[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LYS-420. DOI=10.1093/nar/9.22.6103; PubMed=6171778 [NCBI, ExPASy, EBI, Israel, Japan] Lawn R.M., Adelman J., Bock S.C., Franke A.E., Houck C.M., Najarian R.C., Seeburg P.H., Wion K.L.; "The sequence of human serum albumin cDNA and its expression in E. coli."; Nucleic Acids Res. 9:6103-6114(1981).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-121. DOI=10.1073/pnas.79.1.71; PubMed=6275391 [NCBI, ExPASy, EBI, Israel, Japan] Dugaiczyk A., Law S.W., Dennison O.E.; "Nucleotide sequence and the encoded amino acids of human serum albumin mRNA."; Proc. Natl. Acad. Sci. U.S.A. 79:71-75(1982).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=3009475 [NCBI, ExPASy, EBI, Israel, Japan] Minghetti P.P., Ruffner D.E., Kuang W.J., Dennison O.E., Hawkins J.W., Beattie W.G., Dugaiczyk A.; "Molecular structure of the human albumin gene is revealed by nucleotide sequence within q11-22 of chromosome 4."; J. Biol. Chem. 261:6747-6757(1986).
[4]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Liver; Yang S., Zhang R.A., Qi Z.W., Yuan Z.Y.; "Human serum albumin."; Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT HIROSHIMA-1 LYS-378. Huang M.C., Wu H.T.; "The cDNA sequences of human serum albumin."; Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[6]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Hinchliffe E.; "Induction of galactose regulated gene expression in yeast."; Patent number EP0248637, 09-DEC-1987.
[7]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Liver; Yu Z., Fu Y.; "High expression HSA in Pichia for Pharmaceutical Use."; Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[8]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Wang F., Huang L.; "Cloning and sequence analysis of human albumin gene."; Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
[9]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Kim J.W.; "Identification of a human cell growth inhibition gene."; Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[10]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Fetal liver; DOI=10.1101/gr.175501; PubMed=11483580 [NCBI, ExPASy, EBI, Israel, Japan] Yu Y., Zhang C., Zhou G., Wu S., Qu X., Wei H., Xing G., Dong C., Zhai Y., Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C., He F.; "Gene expression profiling in human fetal liver and identification of tissue- and developmental-stage-specific genes through compiled expression profiles and efficient cloning of full-length cDNAs."; Genome Res. 11:1392-1403(2001).
[11]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT TYR-27. TISSUE=Liver; DOI=10.1186/1471-2164-8-399; PubMed=17974005 [NCBI, ExPASy, EBI, Israel, Japan] Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.; "The full-ORF clone resource of the German cDNA consortium."; BMC Genomics 8:399-399(2007).
[12]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. SeattleSNPs variation discovery resource; Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
[13]	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.
[14]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). TISSUE=Liver, and Skeletal muscle; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[15]	NUCLEOTIDE SEQUENCE [MRNA] OF 1-455. TISSUE=Liver; Menaya J., Parrilla R., Ayuso M.S.; Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
[16]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-167. DOI=10.1101/gr.1293003; PubMed=12975309 [NCBI, ExPASy, EBI, Israel, Japan] Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."; Genome Res. 13:2265-2270(2003).
[17]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26. PubMed=2419329 [NCBI, ExPASy, EBI, Israel, Japan] Urano Y., Watanabe K., Sakai M., Tamaoki T.; "The human albumin gene. Characterization of the 5' and 3' flanking regions and the polymorphic gene transcripts."; J. Biol. Chem. 261:3244-3251(1986).
[18]	PROTEIN SEQUENCE OF 25-609. DOI=10.1016/0014-5793(75)80242-0; PubMed=1225573 [NCBI, ExPASy, EBI, Israel, Japan] Meloun B., Moravek L., Kostka V.; "Complete amino acid sequence of human serum albumin."; FEBS Lett. 58:134-137(1975).
[19]	PROTEIN SEQUENCE OF 25-609. Brown J.R., Shockley P., Behrens P.Q.; (In) Bing D.H. (eds.); The chemistry and physiology of the human plasma proteins, pp.23-40, Pergamon Press, New York (1979).
[20]	PROTEIN SEQUENCE OF 25-44 AND 480-499. TISSUE=Heart; DOI=10.1002/elps.11501501209; PubMed=7895732 [NCBI, ExPASy, EBI, Israel, Japan] Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.; "The human myocardial two-dimensional gel protein database: update 1994."; Electrophoresis 15:1459-1465(1994).
[21]	PROTEIN SEQUENCE OF 25-34. TISSUE=Platelet; DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan] Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.; "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."; Nat. Biotechnol. 21:566-569(2003).
[22]	PROTEIN SEQUENCE OF 45-75; 98-130; 162-183; 239-254; 265-281; 287-298; 348-372; 397-434; 438-452; 500-543; 550-558; 570-581 AND 599-609, AND MASS SPECTROMETRY. TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; Lubec G., Vishwanath V., Chen W.-Q., Sun Y.; Submitted (DEC-2008) to UniProtKB.
[23]	PROTEIN SEQUENCE OF 166-174. DOI=10.1016/0006-291X(86)90429-8; PubMed=3087352 [NCBI, ExPASy, EBI, Israel, Japan] Mogard M.H., Kobayashi R., Chen C.F., Lee T.D., Reeve J.R. Jr., Shively J.E., Walsh J.H.; "The amino acid sequence of kinetensin, a novel peptide isolated from pepsin-treated human plasma: homology with human serum albumin, neurotensin and angiotensin."; Biochem. Biophys. Res. Commun. 136:983-988(1986).
[24]	PROTEIN SEQUENCE OF 166-174. PubMed=2437111 [NCBI, ExPASy, EBI, Israel, Japan] Carraway R.E., Mitra S.P., Cochrane D.E.; "Structure of a biologically active neurotensin-related peptide obtained from pepsin-treated albumin(s)."; J. Biol. Chem. 262:5968-5973(1987).
[25]	PROTEIN SEQUENCE OF 222-229, AND ASPIRIN-ACETYLATION AT LYS-223. DOI=10.1016/0014-5793(76)80496-6; PubMed=955075 [NCBI, ExPASy, EBI, Israel, Japan] Walker J.E.; "Lysine residue 199 of human serum albumin is modified by acetylsalicylic acid."; FEBS Lett. 66:173-175(1976).
[26]	PROTEIN SEQUENCE OF 250-264, GLYCATION AT LYS-75; LYS-161; LYS-186; LYS-249; LYS-257; LYS-300; LYS-337; LYS-347; LYS-375; LYS-402; LYS-437; LYS-468; LYS-560; LYS-549; LYS-569 AND LYS-597, ABSENCE OF GLYCATION AT LYS-28; LYS-44; LYS-65; LYS-88; LYS-97; LYS-117; LYS-130; LYS-160; LYS-183; LYS-198; LYS-205; LYS-214; LYS-219; LYS-229; LYS-236; LYS-264; LYS-286; LYS-298; LYS-310; LYS-383; LYS-396; LYS-413; LYS-426; LYS-438; LYS-456; LYS-460; LYS-490; LYS-499; LYS-524; LYS-543; LYS-548; LYS-562; LYS-565; LYS-581; LYS-584; LYS-588 AND LYS-598, AND MASS SPECTROMETRY. DOI=10.1016/j.jasms.2003.11.014; PubMed=15047055 [NCBI, ExPASy, EBI, Israel, Japan] Lapolla A., Fedele D., Reitano R., Arico N.C., Seraglia R., Traldi P., Marotta E., Tonani R.; "Enzymatic digestion and mass spectrometry in the study of advanced glycation end products/peptides."; J. Am. Soc. Mass Spectrom. 15:496-509(2004).
[27]	DISULFIDE BONDS. Saber M.A., Stockbauer P., Moravek L., Meloun B.; "Disulfide bonds in human serum albumin."; Collect. Czech. Chem. Commun. 42:564-579(1977).
[28]	BILIRUBIN-BINDING SITE. PubMed=656055 [NCBI, ExPASy, EBI, Israel, Japan] Jacobsen C.; "Lysine residue 240 of human serum albumin is involved in high-affinity binding of bilirubin."; Biochem. J. 171:453-459(1978).
[29]	GLYCATION AT LYS-223 AND LYS-549. PubMed=6853480 [NCBI, ExPASy, EBI, Israel, Japan] Garlick R.L., Mazer J.S.; "The principal site of nonenzymatic glycosylation of human serum albumin in vivo."; J. Biol. Chem. 258:6142-6146(1983).
[30]	GLYCATION AT LYS-549. PubMed=6706980 [NCBI, ExPASy, EBI, Israel, Japan] Shaklai N., Garlick R.L., Bunn H.F.; "Nonenzymatic glycosylation of human serum albumin alters its conformation and function."; J. Biol. Chem. 259:3812-3817(1984).
[31]	GLYCATION AT LYS-36; LYS-223; LYS-257; LYS-305; LYS-341; LYS-375; LYS-463; LYS-549 AND LYS-558. PubMed=3759977 [NCBI, ExPASy, EBI, Israel, Japan] Iberg N., Fluckiger R.; "Nonenzymatic glycosylation of albumin in vivo. Identification of multiple glycosylated sites."; J. Biol. Chem. 261:13542-13545(1986).
[32]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-108 AND TYR-164, AND MASS SPECTROMETRY. DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan] Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."; Cell 131:1190-1203(2007).
[33]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1002/pmic.200700884; PubMed=18318008 [NCBI, ExPASy, EBI, Israel, Japan] Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.; "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."; Proteomics 8:1346-1361(2008).
[34]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.
[35]	X-RAY CRYSTALLOGRAPHY (6.0 ANGSTROMS). DOI=10.1126/science.2727704; PubMed=2727704 [NCBI, ExPASy, EBI, Israel, Japan] Carter D.C., He X.-M., Munson S.H., Twigg P.D., Gernert K.M., Broom M.B., Miller T.Y.; "Three-dimensional structure of human serum albumin."; Science 244:1195-1198(1989).
[36]	X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS). DOI=10.1126/science.2374930; PubMed=2374930 [NCBI, ExPASy, EBI, Israel, Japan] Carter D.C., He X.-M.; "Structure of human serum albumin."; Science 249:302-303(1990).
[37]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). DOI=10.1038/358209a0; PubMed=1630489 [NCBI, ExPASy, EBI, Israel, Japan] He X.-M., Carter D.C.; "Atomic structure and chemistry of human serum albumin."; Nature 358:209-215(1992).
[38]	ERRATUM. He X.-M., Carter D.C.; Nature 364:362-362(1993).
[39]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). DOI=10.1038/1869; PubMed=9731778 [NCBI, ExPASy, EBI, Israel, Japan] Curry S., Mandelkow H., Brick P., Franks N.; "Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites."; Nat. Struct. Biol. 5:827-835(1998).
[40]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). DOI=10.1093/protein/12.6.439; PubMed=10388840 [NCBI, ExPASy, EBI, Israel, Japan] Sugio S., Kashima A., Mochizuki S., Noda M., Kobayashi K.; "Crystal structure of human serum albumin at 2.5-A resolution."; Protein Eng. 12:439-446(1999).
[41]	X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-609. DOI=10.1074/jbc.M005460200; PubMed=10940303 [NCBI, ExPASy, EBI, Israel, Japan] Bhattacharya A.A., Curry S., Franks N.P.; "Binding of the general anesthetics propofol and halothane to human serum albumin. High resolution crystal structures."; J. Biol. Chem. 275:38731-38738(2000).
[42]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). DOI=10.1006/jmbi.2000.5208; PubMed=11743713 [NCBI, ExPASy, EBI, Israel, Japan] Petitpas I., Grune T., Bhattacharya A.A., Curry S.; "Crystal structures of human serum albumin complexed with monounsaturated and polyunsaturated fatty acids."; J. Mol. Biol. 314:955-960(2001).
[43]	VARIANT CANTERBURY ASN-337. DOI=10.1016/0167-4838(87)90088-4; PubMed=3828358 [NCBI, ExPASy, EBI, Israel, Japan] Brennan S.O., Herbert P.; "Albumin Canterbury (313 Lys-->Asn). A point mutation in the second domain of serum albumin."; Biochim. Biophys. Acta 912:191-197(1987).
[44]	VARIANTS NASKAPI/MERSIN GLU-396 AND MEXICO GLY-574. DOI=10.1073/pnas.84.13.4413; PubMed=3474609 [NCBI, ExPASy, EBI, Israel, Japan] Takahashi N., Takahashi Y., Blumberg B.S., Putnam F.W.; "Amino acid substitutions in genetic variants of human serum albumin and in sequences inferred from molecular cloning."; Proc. Natl. Acad. Sci. U.S.A. 84:4413-4417(1987).
[45]	VARIANTS NAGASAKI-3 GLN-27 YANOMAMA-2 GLU-396; NAGASAKI-2 ASN-399 AND MAKU GLU-565. DOI=10.1073/pnas.84.22.8001; PubMed=3479777 [NCBI, ExPASy, EBI, Israel, Japan] Takshashi N., Takahashi Y., Isobe T., Putnam F.W., Fujita M., Satoh C., Neel J.V.; "Amino acid substitutions in inherited albumin variants from Amerindian and Japanese populations."; Proc. Natl. Acad. Sci. U.S.A. 84:8001-8005(1987).
[46]	VARIANTS FUKUOKA-2 HIS-23; CHRISTCHURCH/HONOLULU-2 GLN-24; TAGLIACOZZO ASN-337 AND ALBUMIN B/OSAKA-2/PHNOM PHEN LYS-594. DOI=10.1073/pnas.86.2.434; PubMed=2911589 [NCBI, ExPASy, EBI, Israel, Japan] Arai K., Ishioka N., Huss K., Madison J., Putnam F.W.; "Identical structural changes in inherited albumin variants from different populations."; Proc. Natl. Acad. Sci. U.S.A. 86:434-438(1989).
[47]	VARIANTS HONOLULU-2 GLN-24; NAGASAKI-1 GLY-293; HIROSHIMA-1 LYS-378; TOCHIGI LYS-400; HIROSHIMA-2 LYS-406 AND OSAKA-2 LYS-594. DOI=10.1073/pnas.86.16.6092; PubMed=2762316 [NCBI, ExPASy, EBI, Israel, Japan] Arai K., Madison J., Huss K., Ishioka N., Satoh C., Fujita M., Neel J.V., Sakurabayashi I., Putnam F.W.; "Point substitutions in Japanese alloalbumins."; Proc. Natl. Acad. Sci. U.S.A. 86:6092-6096(1989).
[48]	VARIANTS HONOLULU-1 PRO-24; HONOLULU-2 GLN-24; NAGOYA LYS-143; NEW GUINEA ASN-337; MANAUS-1/LAMBADI LYS-525; FUKUOKA-1 ASN-587; OSAKA-1 LYS-589 AND OSAKA-2 LYS-594. DOI=10.1073/pnas.87.1.497; PubMed=2404284 [NCBI, ExPASy, EBI, Israel, Japan] Arai K., Madison J., Shimuzu A., Putnam F.W.; "Point substitutions in albumin genetic variants from Asia."; Proc. Natl. Acad. Sci. U.S.A. 87:497-501(1990).
[49]	CHARACTERIZATION OF VARIANT REDHILL. DOI=10.1073/pnas.87.1.26; PubMed=2104980 [NCBI, ExPASy, EBI, Israel, Japan] Brennan S.O., Myles T., Peach R.J., Donaldson D., George P.M.; "Albumin Redhill (-1 Arg, 320 Ala-->Thr): a glycoprotein variant of human serum albumin whose precursor has an aberrant signal peptidase cleavage site."; Proc. Natl. Acad. Sci. U.S.A. 87:26-30(1990).
[50]	VARIANTS VARESE HIS-23; TORINO LYS-84 AND VIBO VALENTIA LYS-106. DOI=10.1073/pnas.87.22.8721; PubMed=2247440 [NCBI, ExPASy, EBI, Israel, Japan] Galliano M., Minchiotti L., Porta F., Rossi A., Ferri G., Madison J., Watkins S., Putnam F.W.; "Mutations in genetic variants of human serum albumin found in Italy."; Proc. Natl. Acad. Sci. U.S.A. 87:8721-8725(1990).
[51]	CHARACTERIZATION OF VARIANT VENEZIA. DOI=10.1073/pnas.88.14.5959; PubMed=2068071 [NCBI, ExPASy, EBI, Israel, Japan] Watkins S., Madison J., Davis E., Sakamoto Y., Galliano M., Minchiotti L., Putnam F.W.; "A donor splice mutation and a single-base deletion produce two carboxyl-terminal variants of human serum albumin."; Proc. Natl. Acad. Sci. U.S.A. 88:5959-5963(1991).
[52]	VARIANTS KOMAGOME-3 HIS-23; IOWA CITY-2 VAL-25; KOMAGOME-2 ARG-152; IOWA CITY-1 VAL-389 AND KOMAGOME-1 GLU-396. DOI=10.1073/pnas.88.21.9853; PubMed=1946412 [NCBI, ExPASy, EBI, Israel, Japan] Madison J., Arai K., Feld R.D., Kyle R.A., Watkins S., Davis E., Matsuda Y., Amaki I., Putnam F.W.; "Genetic variants of serum albumin in Americans and Japanese."; Proc. Natl. Acad. Sci. U.S.A. 88:9853-9857(1991).
[53]	VARIANT CASEBROOK ASN-518. DOI=10.1016/0925-4439(91)90023-3; PubMed=1859851 [NCBI, ExPASy, EBI, Israel, Japan] Peach R.J., Brennan S.O.; "Structural characterization of a glycoprotein variant of human serum albumin: albumin Casebrook (494 Asp-->Asn)."; Biochim. Biophys. Acta 1097:49-54(1991).
[54]	VARIANTS SONDRIO LYS-357 AND PARIS-2 ASN-587. DOI=10.1016/0167-4838(92)90207-T; PubMed=1347703 [NCBI, ExPASy, EBI, Israel, Japan] Minchiotti L., Galliano M., Stoppini M., Ferri G., Crespeau H., Rochu D., Porta F.; "Two alloalbumins with identical electrophoretic mobility are produced by differently charged amino acid substitutions."; Biochim. Biophys. Acta 1119:232-238(1992).
[55]	VARIANTS MALMO-I CYS-23; MALMO-95 ASN-87; MALMO-10 ARG-292; MALMO-47 LYS-342; MALMO-5 GLN-400 AND MALMO-61 ALA-574. DOI=10.1073/pnas.89.17.8225; PubMed=1518850 [NCBI, ExPASy, EBI, Israel, Japan] Carlson J., Sakamoto Y., Laurell C.-B., Madison J., Watkins S., Putnam F.W.; "Alloalbuminemia in Sweden: structural study and phenotypic distribution of nine albumin variants."; Proc. Natl. Acad. Sci. U.S.A. 89:8225-8229(1992).
[56]	VARIANT HERBORN GLU-264. DOI=10.1111/j.1432-1033.1993.tb17939.x; PubMed=8513793 [NCBI, ExPASy, EBI, Israel, Japan] Minchiotti L., Galliano M., Zapponi M.C., Tenni R.; "The structural characterization and bilirubin-binding properties of albumin Herborn, a [Lys240-->Glu] albumin mutant."; Eur. J. Biochem. 214:437-444(1993).
[57]	VARIANT HAWKES BAY PHE-201. DOI=10.1016/0925-4439(93)90151-P; PubMed=8347685 [NCBI, ExPASy, EBI, Israel, Japan] Brennan S.O., Fellowes A.P.; "Albumin Hawkes Bay; a low level variant caused by loss of a sulphydryl group at position 177."; Biochim. Biophys. Acta 1182:46-50(1993).
[58]	VARIANT ORTONOVO LYS-529. DOI=10.1016/0925-4439(93)90117-J; PubMed=7902134 [NCBI, ExPASy, EBI, Israel, Japan] Galliano M., Minchiotti L., Iadarola P., Stoppini M., Giagnoni P., Watkins S., Madison J., Putnam F.W.; "Protein and DNA sequence analysis of a 'private' genetic variant: albumin Ortonovo (Glu-505-->Lys)."; Biochim. Biophys. Acta 1225:27-32(1993).
[59]	VARIANTS LARINO TYR-27; TRADATE-2 GLN-249 AND CASERTA ASN-300. DOI=10.1073/pnas.91.14.6476; PubMed=8022807 [NCBI, ExPASy, EBI, Israel, Japan] Madison J., Galliano M., Watkins S., Minchiotti L., Porta F., Rossi A., Putnam F.W.; "Genetic variants of human serum albumin in Italy: point mutants and a carboxyl-terminal variant."; Proc. Natl. Acad. Sci. U.S.A. 91:6476-6480(1994).
[60]	VARIANT FDH HIS-242. DOI=10.1006/bbrc.1994.1998; PubMed=8048949 [NCBI, ExPASy, EBI, Israel, Japan] Sunthornthepvarakul T., Angkeow P., Weiss R.E., Hayashi Y., Retetoff S.; "An identical missense mutation in the albumin gene results in familial dysalbuminemic hyperthyroxinemia in 8 unrelated families."; Biochem. Biophys. Res. Commun. 202:781-787(1994).
[61]	VARIANT FDH HIS-242, AND PROTEIN SEQUENCE OF 25-51. DOI=10.1210/jc.80.2.461; PubMed=7852505 [NCBI, ExPASy, EBI, Israel, Japan] Rushbrook J.I., Becker E., Schussler G.C., Divino C.M.; "Identification of a human serum albumin species associated with familial dysalbuminemic hyperthyroxinemia."; J. Clin. Endocrinol. Metab. 80:461-467(1995).
[62]	VARIANT FDH HIS-242. DOI=10.1210/jc.82.10.3246; PubMed=9329347 [NCBI, ExPASy, EBI, Israel, Japan] Wada N., Chiba H., Shimizu C., Kijima H., Kubo M., Koike T.; "A novel missense mutation in codon 218 of the albumin gene in a distinct phenotype of familial dysalbuminemic hyperthyroxinemia in a Japanese kindred."; J. Clin. Endocrinol. Metab. 82:3246-3250(1997).
[63]	VARIANT FDH PRO-90. DOI=10.1210/jc.83.5.1448; PubMed=9589637 [NCBI, ExPASy, EBI, Israel, Japan] Sunthornthepvarakul T., Likitmaskul S., Ngowngarmratana S., Angsusingha K., Kitvitayasak S., Scherberg N.H., Refetoff S.; "Familial dysalbuminemic hypertriiodothyroninemia: a new, dominantly inherited albumin defect."; J. Clin. Endocrinol. Metab. 83:1448-1454(1998).
[64]	VARIANT TYR-73, AND MASS SPECTROMETRY. TISSUE=Urine; DOI=10.1002/1615-9861(200101)1:1<93::AID-PROT93>3.3.CO;2-V; PubMed=11680902 [NCBI, ExPASy, EBI, Israel, Japan] Spahr C.S., Davis M.T., McGinley M.D., Robinson J.H., Bures E.J., Beierle J., Mort J., Courchesne P.L., Chen K., Wahl R.C., Yu W., Luethy R., Patterson S.D.; "Towards defining the urinary proteome using liquid chromatography-tandem mass spectrometry I. Profiling an unfractionated tryptic digest."; Proteomics 1:93-107(2001).
[65]	CHARACTERIZATION OF VARIANT KENITRA. DOI=10.1046/j.1432-1033.2001.01899.x; PubMed=11168369 [NCBI, ExPASy, EBI, Israel, Japan] Minchiotti L., Campagnoli M., Rossi A., Cosulich M.E., Monti M., Pucci P., Kragh-Hansen U., Granel B., Disdier P., Weiller P.J., Galliano M.; "A nucleotide insertion and frameshift cause albumin Kenitra, an extended and O-glycosylated mutant of human serum albumin with two additional disulfide bridges."; Eur. J. Biochem. 268:344-352(2001).

Comments

FUNCTION: Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood.
SUBCELLULAR LOCATION: Secreted.

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	P02768-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	P02768-2
Note: No experimental confirmation available.
Features which should be applied to build the isoform sequence: VSP_021275.

TISSUE SPECIFICITY: Plasma.
PTM: Kenitra variant is partially O-glycosylated at Thr-620. It has two new disulfide bonds Cys-600 to Cys-602 and Cys-601 to Cys-606.
PTM: Glycated in diabetic patients.
POLYMORPHISM: The sequence shown is that of variant albumin A.
DISEASE: Defects in ALB are a cause of familial dysalbuminemic hyperthyroxinemia (FDH) [MIM:103600]. FDH is a form of euthyroid hyperthyroxinemia that is due to increased affinity of ALB for T(4). It is the most common cause of inherited euthyroid hyperthyroxinemia in Caucasian population.
DISEASE: A variant structure of albumin could lead to increased binding of zinc resulting in an asymptomatic augmentation of zinc concentration in the blood [MIM:194470].
MISCELLANEOUS: Acetylated on Lys-223 by acetylsalicylic acid.
SIMILARITY: Belongs to the ALB/AFP/VDB family.
SIMILARITY: Contains 3 albumin domains.
CAUTION: A peptide arising from positions 166 to 174 was originally (PubMed:3087352 and PubMed:2437111) termed neurotensin-related peptide (NRP) or kinetensin and was thought to regulates fat digestion, lipid absorption, and blood flow.
WEB RESOURCE: Name=Albumin Website; URL="http://www.albumin.org";.
WEB RESOURCE: Name=Wikipedia; Note=Serum albumin entry; URL="http://en.wikipedia.org/wiki/Serum_albumin";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=ALB";.
WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/alb/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

V00494; CAA23753.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
V00495; CAA23754.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M12523; AAA98797.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M12523; AAA98798.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF190168; AAF01333.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF542069; AAN17825.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
A06977; CAA00606.1; -; Unassigned_RNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY728024; AAU21642.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ986150; ABJ16448.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY544124; AAT11155.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY550967; AAT52213.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF116645; AAF71067.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF118090; AAF22034.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF119840; AAF69594.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF119890; AAF69644.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF130077; AAG35503.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR749331; CAH18185.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
EF649953; ABS29264.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471057; EAX05676.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC014308; AAH14308.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC034023; AAH34023.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC036003; AAH36003.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC041789; AAH41789.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U22961; AAA64922.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY358313; AAQ89947.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M13075; AAA51688.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00384697; -.
IPI00745872; -.

A93743; ABHUS.

NP_000468.1; -.

3D structure databases

PDB

1AO6; X-ray; 2.50 A; A/B=25-609.	[ExPASy / RCSB / EBI]
1BJ5; X-ray; 2.50 A; A=25-609.	[ExPASy / RCSB / EBI]
1BKE; X-ray; 3.15 A; A=28-608.	[ExPASy / RCSB / EBI]
1BM0; X-ray; 2.50 A; A/B=25-609.	[ExPASy / RCSB / EBI]
1E78; X-ray; 2.60 A; A/B=25-609.	[ExPASy / RCSB / EBI]
1E7A; X-ray; 2.20 A; A/B=25-609.	[ExPASy / RCSB / EBI]
1E7B; X-ray; 2.38 A; A/B=25-609.	[ExPASy / RCSB / EBI]
1E7C; X-ray; 2.40 A; A=25-609.	[ExPASy / RCSB / EBI]
1E7E; X-ray; 2.50 A; A=25-609.	[ExPASy / RCSB / EBI]
1E7F; X-ray; 2.43 A; A=25-609.	[ExPASy / RCSB / EBI]
1E7G; X-ray; 2.50 A; A=25-609.	[ExPASy / RCSB / EBI]
1E7H; X-ray; 2.43 A; A=25-609.	[ExPASy / RCSB / EBI]
1E7I; X-ray; 2.70 A; A=25-609.	[ExPASy / RCSB / EBI]
1GNI; X-ray; 2.40 A; A=25-609.	[ExPASy / RCSB / EBI]
1GNJ; X-ray; 2.60 A; A=25-609.	[ExPASy / RCSB / EBI]
1H9Z; X-ray; 2.50 A; A=25-609.	[ExPASy / RCSB / EBI]
1HA2; X-ray; 2.50 A; A=25-609.	[ExPASy / RCSB / EBI]
1HK1; X-ray; 2.65 A; A=25-609.	[ExPASy / RCSB / EBI]
1HK2; X-ray; 2.80 A; A=25-609.	[ExPASy / RCSB / EBI]
1HK3; X-ray; 2.80 A; A=25-609.	[ExPASy / RCSB / EBI]
1HK4; X-ray; 2.40 A; A=25-609.	[ExPASy / RCSB / EBI]
1HK5; X-ray; 2.70 A; A=25-609.	[ExPASy / RCSB / EBI]
1N5U; X-ray; 1.90 A; A=25-609.	[ExPASy / RCSB / EBI]
1O9X; X-ray; 3.20 A; A=25-609.	[ExPASy / RCSB / EBI]
1TF0; X-ray; 2.70 A; A=25-596.	[ExPASy / RCSB / EBI]
1UOR; X-ray; 2.80 A; A=25-609.	[ExPASy / RCSB / EBI]
1YSX; NMR; -; A=409-609.	[ExPASy / RCSB / EBI]
2BX8; X-ray; 2.70 A; A/B=25-609.	[ExPASy / RCSB / EBI]
2BXA; X-ray; 2.35 A; A/B=25-609.	[ExPASy / RCSB / EBI]
2BXB; X-ray; 3.20 A; A/B=25-609.	[ExPASy / RCSB / EBI]
2BXC; X-ray; 3.10 A; A/B=25-609.	[ExPASy / RCSB / EBI]
2BXD; X-ray; 3.05 A; A/B=25-609.	[ExPASy / RCSB / EBI]
2BXE; X-ray; 2.95 A; A/B=25-609.	[ExPASy / RCSB / EBI]
2BXF; X-ray; 2.95 A; A/B=25-609.	[ExPASy / RCSB / EBI]
2BXG; X-ray; 2.70 A; A/B=25-609.	[ExPASy / RCSB / EBI]
2BXH; X-ray; 2.25 A; A/B=25-609.	[ExPASy / RCSB / EBI]
2BXI; X-ray; 2.50 A; A=25-609.	[ExPASy / RCSB / EBI]
2BXK; X-ray; 2.40 A; A=25-609.	[ExPASy / RCSB / EBI]
2BXL; X-ray; 2.60 A; A=25-609.	[ExPASy / RCSB / EBI]
2BXM; X-ray; 2.50 A; A=25-609.	[ExPASy / RCSB / EBI]
2BXN; X-ray; 2.65 A; A=25-609.	[ExPASy / RCSB / EBI]
2BXO; X-ray; 2.60 A; A=25-609.	[ExPASy / RCSB / EBI]
2BXP; X-ray; 2.30 A; A=25-609.	[ExPASy / RCSB / EBI]
2BXQ; X-ray; 2.60 A; A=25-609.	[ExPASy / RCSB / EBI]
2ESG; X-ray; -; C=25-609.	[ExPASy / RCSB / EBI]
2I2Z; X-ray; 2.70 A; A=25-609.	[ExPASy / RCSB / EBI]
2I30; X-ray; 2.90 A; A=25-609.	[ExPASy / RCSB / EBI]
2VDB; X-ray; 2.52 A; A=30-608.	[ExPASy / RCSB / EBI]
2VUE; X-ray; 2.42 A; A/B=25-609.	[ExPASy / RCSB / EBI]
2VUF; X-ray; 3.05 A; A/B=25-609.	[ExPASy / RCSB / EBI]
3B9L; X-ray; 2.60 A; A=25-609.	[ExPASy / RCSB / EBI]
3B9M; X-ray; 2.70 A; A=25-609.	[ExPASy / RCSB / EBI]
3CX9; X-ray; 2.80 A; A=27-608.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1AO6; -.
1BJ5; -.
1BKE; -.
1BM0; -.
1E78; -.
1E7A; -.
1E7B; -.
1E7C; -.
1E7E; -.
1E7F; -.
1E7G; -.
1E7H; -.
1E7I; -.
1GNI; -.
1GNJ; -.
1H9Z; -.
1HA2; -.
1HK1; -.
1HK2; -.
1HK3; -.
1HK4; -.
1HK5; -.
1N5U; -.
1O9X; -.
1TF0; -.
1UOR; -.
1YSX; -.
2BX8; -.
2BXA; -.
2BXB; -.
2BXC; -.
2BXD; -.
2BXE; -.
2BXF; -.
2BXG; -.
2BXH; -.
2BXI; -.
2BXK; -.
2BXL; -.
2BXM; -.
2BXN; -.
2BXO; -.
2BXP; -.
2BXQ; -.
2ESG; -.
2I2Z; -.
2I30; -.
2VDB; -.
2VUE; -.
2VUF; -.
3B9L; -.
3B9M; -.
3CX9; -.

ModBase

P02768.

Protein-protein interaction databases

IntAct

P02768; 140.

PTM databases

GlycoSuiteDB

P02768; -.

PhosphoSite

P02768; -.

Enzyme and pathway databases

Pathway_Interaction_DB

hnf3bpathway; FOXA2 and FOXA3 transcription factor networks.

Reactome

REACT_602; Lipid and lipoprotein metabolism.
REACT_604; Hemostasis.

2D gel databases

P02768; -.

P02768; -.

P02768; -.

P02768; -.

P02768; -.

IPI00384697; -.
IPI00745872; -.
P02768; -.

Siena-2DPAGE

P02768; -.

Organism-specific databases

GC04P074509; -.

HIX0004278; -.

HGNC:399; ALB.

ALB.

CAB006262; -.

103600; gene+phenotype. [NCBI / EBI]
194470; phenotype. [NCBI / EBI]

Orphanet

86816; Congenital analbuminemia.

PharmGKB

PA24690; -.

Gene expression databases

ArrayExpress

P02768; -.

Bgee

P02768; -.

GermOnline

ENSG00000163631; Homo sapiens.

Ontologies

GO:0005615;	Cellular component: extracellular space (inferred from electronic annotation from InterPro).
GO:0031093;	Cellular component: platelet alpha granule lumen (inferred from experiment from Reactome).
GO:0043234;	Cellular component: protein complex (inferred from direct assay from UniProtKB).
GO:0016209;	Molecular function: antioxidant activity (non-traceable author statement from UniProtKB).
GO:0005507;	Molecular function: copper ion binding (non-traceable author statement from UniProtKB).
GO:0003677;	Molecular function: DNA binding (inferred from direct assay from UniProtKB).
GO:0008144;	Molecular function: drug binding (inferred from direct assay from UniProtKB).
GO:0005504;	Molecular function: fatty acid binding (inferred from direct assay from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0030170;	Molecular function: pyridoxal phosphate binding (inferred from direct assay from UniProtKB).
GO:0015643;	Molecular function: toxin binding (inferred from direct assay from UniProtKB).
GO:0009267;	Biological process: cellular response to starvation (inferred from direct assay from UniProtKB).
GO:0019836;	Biological process: hemolysis by symbiont of host erythrocytes (inferred from direct assay from UniProtKB).
GO:0051659;	Biological process: maintenance of mitochondrion location (inferred from direct assay from UniProtKB).
GO:0043066;	Biological process: negative regulation of apoptosis (inferred from direct assay from UniProtKB).
GO:0006810;	Biological process: transport (traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR001703; Alpha-fetoprotein.
IPR000264; Serum_albumin.
IPR014760; Serum_albumin_N.
Graphical view of domain structure.

Pfam

PF00273; Serum_albumin; 3.
Pfam graphical view of domain structure.

PRINTS

PR00803; AFETOPROTEIN.
PR00802; SERUMALBUMIN.

ProDom

PD002486; Serum_albumin; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00103; ALBUMIN; 3.
SMART graphical view of domain structure.

PROSITE

PS00212; ALBUMIN_1; 3.
PS51438; ALBUMIN_2; 3.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

P02768; -.

Genome annotation databases

Ensembl

ENSG00000163631; Homo sapiens. [Contig view]

GeneID

213; -.

KEGG

hsa:213; -.

Phylogenomic databases

HOVERGEN

P02768; -.

Other

DrugBank

DB01418; Acenocoumarol.
DB00459; Acitretin.
DB00802; Alfentanil.
DB01370; Aluminium.
DB00995; Auranofin.
DB01402; Bismuth.
DB01197; Captopril.
DB00958; Carboplatin.
DB00456; Cefalotin.
DB01327; Cefazolin.
DB01328; Cefonicid.
DB01329; Cefoperazone.
DB01114; Chlorpheniramine.
DB00477; Chlorpromazine.
DB00537; Ciprofloxacin.
DB01068; Clonazepam.
DB01147; Cloxacillin.
DB00987; Cytarabine.
DB01219; Dantrolene.
DB00586; Diclofenac.
DB00861; Diflunisal.
DB01396; Digitoxin.
DB00655; Estrone.
DB00903; Ethacrynic acid.
DB00749; Etodolac.
DB00712; Flurbiprofen.
DB00743; Gadobenate Dimeglumine.
DB01044; Gatifloxacin.
DB01120; Gliclazide.
DB01159; Halothane.
DB00062; Human Serum Albumin.
DB00070; Hyaluronidase.
DB01050; Ibuprofen.
DB01307; Insulin-detemir.
DB01308; Insulin-glargine.
DB04711; Iodipamide.
DB01009; Ketoprofen.
DB00848; Levamisole.
DB00451; Levothyroxine.
DB00279; Liothyronine.
DB00784; Mefenamic acid.
DB00532; Mephenytoin.
DB00563; Methotrexate.
DB00540; Nortriptyline.
DB00842; Oxazepam.
DB01229; Paclitaxel.
DB00946; Phenprocoumon.
DB01032; Probenecid.
DB00818; Propofol.
DB00165; Pyridoxine.
DB00936; Salicyclic acid.
DB01232; Saquinavir.
DB00096; Serum albumin.
DB00064; Serum albumin iodonated.
DB00815; Sodium lauryl sulfate.
DB00364; Sucralfate.
DB00576; Sulfamethizole.
DB00605; Sulindac.
DB00870; Suprofen.
DB00624; Testosterone.
DB00137; Xanthophyll.

862; -.

P02768; -.

ALB; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Cleavage on pair of basic residues; Copper; Direct protein sequencing; Disease mutation; Disulfide bond; Glycation; Glycoprotein; Lipid-binding; Metal-binding; Phosphoprotein; Polymorphism; Repeat; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 18`	`18`
`PROPEP`	`19 24`	`6`		`PRO_0000001067`
`CHAIN`	`25 609`	`585`	`Serum albumin.`	`PRO_0000001068`
`DOMAIN`	`19 210`	`192`	`Albumin 1.`
`DOMAIN`	`211 403`	`193`	`Albumin 2.`
`DOMAIN`	`404 601`	`198`	`Albumin 3.`
`METAL`	`27 27`		`Copper (By similarity).`
`BINDING`	`264 264`		`Bilirubin (Potential).`
`SITE`	`28 28`	`1`	`Not glycated.`
`SITE`	`44 44`	`1`	`Not glycated.`
`SITE`	`65 65`	`1`	`Not glycated.`
`SITE`	`88 88`	`1`	`Not glycated.`
`SITE`	`97 97`	`1`	`Not glycated.`
`SITE`	`117 117`	`1`	`Not glycated.`
`SITE`	`130 130`	`1`	`Not glycated.`
`SITE`	`160 160`	`1`	`Not glycated.`
`SITE`	`183 183`	`1`	`Not glycated.`
`SITE`	`198 198`	`1`	`Not glycated.`
`SITE`	`205 205`	`1`	`Not glycated.`
`SITE`	`214 214`	`1`	`Not glycated.`
`SITE`	`219 219`	`1`	`Not glycated.`
`SITE`	`223 223`	`1`	`Aspirin-acetylated lysine.`
`SITE`	`229 229`	`1`	`Not glycated.`
`SITE`	`236 236`	`1`	`Not glycated.`
`SITE`	`264 264`	`1`	`Not glycated.`
`SITE`	`286 286`	`1`	`Not glycated.`
`SITE`	`298 298`	`1`	`Not glycated.`
`SITE`	`310 310`	`1`	`Not glycated.`
`SITE`	`383 383`	`1`	`Not glycated.`
`SITE`	`396 396`	`1`	`Not glycated.`
`SITE`	`413 413`	`1`	`Not glycated.`
`SITE`	`426 426`	`1`	`Not glycated.`
`SITE`	`438 438`	`1`	`Not glycated.`
`SITE`	`456 456`	`1`	`Not glycated.`
`SITE`	`460 460`	`1`	`Not glycated.`
`SITE`	`490 490`	`1`	`Not glycated.`
`SITE`	`499 499`	`1`	`Not glycated.`
`SITE`	`524 524`	`1`	`Not glycated.`
`SITE`	`543 543`	`1`	`Not glycated.`
`SITE`	`548 548`	`1`	`Not glycated.`
`SITE`	`562 562`	`1`	`Not glycated.`
`SITE`	`565 565`	`1`	`Not glycated.`
`SITE`	`581 581`	`1`	`Not glycated.`
`SITE`	`584 584`	`1`	`Not glycated.`
`SITE`	`588 588`	`1`	`Not glycated.`
`SITE`	`598 598`	`1`	`Not glycated.`
`MOD_RES`	`82 82`		`Phosphoserine.`
`MOD_RES`	`108 108`		`Phosphotyrosine.`
`MOD_RES`	`164 164`		`Phosphotyrosine.`
`CARBOHYD`	`36 36`		`N-linked (Glc) (glycation) (Probable).`
`CARBOHYD`	`75 75`		`N-linked (Glc) (glycation); in vitro.`
`CARBOHYD`	`161 161`		`N-linked (Glc) (glycation); in vitro.`
`CARBOHYD`	`186 186`		`N-linked (Glc) (glycation); in vitro.`
`CARBOHYD`	`223 223`		`N-linked (Glc) (glycation); in vitro.`
`CARBOHYD`	`249 249`		`N-linked (Glc) (glycation); in vitro.`
`CARBOHYD`	`257 257`		`N-linked (Glc) (glycation) (Probable).`
`CARBOHYD`	`300 300`		`N-linked (Glc) (glycation); in vitro.`
`CARBOHYD`	`305 305`		`N-linked (Glc) (glycation).`
`CARBOHYD`	`337 337`		`N-linked (Glc) (glycation); in vitro.`
`CARBOHYD`	`341 341`		`N-linked (Glc) (glycation) (Probable).`
`CARBOHYD`	`342 342`		`N-linked (GlcNAc...); in variant Redhill [GlycoSuiteDB].`	`CAR_000226`
`CARBOHYD`	`347 347`		`N-linked (Glc) (glycation); in vitro.`
`CARBOHYD`	`375 375`		`N-linked (Glc) (glycation) (Probable).`
`CARBOHYD`	`402 402`		`N-linked (Glc) (glycation); in vitro.`
`CARBOHYD`	`437 437`		`N-linked (Glc) (glycation); in vitro.`
`CARBOHYD`	`463 463`		`N-linked (Glc) (glycation).`
`CARBOHYD`	`468 468`		`N-linked (Glc) (glycation); in vitro.`
`CARBOHYD`	`518 518`		`N-linked (GlcNAc...); in variant Casebrook [GlycoSuiteDB].`	`CAR_000069`
`CARBOHYD`	`549 549`		`N-linked (Glc) (glycation).`
`CARBOHYD`	`558 558`		`N-linked (Glc) (glycation) (Probable).`
`CARBOHYD`	`560 560`		`N-linked (Glc) (glycation); in vitro.`
`CARBOHYD`	`569 569`		`N-linked (Glc) (glycation); in vitro.`
`CARBOHYD`	`597 597`		`N-linked (Glc) (glycation); in vitro.`
`DISULFID`	`77 86`
`DISULFID`	`99 115`
`DISULFID`	`114 125`
`DISULFID`	`148 193`
`DISULFID`	`192 201`
`DISULFID`	`224 270`
`DISULFID`	`269 277`
`DISULFID`	`289 303`
`DISULFID`	`302 313`
`DISULFID`	`340 385`
`DISULFID`	`384 393`
`DISULFID`	`416 462`
`DISULFID`	`461 472`
`DISULFID`	`485 501`
`DISULFID`	`500 511`
`DISULFID`	`538 583`
`DISULFID`	`582 591`
`VAR_SEQ`	`43 234`		`Missing (in isoform 2).`	`VSP_021275`
`VARIANT`	`23 23`	`1`	`R -> C (in Redhill/Malmo-I/Tradate; associated with T-344 in Redhill).`	`VAR_000499`
`VARIANT`	`23 23`	`1`	`R -> H (in Fukuoka-2/Lille/Taipei/Varese/Komagome-3).`	`VAR_000500`
`VARIANT`	`24 24`	`1`	`R -> L (in Jaffna).`	`VAR_000501`
`VARIANT`	`24 24`	`1`	`R -> P (in Takefu/Honolulu-1).`	`VAR_000502`
`VARIANT`	`24 24`	`1`	`R -> Q (in Christchurch/Honolulu-2).`	`VAR_000503`
`VARIANT`	`25 25`	`1`	`D -> V (in Bleinheim/Iowa city-2).`	`VAR_000504`
`VARIANT`	`27 27`	`1`	`H -> Q (in Nagasaki-3).`	`VAR_000505 [3D]`
`VARIANT`	`27 27`	`1`	`H -> Y (in Larino).`	`VAR_000506 [3D]`
`VARIANT`	`73 73`	`1`	`F -> Y.`	`VAR_010657 [3D]`
`VARIANT`	`84 84`	`1`	`E -> K (in Torino).`	`VAR_000507 [3D]`
`VARIANT`	`87 87`	`1`	`D -> N (in Malmo-95/Dalakarlia).`	`VAR_000508 [3D]`
`VARIANT`	`90 90`	`1`	`L -> P (in FDH).`	`VAR_013011 [3D]`
`VARIANT`	`106 106`	`1`	`E -> K (in Vibo Valentia).`	`VAR_000509 [3D]`
`VARIANT`	`121 121`	`1`	`E -> G.`	`VAR_014290 [3D]`
`VARIANT`	`138 138`	`1`	`R -> G (in Yanomama-2).`	`VAR_000510 [3D]`
`VARIANT`	`143 143`	`1`	`E -> K (in Nagoya).`	`VAR_000511 [3D]`
`VARIANT`	`146 146`	`1`	`V -> E (in Tregasio).`	`VAR_013012 [3D]`
`VARIANT`	`152 152`	`1`	`H -> R (in Komagome-2).`	`VAR_000512 [3D]`
`VARIANT`	`201 201`	`1`	`C -> F (in Hawkes bay).`	`VAR_000513 [3D]`
`VARIANT`	`215 215`	`1`	`A -> T (in dbSNP:rs3210154 [NCBI]).`	`VAR_014291 [3D]`
`VARIANT`	`215 215`	`1`	`A -> V (in dbSNP:rs3204504 [NCBI]).`	`VAR_014292 [3D]`
`VARIANT`	`220 220`	`1`	`Q -> L (in dbSNP:rs3210163 [NCBI]).`	`VAR_014293 [3D]`
`VARIANT`	`242 242`	`1`	`R -> H (in FDH).`	`VAR_000514 [3D]`
`VARIANT`	`242 242`	`1`	`R -> P (in FDH).`	`VAR_013013 [3D]`
`VARIANT`	`249 249`	`1`	`K -> Q (in Tradate-2).`	`VAR_000515 [3D]`
`VARIANT`	`264 264`	`1`	`K -> E (in Herborn).`	`VAR_000516 [3D]`
`VARIANT`	`292 292`	`1`	`Q -> R (in Malmo-10).`	`VAR_000517 [3D]`
`VARIANT`	`293 293`	`1`	`D -> G (in Nagasaki-1).`	`VAR_000518 [3D]`
`VARIANT`	`300 300`	`1`	`K -> N (in Caserta).`	`VAR_000519 [3D]`
`VARIANT`	`337 337`	`1`	`K -> N (in Canterbury/New Guinea/Tagliacozzo/Cuneo/Cooperstown).`	`VAR_000520 [3D]`
`VARIANT`	`338 338`	`1`	`D -> G (in Bergamo).`	`VAR_013014 [3D]`
`VARIANT`	`338 338`	`1`	`D -> V (in Brest).`	`VAR_013015 [3D]`
`VARIANT`	`342 342`	`1`	`N -> K (in Malmo-47).`	`VAR_000521 [3D]`
`VARIANT`	`344 344`	`1`	`A -> T (in Redhill; associated with C-23).`	`VAR_000522 [3D]`
`VARIANT`	`345 345`	`1`	`E -> K (in Roma).`	`VAR_000523 [3D]`
`VARIANT`	`357 357`	`1`	`E -> K (in Sondrio).`	`VAR_000524 [3D]`
`VARIANT`	`378 378`	`1`	`E -> K (in Hiroshima-1).`	`VAR_000525 [3D]`
`VARIANT`	`382 382`	`1`	`E -> K (in Coari I/Porto Alegre).`	`VAR_000526 [3D]`
`VARIANT`	`383 383`	`1`	`K -> N (in Trieste).`	`VAR_013016 [3D]`
`VARIANT`	`389 389`	`1`	`D -> H (in Parklands).`	`VAR_000527 [3D]`
`VARIANT`	`389 389`	`1`	`D -> V (in Iowa city-1).`	`VAR_000528 [3D]`
`VARIANT`	`396 396`	`1`	`K -> E (in Naskapi/Mersin/Komagome-1).`	`VAR_000529 [3D]`
`VARIANT`	`399 399`	`1`	`D -> N (in Nagasaki-2).`	`VAR_000530 [3D]`
`VARIANT`	`400 400`	`1`	`E -> K (in Tochigi).`	`VAR_000531 [3D]`
`VARIANT`	`400 400`	`1`	`E -> Q (in Malmo-5).`	`VAR_000532 [3D]`
`VARIANT`	`406 406`	`1`	`E -> K (in Hiroshima-2).`	`VAR_000533 [3D]`
`VARIANT`	`420 420`	`1`	`E -> K.`	`VAR_014294 [3D]`
`VARIANT`	`434 434`	`1`	`R -> C (in Liprizzi).`	`VAR_013017 [3D]`
`VARIANT`	`490 490`	`1`	`K -> E (in dbSNP:rs1063469 [NCBI]).`	`VAR_014295 [3D]`
`VARIANT`	`503 503`	`1`	`E -> K (in Dublin).`	`VAR_000534 [3D]`
`VARIANT`	`518 518`	`1`	`D -> N (in Casebrook).`	`VAR_000535 [3D]`
`VARIANT`	`525 525`	`1`	`E -> K (in Manaus-1/Adana/Lambadi/Vancouver).`	`VAR_000536 [3D]`
`VARIANT`	`529 529`	`1`	`E -> K (in Ortonovo).`	`VAR_000537 [3D]`
`VARIANT`	`557 557`	`1`	`V -> M (in Maddaloni).`	`VAR_013018 [3D]`
`VARIANT`	`560 560`	`1`	`K -> E (in Castel di Sangro).`	`VAR_000538 [3D]`
`VARIANT`	`565 565`	`1`	`K -> E (in Maku).`	`VAR_000539 [3D]`
`VARIANT`	`574 574`	`1`	`D -> A (in Malmo-61).`	`VAR_000541 [3D]`
`VARIANT`	`574 574`	`1`	`D -> G (in Mexico).`	`VAR_000540 [3D]`
`VARIANT`	`584 584`	`1`	`K -> E (in Church bay).`	`VAR_013019 [3D]`
`VARIANT`	`587 587`	`1`	`D -> N (in Fukuoka-1/Paris-2).`	`VAR_000542 [3D]`
`VARIANT`	`589 589`	`1`	`E -> K (in Osaka-1).`	`VAR_000543 [3D]`
`VARIANT`	`594 594`	`1`	`E -> K (in Osaka-2/Phnom Phen/albumin B/Verona).`	`VAR_000544 [3D]`
`VARIANT`	`596 609`	`14`	`GKKLVAASQAALGL -> PTMRIRERK (in Venezia).`	`VAR_000547`
`VARIANT`	`597 597`	`1`	`K -> E (in Gent/Milano Fast).`	`VAR_000545 [3D]`
`VARIANT`	`598 598`	`1`	`K -> N (in Vanves).`	`VAR_000546 [3D]`
`VARIANT`	`599 609`	`11`	`LVAASQAALGL -> TCCCKSSCLRLITSHLKASQPTMRIRERK (in Kenitra).`	`VAR_012981`
`CONFLICT`	`55 55`		`L -> P (in Ref. 11; CAH18185).`
`CONFLICT`	`118 119`		`QE -> EQ (in Ref. 5).`
`CONFLICT`	`122 122`		`R -> S (in Ref. 4; AAF01333).`
`CONFLICT`	`155 155`		`E -> Q (in Ref. 18; AA sequence).`
`CONFLICT`	`174 174`		`Y -> L (in Ref. 23 and 24).`
`CONFLICT`	`194 194`		`Q -> E (in Ref. 18; AA sequence).`
`CONFLICT`	`327 332`		`PSLAAD -> MFVLLC (in Ref. 10; AAF71067).`
`CONFLICT`	`405 405`		`V -> A (in Ref. 10; AAF71067).`
`CONFLICT`	`409 409`		`Q -> E (in Ref. 10; AAH14308).`
`CONFLICT`	`441 441`		`Q -> E (in Ref. 2; CAA23753).`
`CONFLICT`	`466 466`		`E -> G (in Ref. 4; AAF01333).`
`CONFLICT`	`488 489`		`HE -> EH (in Ref. 18; AA sequence).`
`CONFLICT`	`490 490`		`K -> R (in Ref. 11; CAH18185).`
`CONFLICT`	`525 525`		`E -> Q (in Ref. 18; AA sequence).`
`CONFLICT`	`551 551`		`T -> A (in Ref. 11; CAH18185).`
`CONFLICT`	`560 560`		`K -> R (in Ref. 11; CAH18185).`
`CONFLICT`	`604 604`		`Q -> R (in Ref. 5; AAN17825).`
`HELIX`	`31 54`	`24`
`HELIX`	`60 79`	`20`
`STRAND`	`83 85`	`3`
`HELIX`	`90 102`	`13`
`HELIX`	`105 108`	`4`
`HELIX`	`111 115`	`5`
`TURN`	`119 123`	`5`
`HELIX`	`124 128`	`5`
`HELIX`	`144 153`	`10`
`HELIX`	`155 167`	`13`
`HELIX`	`175 192`	`18`
`STRAND`	`195 197`	`3`
`HELIX`	`198 230`	`33`
`HELIX`	`232 246`	`15`
`HELIX`	`252 271`	`20`
`HELIX`	`274 290`	`17`
`HELIX`	`292 295`	`4`
`HELIX`	`300 303`	`4`
`HELIX`	`307 314`	`8`
`HELIX`	`330 333`	`4`
`HELIX`	`339 345`	`7`
`HELIX`	`347 360`	`14`
`HELIX`	`367 385`	`19`
`HELIX`	`390 393`	`4`
`HELIX`	`394 397`	`4`
`HELIX`	`398 438`	`41`
`HELIX`	`444 461`	`18`
`HELIX`	`466 490`	`25`
`HELIX`	`495 503`	`9`
`HELIX`	`508 514`	`7`
`HELIX`	`528 530`	`3`
`HELIX`	`535 539`	`5`
`HELIX`	`542 559`	`18`
`STRAND`	`561 563`	`3`
`HELIX`	`567 584`	`18`
`HELIX`	`591 605`	`15`

Sequence information

Length: 609 AA [This is the length of the unprocessed precursor]

Molecular weight: 69367 Da [This is the MW of the unprocessed precursor]

CRC64: F88FF61DD242E818 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKWVTFISLL FLFSSAYSRG VFRRDAHKSE VAHRFKDLGE ENFKALVLIA FAQYLQQCPF 

        70         80         90        100        110        120 
EDHVKLVNEV TEFAKTCVAD ESAENCDKSL HTLFGDKLCT VATLRETYGE MADCCAKQEP 

       130        140        150        160        170        180 
ERNECFLQHK DDNPNLPRLV RPEVDVMCTA FHDNEETFLK KYLYEIARRH PYFYAPELLF 

       190        200        210        220        230        240 
FAKRYKAAFT ECCQAADKAA CLLPKLDELR DEGKASSAKQ RLKCASLQKF GERAFKAWAV 

       250        260        270        280        290        300 
ARLSQRFPKA EFAEVSKLVT DLTKVHTECC HGDLLECADD RADLAKYICE NQDSISSKLK 

       310        320        330        340        350        360 
ECCEKPLLEK SHCIAEVEND EMPADLPSLA ADFVESKDVC KNYAEAKDVF LGMFLYEYAR 

       370        380        390        400        410        420 
RHPDYSVVLL LRLAKTYETT LEKCCAAADP HECYAKVFDE FKPLVEEPQN LIKQNCELFE 

       430        440        450        460        470        480 
QLGEYKFQNA LLVRYTKKVP QVSTPTLVEV SRNLGKVGSK CCKHPEAKRM PCAEDYLSVV 

       490        500        510        520        530        540 
LNQLCVLHEK TPVSDRVTKC CTESLVNRRP CFSALEVDET YVPKEFNAET FTFHADICTL 

       550        560        570        580        590        600 
SEKERQIKKQ TALVELVKHK PKATKEQLKA VMDDFAAFVE KCCKADDKET CFAEEGKKLV 


AASQAALGL

P02768 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools