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Insulin [Cleaved into: Insulin B chain; Insulin A chain]

 INS_HUMAN               Reviewed;         110 AA.
P01308; Q5EEX2;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
20-JUN-2018, entry version 238.
RecName: Full=Insulin;
Contains:
RecName: Full=Insulin B chain;
Contains:
RecName: Full=Insulin A chain;
Flags: Precursor;
Name=INS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6243748; DOI=10.1038/284026a0;
Bell G.I., Pictet R.L., Rutter W.J., Cordell B., Tischer E.,
Goodman H.M.;
"Sequence of the human insulin gene.";
Nature 284:26-32(1980).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6248962; DOI=10.1126/science.6248962;
Ullrich A., Dull T.J., Gray A., Brosius J., Sures I.;
"Genetic variation in the human insulin gene.";
Science 209:612-615(1980).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=503234; DOI=10.1038/282525a0;
Bell G.I., Swain W.F., Pictet R.L., Cordell B., Goodman H.M.,
Rutter W.J.;
"Nucleotide sequence of a cDNA clone encoding human preproinsulin.";
Nature 282:525-527(1979).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6927840; DOI=10.1126/science.6927840;
Sures I., Goeddel D.V., Gray A., Ullrich A.;
"Nucleotide sequence of human preproinsulin complementary DNA.";
Science 208:57-59(1980).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8358440; DOI=10.1038/ng0793-305;
Lucassen A.M., Julier C., Beressi J.-P., Boitard C., Froguel P.,
Lathrop M., Bell J.I.;
"Susceptibility to insulin dependent diabetes mellitus maps to a 4.1
kb segment of DNA spanning the insulin gene and associated VNTR.";
Nat. Genet. 4:305-310(1993).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=15070567; DOI=10.1016/S0140-6736(04)15438-X;
Minn A.H., Kayton M., Lorang D., Hoffmann S.C., Harlan D.M.,
Libutti S.K., Shalev A.;
"Insulinomas and expression of an insulin splice variant.";
Lancet 363:363-367(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=12952878; DOI=10.1101/gr.948003;
Stead J.D.H., Hurles M.E., Jeffreys A.J.;
"Global haplotype diversity in the human insulin gene region.";
Genome Res. 13:2101-2111(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59.
TISSUE=Blood;
Fajardy I.I., Weill J.J., Stuckens C.C., Danze P.M.P.;
"Description of a novel RFLP diallelic polymorphism (-127 BsgI C/G)
within the 5' region of insulin gene.";
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[12]
PROTEIN SEQUENCE OF 25-54 AND 90-110.
PubMed=14426955; DOI=10.1038/187483a0;
Nicol D.S.H.W., Smith L.F.;
"Amino-acid sequence of human insulin.";
Nature 187:483-485(1960).
[13]
PROTEIN SEQUENCE OF 57-87.
PubMed=5101771;
Oyer P.E., Cho S., Peterson J.D., Steiner D.F.;
"Studies on human proinsulin. Isolation and amino acid sequence of the
human pancreatic C-peptide.";
J. Biol. Chem. 246:1375-1386(1971).
[14]
PROTEIN SEQUENCE OF 57-87.
PubMed=5560404; DOI=10.1111/j.1432-1033.1971.tb01378.x;
Ko A., Smyth D.G., Markussen J., Sundby F.;
"The amino acid sequence of the C-peptide of human proinsulin.";
Eur. J. Biochem. 20:190-199(1971).
[15]
SYNTHESIS.
PubMed=4443293; DOI=10.1002/hlca.19740570839;
Sieber P., Kamber B., Hartmann A., Joehl A., Riniker B., Rittel W.;
"Total synthesis of human insulin under directed formation of the
disulfide bonds.";
Helv. Chim. Acta 57:2617-2621(1974).
[16]
SYNTHESIS OF 57-87.
PubMed=4803504;
Naithani V.K.;
"Studies on polypeptides, IV. The synthesis of C-peptide of human
proinsulin.";
Hoppe-Seyler's Z. Physiol. Chem. 354:659-672(1973).
[17]
SYNTHESIS OF 65-69 AND 70-73.
PubMed=4698555; DOI=10.1002/cber.19731060124;
Geiger R., Volk A.;
"Synthesis of peptides with the properties of human proinsulin C
peptides (hC peptide). 3. Synthesis of the sequences 14-17 and 9-13 of
human proinsulin C peptides.";
Chem. Ber. 106:199-205(1973).
[18]
SYNTHESIS OF 84-87.
PubMed=4698553; DOI=10.1002/cber.19731060122;
Geiger R., Jaeger G., Keonig W., Treuth G.;
"Synthesis of peptides with the properties of human proinsulin C
peptides (hC peptide). I. Scheme for the synthesis and preparation of
the sequence 28-31 of human proinsulin C peptide.";
Chem. Ber. 106:188-192(1973).
[19]
VARIANT LOS ANGELES SER-48.
PubMed=6312455; DOI=10.1073/pnas.80.20.6366;
Haneda M., Chan S.J., Kwok S.C.M., Rubenstein A.H., Steiner D.F.;
"Studies on mutant human insulin genes: identification and sequence
analysis of a gene encoding [SerB24]insulin.";
Proc. Natl. Acad. Sci. U.S.A. 80:6366-6370(1983).
[20]
VARIANTS LOS ANGELES SER-48 AND CHICAGO LEU-49.
PubMed=6424111; DOI=10.1073/pnas.80.24.7390;
Shoelson S., Fickova M., Haneda M., Nahum A., Musso G., Kaiser E.T.,
Rubenstein A.H., Tager H.;
"Identification of a mutant human insulin predicted to contain a
serine-for-phenylalanine substitution.";
Proc. Natl. Acad. Sci. U.S.A. 80:7390-7394(1983).
[21]
VARIANT HPRI ASP-34.
PubMed=3470784; DOI=10.1073/pnas.84.8.2194;
Chan S.J., Seino S., Gruppuso P.A., Schwartz R., Steiner D.F.;
"A mutation in the B chain coding region is associated with impaired
proinsulin conversion in a family with hyperproinsulinemia.";
Proc. Natl. Acad. Sci. U.S.A. 84:2194-2197(1987).
[22]
VARIANT WAKAYAMA LEU-92.
PubMed=3537011; DOI=10.1172/JCI112760;
Sakura H., Iwamoto Y., Sakamoto Y., Kuzuya T., Hirata H.;
"Structurally abnormal insulin in a diabetic patient. Characterization
of the mutant insulin A3 (Val-->Leu) isolated from the pancreas.";
J. Clin. Invest. 78:1666-1672(1986).
[23]
VARIANT HPRI HIS-89.
PubMed=2196279; DOI=10.1210/jcem-71-1-164;
Barbetti F., Raben N., Kadowaki T., Cama A., Accili D., Gabbay K.H.,
Merenich J.A., Taylor S.I., Roth J.;
"Two unrelated patients with familial hyperproinsulinemia due to a
mutation substituting histidine for arginine at position 65 in the
proinsulin molecule: identification of the mutation by direct
sequencing of genomic deoxyribonucleic acid amplified by polymerase
chain reaction.";
J. Clin. Endocrinol. Metab. 71:164-169(1990).
[24]
VARIANT HPRI HIS-89.
PubMed=4019786; DOI=10.1172/JCI111973;
Shibasaki Y., Kawakami T., Kanazawa Y., Akanuma Y., Takaku F.;
"Posttranslational cleavage of proinsulin is blocked by a point
mutation in familial hyperproinsulinemia.";
J. Clin. Invest. 76:378-380(1985).
[25]
VARIANT HPRI LEU-89.
PubMed=1601997; DOI=10.1172/JCI115795;
Yano H., Kitano N., Morimoto M., Polonsky K.S., Imura H., Seino Y.;
"A novel point mutation in the human insulin gene giving rise to
hyperproinsulinemia (proinsulin Kyoto).";
J. Clin. Invest. 89:1902-1907(1992).
[26]
STRUCTURE BY NMR.
PubMed=2271664; DOI=10.1021/bi00498a018;
Hua Q.-X., Weiss M.A.;
"Toward the solution structure of human insulin: sequential 2D 1H NMR
assignment of a des-pentapeptide analogue and comparison with crystal
structure.";
Biochemistry 29:10545-10555(1990).
[27]
STRUCTURE BY NMR.
PubMed=2036420; DOI=10.1021/bi00236a025;
Hua Q.-X., Weiss M.A.;
"Comparative 2D NMR studies of human insulin and des-pentapeptide
insulin: sequential resonance assignment and implications for protein
dynamics and receptor recognition.";
Biochemistry 30:5505-5515(1991).
[28]
STRUCTURE BY NMR.
PubMed=1646635; DOI=10.1016/0167-4838(91)90098-K;
Hua Q.-X., Weiss M.A.;
"Two-dimensional NMR studies of Des-(B26-B30)-insulin: sequence-
specific resonance assignments and effects of solvent composition.";
Biochim. Biophys. Acta 1078:101-110(1991).
[29]
STRUCTURE BY NMR OF 90-110 AND 25-54, AND DISULFIDE BONDS.
PubMed=1433291; DOI=10.1016/0022-2836(92)90527-Q;
Joergensen A.M.M., Kristensen S.M., Led J.J., Balschmidt P.;
"Three-dimensional solution structure of an insulin dimer. A study of
the B9(Asp) mutant of human insulin using nuclear magnetic resonance,
distance geometry and restrained molecular dynamics.";
J. Mol. Biol. 227:1146-1163(1992).
[30]
STRUCTURE BY NMR OF 90-110 AND 25-54 OF VARIANT LOS-ANGELES SER-48,
AND DISULFIDE BONDS.
PubMed=8421693; DOI=10.1073/pnas.90.2.582;
Hua Q.-X., Shoelson S.E., Inouye K., Weiss M.A.;
"Paradoxical structure and function in a mutant human insulin
associated with diabetes mellitus.";
Proc. Natl. Acad. Sci. U.S.A. 90:582-586(1993).
[31]
STRUCTURE BY NMR OF 90-110 AND 25-54, AND DISULFIDE BONDS.
PubMed=9235985; DOI=10.1021/bi9631069;
Chang X., Joergensen A.M., Bardrum P., Led J.J.;
"Solution structures of the R6 human insulin hexamer.";
Biochemistry 36:9409-9422(1997).
[32]
VARIANTS PNDM ASP-24; ARG-32; SER-32; GLY-43; VAL-47; CYS-48; CYS-89;
CYS-90; TYR-96 AND CYS-108.
PubMed=17855560; DOI=10.1073/pnas.0707291104;
Stoy J., Edghill E.L., Flanagan S.E., Ye H., Paz V.P., Pluzhnikov A.,
Below J.E., Hayes M.G., Cox N.J., Lipkind G.M., Lipton R.B.,
Greeley S.A., Patch A.M., Ellard S., Steiner D.F., Hattersley A.T.,
Philipson L.H., Bell G.I.;
"Insulin gene mutations as a cause of permanent neonatal diabetes.";
Proc. Natl. Acad. Sci. U.S.A. 104:15040-15044(2007).
[33]
VARIANTS PNDM ASP-24; ASP-29; ARG-32; SER-32; PRO-35; GLY-43; VAL-47;
CYS-48; ARG-84; CYS-89; CYS-90; SER-96; TYR-96; CYS-101; CYS-103 AND
CYS-108, VARIANT MODY10 CYS-6, AND VARIANT MET-68.
PubMed=18162506; DOI=10.2337/db07-1405;
Edghill E.L., Flanagan S.E., Patch A.M., Boustred C., Parrish A.,
Shields B., Shepherd M.H., Hussain K., Kapoor R.R., Malecki M.,
MacDonald M.J., Stoy J., Steiner D.F., Philipson L.H., Bell G.I.,
Hattersley A.T., Ellard S.;
"Insulin mutation screening in 1,044 patients with diabetes: mutations
in the INS gene are a common cause of neonatal diabetes but a rare
cause of diabetes diagnosed in childhood or adulthood.";
Diabetes 57:1034-1042(2008).
[34]
VARIANT MODY10 GLN-46, AND VARIANT IDDM2 CYS-55.
PubMed=18192540; DOI=10.2337/db07-1467;
Molven A., Ringdal M., Nordbo A.M., Raeder H., Stoy J., Lipkind G.M.,
Steiner D.F., Philipson L.H., Bergmann I., Aarskog D., Undlien D.E.,
Joner G., Sovik O., Bell G.I., Njolstad P.R.;
"Mutations in the insulin gene can cause MODY and autoantibody-
negative type 1 diabetes.";
Diabetes 57:1131-1135(2008).
[35]
VARIANTS MODY10 HIS-6 AND GLN-46.
PubMed=20226046; DOI=10.1186/1471-2350-11-42;
Boesgaard T.W., Pruhova S., Andersson E.A., Cinek O., Obermannova B.,
Lauenborg J., Damm P., Bergholdt R., Pociot F., Pisinger C.,
Barbetti F., Lebl J., Pedersen O., Hansen T.;
"Further evidence that mutations in INS can be a rare cause of
Maturity-Onset Diabetes of the Young (MODY).";
BMC Med. Genet. 11:42-42(2010).
[36]
VARIANT MODY10 GLN-46, CHARACTERIZATION OF VARIANT MODY10 GLN-46,
STRUCTURE BY NMR OF 90-110 AND 25-54, DISULFIDE BONDS OF VARIANT
MODY10 GLN-46, AND SUBUNIT.
PubMed=25423173; DOI=10.1371/journal.pone.0112883;
Krizkova K., Veverka V., Maletinska L., Hexnerova R., Brzozowski A.M.,
Jiracek J., Zakova L.;
"Structural and functional study of the GlnB22-insulin mutant
responsible for maturity-onset diabetes of the young.";
PLoS ONE 9:E112883-E112883(2014).
-!- FUNCTION: Insulin decreases blood glucose concentration. It
increases cell permeability to monosaccharides, amino acids and
fatty acids. It accelerates glycolysis, the pentose phosphate
cycle, and glycogen synthesis in liver.
-!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
disulfide bonds (PubMed:25423173). {ECO:0000269|PubMed:25423173}.
-!- INTERACTION:
Self; NbExp=18; IntAct=EBI-7090529, EBI-7090529;
P14735-1:IDE; NbExp=3; IntAct=EBI-7090529, EBI-15607031;
P06213-2:INSR; NbExp=3; IntAct=EBI-7090529, EBI-9984921;
Q07627:KRTAP1-1; NbExp=4; IntAct=EBI-7090529, EBI-11959885;
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P01308-1; Sequence=Displayed;
Name=2; Synonyms=INS-IGF2;
IsoId=F8WCM5-1; Sequence=External;
Note=Based on a readthrough transcript which may produce an
INS-IGF2 fusion protein.;
-!- DISEASE: Hyperproinsulinemia (HPRI) [MIM:616214]: An autosomal
dominant condition characterized by elevated levels of serum
proinsulin-like material. {ECO:0000269|PubMed:1601997,
ECO:0000269|PubMed:2196279, ECO:0000269|PubMed:3470784,
ECO:0000269|PubMed:4019786}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Diabetes mellitus, insulin-dependent, 2 (IDDM2)
[MIM:125852]: A multifactorial disorder of glucose homeostasis
that is characterized by susceptibility to ketoacidosis in the
absence of insulin therapy. Clinical features are polydipsia,
polyphagia and polyuria which result from hyperglycemia-induced
osmotic diuresis and secondary thirst. These derangements result
in long-term complications that affect the eyes, kidneys, nerves,
and blood vessels. {ECO:0000269|PubMed:18192540}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Diabetes mellitus, permanent neonatal (PNDM)
[MIM:606176]: A rare form of diabetes distinct from childhood-
onset autoimmune diabetes mellitus type 1. It is characterized by
insulin-requiring hyperglycemia that is diagnosed within the first
months of life. Permanent neonatal diabetes requires lifelong
therapy. {ECO:0000269|PubMed:17855560,
ECO:0000269|PubMed:18162506}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Maturity-onset diabetes of the young 10 (MODY10)
[MIM:613370]: A form of diabetes that is characterized by an
autosomal dominant mode of inheritance, onset in childhood or
early adulthood (usually before 25 years of age), a primary defect
in insulin secretion and frequent insulin-independence at the
beginning of the disease. {ECO:0000269|PubMed:18162506,
ECO:0000269|PubMed:18192540, ECO:0000269|PubMed:20226046,
ECO:0000269|PubMed:25423173}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- PHARMACEUTICAL: Available under the names Humulin or Humalog (Eli
Lilly) and Novolin (Novo Nordisk). Used in the treatment of
diabetes. Humalog is an insulin analog with 52-Lys-Pro-53 instead
of 52-Pro-Lys-53.
-!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA59179.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Insulin at Eli Lilly; Note=Clinical information
on Eli Lilly insulin products;
URL="http://www.lillyDiabetes.com/Products/PatientInfo.cfm";
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Protein of the 20th
century - Issue 9 of April 2001;
URL="https://web.expasy.org/spotlight/back_issues/009";
-!- WEB RESOURCE: Name=Wikipedia; Note=Insulin entry;
URL="https://en.wikipedia.org/wiki/Insulin";
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EMBL; V00565; CAA23828.1; -; Genomic_DNA.
EMBL; M10039; AAA59173.1; -; Genomic_DNA.
EMBL; J00265; AAA59172.1; -; Genomic_DNA.
EMBL; X70508; CAA49913.1; -; mRNA.
EMBL; L15440; AAA59179.1; ALT_SEQ; Genomic_DNA.
EMBL; AY899304; AAW83741.1; -; mRNA.
EMBL; AY138590; AAN39451.1; -; Genomic_DNA.
EMBL; BT006808; AAP35454.1; -; mRNA.
EMBL; CH471158; EAX02488.1; -; Genomic_DNA.
EMBL; BC005255; AAH05255.1; -; mRNA.
EMBL; AJ009655; CAA08766.1; -; Genomic_DNA.
CCDS; CCDS7729.1; -. [P01308-1]
PIR; A93222; IPHU.
RefSeq; NP_000198.1; NM_000207.2. [P01308-1]
RefSeq; NP_001172026.1; NM_001185097.1. [P01308-1]
RefSeq; NP_001172027.1; NM_001185098.1. [P01308-1]
RefSeq; NP_001278826.1; NM_001291897.1. [P01308-1]
UniGene; Hs.272259; -.
PDB; 1A7F; NMR; -; A=90-110, B=25-53.
PDB; 1AI0; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
PDB; 1AIY; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
PDB; 1B9E; X-ray; 2.50 A; A/C=90-110, B/D=25-54.
PDB; 1BEN; X-ray; 1.40 A; A/C=90-110, B/D=25-54.
PDB; 1EFE; NMR; -; A=25-54, A=90-110.
PDB; 1EV3; X-ray; 1.78 A; A/C=90-110, B/D=25-54.
PDB; 1EV6; X-ray; 1.90 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
PDB; 1EVR; X-ray; 1.90 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
PDB; 1FU2; X-ray; 3.24 A; A/C/E/G=90-110, B/D/F/H=25-54.
PDB; 1FUB; X-ray; 3.09 A; A/C=90-110, B/D=25-54.
PDB; 1G7A; X-ray; 1.20 A; A/C/E/G=90-110, B/D/F/H=25-54.
PDB; 1G7B; X-ray; 1.30 A; A/C/E/G=90-110, B/D/F/H=25-54.
PDB; 1GUJ; X-ray; 1.62 A; A/C=90-110, B/D=25-54.
PDB; 1HIQ; NMR; -; A=90-110, B=25-54.
PDB; 1HIS; NMR; -; A=90-110, B=25-49.
PDB; 1HIT; NMR; -; A=90-110, B=25-54.
PDB; 1HLS; NMR; -; A=90-110, B=25-54.
PDB; 1HTV; X-ray; 1.90 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-51.
PDB; 1HUI; NMR; -; A=90-110, B=26-53.
PDB; 1IOG; NMR; -; A=90-110, B=25-53.
PDB; 1IOH; NMR; -; A=90-110, B=25-53.
PDB; 1J73; X-ray; 2.00 A; A/C=90-110, B/D=25-54.
PDB; 1JCA; X-ray; 2.50 A; A/C=90-110, B/D=25-54.
PDB; 1JCO; NMR; -; A=90-110, B=25-54.
PDB; 1JK8; X-ray; 2.40 A; C=35-47.
PDB; 1K3M; NMR; -; A=90-110, B=25-54.
PDB; 1KMF; NMR; -; A=90-110, B=25-54.
PDB; 1LKQ; NMR; -; A=90-110, B=25-54.
PDB; 1LPH; X-ray; 2.30 A; A/C=90-110, B/D=25-54.
PDB; 1MHI; NMR; -; A=90-110, B=25-54.
PDB; 1MHJ; NMR; -; A=90-110, B=25-54.
PDB; 1MSO; X-ray; 1.00 A; A/C=90-110, B/D=25-54.
PDB; 1OS3; X-ray; 1.95 A; A/C=90-110, B/D=25-54.
PDB; 1OS4; X-ray; 2.25 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
PDB; 1Q4V; X-ray; 2.00 A; A/C=90-110, B/D=25-54.
PDB; 1QIY; X-ray; 2.30 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
PDB; 1QIZ; X-ray; 2.00 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
PDB; 1QJ0; X-ray; 2.40 A; A/C=90-110, B/D=25-54.
PDB; 1RWE; X-ray; 1.80 A; A/C=90-110, B/D=25-54.
PDB; 1SF1; NMR; -; A=90-110, B=25-54.
PDB; 1SJT; NMR; -; A=90-110, B=25-51.
PDB; 1SJU; NMR; -; A=25-110.
PDB; 1T0C; NMR; -; A=57-87.
PDB; 1T1K; NMR; -; A=90-110, B=25-54.
PDB; 1T1P; NMR; -; A=90-110, B=25-54.
PDB; 1T1Q; NMR; -; A=90-110, B=25-54.
PDB; 1TRZ; X-ray; 1.60 A; A/C=90-110, B/D=25-54.
PDB; 1TYL; X-ray; 1.90 A; A/C=90-110, B/D=25-54.
PDB; 1TYM; X-ray; 1.90 A; A/C=90-110, B/D=25-54.
PDB; 1UZ9; X-ray; 1.60 A; A=90-110, B=25-53.
PDB; 1VKT; NMR; -; A=90-110, B=25-54.
PDB; 1W8P; X-ray; 2.08 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
PDB; 1XDA; X-ray; 1.80 A; A/C/E/G=90-110, B/D/F/H=25-53.
PDB; 1XGL; NMR; -; A=90-110, B=25-54.
PDB; 1XW7; X-ray; 2.30 A; A/C=90-110, B/D=25-54.
PDB; 1ZEG; X-ray; 1.60 A; A/C=90-110, B/D=25-54.
PDB; 1ZEH; X-ray; 1.50 A; A/C=90-110, B/D=25-54.
PDB; 1ZNJ; X-ray; 2.00 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
PDB; 2AIY; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
PDB; 2C8Q; X-ray; 1.95 A; A=90-110, B=25-53.
PDB; 2C8R; X-ray; 1.50 A; A=90-110, B=25-53.
PDB; 2CEU; X-ray; 1.80 A; A/C=90-110, B/D=25-49.
PDB; 2G54; X-ray; 2.25 A; C/D=25-54.
PDB; 2G56; X-ray; 2.20 A; C/D=25-54.
PDB; 2H67; NMR; -; A=90-110, B=25-54.
PDB; 2HH4; NMR; -; A=90-110, B=25-54.
PDB; 2HHO; NMR; -; A=90-110, B=25-54.
PDB; 2HIU; NMR; -; A=90-110, B=25-54.
PDB; 2JMN; NMR; -; A=90-110, B=25-54.
PDB; 2JUM; NMR; -; A=90-110, B=25-54.
PDB; 2JUU; NMR; -; A=90-110, B=25-54.
PDB; 2JUV; NMR; -; A=90-110, B=25-54.
PDB; 2JV1; NMR; -; A=90-110, B=25-54.
PDB; 2JZQ; NMR; -; A=25-54, A=90-110.
PDB; 2K91; NMR; -; A=90-110, B=25-54.
PDB; 2K9R; NMR; -; A=90-110, B=25-54.
PDB; 2KJJ; NMR; -; A=90-110, B=25-54.
PDB; 2KJU; NMR; -; A=90-110, B=25-54.
PDB; 2KQP; NMR; -; A=25-110.
PDB; 2KQQ; NMR; -; A=90-110, B=25-54.
PDB; 2KXK; NMR; -; A=90-110, B=25-54.
PDB; 2L1Y; NMR; -; A=90-110, B=25-54.
PDB; 2L1Z; NMR; -; A=90-110, B=25-54.
PDB; 2LGB; NMR; -; A=90-110, B=25-55.
PDB; 2LWZ; NMR; -; A=25-54, A=89-110.
PDB; 2M1D; NMR; -; A=90-110, B=25-54.
PDB; 2M1E; NMR; -; A=90-110, B=25-54.
PDB; 2M2M; NMR; -; A=90-110, B=25-54.
PDB; 2M2N; NMR; -; A=90-110, B=25-54.
PDB; 2M2O; NMR; -; A=90-110, B=25-54.
PDB; 2M2P; NMR; -; A=90-110, B=25-54.
PDB; 2MLI; NMR; -; A=90-110, B=25-54.
PDB; 2MPG; NMR; -; A=90-110, B=25-54.
PDB; 2MPI; NMR; -; A=90-110, B=25-54.
PDB; 2MVC; NMR; -; A=90-110, B=25-54.
PDB; 2MVD; NMR; -; A=90-110, B=25-54.
PDB; 2N2V; NMR; -; A=90-110, B=25-54.
PDB; 2N2W; NMR; -; A=90-110, B=25-54.
PDB; 2N2X; NMR; -; A=90-110, B=25-54.
PDB; 2OLY; X-ray; 1.70 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
PDB; 2OLZ; X-ray; 1.70 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
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.
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.
PDB; 2OMG; X-ray; 1.52 A; A/C/E=90-110, B/D/F=25-54.
PDB; 2OMH; X-ray; 1.36 A; A/C/E=90-110, B/D/F=25-54.
PDB; 2OMI; X-ray; 2.24 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
PDB; 2OMQ; X-ray; 2.00 A; A/B/C/D=36-41.
PDB; 2QIU; X-ray; 2.00 A; A/C=89-110, B/D=25-54.
PDB; 2R34; X-ray; 2.25 A; A/C=89-110, B/D=25-54.
PDB; 2R35; X-ray; 2.08 A; A/C=89-110, B/D=25-54.
PDB; 2R36; X-ray; 2.00 A; A/C=89-110, B/D=25-54.
PDB; 2RN5; NMR; -; A=90-110, B=25-54.
PDB; 2VJZ; X-ray; 1.80 A; A/C=90-110, B/D=25-54.
PDB; 2VK0; X-ray; 2.20 A; A/C=90-110, B/D=25-54.
PDB; 2W44; X-ray; 2.00 A; A/C/E=94-110, B/D/F=25-53.
PDB; 2WBY; X-ray; 2.60 A; C/E=90-109, D/F=25-43.
PDB; 2WC0; X-ray; 2.80 A; C/E=90-110, D/F=25-54.
PDB; 2WRU; X-ray; 1.57 A; A=90-110, B=25-50.
PDB; 2WRV; X-ray; 2.15 A; A=90-110, B=25-50.
PDB; 2WRW; X-ray; 2.41 A; A=90-110, B=25-50.
PDB; 2WRX; X-ray; 1.50 A; A/C=90-110, B/D=25-54.
PDB; 2WS0; X-ray; 2.10 A; A=90-110, B=25-54.
PDB; 2WS1; X-ray; 1.60 A; A=90-110, B=25-54.
PDB; 2WS4; X-ray; 1.90 A; A=90-110, B=25-50.
PDB; 2WS6; X-ray; 1.50 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
PDB; 2WS7; X-ray; 2.59 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-50.
PDB; 3AIY; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
PDB; 3BXQ; X-ray; 1.30 A; A/C=90-110, B/D=25-54.
PDB; 3E7Y; X-ray; 1.60 A; A/C=90-110, B/D=25-53.
PDB; 3E7Z; X-ray; 1.70 A; A/C=90-110, B/D=25-53.
PDB; 3EXX; X-ray; 1.35 A; A/C=90-110, B/D=25-54.
PDB; 3FQ9; X-ray; 1.35 A; A/C=91-110, B/D=25-54.
PDB; 3HYD; X-ray; 1.00 A; A=35-41.
PDB; 3I3Z; X-ray; 1.60 A; A=90-110, B=25-54.
PDB; 3I40; X-ray; 1.85 A; A=90-110, B=25-54.
PDB; 3ILG; X-ray; 1.90 A; A/C=90-110, B/D=25-54.
PDB; 3INC; X-ray; 1.85 A; A/C=90-110, B/D=25-54.
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.
PDB; 3JSD; X-ray; 2.50 A; A/C=90-110, B/D=25-54.
PDB; 3KQ6; X-ray; 1.90 A; A/C=90-110, B/D=25-54.
PDB; 3P2X; X-ray; 2.00 A; A/C=90-110, B/D=25-54.
PDB; 3P33; X-ray; 2.30 A; A/C/E/G=90-110, B/D/F/H=25-54.
PDB; 3Q6E; X-ray; 2.05 A; A/C=90-110, B/D=25-54.
PDB; 3ROV; X-ray; 2.30 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
PDB; 3TT8; X-ray; 1.12 A; A/C=90-110, B/D=25-54.
PDB; 3U4N; X-ray; 1.98 A; A=90-110, B=25-53.
PDB; 3UTQ; X-ray; 1.67 A; C=15-24.
PDB; 3UTS; X-ray; 2.71 A; C/H=15-24.
PDB; 3UTT; X-ray; 2.60 A; C/H=15-24.
PDB; 3V19; X-ray; 2.00 A; A/C=90-110, B/D=25-54.
PDB; 3V1G; X-ray; 2.20 A; A/C=90-110, B/D=25-54.
PDB; 3W11; X-ray; 3.90 A; A=90-110, B=25-54.
PDB; 3W12; X-ray; 4.30 A; A=90-110, B=25-50.
PDB; 3W13; X-ray; 4.30 A; A=90-110, B=25-50.
PDB; 3W7Y; X-ray; 0.92 A; A/C=90-110, B/D=25-54.
PDB; 3W7Z; X-ray; 1.15 A; A/C=90-110, B/D=25-54.
PDB; 3W80; X-ray; 1.40 A; A/C/E/G=90-110, B/D/F/H=25-54.
PDB; 3ZI3; X-ray; 1.70 A; A=90-110, B=25-54.
PDB; 3ZQR; X-ray; 1.90 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
PDB; 3ZS2; X-ray; 1.97 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
PDB; 3ZU1; X-ray; 1.60 A; A/C=90-110, B/D=25-54.
PDB; 4AIY; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
PDB; 4AJX; X-ray; 1.20 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-53.
PDB; 4AJZ; X-ray; 1.80 A; A/C=90-110, B/D=25-53.
PDB; 4AK0; X-ray; 2.28 A; A=90-110, B=25-53.
PDB; 4AKJ; X-ray; 2.01 A; A/C=90-110, B/D=25-53.
PDB; 4CXL; X-ray; 1.50 A; A=90-110, B=25-54.
PDB; 4CXN; X-ray; 1.70 A; A=90-110, B=25-54.
PDB; 4CY7; X-ray; 1.40 A; A/C=90-110, B/D=25-54.
PDB; 4EFX; X-ray; 1.98 A; A/C=90-110, B/D=25-52.
PDB; 4EWW; X-ray; 2.30 A; A/C=90-110, B/D=25-54.
PDB; 4EWX; X-ray; 2.20 A; A/C=90-110, B/D=25-54.
PDB; 4EWZ; X-ray; 1.79 A; A/C=90-110, B/D=25-54.
PDB; 4EX0; X-ray; 1.86 A; A/C=90-110, B/D=25-54.
PDB; 4EX1; X-ray; 1.66 A; A/C=90-110, B/D=25-54.
PDB; 4EXX; X-ray; 1.55 A; A/C=90-110, B/D=25-54.
PDB; 4EY1; X-ray; 1.47 A; A/C=90-110, B/D=25-54.
PDB; 4EY9; X-ray; 1.47 A; A/C=90-110, B/D=25-54.
PDB; 4EYD; X-ray; 1.47 A; A/C=90-110, B/D=25-54.
PDB; 4EYN; X-ray; 1.53 A; A/C=90-110, B/D=25-54.
PDB; 4EYP; X-ray; 1.59 A; A/C=90-110, B/D=25-54.
PDB; 4F0N; X-ray; 1.68 A; A/C=90-110, B/D=25-54.
PDB; 4F0O; X-ray; 1.67 A; A/C=90-110, B/D=25-54.
PDB; 4F1A; X-ray; 1.80 A; A/C=90-110, B/D=25-54.
PDB; 4F1B; X-ray; 1.59 A; A/C=90-110, B/D=25-54.
PDB; 4F1C; X-ray; 1.70 A; A/C=90-110, B/D=25-54.
PDB; 4F1D; X-ray; 1.64 A; A/C=90-110, B/D=25-54.
PDB; 4F1F; X-ray; 1.68 A; A/C=90-110, B/D=25-54.
PDB; 4F1G; X-ray; 1.64 A; A/C=90-110, B/D=25-54.
PDB; 4F4T; X-ray; 1.64 A; A/C=90-110, B/D=25-54.
PDB; 4F4V; X-ray; 1.64 A; A/C=90-110, B/D=25-54.
PDB; 4F51; X-ray; 1.64 A; A/C=90-110, B/D=25-54.
PDB; 4F8F; X-ray; 1.68 A; A/C=90-110, B/D=25-54.
PDB; 4FG3; X-ray; 2.00 A; A/C=90-110, B/D=25-54.
PDB; 4FKA; X-ray; 1.08 A; A/C=90-110, B/D=25-54.
PDB; 4GBC; X-ray; 1.78 A; A/C=90-110, B/D=25-54.
PDB; 4GBI; X-ray; 2.50 A; A/C=90-110, B/D=25-54.
PDB; 4GBK; X-ray; 2.40 A; A/C=90-110, B/D=25-54.
PDB; 4GBL; X-ray; 2.50 A; A/C=90-110, B/D=25-54.
PDB; 4GBN; X-ray; 1.87 A; A/C=90-110, B/D=25-54.
PDB; 4IUZ; X-ray; 1.60 A; A=90-110, B=25-54.
PDB; 4IYD; X-ray; 1.66 A; A=90-109, B=25-53.
PDB; 4IYF; X-ray; 1.80 A; A=90-109, B=25-53.
PDB; 4NIB; X-ray; 1.40 A; A=90-110, B=25-54.
PDB; 4OGA; X-ray; 3.50 A; A=90-110, B=25-54.
PDB; 4P65; X-ray; 1.50 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
PDB; 4RXW; X-ray; 1.73 A; A/C=90-110, B/D=25-54.
PDB; 4UNE; X-ray; 1.59 A; A/C=90-110, B/D=25-54.
PDB; 4UNG; X-ray; 1.81 A; A/C=90-110, B/D=25-54.
PDB; 4UNH; X-ray; 2.75 A; A=90-110, B=25-54.
PDB; 4WDI; X-ray; 2.31 A; C/F=39-47.
PDB; 4XC4; X-ray; 1.50 A; A/C=90-110, B/D=25-54.
PDB; 4Y19; X-ray; 2.50 A; C=75-90.
PDB; 4Y1A; X-ray; 4.00 A; C=75-90.
PDB; 4Z76; X-ray; 1.88 A; C/F=39-46.
PDB; 4Z77; X-ray; 1.85 A; C/F=39-47.
PDB; 4Z78; X-ray; 2.30 A; C/F/I=39-48.
PDB; 5AIY; NMR; -; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
PDB; 5BOQ; X-ray; 1.70 A; A/C/E/G=90-110, B/D/F/H=25-54.
PDB; 5BPO; X-ray; 1.90 A; A/C=90-110, B/D=25-54.
PDB; 5BQQ; X-ray; 1.54 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-50.
PDB; 5BTS; X-ray; 1.77 A; A=90-110, B=25-54.
PDB; 5C0D; X-ray; 1.68 A; C=15-24.
PDB; 5CJO; X-ray; 3.29 A; a=90-109.
PDB; 5CNY; X-ray; 1.70 A; A/C=90-110, B/D=25-54.
PDB; 5CO2; X-ray; 1.70 A; A/C=90-110, B/D=25-54.
PDB; 5CO6; X-ray; 1.80 A; A/C=90-110, B/D=25-54.
PDB; 5CO9; X-ray; 1.92 A; A/C=90-110, B/D=25-54.
PDB; 5E7W; X-ray; 0.95 A; A/C=90-110, B/D=25-54.
PDB; 5EMS; X-ray; 2.30 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-52.
PDB; 5EN9; X-ray; 1.50 A; A=90-110, B=25-54.
PDB; 5ENA; X-ray; 1.35 A; A=90-110, B=25-54.
PDB; 5HPR; X-ray; 1.33 A; A=90-110, B=25-54.
PDB; 5HPU; X-ray; 2.20 A; A/C=90-110, B/D=25-54.
PDB; 5HQI; X-ray; 0.97 A; A=90-110, B=25-54.
PDB; 5HRQ; X-ray; 1.28 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
PDB; 5HYJ; X-ray; 3.06 A; C/H=15-24.
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.
PDB; 5MHD; NMR; -; A=90-110, B=25-55.
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.
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.
PDB; 5MWQ; NMR; -; A=90-110, B=25-56.
PDB; 5T7R; X-ray; 1.55 A; A/C=90-110, B/D=25-54.
PDB; 5UDP; X-ray; 1.35 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
PDB; 5UOZ; X-ray; 1.17 A; A=90-110, B=25-54.
PDB; 5UQA; X-ray; 1.31 A; A/C/E/G/I/K=90-110, B/D/F/H/J/L=25-54.
PDB; 5URT; X-ray; 1.18 A; A=90-110, B=25-54.
PDB; 5URU; X-ray; 2.41 A; A/C/E/G=90-110, B/D/F/H=25-54.
PDB; 5USP; X-ray; 1.17 A; A=90-110, B=25-54.
PDB; 5USS; X-ray; 2.06 A; A/C=90-110, B/D=25-54.
PDB; 5USV; X-ray; 1.30 A; A=90-110, B=25-54.
PDB; 5UU2; X-ray; 1.22 A; A=90-110, B=25-54.
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.
PDB; 5UU4; X-ray; 1.97 A; A/C=90-110, B/D=25-54.
PDB; 5VIZ; X-ray; 1.70 A; A=90-109, B=25-53.
PDB; 5WBT; NMR; -; A=25-54, A=90-110.
PDB; 5WDM; X-ray; 2.80 A; A/B/C/D/E/F=25-110.
PDB; 5WOB; X-ray; 3.95 A; a/b/c/d/e/f/g/h=90-109.
PDB; 6B3Q; EM; 3.70 A; a/b=1-110.
PDB; 6B70; EM; 3.70 A; a/c=1-110.
PDB; 6BFC; EM; 3.70 A; a/b=1-110.
PDB; 6CE7; EM; 7.40 A; N=90-110.
PDB; 6CE9; EM; 4.30 A; K/N=90-110.
PDB; 6CEB; EM; 4.70 A; K/N=90-110.
PDBsum; 1A7F; -.
PDBsum; 1AI0; -.
PDBsum; 1AIY; -.
PDBsum; 1B9E; -.
PDBsum; 1BEN; -.
PDBsum; 1EFE; -.
PDBsum; 1EV3; -.
PDBsum; 1EV6; -.
PDBsum; 1EVR; -.
PDBsum; 1FU2; -.
PDBsum; 1FUB; -.
PDBsum; 1G7A; -.
PDBsum; 1G7B; -.
PDBsum; 1GUJ; -.
PDBsum; 1HIQ; -.
PDBsum; 1HIS; -.
PDBsum; 1HIT; -.
PDBsum; 1HLS; -.
PDBsum; 1HTV; -.
PDBsum; 1HUI; -.
PDBsum; 1IOG; -.
PDBsum; 1IOH; -.
PDBsum; 1J73; -.
PDBsum; 1JCA; -.
PDBsum; 1JCO; -.
PDBsum; 1JK8; -.
PDBsum; 1K3M; -.
PDBsum; 1KMF; -.
PDBsum; 1LKQ; -.
PDBsum; 1LPH; -.
PDBsum; 1MHI; -.
PDBsum; 1MHJ; -.
PDBsum; 1MSO; -.
PDBsum; 1OS3; -.
PDBsum; 1OS4; -.
PDBsum; 1Q4V; -.
PDBsum; 1QIY; -.
PDBsum; 1QIZ; -.
PDBsum; 1QJ0; -.
PDBsum; 1RWE; -.
PDBsum; 1SF1; -.
PDBsum; 1SJT; -.
PDBsum; 1SJU; -.
PDBsum; 1T0C; -.
PDBsum; 1T1K; -.
PDBsum; 1T1P; -.
PDBsum; 1T1Q; -.
PDBsum; 1TRZ; -.
PDBsum; 1TYL; -.
PDBsum; 1TYM; -.
PDBsum; 1UZ9; -.
PDBsum; 1VKT; -.
PDBsum; 1W8P; -.
PDBsum; 1XDA; -.
PDBsum; 1XGL; -.
PDBsum; 1XW7; -.
PDBsum; 1ZEG; -.
PDBsum; 1ZEH; -.
PDBsum; 1ZNJ; -.
PDBsum; 2AIY; -.
PDBsum; 2C8Q; -.
PDBsum; 2C8R; -.
PDBsum; 2CEU; -.
PDBsum; 2G54; -.
PDBsum; 2G56; -.
PDBsum; 2H67; -.
PDBsum; 2HH4; -.
PDBsum; 2HHO; -.
PDBsum; 2HIU; -.
PDBsum; 2JMN; -.
PDBsum; 2JUM; -.
PDBsum; 2JUU; -.
PDBsum; 2JUV; -.
PDBsum; 2JV1; -.
PDBsum; 2JZQ; -.
PDBsum; 2K91; -.
PDBsum; 2K9R; -.
PDBsum; 2KJJ; -.
PDBsum; 2KJU; -.
PDBsum; 2KQP; -.
PDBsum; 2KQQ; -.
PDBsum; 2KXK; -.
PDBsum; 2L1Y; -.
PDBsum; 2L1Z; -.
PDBsum; 2LGB; -.
PDBsum; 2LWZ; -.
PDBsum; 2M1D; -.
PDBsum; 2M1E; -.
PDBsum; 2M2M; -.
PDBsum; 2M2N; -.
PDBsum; 2M2O; -.
PDBsum; 2M2P; -.
PDBsum; 2MLI; -.
PDBsum; 2MPG; -.
PDBsum; 2MPI; -.
PDBsum; 2MVC; -.
PDBsum; 2MVD; -.
PDBsum; 2N2V; -.
PDBsum; 2N2W; -.
PDBsum; 2N2X; -.
PDBsum; 2OLY; -.
PDBsum; 2OLZ; -.
PDBsum; 2OM0; -.
PDBsum; 2OM1; -.
PDBsum; 2OMG; -.
PDBsum; 2OMH; -.
PDBsum; 2OMI; -.
PDBsum; 2OMQ; -.
PDBsum; 2QIU; -.
PDBsum; 2R34; -.
PDBsum; 2R35; -.
PDBsum; 2R36; -.
PDBsum; 2RN5; -.
PDBsum; 2VJZ; -.
PDBsum; 2VK0; -.
PDBsum; 2W44; -.
PDBsum; 2WBY; -.
PDBsum; 2WC0; -.
PDBsum; 2WRU; -.
PDBsum; 2WRV; -.
PDBsum; 2WRW; -.
PDBsum; 2WRX; -.
PDBsum; 2WS0; -.
PDBsum; 2WS1; -.
PDBsum; 2WS4; -.
PDBsum; 2WS6; -.
PDBsum; 2WS7; -.
PDBsum; 3AIY; -.
PDBsum; 3BXQ; -.
PDBsum; 3E7Y; -.
PDBsum; 3E7Z; -.
PDBsum; 3EXX; -.
PDBsum; 3FQ9; -.
PDBsum; 3HYD; -.
PDBsum; 3I3Z; -.
PDBsum; 3I40; -.
PDBsum; 3ILG; -.
PDBsum; 3INC; -.
PDBsum; 3IR0; -.
PDBsum; 3JSD; -.
PDBsum; 3KQ6; -.
PDBsum; 3P2X; -.
PDBsum; 3P33; -.
PDBsum; 3Q6E; -.
PDBsum; 3ROV; -.
PDBsum; 3TT8; -.
PDBsum; 3U4N; -.
PDBsum; 3UTQ; -.
PDBsum; 3UTS; -.
PDBsum; 3UTT; -.
PDBsum; 3V19; -.
PDBsum; 3V1G; -.
PDBsum; 3W11; -.
PDBsum; 3W12; -.
PDBsum; 3W13; -.
PDBsum; 3W7Y; -.
PDBsum; 3W7Z; -.
PDBsum; 3W80; -.
PDBsum; 3ZI3; -.
PDBsum; 3ZQR; -.
PDBsum; 3ZS2; -.
PDBsum; 3ZU1; -.
PDBsum; 4AIY; -.
PDBsum; 4AJX; -.
PDBsum; 4AJZ; -.
PDBsum; 4AK0; -.
PDBsum; 4AKJ; -.
PDBsum; 4CXL; -.
PDBsum; 4CXN; -.
PDBsum; 4CY7; -.
PDBsum; 4EFX; -.
PDBsum; 4EWW; -.
PDBsum; 4EWX; -.
PDBsum; 4EWZ; -.
PDBsum; 4EX0; -.
PDBsum; 4EX1; -.
PDBsum; 4EXX; -.
PDBsum; 4EY1; -.
PDBsum; 4EY9; -.
PDBsum; 4EYD; -.
PDBsum; 4EYN; -.
PDBsum; 4EYP; -.
PDBsum; 4F0N; -.
PDBsum; 4F0O; -.
PDBsum; 4F1A; -.
PDBsum; 4F1B; -.
PDBsum; 4F1C; -.
PDBsum; 4F1D; -.
PDBsum; 4F1F; -.
PDBsum; 4F1G; -.
PDBsum; 4F4T; -.
PDBsum; 4F4V; -.
PDBsum; 4F51; -.
PDBsum; 4F8F; -.
PDBsum; 4FG3; -.
PDBsum; 4FKA; -.
PDBsum; 4GBC; -.
PDBsum; 4GBI; -.
PDBsum; 4GBK; -.
PDBsum; 4GBL; -.
PDBsum; 4GBN; -.
PDBsum; 4IUZ; -.
PDBsum; 4IYD; -.
PDBsum; 4IYF; -.
PDBsum; 4NIB; -.
PDBsum; 4OGA; -.
PDBsum; 4P65; -.
PDBsum; 4RXW; -.
PDBsum; 4UNE; -.
PDBsum; 4UNG; -.
PDBsum; 4UNH; -.
PDBsum; 4WDI; -.
PDBsum; 4XC4; -.
PDBsum; 4Y19; -.
PDBsum; 4Y1A; -.
PDBsum; 4Z76; -.
PDBsum; 4Z77; -.
PDBsum; 4Z78; -.
PDBsum; 5AIY; -.
PDBsum; 5BOQ; -.
PDBsum; 5BPO; -.
PDBsum; 5BQQ; -.
PDBsum; 5BTS; -.
PDBsum; 5C0D; -.
PDBsum; 5CJO; -.
PDBsum; 5CNY; -.
PDBsum; 5CO2; -.
PDBsum; 5CO6; -.
PDBsum; 5CO9; -.
PDBsum; 5E7W; -.
PDBsum; 5EMS; -.
PDBsum; 5EN9; -.
PDBsum; 5ENA; -.
PDBsum; 5HPR; -.
PDBsum; 5HPU; -.
PDBsum; 5HQI; -.
PDBsum; 5HRQ; -.
PDBsum; 5HYJ; -.
PDBsum; 5MAM; -.
PDBsum; 5MHD; -.
PDBsum; 5MT3; -.
PDBsum; 5MT9; -.
PDBsum; 5MWQ; -.
PDBsum; 5T7R; -.
PDBsum; 5UDP; -.
PDBsum; 5UOZ; -.
PDBsum; 5UQA; -.
PDBsum; 5URT; -.
PDBsum; 5URU; -.
PDBsum; 5USP; -.
PDBsum; 5USS; -.
PDBsum; 5USV; -.
PDBsum; 5UU2; -.
PDBsum; 5UU3; -.
PDBsum; 5UU4; -.
PDBsum; 5VIZ; -.
PDBsum; 5WBT; -.
PDBsum; 5WDM; -.
PDBsum; 5WOB; -.
PDBsum; 6B3Q; -.
PDBsum; 6B70; -.
PDBsum; 6BFC; -.
PDBsum; 6CE7; -.
PDBsum; 6CE9; -.
PDBsum; 6CEB; -.
ProteinModelPortal; P01308; -.
SMR; P01308; -.
BioGrid; 109842; 13.
DIP; DIP-6024N; -.
IntAct; P01308; 11.
MINT; P01308; -.
STRING; 9606.ENSP00000250971; -.
ChEMBL; CHEMBL5881; -.
DrugBank; DB01776; M-Cresol.
DrugBank; DB08231; MYRISTIC ACID.
Allergome; 2121; Hom s Insulin.
CarbonylDB; P01308; -.
iPTMnet; P01308; -.
PhosphoSitePlus; P01308; -.
BioMuta; INS; -.
DMDM; 124617; -.
PaxDb; P01308; -.
PeptideAtlas; P01308; -.
PRIDE; P01308; -.
ProteomicsDB; 51374; -.
DNASU; 3630; -.
Ensembl; ENST00000250971; ENSP00000250971; ENSG00000254647. [P01308-1]
Ensembl; ENST00000381330; ENSP00000370731; ENSG00000254647. [P01308-1]
Ensembl; ENST00000397262; ENSP00000380432; ENSG00000254647. [P01308-1]
GeneID; 3630; -.
KEGG; hsa:3630; -.
UCSC; uc001lvn.3; human. [P01308-1]
CTD; 3630; -.
DisGeNET; 3630; -.
EuPathDB; HostDB:ENSG00000254647.6; -.
GeneCards; INS; -.
GeneReviews; INS; -.
HGNC; HGNC:6081; INS.
HPA; CAB000048; -.
HPA; CAB012098; -.
HPA; CAB053843; -.
HPA; HPA004932; -.
MalaCards; INS; -.
MIM; 125852; phenotype.
MIM; 176730; gene.
MIM; 606176; phenotype.
MIM; 613370; phenotype.
MIM; 616214; phenotype.
neXtProt; NX_P01308; -.
OpenTargets; ENSG00000254647; -.
Orphanet; 552; MODY.
Orphanet; 99885; Permanent neonatal diabetes mellitus.
PharmGKB; PA201; -.
eggNOG; ENOG410J0XC; Eukaryota.
eggNOG; ENOG4111VJB; LUCA.
GeneTree; ENSGT00390000015440; -.
HOGENOM; HOG000261669; -.
HOVERGEN; HBG006137; -.
InParanoid; P01308; -.
KO; K04526; -.
OMA; PQHLCGS; -.
OrthoDB; EOG091G0H56; -.
PhylomeDB; P01308; -.
TreeFam; TF332820; -.
BioCyc; MetaCyc:MONOMER-16190; -.
Reactome; R-HSA-210745; Regulation of gene expression in beta cells.
Reactome; R-HSA-264876; Insulin processing.
Reactome; R-HSA-422085; Synthesis, secretion, and deacylation of Ghrelin.
Reactome; R-HSA-422356; Regulation of insulin secretion.
Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-74713; IRS activation.
Reactome; R-HSA-74749; Signal attenuation.
Reactome; R-HSA-74751; Insulin receptor signalling cascade.
Reactome; R-HSA-74752; Signaling by Insulin receptor.
Reactome; R-HSA-77387; Insulin receptor recycling.
Reactome; R-HSA-977225; Amyloid fiber formation.
SignaLink; P01308; -.
SIGNOR; P01308; -.
ChiTaRS; INS; human.
EvolutionaryTrace; P01308; -.
GeneWiki; Insulin; -.
GenomeRNAi; 3630; -.
PMAP-CutDB; P01308; -.
PRO; PR:P01308; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000254647; -.
ExpressionAtlas; P01308; baseline and differential.
Genevisible; P01308; HS.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
GO; GO:0031904; C:endosome lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0030133; C:transport vesicle; TAS:Reactome.
GO; GO:0005179; F:hormone activity; IMP:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005158; F:insulin receptor binding; IDA:UniProtKB.
GO; GO:0005159; F:insulin-like growth factor receptor binding; IPI:BHF-UCL.
GO; GO:0002020; F:protease binding; IPI:UniProtKB.
GO; GO:0032148; P:activation of protein kinase B activity; IDA:BHF-UCL.
GO; GO:0006953; P:acute-phase response; IDA:BHF-UCL.
GO; GO:0046631; P:alpha-beta T cell activation; IDA:UniProtKB.
GO; GO:0007267; P:cell-cell signaling; IC:UniProtKB.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0050890; P:cognition; TAS:ARUK-UCL.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0055089; P:fatty acid homeostasis; IMP:BHF-UCL.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0042593; P:glucose homeostasis; IMP:BHF-UCL.
GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
GO; GO:0008286; P:insulin receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0000165; P:MAPK cascade; IDA:BHF-UCL.
GO; GO:0002674; P:negative regulation of acute inflammatory response; IDA:BHF-UCL.
GO; GO:0097756; P:negative regulation of blood vessel diameter; NAS:UniProtKB.
GO; GO:0045922; P:negative regulation of fatty acid metabolic process; IMP:BHF-UCL.
GO; GO:2000252; P:negative regulation of feeding behavior; IDA:DFLAT.
GO; GO:0045721; P:negative regulation of gluconeogenesis; NAS:BHF-UCL.
GO; GO:0045818; P:negative regulation of glycogen catabolic process; IMP:BHF-UCL.
GO; GO:0050995; P:negative regulation of lipid catabolic process; IMP:AgBase.
GO; GO:0033861; P:negative regulation of NAD(P)H oxidase activity; IDA:BHF-UCL.
GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; NAS:BHF-UCL.
GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:UniProtKB.
GO; GO:0032460; P:negative regulation of protein oligomerization; IDA:UniProtKB.
GO; GO:0050709; P:negative regulation of protein secretion; IDA:BHF-UCL.
GO; GO:0045861; P:negative regulation of proteolysis; IMP:BHF-UCL.
GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IGI:ARUK-UCL.
GO; GO:0060266; P:negative regulation of respiratory burst involved in inflammatory response; IDA:BHF-UCL.
GO; GO:1990535; P:neuron projection maintenance; IGI:ARUK-UCL.
GO; GO:0097755; P:positive regulation of blood vessel diameter; NAS:UniProtKB.
GO; GO:0090336; P:positive regulation of brown fat cell differentiation; TAS:BHF-UCL.
GO; GO:0045597; P:positive regulation of cell differentiation; NAS:BHF-UCL.
GO; GO:0030307; P:positive regulation of cell growth; NAS:BHF-UCL.
GO; GO:0030335; P:positive regulation of cell migration; ISS:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:0032270; P:positive regulation of cellular protein metabolic process; IMP:BHF-UCL.
GO; GO:0050715; P:positive regulation of cytokine secretion; IDA:UniProtKB.
GO; GO:1902952; P:positive regulation of dendritic spine maintenance; IGI:ARUK-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IGI:BHF-UCL.
GO; GO:0046326; P:positive regulation of glucose import; IDA:UniProtKB.
GO; GO:2001275; P:positive regulation of glucose import in response to insulin stimulus; IDA:UniProtKB.
GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IDA:BHF-UCL.
GO; GO:0045821; P:positive regulation of glycolytic process; IDA:BHF-UCL.
GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0046889; P:positive regulation of lipid biosynthetic process; NAS:BHF-UCL.
GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; TAS:ARUK-UCL.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:BHF-UCL.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
GO; GO:0010750; P:positive regulation of nitric oxide mediated signal transduction; IMP:UniProtKB.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; NAS:UniProtKB.
GO; GO:0090277; P:positive regulation of peptide hormone secretion; TAS:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:BHF-UCL.
GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISS:BHF-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:BHF-UCL.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IDA:BHF-UCL.
GO; GO:0060267; P:positive regulation of respiratory burst; IDA:BHF-UCL.
GO; GO:0006521; P:regulation of cellular amino acid metabolic process; IMP:BHF-UCL.
GO; GO:0032880; P:regulation of protein localization; IDA:BHF-UCL.
GO; GO:1903076; P:regulation of protein localization to plasma membrane; IGI:ARUK-UCL.
GO; GO:0050708; P:regulation of protein secretion; IDA:UniProtKB.
GO; GO:0048167; P:regulation of synaptic plasticity; TAS:ARUK-UCL.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:BHF-UCL.
GO; GO:0022898; P:regulation of transmembrane transporter activity; IDA:BHF-UCL.
GO; GO:0042060; P:wound healing; IDA:BHF-UCL.
InterPro; IPR004825; Insulin.
InterPro; IPR016179; Insulin-like.
InterPro; IPR036438; Insulin-like_sf.
InterPro; IPR022353; Insulin_CS.
InterPro; IPR022352; Insulin_family.
Pfam; PF00049; Insulin; 1.
PRINTS; PR00277; INSULIN.
PRINTS; PR00276; INSULINFAMLY.
SMART; SM00078; IlGF; 1.
SUPFAM; SSF56994; SSF56994; 1.
PROSITE; PS00262; INSULIN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Carbohydrate metabolism;
Cleavage on pair of basic residues; Complete proteome;
Diabetes mellitus; Direct protein sequencing; Disease mutation;
Disulfide bond; Glucose metabolism; Hormone; Pharmaceutical;
Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 24 {ECO:0000269|PubMed:14426955}.
PEPTIDE 25 54 Insulin B chain.
/FTId=PRO_0000015819.
PROPEP 57 87 C peptide.
/FTId=PRO_0000015820.
PEPTIDE 90 110 Insulin A chain.
/FTId=PRO_0000015821.
DISULFID 31 96 Interchain (between B and A chains).
{ECO:0000244|PDB:1AI0,
ECO:0000244|PDB:1AIY,
ECO:0000244|PDB:1HIQ,
ECO:0000244|PDB:1MHI,
ECO:0000244|PDB:2MVC,
ECO:0000244|PDB:2MVD,
ECO:0000269|PubMed:1433291,
ECO:0000269|PubMed:25423173,
ECO:0000269|PubMed:8421693}.
DISULFID 43 109 Interchain (between B and A chains).
{ECO:0000244|PDB:1AI0,
ECO:0000244|PDB:1AIY,
ECO:0000244|PDB:1HIQ,
ECO:0000244|PDB:1MHI,
ECO:0000244|PDB:2MVC,
ECO:0000244|PDB:2MVD,
ECO:0000269|PubMed:1433291,
ECO:0000269|PubMed:25423173,
ECO:0000269|PubMed:8421693}.
DISULFID 95 100 {ECO:0000244|PDB:1AI0,
ECO:0000244|PDB:1AIY,
ECO:0000244|PDB:1HIQ,
ECO:0000244|PDB:1MHI,
ECO:0000244|PDB:2MVC,
ECO:0000244|PDB:2MVD,
ECO:0000269|PubMed:1433291,
ECO:0000269|PubMed:25423173,
ECO:0000269|PubMed:5101771,
ECO:0000269|PubMed:8421693,
ECO:0000269|PubMed:9235985}.
VARIANT 6 6 R -> C (in MODY10; dbSNP:rs121908278).
{ECO:0000269|PubMed:18162506}.
/FTId=VAR_063721.
VARIANT 6 6 R -> H (in MODY10; dbSNP:rs121908259).
{ECO:0000269|PubMed:20226046}.
/FTId=VAR_063722.
VARIANT 24 24 A -> D (in PNDM; dbSNP:rs80356663).
{ECO:0000269|PubMed:17855560,
ECO:0000269|PubMed:18162506}.
/FTId=VAR_063723.
VARIANT 29 29 H -> D (in PNDM; dbSNP:rs121908272).
{ECO:0000269|PubMed:18162506}.
/FTId=VAR_063724.
VARIANT 32 32 G -> R (in PNDM; dbSNP:rs80356664).
{ECO:0000269|PubMed:17855560,
ECO:0000269|PubMed:18162506}.
/FTId=VAR_063725.
VARIANT 32 32 G -> S (in PNDM; dbSNP:rs80356664).
{ECO:0000269|PubMed:17855560,
ECO:0000269|PubMed:18162506}.
/FTId=VAR_063726.
VARIANT 34 34 H -> D (in HPRI; Providence;
dbSNP:rs121918101).
{ECO:0000269|PubMed:3470784}.
/FTId=VAR_003971.
VARIANT 35 35 L -> P (in PNDM; dbSNP:rs121908273).
{ECO:0000269|PubMed:18162506}.
/FTId=VAR_063727.
VARIANT 43 43 C -> G (in PNDM; dbSNP:rs80356666).
{ECO:0000269|PubMed:17855560,
ECO:0000269|PubMed:18162506}.
/FTId=VAR_063728.
VARIANT 46 46 R -> Q (in MODY10; reduces binding
affinity to INSR; reduces biological
activity; reduces folding properties;
dbSNP:rs121908260).
{ECO:0000269|PubMed:18192540,
ECO:0000269|PubMed:20226046,
ECO:0000269|PubMed:25423173}.
/FTId=VAR_063729.
VARIANT 47 47 G -> V (in PNDM; dbSNP:rs80356667).
{ECO:0000269|PubMed:17855560,
ECO:0000269|PubMed:18162506}.
/FTId=VAR_063730.
VARIANT 48 48 F -> C (in PNDM; dbSNP:rs80356668).
{ECO:0000269|PubMed:17855560,
ECO:0000269|PubMed:18162506}.
/FTId=VAR_063731.
VARIANT 48 48 F -> S (associated with diabetes mellitus
type-II; Los-Angeles; dbSNP:rs80356668).
{ECO:0000269|PubMed:6312455,
ECO:0000269|PubMed:6424111,
ECO:0000269|PubMed:8421693}.
/FTId=VAR_003972.
VARIANT 49 49 F -> L (in Chicago; dbSNP:rs148685531).
{ECO:0000269|PubMed:6424111}.
/FTId=VAR_003973.
VARIANT 55 55 R -> C (in IDDM2; dbSNP:rs121908261).
{ECO:0000269|PubMed:18192540}.
/FTId=VAR_063732.
VARIANT 68 68 L -> M (in dbSNP:rs121908279).
{ECO:0000269|PubMed:18162506}.
/FTId=VAR_063733.
VARIANT 84 84 G -> R (in PNDM; uncertain pathological
significance; dbSNP:rs121908274).
{ECO:0000269|PubMed:18162506}.
/FTId=VAR_063734.
VARIANT 89 89 R -> C (in PNDM; dbSNP:rs80356669).
{ECO:0000269|PubMed:17855560,
ECO:0000269|PubMed:18162506}.
/FTId=VAR_063735.
VARIANT 89 89 R -> H (in HPRI; impairs post-
translational cleavage;
dbSNP:rs28933985).
{ECO:0000269|PubMed:2196279,
ECO:0000269|PubMed:4019786}.
/FTId=VAR_003974.
VARIANT 89 89 R -> L (in HPRI; Kyoto;
dbSNP:rs28933985).
{ECO:0000269|PubMed:1601997}.
/FTId=VAR_003975.
VARIANT 90 90 G -> C (in PNDM; dbSNP:rs80356670).
{ECO:0000269|PubMed:17855560,
ECO:0000269|PubMed:18162506}.
/FTId=VAR_063736.
VARIANT 92 92 V -> L (in Wakayama; dbSNP:rs121918102).
{ECO:0000269|PubMed:3537011}.
/FTId=VAR_003976.
VARIANT 96 96 C -> S (in PNDM; dbSNP:rs80356671).
{ECO:0000269|PubMed:18162506}.
/FTId=VAR_063737.
VARIANT 96 96 C -> Y (in PNDM; dbSNP:rs80356671).
{ECO:0000269|PubMed:17855560,
ECO:0000269|PubMed:18162506}.
/FTId=VAR_063738.
VARIANT 101 101 S -> C (in PNDM; dbSNP:rs121908276).
{ECO:0000269|PubMed:18162506}.
/FTId=VAR_063739.
VARIANT 103 103 Y -> C (in PNDM; dbSNP:rs121908277).
{ECO:0000269|PubMed:18162506}.
/FTId=VAR_063740.
VARIANT 108 108 Y -> C (in PNDM; dbSNP:rs80356672).
{ECO:0000269|PubMed:17855560,
ECO:0000269|PubMed:18162506}.
/FTId=VAR_063741.
STRAND 26 29 {ECO:0000244|PDB:4EFX}.
HELIX 33 43 {ECO:0000244|PDB:3W7Y}.
HELIX 44 46 {ECO:0000244|PDB:3W7Y}.
STRAND 48 50 {ECO:0000244|PDB:3W7Y}.
STRAND 56 58 {ECO:0000244|PDB:1EFE}.
TURN 59 66 {ECO:0000244|PDB:1T0C}.
STRAND 74 76 {ECO:0000244|PDB:1T0C}.
HELIX 79 81 {ECO:0000244|PDB:1T0C}.
TURN 84 86 {ECO:0000244|PDB:1T0C}.
HELIX 91 97 {ECO:0000244|PDB:3W7Y}.
STRAND 98 101 {ECO:0000244|PDB:4EFX}.
HELIX 102 106 {ECO:0000244|PDB:3W7Y}.
TURN 107 109 {ECO:0000244|PDB:1HIQ}.
SEQUENCE 110 AA; 11981 MW; C2C3B23B85E520E5 CRC64;
MALWMRLLPL LALLALWGPD PAAAFVNQHL CGSHLVEALY LVCGERGFFY TPKTRREAED
LQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC SLYQLENYCN


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