GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

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.
13-FEB-2019, entry version 244.
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;
P11142:HSPA8; NbExp=2; IntAct=EBI-20765227, EBI-351896;
P14735-1:IDE; NbExp=3; IntAct=EBI-7090529, EBI-15607031;
P06213-2:INSR; NbExp=3; IntAct=EBI-7090529, EBI-9984921;
-!- 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";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
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.
PDB; 6CK2; X-ray; 2.25 A; A/C=90-110, B/D=25-54.
PDB; 6HN5; EM; 3.20 A; A=90-110, B=25-54.
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; -.
PDBsum; 6CK2; -.
PDBsum; 6HN5; -.
ProteinModelPortal; P01308; -.
SMR; P01308; -.
BioGrid; 109842; 13.
DIP; DIP-6024N; -.
IntAct; P01308; 16.
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; -.
EPD; P01308; -.
jPOST; P01308; -.
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; GFFYSPK; -.
OrthoDB; 1438615at2759; -.
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-9615017; FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes.
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; Expressed in 72 organ(s), highest expression level in type B pancreatic cell.
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:endoplasmic reticulum 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: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 population 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: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:UniProtKB.
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; IDA: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: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


Related products :

Catalog number Product name Quantity
orb80481 Human Insulin protein Insulin Human Recombinant produced in E.coli is two chain, non-glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 5807 Dalton. Insulin is pur 25 mg
orb80483 Porcine Insulin protein Insulin Porcine is two chain, glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 5777 Dalton. The and chains are joined by two interchain d 25 mg
orb80482 Human Insulin Yeast protein Insulin Human Recombinant produced in Yeast is two chain, glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 5807 Dalton. Zinc content 2 mg
630-01461 Insulin ELISA, Porcine Porcine Insulin ELISA Kit to quantify Insulin using a sandwich enzyme immunoassay. In less than 4 hours, the Porcine Insulin ELISA Kit measures insulin quantities in as little 96tests
SCH-5329-4102 SYNTHETIC HUMAN INSULIN B CHAIN, Product Type Purified Protein, Specificity INSULIN, Target Species Human, Host N_A, Format Purified, Isotypes , Applications E, Clone 5 mg
5329-4102 SYNTHETIC HUMAN INSULIN B CHAIN, Product Type Purified Protein, Specificity INSULIN, Target Species Human, Host N_A, Format Purified, Isotypes , Applications E, Clone 5 mg
637-07113 Insulin Standard Solution, Rabbit (10ng_ml) Insulin is a hormone that is central to regulating carbohydrate and fat metabolism in the body. Insulin causes cells in the liver, muscle, and fat tissue t 5X500UL
630-07103 Insulin Standard Solution, Humster (10ng_ml) Insulin is a hormone that is central to regulating carbohydrate and fat metabolism in the body. Insulin causes cells in the liver, muscle, and fat tissue 5X500UL
637-01471 Insulin (T_type) ELISA, Rat Rat Insulin ELISA Kit is a reagent kit for quantitation of Insulin by sandwich  technique of enzyme immunoassay.   96tests
orb21787 Guinea Pig IgG Against Swine Insulin Polyclonal Purified IgG fraction of polyclonal guinea pig antiserum to swine insulin. Insulin is a hormone produced by the beta cells of the islets of Langerhans i 10 mg
orb21788 Guinea Pig IgG Against Swine Insulin Polyclonal Fluorescein isothiocyanate-conjugated IgG fraction of polyclonal guinea pig antiserum to swine insulin. Insulin is a hormone produced by the beta cells 1 ml
2I1-C7C9 Insulin (beta chain) 1 mg
KP1016 Insulin β Chain Peptide (15 - 23) 1 mg
RP20501 Insulin alpha-chain (1-13) 1,0mg
BMA1025 Insulin B chain, Monoclonal antibody 100 μg
RP21067 Insulin beta Chain Peptide (15-23)
10-783-79566 SYNTHETIC HUMAN INSULIN B CHAIN - 5 mg
SP2656a Insulin-like 6 (INSL 6) _ RIF-1 B-Chain, human
BMA1025 Insulin B chain Monoclonal Antibodie 100 μg
BPA1067 Insulin (B chain) Polyclonal Antibodie 100 μg
Y103558 Insulin (human) beta chain 1 mg
SP2656b Insulin-like 6 (INSL 6) _ RIF-1 B-Chain, human
ABS2556 SYNTHETIC HUMAN INSULIN B CHAIN 5 mg
SP2656a Insulin-like 6 (INSL 6) _ RIF-1 B-Chain, human 0.1 mg
SP2656b Insulin-like 6 (INSL 6) _ RIF-1 B-Chain, human 0.5 mg

Kits Elisa; taq POLYMERASE

Search in Google:

google

Share this page:
share on twitter rss feedsfacebookgoogle gentaur



Quick order!
Enter catalog number :


Gentaur; yes we can

Pathways :
WP1085: Insulin Signaling
WP1313: Insulin Signaling
WP1403: AMPK signaling
WP17: daf-2 or insulin signaling pathway
WP1789: Binding of RNA by Insulin-like Growth Factor-2 mRNA Binding Proteins (IGF2BPs/IMPs/VICKZs)
WP1830: Insulin Synthesis and Processing
WP1899: Regulation of Insulin-like Growth Factor (IGF) Activity by Insulin-like Growth Factor Binding Proteins (IGFBPs)
WP1913: Signaling by Insulin receptor
WP2047: Insulin Leptin Adiponectin Resistin
WP439: Insulin Signaling
WP481: Insulin Signaling
WP578: Leptin Insulin Overlap
WP65: Insulin Signaling
WP731: Sterol regulatory element binding protein related
WP743: Insulin Signaling
WP847: Insulin Signaling
WP966: Insulin Signaling
WP1002: Electron Transport Chain
WP111: Electron Transport Chain
WP1119: Electron Transport Chain
WP1339: Electron Transport Chain
WP1502: Mitochondrial biogenesis
WP1614: 1- and 2-Methylnaphthalene degradation
WP1626: Benzoate degradation via CoA ligation
WP1633: Bisphenol A degradation

Related Genes :
[INS] Insulin [Cleaved into: Insulin B chain; Insulin A chain]
[IGF1R] Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain]
[Igf1r] Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain]
[Igf1r] Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain]
[IGF1R] Insulin-like growth factor 1 receptor (EC 2.7.10.1) (Insulin-like growth factor I receptor) (IGF-I receptor) (CD antigen CD221) [Cleaved into: Insulin-like growth factor 1 receptor alpha chain; Insulin-like growth factor 1 receptor beta chain] (Fragment)
[INSL5 UNQ156/PRO182] Insulin-like peptide INSL5 (Insulin-like peptide 5) [Cleaved into: Insulin-like peptide INSL5 B chain; Insulin-like peptide INSL5 A chain]
[InR dinr Dir-a Inr-a CG18402] Insulin-like receptor (dIR) (dInr) (EC 2.7.10.1) (dIRH) [Cleaved into: Insulin-like receptor subunit alpha; Insulin-like receptor subunit beta 1; Insulin-like receptor subunit beta 2]
[INSR] Insulin receptor (IR) (EC 2.7.10.1) (CD antigen CD220) [Cleaved into: Insulin receptor subunit alpha; Insulin receptor subunit beta]
[daf-2 Y55D5A.5] Insulin-like receptor (IR) (EC 2.7.10.1) (Abnormal dauer formation protein 2) [Cleaved into: Insulin-like receptor subunit alpha; Insulin-like receptor subunit beta]
[Insr] Insulin receptor (IR) (EC 2.7.10.1) (CD antigen CD220) [Cleaved into: Insulin receptor subunit alpha; Insulin receptor subunit beta]
[Insr] Insulin receptor (IR) (EC 2.7.10.1) (CD antigen CD220) [Cleaved into: Insulin receptor subunit alpha; Insulin receptor subunit beta]
[IGF2 PP1446] Insulin-like growth factor II (IGF-II) (Somatomedin-A) (T3M-11-derived growth factor) [Cleaved into: Insulin-like growth factor II; Insulin-like growth factor II Ala-25 Del; Preptin]
[PIN] Insulin [Cleaved into: Insulin B chain; Insulin B chain'; Insulin A chain]
[BAIAP2] Brain-specific angiogenesis inhibitor 1-associated protein 2 (BAI-associated protein 2) (BAI1-associated protein 2) (Protein BAP2) (Fas ligand-associated factor 3) (FLAF3) (Insulin receptor substrate p53/p58) (IRS-58) (IRSp53/58) (Insulin receptor substrate protein of 53 kDa) (IRSp53) (Insulin receptor substrate p53)
[Baiap2] Brain-specific angiogenesis inhibitor 1-associated protein 2 (BAI-associated protein 2) (BAI1-associated protein 2) (Insulin receptor substrate protein of 53 kDa) (IRSp53) (Insulin receptor substrate p53) (Insulin receptor tyrosine kinase 53 kDa substrate)
[PDX1 IPF1 STF1] Pancreas/duodenum homeobox protein 1 (PDX-1) (Glucose-sensitive factor) (GSF) (Insulin promoter factor 1) (IPF-1) (Insulin upstream factor 1) (IUF-1) (Islet/duodenum homeobox-1) (IDX-1) (Somatostatin-transactivating factor 1) (STF-1)
[LNPEP OTASE] Leucyl-cystinyl aminopeptidase (Cystinyl aminopeptidase) (EC 3.4.11.3) (Insulin-regulated membrane aminopeptidase) (Insulin-responsive aminopeptidase) (IRAP) (Oxytocinase) (OTase) (Placental leucine aminopeptidase) (P-LAP) [Cleaved into: Leucyl-cystinyl aminopeptidase, pregnancy serum form]
[Baiap2] Brain-specific angiogenesis inhibitor 1-associated protein 2 (BAI-associated protein 2) (BAI1-associated protein 2) (Insulin receptor substrate protein of 53 kDa) (IRSp53) (Insulin receptor substrate p53) (Insulin receptor tyrosine kinase substrate protein p53)
[Lnpep Irap Otase] Leucyl-cystinyl aminopeptidase (Cystinyl aminopeptidase) (EC 3.4.11.3) (GP160) (Insulin-regulated membrane aminopeptidase) (Insulin-responsive aminopeptidase) (IRAP) (Oxytocinase) (OTase) (Placental leucine aminopeptidase) (P-LAP) (Vesicle protein of 165 kDa) (Vp165)
[igfbp2a igfbp2 igfbp2b] Insulin-like growth factor-binding protein 2-A (IGF-binding protein 2-A) (IGFBP-2-A) (IGFBP-2a)
[Insl5 Rif Rif2 Zins3] Insulin-like peptide INSL5 (Insulin-like peptide 5) (Relaxin/insulin-like factor 2) (Relaxin/insulin-like protein) [Cleaved into: Insulin-like peptide INSL5 B chain; Insulin-like peptide INSL5 A chain]
[RPS6KA3 ISPK1 MAPKAPK1B RSK2] Ribosomal protein S6 kinase alpha-3 (S6K-alpha-3) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 3) (p90-RSK 3) (p90RSK3) (Insulin-stimulated protein kinase 1) (ISPK-1) (MAP kinase-activated protein kinase 1b) (MAPK-activated protein kinase 1b) (MAPKAP kinase 1b) (MAPKAPK-1b) (Ribosomal S6 kinase 2) (RSK-2) (pp90RSK2)
[IRS1] Insulin receptor substrate 1 (IRS-1)
[Irs1 Irs-1] Insulin receptor substrate 1 (IRS-1) (pp185)
[Irs1 Irs-1] Insulin receptor substrate 1 (IRS-1)
[IRS4] Insulin receptor substrate 4 (IRS-4) (160 kDa phosphotyrosine protein) (py160) (Phosphoprotein of 160 kDa) (pp160)
[PAPPA] Pappalysin-1 (EC 3.4.24.79) (Insulin-like growth factor-dependent IGF-binding protein 4 protease) (IGF-dependent IGFBP-4 protease) (IGFBP-4ase) (Pregnancy-associated plasma protein A) (PAPP-A)
[IGFBP3 IBP3] Insulin-like growth factor-binding protein 3 (IBP-3) (IGF-binding protein 3) (IGFBP-3)
[IGFBP1 IBP1] Insulin-like growth factor-binding protein 1 (IBP-1) (IGF-binding protein 1) (IGFBP-1) (Placental protein 12) (PP12)
[Igf1 Igf-1] Insulin-like growth factor I (IGF-I) (Somatomedin)

Bibliography :
[30889626] Inositol and Antioxidant Supplementation: Safety and Efficacy in Pregnancy.
[30889572] Probiotic Foods and Supplements Interventions for Metabolic Syndromes: A Systematic Review and Meta-Analysis of Recent Clinical Trials.
[30889454] Influence of enhanced bioavailable curcumin on obesity-associated cardiovascular disease risk factors and arterial function: A double-blinded, randomized, controlled trial.
[30889368] Skeletal muscle ceramides do not contribute to physical inactivity-induced insulin resistance.
[30889343] Nonalcoholic hepatic steatosis: a silent disease
[30889046] Liraglutide protects against diabetes mellitus complicated with focal cerebral ischemic injury by activating mitochondrial ATP-sensitive potassium channels.
[30888989] Safety, Biodistribution, and Dosimetry of 123I-6-Deoxy-6-Iodo-D-Glucose, a Tracer of Glucose Transport, in Healthy and Diabetic Volunteers.
[30888963] Association of IRS1 genetic variants with glucose control and insulin resistance in type 2 diabetic patients from Bosnia and Herzegovina.
[30888961] Antihyperglycemic and antihyperlipidemic activities of Nannochloropsis oculata microalgae in Streptozotocin-induced diabetic rats.
[30888862] MYOSTATIN REGULATES PITUITARY DEVELOPMENT AND HEPATIC IGF1.
?>