b=1-110.
DR   PDB; 6B70; EM; 3.70 A; a/c=1-110.
DR   PDB; 6BFC; EM; 3.70 A; a/b=1-110.
DR   PDB; 6CE7; EM; 7.40 A; N=90-110.
DR   PDB; 6CE9; EM; 4.30 A; K/N=90-110.
DR   PDB; 6CEB; EM; 4.70 A; K/N=90-110.
DR   PDB; 6CK2; X-ray; 2.25 A; A/C=90-110, B/D=25-54.
DR   PDB; 6GNQ; X-ray; 2.20 A; 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.
DR   PDB; 6GV0; X-ray; 1.26 A; B/D=25-54, G/I=90-110.
DR   PDB; 6H3M; X-ray; 1.82 A; A/C/E/G/I/K/N/R=90-110, B/D/F/H/J/L/P/Q=25-54.
DR   PDB; 6HN5; EM; 3.20 A; A=90-110, B=25-54.
DR   PDB; 6JK8; EM; 4.70 A; C/D=1-110.
DR   PDB; 6JR3; EM; 14.50 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 6K59; NMR; -; A=90-109, B=25-56.
DR   PDB; 6NWV; X-ray; 1.60 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 6O17; X-ray; 1.58 A; A=90-110, B=25-53.
DR   PDB; 6P4Z; X-ray; 1.80 A; A/C=90-110, B/D=25-54.
DR   PDB; 6S34; X-ray; 1.35 A; A=90-110, B=25-54.
DR   PDB; 6S4I; X-ray; 1.51 A; A=90-110, B=25-53.
DR   PDB; 6S4J; X-ray; 1.50 A; A=90-110, B=25-53.
DR   PDB; 6SOF; EM; 4.30 A; E/G/I/K=90-110, F/H/J/L=25-54.
DR   PDB; 6TC2; X-ray; 1.36 A; A/B/C/D/E/F/G/H/I/J/K/L=1-110.
DR   PDB; 6TYH; X-ray; 1.60 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 6U46; NMR; -; A=25-109.
DR   PDB; 6VEP; X-ray; 2.90 A; A/G/M/S=90-110, B/H/N/T=25-54.
DR   PDB; 6VER; X-ray; 1.05 A; A=90-110, B=25-46.
DR   PDB; 6VES; X-ray; 1.85 A; A=90-110, B=25-46.
DR   PDB; 6VET; X-ray; 1.46 A; A/C/E=90-110, B/D/F=25-46.
DR   PDB; 6X4X; NMR; -; A=90-110, B=25-54.
DR   PDB; 6Z7W; X-ray; 2.42 A; I/K/M/O=90-110, J/L/N/P=25-54.
DR   PDB; 6Z7Y; X-ray; 2.20 A; E/G=90-110, F/H=25-54.
DR   PDB; 7BW7; EM; 4.10 A; D=25-110.
DR   PDB; 7BW8; EM; 3.80 A; D=25-110.
DR   PDB; 7BWA; EM; 4.90 A; D/E=25-110.
DR   PDB; 7JP3; X-ray; 1.95 A; A/B/C/D/E/F=25-110.
DR   PDB; 7MD4; EM; 4.50 A; O/Q/S/U=90-110, P/R/T/V=25-54.
DR   PDB; 7MD5; EM; 5.20 A; O/Q/S/U=90-110, P/R/T/V=25-54.
DR   PDB; 7MQO; EM; 3.40 A; A/C=90-110, B/D=25-46.
DR   PDB; 7MQR; EM; 4.10 A; A/C/G/I=90-110, B/D/H/J=25-46.
DR   PDB; 7MQS; EM; 4.40 A; A/C/G=90-110, B/D/H=25-46.
DR   PDB; 7NHU; X-ray; 1.40 A; A=90-110, B=25-53.
DR   PDB; 7PG0; EM; 7.60 A; C/E/I=90-110, D/F/J=25-54.
DR   PDB; 7PG2; EM; 6.70 A; C/E/I=90-110, D/F/J=25-54.
DR   PDB; 7PG3; EM; 7.30 A; C/E/I=90-110, D/F/J=25-54.
DR   PDB; 7PG4; EM; 9.10 A; C/I=90-110, D/J=25-54.
DR   PDB; 7QID; EM; 5.00 A; E/I/K=90-110, F/J/L=25-54.
DR   PDB; 7S4Y; X-ray; 1.71 A; A/C=90-110, B/D=25-54.
DR   PDB; 7SL1; EM; 3.40 A; C/D=25-54, E/F=90-110.
DR   PDB; 7SL2; EM; 3.60 A; C/D/E/F=25-54, G/H/I/J=90-110.
DR   PDB; 7SL3; EM; 3.40 A; C/D=25-54, E/F=90-110.
DR   PDB; 7SL4; EM; 5.00 A; C/D=25-54, E/F=90-110.
DR   PDB; 7SL6; EM; 3.70 A; C/D=90-110, E/F=25-54.
DR   PDB; 7SL7; EM; 3.10 A; C/D/E/F=90-110, G/H/I/J=25-54.
DR   PDB; 7STH; EM; 3.50 A; C/D=1-110.
DR   PDB; 7STI; EM; 4.90 A; C=1-110.
DR   PDB; 7STJ; EM; 4.40 A; C/D=1-110.
DR   PDB; 7STK; EM; 4.00 A; C/D=1-110.
DR   PDBsum; 1A7F; -.
DR   PDBsum; 1AI0; -.
DR   PDBsum; 1AIY; -.
DR   PDBsum; 1B9E; -.
DR   PDBsum; 1BEN; -.
DR   PDBsum; 1EFE; -.
DR   PDBsum; 1EV3; -.
DR   PDBsum; 1EV6; -.
DR   PDBsum; 1EVR; -.
DR   PDBsum; 1FU2; -.
DR   PDBsum; 1FUB; -.
DR   PDBsum; 1G7A; -.
DR   PDBsum; 1G7B; -.
DR   PDBsum; 1GUJ; -.
DR   PDBsum; 1HIQ; -.
DR   PDBsum; 1HIS; -.
DR   PDBsum; 1HIT; -.
DR   PDBsum; 1HLS; -.
DR   PDBsum; 1HTV; -.
DR   PDBsum; 1HUI; -.
DR   PDBsum; 1IOG; -.
DR   PDBsum; 1IOH; -.
DR   PDBsum; 1J73; -.
DR   PDBsum; 1JCA; -.
DR   PDBsum; 1JCO; -.
DR   PDBsum; 1JK8; -.
DR   PDBsum; 1K3M; -.
DR   PDBsum; 1KMF; -.
DR   PDBsum; 1LKQ; -.
DR   PDBsum; 1LPH; -.
DR   PDBsum; 1MHI; -.
DR   PDBsum; 1MHJ; -.
DR   PDBsum; 1MSO; -.
DR   PDBsum; 1OS3; -.
DR   PDBsum; 1OS4; -.
DR   PDBsum; 1Q4V; -.
DR   PDBsum; 1QIY; -.
DR   PDBsum; 1QIZ; -.
DR   PDBsum; 1QJ0; -.
DR   PDBsum; 1RWE; -.
DR   PDBsum; 1SF1; -.
DR   PDBsum; 1SJT; -.
DR   PDBsum; 1SJU; -.
DR   PDBsum; 1T0C; -.
DR   PDBsum; 1T1K; -.
DR   PDBsum; 1T1P; -.
DR   PDBsum; 1T1Q; -.
DR   PDBsum; 1TRZ; -.
DR   PDBsum; 1TYL; -.
DR   PDBsum; 1TYM; -.
DR   PDBsum; 1UZ9; -.
DR   PDBsum; 1VKT; -.
DR   PDBsum; 1W8P; -.
DR   PDBsum; 1XDA; -.
DR   PDBsum; 1XGL; -.
DR   PDBsum; 1XW7; -.
DR   PDBsum; 1ZEG; -.
DR   PDBsum; 1ZEH; -.
DR   PDBsum; 1ZNJ; -.
DR   PDBsum; 2AIY; -.
DR   PDBsum; 2C8Q; -.
DR   PDBsum; 2C8R; -.
DR   PDBsum; 2CEU; -.
DR   PDBsum; 2G54; -.
DR   PDBsum; 2G56; -.
DR   PDBsum; 2H67; -.
DR   PDBsum; 2HH4; -.
DR   PDBsum; 2HHO; -.
DR   PDBsum; 2HIU; -.
DR   PDBsum; 2JMN; -.
DR   PDBsum; 2JUM; -.
DR   PDBsum; 2JUU; -.
DR   PDBsum; 2JUV; -.
DR   PDBsum; 2JV1; -.
DR   PDBsum; 2JZQ; -.
DR   PDBsum; 2K91; -.
DR   PDBsum; 2K9R; -.
DR   PDBsum; 2KJJ; -.
DR   PDBsum; 2KJU; -.
DR   PDBsum; 2KQP; -.
DR   PDBsum; 2KQQ; -.
DR   PDBsum; 2KXK; -.
DR   PDBsum; 2L1Y; -.
DR   PDBsum; 2L1Z; -.
DR   PDBsum; 2LGB; -.
DR   PDBsum; 2LWZ; -.
DR   PDBsum; 2M1D; -.
DR   PDBsum; 2M1E; -.
DR   PDBsum; 2M2M; -.
DR   PDBsum; 2M2N; -.
DR   PDBsum; 2M2O; -.
DR   PDBsum; 2M2P; -.
DR   PDBsum; 2MLI; -.
DR   PDBsum; 2MPG; -.
DR   PDBsum; 2MPI; -.
DR   PDBsum; 2MVC; -.
DR   PDBsum; 2MVD; -.
DR   PDBsum; 2N2V; -.
DR   PDBsum; 2N2W; -.
DR   PDBsum; 2N2X; -.
DR   PDBsum; 2OLY; -.
DR   PDBsum; 2OLZ; -.
DR   PDBsum; 2OM0; -.
DR   PDBsum; 2OM1; -.
DR   PDBsum; 2OMG; -.
DR   PDBsum; 2OMH; -.
DR   PDBsum; 2OMI; -.
DR   PDBsum; 2OMQ; -.
DR   PDBsum; 2QIU; -.
DR   PDBsum; 2R34; -.
DR   PDBsum; 2R35; -.
DR   PDBsum; 2R36; -.
DR   PDBsum; 2RN5; -.
DR   PDBsum; 2VJZ; -.
DR   PDBsum; 2VK0; -.
DR   PDBsum; 2W44; -.
DR   PDBsum; 2WBY; -.
DR   PDBsum; 2WC0; -.
DR   PDBsum; 2WRU; -.
DR   PDBsum; 2WRV; -.
DR   PDBsum; 2WRW; -.
DR   PDBsum; 2WRX; -.
DR   PDBsum; 2WS0; -.
DR   PDBsum; 2WS1; -.
DR   PDBsum; 2WS4; -.
DR   PDBsum; 2WS6; -.
DR   PDBsum; 2WS7; -.
DR   PDBsum; 3AIY; -.
DR   PDBsum; 3BXQ; -.
DR   PDBsum; 3E7Y; -.
DR   PDBsum; 3E7Z; -.
DR   PDBsum; 3EXX; -.
DR   PDBsum; 3FQ9; -.
DR   PDBsum; 3HYD; -.
DR   PDBsum; 3I3Z; -.
DR   PDBsum; 3I40; -.
DR   PDBsum; 3ILG; -.
DR   PDBsum; 3INC; -.
DR   PDBsum; 3IR0; -.
DR   PDBsum; 3JSD; -.
DR   PDBsum; 3KQ6; -.
DR   PDBsum; 3P2X; -.
DR   PDBsum; 3P33; -.
DR   PDBsum; 3Q6E; -.
DR   PDBsum; 3ROV; -.
DR   PDBsum; 3TT8; -.
DR   PDBsum; 3U4N; -.
DR   PDBsum; 3UTQ; -.
DR   PDBsum; 3UTS; -.
DR   PDBsum; 3UTT; -.
DR   PDBsum; 3V19; -.
DR   PDBsum; 3V1G; -.
DR   PDBsum; 3W11; -.
DR   PDBsum; 3W12; -.
DR   PDBsum; 3W13; -.
DR   PDBsum; 3W7Y; -.
DR   PDBsum; 3W7Z; -.
DR   PDBsum; 3W80; -.
DR   PDBsum; 3ZI3; -.
DR   PDBsum; 3ZQR; -.
DR   PDBsum; 3ZS2; -.
DR   PDBsum; 3ZU1; -.
DR   PDBsum; 4AIY; -.
DR   PDBsum; 4AJX; -.
DR   PDBsum; 4AJZ; -.
DR   PDBsum; 4AK0; -.
DR   PDBsum; 4AKJ; -.
DR   PDBsum; 4CXL; -.
DR   PDBsum; 4CXN; -.
DR   PDBsum; 4CY7; -.
DR   PDBsum; 4EFX; -.
DR   PDBsum; 4EWW; -.
DR   PDBsum; 4EWX; -.
DR   PDBsum; 4EWZ; -.
DR   PDBsum; 4EX0; -.
DR   PDBsum; 4EX1; -.
DR   PDBsum; 4EXX; -.
DR   PDBsum; 4EY1; -.
DR   PDBsum; 4EY9; -.
DR   PDBsum; 4EYD; -.
DR   PDBsum; 4EYN; -.
DR   PDBsum; 4EYP; -.
DR   PDBsum; 4F0N; -.
DR   PDBsum; 4F0O; -.
DR   PDBsum; 4F1A; -.
DR   PDBsum; 4F1B; -.
DR   PDBsum; 4F1C; -.
DR   PDBsum; 4F1D; -.
DR   PDBsum; 4F1F; -.
DR   PDBsum; 4F1G; -.
DR   PDBsum; 4F4T; -.
DR   PDBsum; 4F4V; -.
DR   PDBsum; 4F51; -.
DR   PDBsum; 4F8F; -.
DR   PDBsum; 4FG3; -.
DR   PDBsum; 4FKA; -.
DR   PDBsum; 4GBC; -.
DR   PDBsum; 4GBI; -.
DR   PDBsum; 4GBK; -.
DR   PDBsum; 4GBL; -.
DR   PDBsum; 4GBN; -.
DR   PDBsum; 4IUZ; -.
DR   PDBsum; 4IYD; -.
DR   PDBsum; 4IYF; -.
DR   PDBsum; 4NIB; -.
DR   PDBsum; 4OGA; -.
DR   PDBsum; 4P65; -.
DR   PDBsum; 4RXW; -.
DR   PDBsum; 4UNE; -.
DR   PDBsum; 4UNG; -.
DR   PDBsum; 4UNH; -.
DR   PDBsum; 4WDI; -.
DR   PDBsum; 4XC4; -.
DR   PDBsum; 4Y19; -.
DR   PDBsum; 4Y1A; -.
DR   PDBsum; 4Z76; -.
DR   PDBsum; 4Z77; -.
DR   PDBsum; 4Z78; -.
DR   PDBsum; 5AIY; -.
DR   PDBsum; 5BOQ; -.
DR   PDBsum; 5BPO; -.
DR   PDBsum; 5BQQ; -.
DR   PDBsum; 5BTS; -.
DR   PDBsum; 5C0D; -.
DR   PDBsum; 5CJO; -.
DR   PDBsum; 5CNY; -.
DR   PDBsum; 5CO2; -.
DR   PDBsum; 5CO6; -.
DR   PDBsum; 5CO9; -.
DR   PDBsum; 5E7W; -.
DR   PDBsum; 5EMS; -.
DR   PDBsum; 5EN9; -.
DR   PDBsum; 5ENA; -.
DR   PDBsum; 5HPR; -.
DR   PDBsum; 5HPU; -.
DR   PDBsum; 5HQI; -.
DR   PDBsum; 5HRQ; -.
DR   PDBsum; 5HYJ; -.
DR   PDBsum; 5MAM; -.
DR   PDBsum; 5MHD; -.
DR   PDBsum; 5MT3; -.
DR   PDBsum; 5MT9; -.
DR   PDBsum; 5MWQ; -.
DR   PDBsum; 5T7R; -.
DR   PDBsum; 5UDP; -.
DR   PDBsum; 5UOZ; -.
DR   PDBsum; 5UQA; -.
DR   PDBsum; 5URT; -.
DR   PDBsum; 5URU; -.
DR   PDBsum; 5USP; -.
DR   PDBsum; 5USS; -.
DR   PDBsum; 5USV; -.
DR   PDBsum; 5UU2; -.
DR   PDBsum; 5UU3; -.
DR   PDBsum; 5UU4; -.
DR   PDBsum; 5VIZ; -.
DR   PDBsum; 5WBT; -.
DR   PDBsum; 5WDM; -.
DR   PDBsum; 5WOB; -.
DR   PDBsum; 6B3Q; -.
DR   PDBsum; 6B70; -.
DR   PDBsum; 6BFC; -.
DR   PDBsum; 6CE7; -.
DR   PDBsum; 6CE9; -.
DR   PDBsum; 6CEB; -.
DR   PDBsum; 6CK2; -.
DR   PDBsum; 6GNQ; -.
DR   PDBsum; 6GV0; -.
DR   PDBsum; 6H3M; -.
DR   PDBsum; 6HN5; -.
DR   PDBsum; 6JK8; -.
DR   PDBsum; 6JR3; -.
DR   PDBsum; 6K59; -.
DR   PDBsum; 6NWV; -.
DR   PDBsum; 6O17; -.
DR   PDBsum; 6P4Z; -.
DR   PDBsum; 6S34; -.
DR   PDBsum; 6S4I; -.
DR   PDBsum; 6S4J; -.
DR   PDBsum; 6SOF; -.
DR   PDBsum; 6TC2; -.
DR   PDBsum; 6TYH; -.
DR   PDBsum; 6U46; -.
DR   PDBsum; 6VEP; -.
DR   PDBsum; 6VER; -.
DR   PDBsum; 6VES; -.
DR   PDBsum; 6VET; -.
DR   PDBsum; 6X4X; -.
DR   PDBsum; 6Z7W; -.
DR   PDBsum; 6Z7Y; -.
DR   PDBsum; 7BW7; -.
DR   PDBsum; 7BW8; -.
DR   PDBsum; 7BWA; -.
DR   PDBsum; 7JP3; -.
DR   PDBsum; 7MD4; -.
DR   PDBsum; 7MD5; -.
DR   PDBsum; 7MQO; -.
DR   PDBsum; 7MQR; -.
DR   PDBsum; 7MQS; -.
DR   PDBsum; 7NHU; -.
DR   PDBsum; 7PG0; -.
DR   PDBsum; 7PG2; -.
DR   PDBsum; 7PG3; -.
DR   PDBsum; 7PG4; -.
DR   PDBsum; 7QID; -.
DR   PDBsum; 7S4Y; -.
DR   PDBsum; 7SL1; -.
DR   PDBsum; 7SL2; -.
DR   PDBsum; 7SL3; -.
DR   PDBsum; 7SL4; -.
DR   PDBsum; 7SL6; -.
DR   PDBsum; 7SL7; -.
DR   PDBsum; 7STH; -.
DR   PDBsum; 7STI; -.
DR   PDBsum; 7STJ; -.
DR   PDBsum; 7STK; -.
DR   AlphaFoldDB; P01308; -.
DR   BMRB; P01308; -.
DR   PCDDB; P01308; -.
DR   SASBDB; P01308; -.
DR   SMR; P01308; -.
DR   BioGRID; 109842; 524.
DR   DIP; DIP-6024N; -.
DR   IntAct; P01308; 20.
DR   MINT; P01308; -.
DR   STRING; 9606.ENSP00000380432; -.
DR   ChEMBL; CHEMBL5881; -.
DR   DrugBank; DB01776; M-Cresol.
DR   DrugBank; DB08231; Myristic acid.
DR   DrugBank; DB01593; Zinc.
DR   DrugBank; DB14487; Zinc acetate.
DR   DrugBank; DB14533; Zinc chloride.
DR   DrugBank; DB14548; Zinc sulfate, unspecified form.
DR   Allergome; 2121; Hom s Insulin.
DR   CarbonylDB; P01308; -.
DR   iPTMnet; P01308; -.
DR   PhosphoSitePlus; P01308; -.
DR   BioMuta; INS; -.
DR   DMDM; 124617; -.
DR   EPD; P01308; -.
DR   jPOST; P01308; -.
DR   MassIVE; P01308; -.
DR   PaxDb; P01308; -.
DR   PeptideAtlas; P01308; -.
DR   PRIDE; P01308; -.
DR   ProteomicsDB; 51374; -. [P01308-1]
DR   ABCD; P01308; 35 sequenced antibodies.
DR   Antibodypedia; 56056; 3470 antibodies from 50 providers.
DR   DNASU; 3630; -.
DR   Ensembl; ENST00000250971.7; ENSP00000250971.3; ENSG00000254647.7. [P01308-1]
DR   Ensembl; ENST00000381330.5; ENSP00000370731.5; ENSG00000254647.7. [P01308-1]
DR   Ensembl; ENST00000397262.5; ENSP00000380432.1; ENSG00000254647.7. [P01308-1]
DR   GeneID; 3630; -.
DR   KEGG; hsa:3630; -.
DR   MANE-Select; ENST00000381330.5; ENSP00000370731.5; NM_000207.3; NP_000198.1.
DR   UCSC; uc001lvn.3; human. [P01308-1]
DR   CTD; 3630; -.
DR   DisGeNET; 3630; -.
DR   GeneCards; INS; -.
DR   GeneReviews; INS; -.
DR   HGNC; HGNC:6081; INS.
DR   HPA; ENSG00000254647; Tissue enriched (pancreas).
DR   MalaCards; INS; -.
DR   MIM; 125852; phenotype.
DR   MIM; 176730; gene.
DR   MIM; 613370; phenotype.
DR   MIM; 616214; phenotype.
DR   MIM; 618858; phenotype.
DR   neXtProt; NX_P01308; -.
DR   OpenTargets; ENSG00000254647; -.
DR   Orphanet; 99885; Isolated permanent neonatal diabetes mellitus.
DR   Orphanet; 552; MODY.
DR   PharmGKB; PA201; -.
DR   VEuPathDB; HostDB:ENSG00000254647; -.
DR   eggNOG; ENOG502S5P5; Eukaryota.
DR   GeneTree; ENSGT00390000015440; -.
DR   InParanoid; P01308; -.
DR   OMA; LANQHLC; -.
DR   PhylomeDB; P01308; -.
DR   TreeFam; TF332820; -.
DR   BioCyc; MetaCyc:MON-16190; -.
DR   PathwayCommons; P01308; -.
DR   Reactome; R-HSA-210745; Regulation of gene expression in beta cells.
DR   Reactome; R-HSA-264876; Insulin processing.
DR   Reactome; R-HSA-422085; Synthesis, secretion, and deacylation of Ghrelin.
DR   Reactome; R-HSA-422356; Regulation of insulin secretion.
DR   Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-HSA-74713; IRS activation.
DR   Reactome; R-HSA-74749; Signal attenuation.
DR   Reactome; R-HSA-74751; Insulin receptor signalling cascade.
DR   Reactome; R-HSA-74752; Signaling by Insulin receptor.
DR   Reactome; R-HSA-77387; Insulin receptor recycling.
DR   Reactome; R-HSA-9615017; FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes.
DR   Reactome; R-HSA-977225; Amyloid fiber formation.
DR   SignaLink; P01308; -.
DR   SIGNOR; P01308; -.
DR   BioGRID-ORCS; 3630; 378 hits in 1045 CRISPR screens.
DR   EvolutionaryTrace; P01308; -.
DR   GeneWiki; Insulin; -.
DR   GenomeRNAi; 3630; -.
DR   Pharos; P01308; Tbio.
DR   PRO; PR:P01308; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; P01308; protein.
DR   Bgee; ENSG00000254647; Expressed in type B pancreatic cell and 92 other tissues.
DR   ExpressionAtlas; P01308; baseline and differential.
DR   Genevisible; P01308; HS.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
DR   GO; GO:0031904; C:endosome lumen; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR   GO; GO:0030133; C:transport vesicle; TAS:Reactome.
DR   GO; GO:0005179; F:hormone activity; IMP:BHF-UCL.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0005158; F:insulin receptor binding; IDA:UniProtKB.
DR   GO; GO:0005159; F:insulin-like growth factor receptor binding; IPI:BHF-UCL.
DR   GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR   GO; GO:0032148; P:activation of protein kinase B activity; IDA:BHF-UCL.
DR   GO; GO:0006953; P:acute-phase response; IDA:BHF-UCL.
DR   GO; GO:0046631; P:alpha-beta T cell activation; IDA:UniProtKB.
DR   GO; GO:0007267; P:cell-cell signaling; IC:UniProtKB.
DR   GO; GO:0050890; P:cognition; TAS:ARUK-UCL.
DR   GO; GO:0055089; P:fatty acid homeostasis; IMP:BHF-UCL.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:BHF-UCL.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0002674; P:negative regulation of acute inflammatory response; IDA:BHF-UCL.
DR   GO; GO:0045922; P:negative regulation of fatty acid metabolic process; IMP:BHF-UCL.
DR   GO; GO:2000252; P:negative regulation of feeding behavior; IDA:DFLAT.
DR   GO; GO:0010629; P:negative regulation of gene expression; IDA:ARUK-UCL.
DR   GO; GO:0045721; P:negative regulation of gluconeogenesis; NAS:BHF-UCL.
DR   GO; GO:0045818; P:negative regulation of glycogen catabolic process; IMP:BHF-UCL.
DR   GO; GO:0050995; P:negative regulation of lipid catabolic process; IMP:AgBase.
DR   GO; GO:0033861; P:negative regulation of NAD(P)H oxidase activity; IDA:BHF-UCL.
DR   GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; NAS:BHF-UCL.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:UniProtKB.
DR   GO; GO:0050709; P:negative regulation of protein secretion; IDA:BHF-UCL.
DR   GO; GO:0045861; P:negative regulation of proteolysis; IMP:BHF-UCL.
DR   GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IGI:ARUK-UCL.
DR   GO; GO:0060266; P:negative regulation of respiratory burst involved in inflammatory response; IDA:BHF-UCL.
DR   GO; GO:1990535; P:neuron projection maintenance; IGI:ARUK-UCL.
DR   GO; GO:0038060; P:nitric oxide-cGMP-mediated signaling pathway; IDA:UniProtKB.
DR   GO; GO:0090336; P:positive regulation of brown fat cell differentiation; TAS:BHF-UCL.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; NAS:BHF-UCL.
DR   GO; GO:0030307; P:positive regulation of cell growth; NAS:BHF-UCL.
DR   GO; GO:0030335; P:positive regulation of cell migration; ISS:BHF-UCL.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL.
DR   GO; GO:0001819; P:positive regulation of cytokine production; IDA:UniProtKB.
DR   GO; GO:1902952; P:positive regulation of dendritic spine maintenance; IGI:ARUK-UCL.
DR   GO; GO:0010628; P:positive regulation of gene expression; IGI:BHF-UCL.
DR   GO; GO:0046326; P:positive regulation of glucose import; IDA:UniProtKB.
DR   GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0045821; P:positive regulation of glycolytic process; IDA:BHF-UCL.
DR   GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0046889; P:positive regulation of lipid biosynthetic process; NAS:BHF-UCL.
DR   GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; TAS:ARUK-UCL.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:BHF-UCL.
DR   GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:UniProtKB.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0010750; P:positive regulation of nitric oxide mediated signal transduction; IDA:UniProtKB.
DR   GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; NAS:UniProtKB.
DR   GO; GO:0090277; P:positive regulation of peptide hormone secretion; TAS:BHF-UCL.
DR   GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:BHF-UCL.
DR   GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISS:BHF-UCL.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:BHF-UCL.
DR   GO; GO:1900182; P:positive regulation of protein localization to nucleus; IDA:BHF-UCL.
DR   GO; GO:0051247; P:positive regulation of protein metabolic process; IMP:BHF-UCL.
DR   GO; GO:0050714; P:positive regulation of protein secretion; IBA:GO_Central.
DR   GO; GO:0060267; P:positive regulation of respiratory burst; IDA:BHF-UCL.
DR   GO; GO:0006521; P:regulation of cellular amino acid metabolic process; IMP:BHF-UCL.
DR   GO; GO:0032880; P:regulation of protein localization; IDA:BHF-UCL.
DR   GO; GO:1903076; P:regulation of protein localization to plasma membrane; IGI:ARUK-UCL.
DR   GO; GO:0050708; P:regulation of protein secretion; IDA:UniProtKB.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; TAS:ARUK-UCL.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:BHF-UCL.
DR   GO; GO:0022898; P:regulation of transmembrane transporter activity; IDA:BHF-UCL.
DR   GO; GO:0042311; P:vasodilation; IDA:UniProtKB.
DR   GO; GO:0042060; P:wound healing; IDA:BHF-UCL.
DR   CDD; cd04367; IlGF_insulin_like; 1.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR036438; Insulin-like_sf.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
DR   PANTHER; PTHR11454; PTHR11454; 1.
DR   Pfam; PF00049; Insulin; 1.
DR   PRINTS; PR00277; INSULIN.
DR   PRINTS; PR00276; INSULINFAMLY.
DR   SMART; SM00078; IlGF; 1.
DR   SUPFAM; SSF56994; SSF56994; 1.
DR   PROSITE; PS00262; INSULIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Carbohydrate metabolism;
KW   Cleavage on pair of basic residues; Diabetes mellitus;
KW   Direct protein sequencing; Disease variant; Disulfide bond;
KW   Glucose metabolism; Hormone; Pharmaceutical; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:14426955"
FT   PEPTIDE         25..54
FT                   /note="Insulin B chain"
FT                   /id="PRO_0000015819"
FT   PROPEP          57..87
FT                   /note="C peptide"
FT                   /id="PRO_0000015820"
FT   PEPTIDE         90..110
FT                   /note="Insulin A chain"
FT                   /id="PRO_0000015821"
FT   DISULFID        31..96
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000269|PubMed:1433291,
FT                   ECO:0000269|PubMed:25423173, ECO:0000269|PubMed:8421693,
FT                   ECO:0007744|PDB:1AI0, ECO:0007744|PDB:1AIY,
FT                   ECO:0007744|PDB:1HIQ, ECO:0007744|PDB:1MHI,
FT                   ECO:0007744|PDB:2MVC, ECO:0007744|PDB:2MVD"
FT   DISULFID        43..109
FT                   /note="Interchain (between B and A chains)"
FT                   /evidence="ECO:0000269|PubMed:1433291,
FT                   ECO:0000269|PubMed:25423173, ECO:0000269|PubMed:8421693,
FT                   ECO:0007744|PDB:1AI0, ECO:0007744|PDB:1AIY,
FT                   ECO:0007744|PDB:1HIQ, ECO:0007744|PDB:1MHI,
FT                   ECO:0007744|PDB:2MVC, ECO:0007744|PDB:2MVD"
FT   DISULFID        95..100
FT                   /evidence="ECO:0000269|PubMed:1433291,
FT                   ECO:0000269|PubMed:25423173, ECO:0000269|PubMed:5101771,
FT                   ECO:0000269|PubMed:8421693, ECO:0000269|PubMed:9235985,
FT                   ECO:0007744|PDB:1AI0, ECO:0007744|PDB:1AIY,
FT                   ECO:0007744|PDB:1HIQ, ECO:0007744|PDB:1MHI,
FT                   ECO:0007744|PDB:2MVC, ECO:0007744|PDB:2MVD"
FT   VARIANT         6
FT                   /note="R -> C (in MODY10; dbSNP:rs121908278)"
FT                   /evidence="ECO:0000269|PubMed:18162506"
FT                   /id="VAR_063721"
FT   VARIANT         6
FT                   /note="R -> H (in MODY10; dbSNP:rs121908259)"
FT                   /evidence="ECO:0000269|PubMed:20226046"
FT                   /id="VAR_063722"
FT   VARIANT         24
FT                   /note="A -> D (in PNDM4; dbSNP:rs80356663)"
FT                   /evidence="ECO:0000269|PubMed:17855560,
FT                   ECO:0000269|PubMed:18162506"
FT                   /id="VAR_063723"
FT   VARIANT         29
FT                   /note="H -> D (in PNDM4; dbSNP:rs121908272)"
FT                   /evidence="ECO:0000269|PubMed:18162506"
FT                   /id="VAR_063724"
FT   VARIANT         32
FT                   /note="G -> R (in PNDM4; dbSNP:rs80356664)"
FT                   /evidence="ECO:0000269|PubMed:17855560,
FT                   ECO:0000269|PubMed:18162506"
FT                   /id="VAR_063725"
FT   VARIANT         32
FT                   /note="G -> S (in PNDM4; dbSNP:rs80356664)"
FT                   /evidence="ECO:0000269|PubMed:17855560,
FT                   ECO:0000269|PubMed:18162506"
FT                   /id="VAR_063726"
FT   VARIANT         34
FT                   /note="H -> D (in HPRI; Providence; dbSNP:rs121918101)"
FT                   /evidence="ECO:0000269|PubMed:3470784"
FT                   /id="VAR_003971"
FT   VARIANT         35
FT                   /note="L -> P (in PNDM4; dbSNP:rs121908273)"
FT                   /evidence="ECO:0000269|PubMed:18162506"
FT                   /id="VAR_063727"
FT   VARIANT         43
FT                   /note="C -> G (in PNDM4; dbSNP:rs80356666)"
FT                   /evidence="ECO:0000269|PubMed:17855560,
FT                   ECO:0000269|PubMed:18162506"
FT                   /id="VAR_063728"
FT   VARIANT         46
FT                   /note="R -> Q (in MODY10; reduces binding affinity to INSR;
FT                   reduces biological activity; reduces folding properties;
FT                   dbSNP:rs121908260)"
FT                   /evidence="ECO:0000269|PubMed:18192540,
FT                   ECO:0000269|PubMed:20226046, ECO:0000269|PubMed:25423173"
FT                   /id="VAR_063729"
FT   VARIANT         47
FT                   /note="G -> V (in PNDM4; dbSNP:rs80356667)"
FT                   /evidence="ECO:0000269|PubMed:17855560,
FT                   ECO:0000269|PubMed:18162506"
FT                   /id="VAR_063730"
FT   VARIANT         48
FT                   /note="F -> C (in PNDM4; dbSNP:rs80356668)"
FT                   /evidence="ECO:0000269|PubMed:17855560,
FT                   ECO:0000269|PubMed:18162506"
FT                   /id="VAR_063731"
FT   VARIANT         48
FT                   /note="F -> S (associated with diabetes mellitus type-II;
FT                   Los-Angeles; dbSNP:rs80356668)"
FT                   /evidence="ECO:0000269|PubMed:6312455,
FT                   ECO:0000269|PubMed:6424111, ECO:0000269|PubMed:8421693"
FT                   /id="VAR_003972"
FT   VARIANT         49
FT                   /note="F -> L (in Chicago; dbSNP:rs148685531)"
FT                   /evidence="ECO:0000269|PubMed:6424111"
FT                   /id="VAR_003973"
FT   VARIANT         55
FT                   /note="R -> C (in IDDM2; dbSNP:rs121908261)"
FT                   /evidence="ECO:0000269|PubMed:18192540"
FT                   /id="VAR_063732"
FT   VARIANT         68
FT                   /note="L -> M (in dbSNP:rs121908279)"
FT                   /evidence="ECO:0000269|PubMed:18162506"
FT                   /id="VAR_063733"
FT   VARIANT         84
FT                   /note="G -> R (in PNDM4; uncertain pathological
FT                   significance; dbSNP:rs121908274)"
FT                   /evidence="ECO:0000269|PubMed:18162506"
FT                   /id="VAR_063734"
FT   VARIANT         89
FT                   /note="R -> C (in PNDM4; dbSNP:rs80356669)"
FT                   /evidence="ECO:0000269|PubMed:17855560,
FT                   ECO:0000269|PubMed:18162506"
FT                   /id="VAR_063735"
FT   VARIANT         89
FT                   /note="R -> H (in HPRI; impairs post-translational
FT                   cleavage; dbSNP:rs28933985)"
FT                   /evidence="ECO:0000269|PubMed:2196279,
FT                   ECO:0000269|PubMed:4019786"
FT                   /id="VAR_003974"
FT   VARIANT         89
FT                   /note="R -> L (in HPRI; Kyoto; dbSNP:rs28933985)"
FT                   /evidence="ECO:0000269|PubMed:1601997"
FT                   /id="VAR_003975"
FT   VARIANT         90
FT                   /note="G -> C (in PNDM4; dbSNP:rs80356670)"
FT                   /evidence="ECO:0000269|PubMed:17855560,
FT                   ECO:0000269|PubMed:18162506"
FT                   /id="VAR_063736"
FT   VARIANT         92
FT                   /note="V -> L (in Wakayama; dbSNP:rs121918102)"
FT                   /evidence="ECO:0000269|PubMed:3537011"
FT                   /id="VAR_003976"
FT   VARIANT         96
FT                   /note="C -> S (in PNDM4; dbSNP:rs80356671)"
FT                   /evidence="ECO:0000269|PubMed:18162506"
FT                   /id="VAR_063737"
FT   VARIANT         96
FT                   /note="C -> Y (in PNDM4; dbSNP:rs80356671)"
FT                   /evidence="ECO:0000269|PubMed:17855560,
FT                   ECO:0000269|PubMed:18162506"
FT                   /id="VAR_063738"
FT   VARIANT         101
FT                   /note="S -> C (in PNDM4; dbSNP:rs121908276)"
FT                   /evidence="ECO:0000269|PubMed:18162506"
FT                   /id="VAR_063739"
FT   VARIANT         103
FT                   /note="Y -> C (in PNDM4; dbSNP:rs121908277)"
FT                   /evidence="ECO:0000269|PubMed:18162506"
FT                   /id="VAR_063740"
FT   VARIANT         108
FT                   /note="Y -> C (in PNDM4; dbSNP:rs80356672)"
FT                   /evidence="ECO:0000269|PubMed:17855560,
FT                   ECO:0000269|PubMed:18162506"
FT                   /id="VAR_063741"
FT   STRAND          26..29
FT                   /evidence="ECO:0007829|PDB:4EFX"
FT   HELIX           33..43
FT                   /evidence="ECO:0007829|PDB:3W7Y"
FT   HELIX           44..46
FT                   /evidence="ECO:0007829|PDB:3W7Y"
FT   STRAND          48..50
FT                   /evidence="ECO:0007829|PDB:3W7Y"
FT   STRAND          56..58
FT                   /evidence="ECO:0007829|PDB:1EFE"
FT   TURN            59..66
FT                   /evidence="ECO:0007829|PDB:1T0C"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:1T0C"
FT   HELIX           79..81
FT                   /evidence="ECO:0007829|PDB:1T0C"
FT   TURN            84..86
FT                   /evidence="ECO:0007829|PDB:1T0C"
FT   HELIX           91..97
FT                   /evidence="ECO:0007829|PDB:3W7Y"
FT   STRAND          98..101
FT                   /evidence="ECO:0007829|PDB:4EFX"
FT   HELIX           102..106
FT                   /evidence="ECO:0007829|PDB:3W7Y"
FT   TURN            107..109
FT                   /evidence="ECO:0007829|PDB:1HIQ"
SQ   SEQUENCE   110 AA;  11981 MW;  C2C3B23B85E520E5 CRC64;
     MALWMRLLPL LALLALWGPD PAAAFVNQHL CGSHLVEALY LVCGERGFFY TPKTRREAED
     LQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC SLYQLENYCN
 
 
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