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Database: UniProt
Entry: P01308
LinkDB: P01308
Original site: P01308 
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   16-APR-2014, entry version 191.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   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.,
RA   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
RT   kb 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.,
RA   Libutti S.K., 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
RT   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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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)
RT   within 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;
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
RT   disulfide bonds.";
RL   Helv. Chim. Acta 57:2617-2621(1974).
RN   [16]
RP   SYNTHESIS OF 57-87.
RX   PubMed=4803504;
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
RT   peptides (hC peptide). 3. Synthesis of the sequences 14-17 and 9-13 of
RT   human 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
RT   peptides (hC peptide). I. Scheme for the synthesis and preparation of
RT   the sequence 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
RT   serine-for-phenylalanine substitution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 80:7390-7394(1983).
RN   [21]
RP   VARIANT FHPRI 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
RT   of the mutant insulin A3 (Val-->Leu) isolated from the pancreas.";
RL   J. Clin. Invest. 78:1666-1672(1986).
RN   [23]
RP   VARIANT FHPRI HIS-89.
RX   PubMed=2196279;
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
RT   mutation substituting histidine for arginine at position 65 in the
RT   proinsulin molecule: identification of the mutation by direct
RT   sequencing of genomic deoxyribonucleic acid amplified by polymerase
RT   chain reaction.";
RL   J. Clin. Endocrinol. Metab. 71:164-169(1990).
RN   [24]
RP   VARIANT FHPRI 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
RT   mutation in familial hyperproinsulinemia.";
RL   J. Clin. Invest. 76:378-380(1985).
RN   [25]
RP   VARIANT FHPRI 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
RT   insulin: sequential resonance assignment and implications for protein
RT   dynamics and 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-
RT   specific resonance assignments and effects of solvent composition.";
RL   Biochim. Biophys. Acta 1078:101-110(1991).
RN   [29]
RP   STRUCTURE BY NMR.
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
RT   the B9(Asp) mutant of human insulin using nuclear magnetic resonance,
RT   distance geometry and restrained molecular dynamics.";
RL   J. Mol. Biol. 227:1146-1163(1992).
RN   [30]
RP   STRUCTURE BY NMR OF VARIANT LOS-ANGELES SER-48.
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
RT   associated with diabetes mellitus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:582-586(1993).
RN   [31]
RP   STRUCTURE BY NMR.
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 PNDM 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.,
RA   Greeley S.A., Patch A.M., Ellard S., Steiner D.F., Hattersley A.T.,
RA   Philipson L.H., 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 PNDM 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
RT   in the INS gene are a common cause of neonatal diabetes but a rare
RT   cause of 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-
RT   negative 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.,
RA   Barbetti F., Lebl J., Pedersen O., Hansen T.;
RT   "Further evidence that mutations in INS can be a rare cause of
RT   Maturity-Onset Diabetes of the Young (MODY).";
RL   BMC Med. Genet. 11:42-42(2010).
CC   -!- FUNCTION: Insulin decreases blood glucose concentration. It
CC       increases cell permeability to monosaccharides, amino acids and
CC       fatty acids. It accelerates glycolysis, the pentose phosphate
CC       cycle, and glycogen synthesis in liver.
CC   -!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
CC       disulfide bonds.
CC   -!- INTERACTION:
CC       Self; NbExp=16; IntAct=EBI-7090529, EBI-7090529;
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         Note=Based on a readthrough transcript which may produce an
CC         INS-IGF2 fusion protein;
CC   -!- DISEASE: Hyperproinsulinemia, familial (FHPRI) [MIM:176730]: An
CC       autosomal dominant condition characterized by elevated levels of
CC       serum proinsulin-like material. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Diabetes mellitus, insulin-dependent, 2 (IDDM2)
CC       [MIM:125852]: A multifactorial disorder of glucose homeostasis
CC       that is characterized by susceptibility to ketoacidosis in the
CC       absence of insulin therapy. Clinical features are polydipsia,
CC       polyphagia and polyuria which result from hyperglycemia-induced
CC       osmotic diuresis and secondary thirst. These derangements result
CC       in long-term complications that affect the eyes, kidneys, nerves,
CC       and blood vessels. Note=The disease is caused by mutations
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Diabetes mellitus, permanent neonatal (PNDM)
CC       [MIM:606176]: A rare form of diabetes distinct from childhood-
CC       onset autoimmune diabetes mellitus type 1. It is characterized by
CC       insulin-requiring hyperglycemia that is diagnosed within the first
CC       months of life. Permanent neonatal diabetes requires lifelong
CC       therapy. Note=The disease is caused by mutations affecting the
CC       gene represented in this entry.
CC   -!- DISEASE: Maturity-onset diabetes of the young 10 (MODY10)
CC       [MIM:613370]: A form of diabetes that is characterized by an
CC       autosomal dominant mode of inheritance, onset in childhood or
CC       early adulthood (usually before 25 years of age), a primary defect
CC       in insulin secretion and frequent insulin-independence at the
CC       beginning of the disease. Note=The disease is caused by mutations
CC       affecting the gene represented in this entry.
CC   -!- PHARMACEUTICAL: Available under the names Humulin or Humalog (Eli
CC       Lilly) and Novolin (Novo Nordisk). Used in the treatment of
CC       diabetes. Humalog is an insulin analog with 52-Lys-Pro-53 instead
CC       of 52-Pro-Lys-53.
CC   -!- SIMILARITY: Belongs to the insulin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA59179.1; Type=Erroneous gene model prediction;
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.ncbi.nlm.nih.gov/books/NBK1116/?term=INS[genesymbol]";
CC   -!- WEB RESOURCE: Name=Insulin at Eli Lilly; Note=Clinical information
CC       on Eli Lilly insulin products;
CC       URL="http://www.lillyDiabetes.com/Products/PatientInfo.cfm";
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Protein of the 20th
CC       century - Issue 9 of April 2001;
CC       URL="http://web.expasy.org/spotlight/back_issues/009";
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Insulin entry;
CC       URL="http://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   PIR; A93222; IPHU.
DR   RefSeq; NP_000198.1; NM_000207.2.
DR   RefSeq; NP_001172026.1; NM_001185097.1.
DR   RefSeq; NP_001172027.1; NM_001185098.1.
DR   UniGene; Hs.272259; -.
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=25-110.
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=26-53.
DR   PDB; 1IOH; NMR; -; A=90-110, B=26-53.
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=12-24.
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=25-48.
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=25-53.
DR   PDB; 1SJU; NMR; -; A=25-53, A=90-110.
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; -; 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.
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=25-51.
DR   PDB; 2JUU; NMR; -; A=90-110, B=25-51.
DR   PDB; 2JUV; NMR; -; A=90-110, B=25-51.
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=25-51.
DR   PDB; 2K9R; NMR; -; A=90-110, B=25-51.
DR   PDB; 2KJJ; NMR; -; A=90-110, B=25-51.
DR   PDB; 2KJU; NMR; -; A=90-110, B=25-51.
DR   PDB; 2KQP; NMR; -; A=25-110.
DR   PDB; 2KQQ; NMR; -; A=90-110, B=25-51.
DR   PDB; 2KXK; NMR; -; A=90-110, B=25-54.
DR   PDB; 2L1Y; NMR; -; A=90-110, B=25-51.
DR   PDB; 2L1Z; NMR; -; A=93-110, B=25-51.
DR   PDB; 2LGB; NMR; -; A=90-110, B=25-55.
DR   PDB; 2LWZ; NMR; -; A=25-54.
DR   PDB; 2M1D; NMR; -; A=90-110, B=25-51.
DR   PDB; 2M1E; NMR; -; A=90-110, B=25-51.
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; 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; 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=25-56.
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=25-49.
DR   PDB; 2WRV; X-ray; 2.15 A; A=90-110, B=25-49.
DR   PDB; 2WRW; X-ray; 2.41 A; A=90-110, B=25-49.
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=25-49.
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=25-49.
DR   PDB; 3AIY; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
DR   PDB; 3BRR; X-ray; 1.70 A; A/C=90-110, B/D=25-53.
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=25-53.
DR   PDB; 3I40; X-ray; 1.85 A; A=90-110, B=25-53.
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=25-51.
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=93-110, 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=25-49.
DR   PDB; 3W13; X-ray; 4.30 A; A=90-110, B=25-49.
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=25-48.
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; 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=25-51.
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; 5AIY; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
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; 2OLY; -.
DR   PDBsum; 2OLZ; -.
DR   PDBsum; 2OM0; -.
DR   PDBsum; 2OM1; -.
DR   PDBsum; 2OMG; -.
DR   PDBsum; 2OMH; -.
DR   PDBsum; 2OMI; -.
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; 3BRR; -.
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; 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; 5AIY; -.
DR   ProteinModelPortal; P01308; -.
DR   SMR; P01308; 25-110.
DR   BioGrid; 109842; 10.
DR   DIP; DIP-6024N; -.
DR   IntAct; P01308; 2.
DR   MINT; MINT-106847; -.
DR   STRING; 9606.ENSP00000348986; -.
DR   ChEMBL; CHEMBL5881; -.
DR   Allergome; 2121; Hom s Insulin.
DR   PhosphoSite; P01308; -.
DR   DMDM; 124617; -.
DR   PaxDb; P01308; -.
DR   PeptideAtlas; P01308; -.
DR   PRIDE; P01308; -.
DR   DNASU; 3630; -.
DR   Ensembl; ENST00000250971; ENSP00000250971; ENSG00000254647. [P01308-1]
DR   Ensembl; ENST00000381330; ENSP00000370731; ENSG00000254647. [P01308-1]
DR   Ensembl; ENST00000397262; ENSP00000380432; ENSG00000254647. [P01308-1]
DR   GeneID; 3630; -.
DR   KEGG; hsa:3630; -.
DR   UCSC; uc001lvn.2; human. [P01308-1]
DR   CTD; 3630; -.
DR   GeneCards; GC11M002181; -.
DR   HGNC; HGNC:6081; INS.
DR   HPA; CAB000048; -.
DR   HPA; CAB012098; -.
DR   HPA; CAB053843; -.
DR   HPA; HPA004932; -.
DR   MIM; 125852; phenotype.
DR   MIM; 176730; gene+phenotype.
DR   MIM; 606176; phenotype.
DR   MIM; 613370; phenotype.
DR   neXtProt; NX_P01308; -.
DR   Orphanet; 552; MODY syndrome.
DR   Orphanet; 99885; Permanent neonatal diabetes mellitus.
DR   PharmGKB; PA201; -.
DR   eggNOG; NOG45999; -.
DR   HOGENOM; HOG000261669; -.
DR   HOVERGEN; HBG006137; -.
DR   KO; K04526; -.
DR   OMA; VEQCCHN; -.
DR   PhylomeDB; P01308; -.
DR   TreeFam; TF332820; -.
DR   BioCyc; MetaCyc:MONOMER-16190; -.
DR   Reactome; REACT_111045; Developmental Biology.
DR   Reactome; REACT_111102; Signal Transduction.
DR   Reactome; REACT_111217; Metabolism.
DR   Reactome; REACT_116125; Disease.
DR   Reactome; REACT_17015; Metabolism of proteins.
DR   SignaLink; P01308; -.
DR   EvolutionaryTrace; P01308; -.
DR   GeneWiki; Insulin; -.
DR   GenomeRNAi; 3630; -.
DR   NextBio; 14203; -.
DR   PMAP-CutDB; P01308; -.
DR   PRO; PR:P01308; -.
DR   ArrayExpress; P01308; -.
DR   Bgee; P01308; -.
DR   Genevestigator; P01308; -.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0031904; C:endosome lumen; TAS:Reactome.
DR   GO; GO:0005576; C:extracellular region; IC:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR   GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR   GO; GO:0005179; F:hormone activity; NAS:UniProtKB.
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:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR   GO; GO:0031018; P:endocrine pancreas development; TAS:Reactome.
DR   GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
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:0015758; P:glucose transport; IDA:UniProtKB.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0000165; P:MAPK cascade; 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: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:1902176; P:negative regulation of intrinsic apoptotic signaling pathway in response to oxidative stress; NAS:BHF-UCL.
DR   GO; GO:0050995; P:negative regulation of lipid catabolic process; NAS:BHF-UCL.
DR   GO; GO:0033861; P:negative regulation of NAD(P)H oxidase activity; IDA:BHF-UCL.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:UniProtKB.
DR   GO; GO:0032460; P:negative regulation of protein oligomerization; 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:0060266; P:negative regulation of respiratory burst involved in inflammatory response; IDA:BHF-UCL.
DR   GO; GO:0045908; P:negative regulation of vasodilation; NAS: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 proliferation; IDA:BHF-UCL.
DR   GO; GO:0032270; P:positive regulation of cellular protein metabolic process; IMP:BHF-UCL.
DR   GO; GO:0050715; P:positive regulation of cytokine secretion; IDA:UniProtKB.
DR   GO; GO:0045740; P:positive regulation of DNA replication; IDA:BHF-UCL.
DR   GO; GO:0046326; P:positive regulation of glucose import; IDA:BHF-UCL.
DR   GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0045821; P:positive regulation of glycolysis; IDA:BHF-UCL.
DR   GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0046889; P:positive regulation of lipid biosynthetic process; NAS:BHF-UCL.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:BHF-UCL.
DR   GO; GO:0045840; P:positive regulation of mitosis; IDA:UniProtKB.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; NAS: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:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA: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:0060267; P:positive regulation of respiratory burst; IDA:BHF-UCL.
DR   GO; GO:0045909; P:positive regulation of vasodilation; NAS:UniProtKB.
DR   GO; GO:0006521; P:regulation of cellular amino acid metabolic process; IMP:BHF-UCL.
DR   GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
DR   GO; GO:0032880; P:regulation of protein localization; IDA:BHF-UCL.
DR   GO; GO:0050708; P:regulation of protein secretion; IDA:UniProtKB.
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:0044281; P:small molecule metabolic process; TAS:Reactome.
DR   GO; GO:0042060; P:wound healing; IDA:BHF-UCL.
DR   Gene3D; 1.10.100.10; -; 2.
DR   InterPro; IPR004825; Insulin.
DR   InterPro; IPR016179; Insulin-like.
DR   InterPro; IPR022353; Insulin_CS.
DR   InterPro; IPR022352; Insulin_family.
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; Complete proteome;
KW   Diabetes mellitus; Direct protein sequencing; Disease mutation;
KW   Disulfide bond; Glucose metabolism; Hormone; Pharmaceutical;
KW   Polymorphism; Reference proteome; Secreted; Signal.
FT   SIGNAL        1     24
FT   PEPTIDE      25     54       Insulin B chain.
FT                                /FTId=PRO_0000015819.
FT   PROPEP       57     87       C peptide.
FT                                /FTId=PRO_0000015820.
FT   PEPTIDE      90    110       Insulin A chain.
FT                                /FTId=PRO_0000015821.
FT   DISULFID     31     96       Interchain (between B and A chains).
FT   DISULFID     43    109       Interchain (between B and A chains).
FT   DISULFID     95    100
FT   VARIANT       6      6       R -> C (in MODY10; dbSNP:rs121908278).
FT                                /FTId=VAR_063721.
FT   VARIANT       6      6       R -> H (in MODY10; dbSNP:rs121908259).
FT                                /FTId=VAR_063722.
FT   VARIANT      24     24       A -> D (in PNDM; dbSNP:rs80356663).
FT                                /FTId=VAR_063723.
FT   VARIANT      29     29       H -> D (in PNDM; dbSNP:rs121908272).
FT                                /FTId=VAR_063724.
FT   VARIANT      32     32       G -> R (in PNDM; dbSNP:rs80356664).
FT                                /FTId=VAR_063725.
FT   VARIANT      32     32       G -> S (in PNDM; dbSNP:rs80356664).
FT                                /FTId=VAR_063726.
FT   VARIANT      34     34       H -> D (in FHPRI; Providence).
FT                                /FTId=VAR_003971.
FT   VARIANT      35     35       L -> P (in PNDM; dbSNP:rs121908273).
FT                                /FTId=VAR_063727.
FT   VARIANT      43     43       C -> G (in PNDM; dbSNP:rs80356666).
FT                                /FTId=VAR_063728.
FT   VARIANT      46     46       R -> Q (in MODY10; dbSNP:rs121908260).
FT                                /FTId=VAR_063729.
FT   VARIANT      47     47       G -> V (in PNDM; dbSNP:rs80356667).
FT                                /FTId=VAR_063730.
FT   VARIANT      48     48       F -> C (in PNDM; dbSNP:rs80356668).
FT                                /FTId=VAR_063731.
FT   VARIANT      48     48       F -> S (associated with diabetes mellitus
FT                                type-II; Los-Angeles).
FT                                /FTId=VAR_003972.
FT   VARIANT      49     49       F -> L (in Chicago).
FT                                /FTId=VAR_003973.
FT   VARIANT      55     55       R -> C (in IDDM2; dbSNP:rs121908261).
FT                                /FTId=VAR_063732.
FT   VARIANT      68     68       L -> M (in dbSNP:rs121908279).
FT                                /FTId=VAR_063733.
FT   VARIANT      84     84       G -> R (in PNDM; uncertain pathological
FT                                significance; dbSNP:rs121908274).
FT                                /FTId=VAR_063734.
FT   VARIANT      89     89       R -> C (in PNDM; dbSNP:rs80356669).
FT                                /FTId=VAR_063735.
FT   VARIANT      89     89       R -> H (in FHPRI; impairs
FT                                posttranslational cleavage;
FT                                dbSNP:rs28933985).
FT                                /FTId=VAR_003974.
FT   VARIANT      89     89       R -> L (in FHPRI; Kyoto).
FT                                /FTId=VAR_003975.
FT   VARIANT      90     90       G -> C (in PNDM; dbSNP:rs80356670).
FT                                /FTId=VAR_063736.
FT   VARIANT      92     92       V -> L (in Wakayama).
FT                                /FTId=VAR_003976.
FT   VARIANT      96     96       C -> S (in PNDM; dbSNP:rs80356671).
FT                                /FTId=VAR_063737.
FT   VARIANT      96     96       C -> Y (in PNDM; dbSNP:rs80356671).
FT                                /FTId=VAR_063738.
FT   VARIANT     101    101       S -> C (in PNDM; dbSNP:rs121908276).
FT                                /FTId=VAR_063739.
FT   VARIANT     103    103       Y -> C (in PNDM; dbSNP:rs121908277).
FT                                /FTId=VAR_063740.
FT   VARIANT     108    108       Y -> C (in PNDM; dbSNP:rs80356672).
FT                                /FTId=VAR_063741.
FT   STRAND       26     29
FT   HELIX        33     43
FT   HELIX        44     46
FT   STRAND       48     50
FT   TURN         59     66
FT   STRAND       74     76
FT   HELIX        79     81
FT   TURN         84     86
FT   HELIX        91     97
FT   STRAND       98    101
FT   HELIX       102    106
FT   TURN        107    109
SQ   SEQUENCE   110 AA;  11981 MW;  C2C3B23B85E520E5 CRC64;
     MALWMRLLPL LALLALWGPD PAAAFVNQHL CGSHLVEALY LVCGERGFFY TPKTRREAED
     LQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC SLYQLENYCN
//
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