ID ALBU_HUMAN Reviewed; 609 AA. AC P02768; O95574; P04277; Q13140; Q645G4; Q68DN5; Q6UXK4; Q86YG0; AC Q9P157; Q9P1I7; Q9UHS3; Q9UJZ0; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 2. DT 16-JUN-2009, entry version 148. DE RecName: Full=Serum albumin; DE Flags: Precursor; GN Name=ALB; GN ORFNames=GIG20, GIG42, PRO0903, PRO1708, PRO2044, PRO2619, PRO2675, GN UNQ696/PRO1341; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LYS-420. RX MEDLINE=82081882; PubMed=6171778; DOI=10.1093/nar/9.22.6103; RA Lawn R.M., Adelman J., Bock S.C., Franke A.E., Houck C.M., RA Najarian R.C., Seeburg P.H., Wion K.L.; RT "The sequence of human serum albumin cDNA and its expression in E. RT coli."; RL Nucleic Acids Res. 9:6103-6114(1981). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-121. RX MEDLINE=82105994; PubMed=6275391; DOI=10.1073/pnas.79.1.71; RA Dugaiczyk A., Law S.W., Dennison O.E.; RT "Nucleotide sequence and the encoded amino acids of human serum RT albumin mRNA."; RL Proc. Natl. Acad. Sci. U.S.A. 79:71-75(1982). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=86196112; PubMed=3009475; RA Minghetti P.P., Ruffner D.E., Kuang W.J., Dennison O.E., Hawkins J.W., RA Beattie W.G., Dugaiczyk A.; RT "Molecular structure of the human albumin gene is revealed by RT nucleotide sequence within q11-22 of chromosome 4."; RL J. Biol. Chem. 261:6747-6757(1986). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RA Yang S., Zhang R.A., Qi Z.W., Yuan Z.Y.; RT "Human serum albumin."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT HIROSHIMA-1 RP LYS-378. RA Huang M.C., Wu H.T.; RT "The cDNA sequences of human serum albumin."; RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Hinchliffe E.; RT "Induction of galactose regulated gene expression in yeast."; RL Patent number EP0248637, 09-DEC-1987. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RA Yu Z., Fu Y.; RT "High expression HSA in Pichia for Pharmaceutical Use."; RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Wang F., Huang L.; RT "Cloning and sequence analysis of human albumin gene."; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RA Kim J.W.; RT "Identification of a human cell growth inhibition gene."; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Fetal liver; RX MEDLINE=21376145; PubMed=11483580; DOI=10.1101/gr.175501; RA Yu Y., Zhang C., Zhou G., Wu S., Qu X., Wei H., Xing G., Dong C., RA Zhai Y., Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C., RA He F.; RT "Gene expression profiling in human fetal liver and identification of RT tissue- and developmental-stage-specific genes through compiled RT expression profiles and efficient cloning of full-length cDNAs."; RL Genome Res. 11:1392-1403(2001). RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP TYR-27. RC TISSUE=Liver; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., RA Ottenwalder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG SeattleSNPs variation discovery resource; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [14] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Liver, and Skeletal muscle; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [15] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-455. RC TISSUE=Liver; RA Menaya J., Parrilla R., Ayuso M.S.; RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases. RN [16] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-167. RX MEDLINE=22887296; PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., RA Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale RT effort to identify novel human secreted and transmembrane proteins: a RT bioinformatics assessment."; RL Genome Res. 13:2265-2270(2003). RN [17] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26. RX MEDLINE=86140099; PubMed=2419329; RA Urano Y., Watanabe K., Sakai M., Tamaoki T.; RT "The human albumin gene. Characterization of the 5' and 3' flanking RT regions and the polymorphic gene transcripts."; RL J. Biol. Chem. 261:3244-3251(1986). RN [18] RP PROTEIN SEQUENCE OF 25-609. RX MEDLINE=76187907; PubMed=1225573; DOI=10.1016/0014-5793(75)80242-0; RA Meloun B., Moravek L., Kostka V.; RT "Complete amino acid sequence of human serum albumin."; RL FEBS Lett. 58:134-137(1975). RN [19] RP PROTEIN SEQUENCE OF 25-609. RA Brown J.R., Shockley P., Behrens P.Q.; RL (In) Bing D.H. (eds.); RL The chemistry and physiology of the human plasma proteins, pp.23-40, RL Pergamon Press, New York (1979). RN [20] RP PROTEIN SEQUENCE OF 25-44 AND 480-499. RC TISSUE=Heart; RX MEDLINE=95203287; PubMed=7895732; DOI=10.1002/elps.11501501209; RA Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.; RT "The human myocardial two-dimensional gel protein database: update RT 1994."; RL Electrophoresis 15:1459-1465(1994). RN [21] RP PROTEIN SEQUENCE OF 25-34. RC TISSUE=Platelet; RX MEDLINE=22608298; PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [22] RP PROTEIN SEQUENCE OF 45-75; 98-130; 162-183; 239-254; 265-281; 287-298; RP 348-372; 397-434; 438-452; 500-543; 550-558; 570-581 AND 599-609, AND RP MASS SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [23] RP PROTEIN SEQUENCE OF 166-174. RX MEDLINE=86242180; PubMed=3087352; DOI=10.1016/0006-291X(86)90429-8; RA Mogard M.H., Kobayashi R., Chen C.F., Lee T.D., Reeve J.R. Jr., RA Shively J.E., Walsh J.H.; RT "The amino acid sequence of kinetensin, a novel peptide isolated from RT pepsin-treated human plasma: homology with human serum albumin, RT neurotensin and angiotensin."; RL Biochem. Biophys. Res. Commun. 136:983-988(1986). RN [24] RP PROTEIN SEQUENCE OF 166-174. RX MEDLINE=87194805; PubMed=2437111; RA Carraway R.E., Mitra S.P., Cochrane D.E.; RT "Structure of a biologically active neurotensin-related peptide RT obtained from pepsin-treated albumin(s)."; RL J. Biol. Chem. 262:5968-5973(1987). RN [25] RP PROTEIN SEQUENCE OF 222-229, AND ASPIRIN-ACETYLATION AT LYS-223. RX MEDLINE=76257808; PubMed=955075; DOI=10.1016/0014-5793(76)80496-6; RA Walker J.E.; RT "Lysine residue 199 of human serum albumin is modified by RT acetylsalicylic acid."; RL FEBS Lett. 66:173-175(1976). RN [26] RP PROTEIN SEQUENCE OF 250-264, GLYCATION AT LYS-75; LYS-161; LYS-186; RP LYS-249; LYS-257; LYS-300; LYS-337; LYS-347; LYS-375; LYS-402; RP LYS-437; LYS-468; LYS-560; LYS-549; LYS-569 AND LYS-597, ABSENCE OF RP GLYCATION AT LYS-28; LYS-44; LYS-65; LYS-88; LYS-97; LYS-117; LYS-130; RP LYS-160; LYS-183; LYS-198; LYS-205; LYS-214; LYS-219; LYS-229; RP LYS-236; LYS-264; LYS-286; LYS-298; LYS-310; LYS-383; LYS-396; RP LYS-413; LYS-426; LYS-438; LYS-456; LYS-460; LYS-490; LYS-499; RP LYS-524; LYS-543; LYS-548; LYS-562; LYS-565; LYS-581; LYS-584; LYS-588 RP AND LYS-598, AND MASS SPECTROMETRY. RX PubMed=15047055; DOI=10.1016/j.jasms.2003.11.014; RA Lapolla A., Fedele D., Reitano R., Arico N.C., Seraglia R., Traldi P., RA Marotta E., Tonani R.; RT "Enzymatic digestion and mass spectrometry in the study of advanced RT glycation end products/peptides."; RL J. Am. Soc. Mass Spectrom. 15:496-509(2004). RN [27] RP DISULFIDE BONDS. RA Saber M.A., Stockbauer P., Moravek L., Meloun B.; RT "Disulfide bonds in human serum albumin."; RL Collect. Czech. Chem. Commun. 42:564-579(1977). RN [28] RP BILIRUBIN-BINDING SITE. RX MEDLINE=78186630; PubMed=656055; RA Jacobsen C.; RT "Lysine residue 240 of human serum albumin is involved in high- RT affinity binding of bilirubin."; RL Biochem. J. 171:453-459(1978). RN [29] RP GLYCATION AT LYS-223 AND LYS-549. RX PubMed=6853480; RA Garlick R.L., Mazer J.S.; RT "The principal site of nonenzymatic glycosylation of human serum RT albumin in vivo."; RL J. Biol. Chem. 258:6142-6146(1983). RN [30] RP GLYCATION AT LYS-549. RX PubMed=6706980; RA Shaklai N., Garlick R.L., Bunn H.F.; RT "Nonenzymatic glycosylation of human serum albumin alters its RT conformation and function."; RL J. Biol. Chem. 259:3812-3817(1984). RN [31] RP GLYCATION AT LYS-36; LYS-223; LYS-257; LYS-305; LYS-341; LYS-375; RP LYS-463; LYS-549 AND LYS-558. RX PubMed=3759977; RA Iberg N., Fluckiger R.; RT "Nonenzymatic glycosylation of albumin in vivo. Identification of RT multiple glycosylated sites."; RL J. Biol. Chem. 261:13542-13545(1986). RN [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-108 AND TYR-164, AND RP MASS SPECTROMETRY. RX PubMed=18083107; DOI=10.1016/j.cell.2007.11.025; RA Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., RA Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., RA Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., RA Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., RA Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; RT "Global survey of phosphotyrosine signaling identifies oncogenic RT kinases in lung cancer."; RL Cell 131:1190-1203(2007). RN [33] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND MASS RP SPECTROMETRY. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by RT enrichment and fractionation of phosphopeptides with strong anion RT exchange chromatography."; RL Proteomics 8:1346-1361(2008). RN [34] RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [35] RP X-RAY CRYSTALLOGRAPHY (6.0 ANGSTROMS). RX MEDLINE=89266946; PubMed=2727704; DOI=10.1126/science.2727704; RA Carter D.C., He X.-M., Munson S.H., Twigg P.D., Gernert K.M., RA Broom M.B., Miller T.Y.; RT "Three-dimensional structure of human serum albumin."; RL Science 244:1195-1198(1989). RN [36] RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS). RX MEDLINE=90327082; PubMed=2374930; DOI=10.1126/science.2374930; RA Carter D.C., He X.-M.; RT "Structure of human serum albumin."; RL Science 249:302-303(1990). RN [37] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX MEDLINE=92334427; PubMed=1630489; DOI=10.1038/358209a0; RA He X.-M., Carter D.C.; RT "Atomic structure and chemistry of human serum albumin."; RL Nature 358:209-215(1992). RN [38] RP ERRATUM. RA He X.-M., Carter D.C.; RL Nature 364:362-362(1993). RN [39] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX MEDLINE=98400504; PubMed=9731778; DOI=10.1038/1869; RA Curry S., Mandelkow H., Brick P., Franks N.; RT "Crystal structure of human serum albumin complexed with fatty acid RT reveals an asymmetric distribution of binding sites."; RL Nat. Struct. Biol. 5:827-835(1998). RN [40] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX MEDLINE=99318973; PubMed=10388840; DOI=10.1093/protein/12.6.439; RA Sugio S., Kashima A., Mochizuki S., Noda M., Kobayashi K.; RT "Crystal structure of human serum albumin at 2.5-A resolution."; RL Protein Eng. 12:439-446(1999). RN [41] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-609. RX MEDLINE=20556323; PubMed=10940303; DOI=10.1074/jbc.M005460200; RA Bhattacharya A.A., Curry S., Franks N.P.; RT "Binding of the general anesthetics propofol and halothane to human RT serum albumin. High resolution crystal structures."; RL J. Biol. Chem. 275:38731-38738(2000). RN [42] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX MEDLINE=21611699; PubMed=11743713; DOI=10.1006/jmbi.2000.5208; RA Petitpas I., Grune T., Bhattacharya A.A., Curry S.; RT "Crystal structures of human serum albumin complexed with RT monounsaturated and polyunsaturated fatty acids."; RL J. Mol. Biol. 314:955-960(2001). RN [43] RP VARIANT CANTERBURY ASN-337. RX MEDLINE=87157744; PubMed=3828358; DOI=10.1016/0167-4838(87)90088-4; RA Brennan S.O., Herbert P.; RT "Albumin Canterbury (313 Lys-->Asn). A point mutation in the second RT domain of serum albumin."; RL Biochim. Biophys. Acta 912:191-197(1987). RN [44] RP VARIANTS NASKAPI/MERSIN GLU-396 AND MEXICO GLY-574. RX MEDLINE=87260818; PubMed=3474609; DOI=10.1073/pnas.84.13.4413; RA Takahashi N., Takahashi Y., Blumberg B.S., Putnam F.W.; RT "Amino acid substitutions in genetic variants of human serum albumin RT and in sequences inferred from molecular cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 84:4413-4417(1987). RN [45] RP VARIANTS NAGASAKI-3 GLN-27 YANOMAMA-2 GLU-396; NAGASAKI-2 ASN-399 AND RP MAKU GLU-565. RX MEDLINE=88068523; PubMed=3479777; DOI=10.1073/pnas.84.22.8001; RA Takshashi N., Takahashi Y., Isobe T., Putnam F.W., Fujita M., RA Satoh C., Neel J.V.; RT "Amino acid substitutions in inherited albumin variants from RT Amerindian and Japanese populations."; RL Proc. Natl. Acad. Sci. U.S.A. 84:8001-8005(1987). RN [46] RP VARIANTS FUKUOKA-2 HIS-23; CHRISTCHURCH/HONOLULU-2 GLN-24; TAGLIACOZZO RP ASN-337 AND ALBUMIN B/OSAKA-2/PHNOM PHEN LYS-594. RX MEDLINE=89098947; PubMed=2911589; DOI=10.1073/pnas.86.2.434; RA Arai K., Ishioka N., Huss K., Madison J., Putnam F.W.; RT "Identical structural changes in inherited albumin variants from RT different populations."; RL Proc. Natl. Acad. Sci. U.S.A. 86:434-438(1989). RN [47] RP VARIANTS HONOLULU-2 GLN-24; NAGASAKI-1 GLY-293; HIROSHIMA-1 LYS-378; RP TOCHIGI LYS-400; HIROSHIMA-2 LYS-406 AND OSAKA-2 LYS-594. RX MEDLINE=89345611; PubMed=2762316; DOI=10.1073/pnas.86.16.6092; RA Arai K., Madison J., Huss K., Ishioka N., Satoh C., Fujita M., RA Neel J.V., Sakurabayashi I., Putnam F.W.; RT "Point substitutions in Japanese alloalbumins."; RL Proc. Natl. Acad. Sci. U.S.A. 86:6092-6096(1989). RN [48] RP VARIANTS HONOLULU-1 PRO-24; HONOLULU-2 GLN-24; NAGOYA LYS-143; NEW RP GUINEA ASN-337; MANAUS-1/LAMBADI LYS-525; FUKUOKA-1 ASN-587; OSAKA-1 RP LYS-589 AND OSAKA-2 LYS-594. RX MEDLINE=90115905; PubMed=2404284; DOI=10.1073/pnas.87.1.497; RA Arai K., Madison J., Shimuzu A., Putnam F.W.; RT "Point substitutions in albumin genetic variants from Asia."; RL Proc. Natl. Acad. Sci. U.S.A. 87:497-501(1990). RN [49] RP CHARACTERIZATION OF VARIANT REDHILL. RX MEDLINE=90115852; PubMed=2104980; DOI=10.1073/pnas.87.1.26; RA Brennan S.O., Myles T., Peach R.J., Donaldson D., George P.M.; RT "Albumin Redhill (-1 Arg, 320 Ala-->Thr): a glycoprotein variant of RT human serum albumin whose precursor has an aberrant signal peptidase RT cleavage site."; RL Proc. Natl. Acad. Sci. U.S.A. 87:26-30(1990). RN [50] RP VARIANTS VARESE HIS-23; TORINO LYS-84 AND VIBO VALENTIA LYS-106. RX MEDLINE=91062352; PubMed=2247440; DOI=10.1073/pnas.87.22.8721; RA Galliano M., Minchiotti L., Porta F., Rossi A., Ferri G., Madison J., RA Watkins S., Putnam F.W.; RT "Mutations in genetic variants of human serum albumin found in RT Italy."; RL Proc. Natl. Acad. Sci. U.S.A. 87:8721-8725(1990). RN [51] RP CHARACTERIZATION OF VARIANT VENEZIA. RX MEDLINE=91296740; PubMed=2068071; DOI=10.1073/pnas.88.14.5959; RA Watkins S., Madison J., Davis E., Sakamoto Y., Galliano M., RA Minchiotti L., Putnam F.W.; RT "A donor splice mutation and a single-base deletion produce two RT carboxyl-terminal variants of human serum albumin."; RL Proc. Natl. Acad. Sci. U.S.A. 88:5959-5963(1991). RN [52] RP VARIANTS KOMAGOME-3 HIS-23; IOWA CITY-2 VAL-25; KOMAGOME-2 ARG-152; RP IOWA CITY-1 VAL-389 AND KOMAGOME-1 GLU-396. RX MEDLINE=92052189; PubMed=1946412; DOI=10.1073/pnas.88.21.9853; RA Madison J., Arai K., Feld R.D., Kyle R.A., Watkins S., Davis E., RA Matsuda Y., Amaki I., Putnam F.W.; RT "Genetic variants of serum albumin in Americans and Japanese."; RL Proc. Natl. Acad. Sci. U.S.A. 88:9853-9857(1991). RN [53] RP VARIANT CASEBROOK ASN-518. RX MEDLINE=91316157; PubMed=1859851; DOI=10.1016/0925-4439(91)90023-3; RA Peach R.J., Brennan S.O.; RT "Structural characterization of a glycoprotein variant of human serum RT albumin: albumin Casebrook (494 Asp-->Asn)."; RL Biochim. Biophys. Acta 1097:49-54(1991). RN [54] RP VARIANTS SONDRIO LYS-357 AND PARIS-2 ASN-587. RX MEDLINE=92190239; PubMed=1347703; DOI=10.1016/0167-4838(92)90207-T; RA Minchiotti L., Galliano M., Stoppini M., Ferri G., Crespeau H., RA Rochu D., Porta F.; RT "Two alloalbumins with identical electrophoretic mobility are produced RT by differently charged amino acid substitutions."; RL Biochim. Biophys. Acta 1119:232-238(1992). RN [55] RP VARIANTS MALMO-I CYS-23; MALMO-95 ASN-87; MALMO-10 ARG-292; MALMO-47 RP LYS-342; MALMO-5 GLN-400 AND MALMO-61 ALA-574. RX MEDLINE=92390419; PubMed=1518850; DOI=10.1073/pnas.89.17.8225; RA Carlson J., Sakamoto Y., Laurell C.-B., Madison J., Watkins S., RA Putnam F.W.; RT "Alloalbuminemia in Sweden: structural study and phenotypic RT distribution of nine albumin variants."; RL Proc. Natl. Acad. Sci. U.S.A. 89:8225-8229(1992). RN [56] RP VARIANT HERBORN GLU-264. RX MEDLINE=93292504; PubMed=8513793; RX DOI=10.1111/j.1432-1033.1993.tb17939.x; RA Minchiotti L., Galliano M., Zapponi M.C., Tenni R.; RT "The structural characterization and bilirubin-binding properties of RT albumin Herborn, a [Lys240-->Glu] albumin mutant."; RL Eur. J. Biochem. 214:437-444(1993). RN [57] RP VARIANT HAWKES BAY PHE-201. RX MEDLINE=93349998; PubMed=8347685; DOI=10.1016/0925-4439(93)90151-P; RA Brennan S.O., Fellowes A.P.; RT "Albumin Hawkes Bay; a low level variant caused by loss of a RT sulphydryl group at position 177."; RL Biochim. Biophys. Acta 1182:46-50(1993). RN [58] RP VARIANT ORTONOVO LYS-529. RX MEDLINE=94060122; PubMed=7902134; DOI=10.1016/0925-4439(93)90117-J; RA Galliano M., Minchiotti L., Iadarola P., Stoppini M., Giagnoni P., RA Watkins S., Madison J., Putnam F.W.; RT "Protein and DNA sequence analysis of a 'private' genetic variant: RT albumin Ortonovo (Glu-505-->Lys)."; RL Biochim. Biophys. Acta 1225:27-32(1993). RN [59] RP VARIANTS LARINO TYR-27; TRADATE-2 GLN-249 AND CASERTA ASN-300. RX MEDLINE=94294404; PubMed=8022807; DOI=10.1073/pnas.91.14.6476; RA Madison J., Galliano M., Watkins S., Minchiotti L., Porta F., RA Rossi A., Putnam F.W.; RT "Genetic variants of human serum albumin in Italy: point mutants and a RT carboxyl-terminal variant."; RL Proc. Natl. Acad. Sci. U.S.A. 91:6476-6480(1994). RN [60] RP VARIANT FDH HIS-242. RX MEDLINE=94324967; PubMed=8048949; DOI=10.1006/bbrc.1994.1998; RA Sunthornthepvarakul T., Angkeow P., Weiss R.E., Hayashi Y., RA Retetoff S.; RT "An identical missense mutation in the albumin gene results in RT familial dysalbuminemic hyperthyroxinemia in 8 unrelated families."; RL Biochem. Biophys. Res. Commun. 202:781-787(1994). RN [61] RP VARIANT FDH HIS-242, AND PROTEIN SEQUENCE OF 25-51. RX MEDLINE=95155525; PubMed=7852505; DOI=10.1210/jc.80.2.461; RA Rushbrook J.I., Becker E., Schussler G.C., Divino C.M.; RT "Identification of a human serum albumin species associated with RT familial dysalbuminemic hyperthyroxinemia."; RL J. Clin. Endocrinol. Metab. 80:461-467(1995). RN [62] RP VARIANT FDH HIS-242. RX MEDLINE=97469930; PubMed=9329347; DOI=10.1210/jc.82.10.3246; RA Wada N., Chiba H., Shimizu C., Kijima H., Kubo M., Koike T.; RT "A novel missense mutation in codon 218 of the albumin gene in a RT distinct phenotype of familial dysalbuminemic hyperthyroxinemia in a RT Japanese kindred."; RL J. Clin. Endocrinol. Metab. 82:3246-3250(1997). RN [63] RP VARIANT FDH PRO-90. RX MEDLINE=98251548; PubMed=9589637; DOI=10.1210/jc.83.5.1448; RA Sunthornthepvarakul T., Likitmaskul S., Ngowngarmratana S., RA Angsusingha K., Kitvitayasak S., Scherberg N.H., Refetoff S.; RT "Familial dysalbuminemic hypertriiodothyroninemia: a new, dominantly RT inherited albumin defect."; RL J. Clin. Endocrinol. Metab. 83:1448-1454(1998). RN [64] RP VARIANT TYR-73, AND MASS SPECTROMETRY. RC TISSUE=Urine; RX MEDLINE=21537959; PubMed=11680902; RX DOI=10.1002/1615-9861(200101)1:1<93::AID-PROT93>3.3.CO;2-V; RA Spahr C.S., Davis M.T., McGinley M.D., Robinson J.H., Bures E.J., RA Beierle J., Mort J., Courchesne P.L., Chen K., Wahl R.C., Yu W., RA Luethy R., Patterson S.D.; RT "Towards defining the urinary proteome using liquid chromatography- RT tandem mass spectrometry I. Profiling an unfractionated tryptic RT digest."; RL Proteomics 1:93-107(2001). RN [65] RP CHARACTERIZATION OF VARIANT KENITRA. RX MEDLINE=21099299; PubMed=11168369; RX DOI=10.1046/j.1432-1033.2001.01899.x; RA Minchiotti L., Campagnoli M., Rossi A., Cosulich M.E., Monti M., RA Pucci P., Kragh-Hansen U., Granel B., Disdier P., Weiller P.J., RA Galliano M.; RT "A nucleotide insertion and frameshift cause albumin Kenitra, an RT extended and O-glycosylated mutant of human serum albumin with two RT additional disulfide bridges."; RL Eur. J. Biochem. 268:344-352(2001). CC -!- FUNCTION: Serum albumin, the main protein of plasma, has a good CC binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, CC hormones, bilirubin and drugs. Its main function is the regulation CC of the colloidal osmotic pressure of blood. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P02768-1; Sequence=Displayed; CC Name=2; CC IsoId=P02768-2; Sequence=VSP_021275; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Plasma. CC -!- PTM: Kenitra variant is partially O-glycosylated at Thr-620. It CC has two new disulfide bonds Cys-600 to Cys-602 and Cys-601 to Cys- CC 606. CC -!- PTM: Glycated in diabetic patients. CC -!- POLYMORPHISM: The sequence shown is that of variant albumin A. CC -!- DISEASE: Defects in ALB are a cause of familial dysalbuminemic CC hyperthyroxinemia (FDH) [MIM:103600]. FDH is a form of euthyroid CC hyperthyroxinemia that is due to increased affinity of ALB for CC T(4). It is the most common cause of inherited euthyroid CC hyperthyroxinemia in Caucasian population. CC -!- DISEASE: A variant structure of albumin could lead to increased CC binding of zinc resulting in an asymptomatic augmentation of zinc CC concentration in the blood [MIM:194470]. CC -!- MISCELLANEOUS: Acetylated on Lys-223 by acetylsalicylic acid. CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. CC -!- SIMILARITY: Contains 3 albumin domains. CC -!- CAUTION: A peptide arising from positions 166 to 174 was CC originally (PubMed:3087352 and PubMed:2437111) termed neurotensin- CC related peptide (NRP) or kinetensin and was thought to regulates CC fat digestion, lipid absorption, and blood flow. CC -!- WEB RESOURCE: Name=Albumin Website; CC URL="http://www.albumin.org"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Serum albumin entry; CC URL="http://en.wikipedia.org/wiki/Serum_albumin"; CC -!- WEB RESOURCE: Name=GeneReviews; CC URL="http://www.genetests.org/query?gene=ALB"; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/alb/"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; V00494; CAA23753.1; -; mRNA. DR EMBL; V00495; CAA23754.1; -; mRNA. DR EMBL; M12523; AAA98797.1; -; Genomic_DNA. DR EMBL; M12523; AAA98798.1; -; Genomic_DNA. DR EMBL; AF190168; AAF01333.1; -; mRNA. DR EMBL; AF542069; AAN17825.1; -; mRNA. DR EMBL; A06977; CAA00606.1; -; Unassigned_RNA. DR EMBL; AY728024; AAU21642.1; -; mRNA. DR EMBL; DQ986150; ABJ16448.1; -; mRNA. DR EMBL; AY544124; AAT11155.1; -; mRNA. DR EMBL; AY550967; AAT52213.1; -; mRNA. DR EMBL; AF116645; AAF71067.1; -; mRNA. DR EMBL; AF118090; AAF22034.1; ALT_INIT; mRNA. DR EMBL; AF119840; AAF69594.1; -; mRNA. DR EMBL; AF119890; AAF69644.1; ALT_INIT; mRNA. DR EMBL; AF130077; AAG35503.1; ALT_INIT; mRNA. DR EMBL; CR749331; CAH18185.1; -; mRNA. DR EMBL; EF649953; ABS29264.1; -; Genomic_DNA. DR EMBL; CH471057; EAX05676.1; -; Genomic_DNA. DR EMBL; BC014308; AAH14308.1; -; mRNA. DR EMBL; BC034023; AAH34023.1; -; mRNA. DR EMBL; BC036003; AAH36003.1; -; mRNA. DR EMBL; BC041789; AAH41789.1; -; mRNA. DR EMBL; U22961; AAA64922.1; -; mRNA. DR EMBL; AY358313; AAQ89947.1; -; mRNA. DR EMBL; M13075; AAA51688.1; -; Genomic_DNA. DR IPI; IPI00384697; -. DR IPI; IPI00745872; -. DR PIR; A93743; ABHUS. DR RefSeq; NP_000468.1; -. DR UniGene; Hs.418167; -. DR PDB; 1AO6; X-ray; 2.50 A; A/B=25-609. DR PDB; 1BJ5; X-ray; 2.50 A; A=25-609. DR PDB; 1BKE; X-ray; 3.15 A; A=28-608. DR PDB; 1BM0; X-ray; 2.50 A; A/B=25-609. DR PDB; 1E78; X-ray; 2.60 A; A/B=25-609. DR PDB; 1E7A; X-ray; 2.20 A; A/B=25-609. DR PDB; 1E7B; X-ray; 2.38 A; A/B=25-609. DR PDB; 1E7C; X-ray; 2.40 A; A=25-609. DR PDB; 1E7E; X-ray; 2.50 A; A=25-609. DR PDB; 1E7F; X-ray; 2.43 A; A=25-609. DR PDB; 1E7G; X-ray; 2.50 A; A=25-609. DR PDB; 1E7H; X-ray; 2.43 A; A=25-609. DR PDB; 1E7I; X-ray; 2.70 A; A=25-609. DR PDB; 1GNI; X-ray; 2.40 A; A=25-609. DR PDB; 1GNJ; X-ray; 2.60 A; A=25-609. DR PDB; 1H9Z; X-ray; 2.50 A; A=25-609. DR PDB; 1HA2; X-ray; 2.50 A; A=25-609. DR PDB; 1HK1; X-ray; 2.65 A; A=25-609. DR PDB; 1HK2; X-ray; 2.80 A; A=25-609. DR PDB; 1HK3; X-ray; 2.80 A; A=25-609. DR PDB; 1HK4; X-ray; 2.40 A; A=25-609. DR PDB; 1HK5; X-ray; 2.70 A; A=25-609. DR PDB; 1N5U; X-ray; 1.90 A; A=25-609. DR PDB; 1O9X; X-ray; 3.20 A; A=25-609. DR PDB; 1TF0; X-ray; 2.70 A; A=25-596. DR PDB; 1UOR; X-ray; 2.80 A; A=25-609. DR PDB; 1YSX; NMR; -; A=409-609. DR PDB; 2BX8; X-ray; 2.70 A; A/B=25-609. DR PDB; 2BXA; X-ray; 2.35 A; A/B=25-609. DR PDB; 2BXB; X-ray; 3.20 A; A/B=25-609. DR PDB; 2BXC; X-ray; 3.10 A; A/B=25-609. DR PDB; 2BXD; X-ray; 3.05 A; A/B=25-609. DR PDB; 2BXE; X-ray; 2.95 A; A/B=25-609. DR PDB; 2BXF; X-ray; 2.95 A; A/B=25-609. DR PDB; 2BXG; X-ray; 2.70 A; A/B=25-609. DR PDB; 2BXH; X-ray; 2.25 A; A/B=25-609. DR PDB; 2BXI; X-ray; 2.50 A; A=25-609. DR PDB; 2BXK; X-ray; 2.40 A; A=25-609. DR PDB; 2BXL; X-ray; 2.60 A; A=25-609. DR PDB; 2BXM; X-ray; 2.50 A; A=25-609. DR PDB; 2BXN; X-ray; 2.65 A; A=25-609. DR PDB; 2BXO; X-ray; 2.60 A; A=25-609. DR PDB; 2BXP; X-ray; 2.30 A; A=25-609. DR PDB; 2BXQ; X-ray; 2.60 A; A=25-609. DR PDB; 2ESG; X-ray; -; C=25-609. DR PDB; 2I2Z; X-ray; 2.70 A; A=25-609. DR PDB; 2I30; X-ray; 2.90 A; A=25-609. DR PDB; 2VDB; X-ray; 2.52 A; A=30-608. DR PDB; 2VUE; X-ray; 2.42 A; A/B=25-609. DR PDB; 2VUF; X-ray; 3.05 A; A/B=25-609. DR PDB; 3B9L; X-ray; 2.60 A; A=25-609. DR PDB; 3B9M; X-ray; 2.70 A; A=25-609. DR PDB; 3CX9; X-ray; 2.80 A; A=27-608. DR PDBsum; 1AO6; -. DR PDBsum; 1BJ5; -. DR PDBsum; 1BKE; -. DR PDBsum; 1BM0; -. DR PDBsum; 1E78; -. DR PDBsum; 1E7A; -. DR PDBsum; 1E7B; -. DR PDBsum; 1E7C; -. DR PDBsum; 1E7E; -. DR PDBsum; 1E7F; -. DR PDBsum; 1E7G; -. DR PDBsum; 1E7H; -. DR PDBsum; 1E7I; -. DR PDBsum; 1GNI; -. DR PDBsum; 1GNJ; -. DR PDBsum; 1H9Z; -. DR PDBsum; 1HA2; -. DR PDBsum; 1HK1; -. DR PDBsum; 1HK2; -. DR PDBsum; 1HK3; -. DR PDBsum; 1HK4; -. DR PDBsum; 1HK5; -. DR PDBsum; 1N5U; -. DR PDBsum; 1O9X; -. DR PDBsum; 1TF0; -. DR PDBsum; 1UOR; -. DR PDBsum; 1YSX; -. DR PDBsum; 2BX8; -. DR PDBsum; 2BXA; -. DR PDBsum; 2BXB; -. DR PDBsum; 2BXC; -. DR PDBsum; 2BXD; -. DR PDBsum; 2BXE; -. DR PDBsum; 2BXF; -. DR PDBsum; 2BXG; -. DR PDBsum; 2BXH; -. DR PDBsum; 2BXI; -. DR PDBsum; 2BXK; -. DR PDBsum; 2BXL; -. DR PDBsum; 2BXM; -. DR PDBsum; 2BXN; -. DR PDBsum; 2BXO; -. DR PDBsum; 2BXP; -. DR PDBsum; 2BXQ; -. DR PDBsum; 2ESG; -. DR PDBsum; 2I2Z; -. DR PDBsum; 2I30; -. DR PDBsum; 2VDB; -. DR PDBsum; 2VUE; -. DR PDBsum; 2VUF; -. DR PDBsum; 3B9L; -. DR PDBsum; 3B9M; -. DR PDBsum; 3CX9; -. DR IntAct; P02768; 140. DR GlycoSuiteDB; P02768; -. DR PhosphoSite; P02768; -. DR SWISS-2DPAGE; P02768; -. DR Cornea-2DPAGE; P02768; -. DR DOSAC-COBS-2DPAGE; P02768; -. DR HSC-2DPAGE; P02768; -. DR OGP; P02768; -. DR REPRODUCTION-2DPAGE; IPI00384697; -. DR REPRODUCTION-2DPAGE; IPI00745872; -. DR REPRODUCTION-2DPAGE; P02768; -. DR Siena-2DPAGE; P02768; -. DR PRIDE; P02768; -. DR Ensembl; ENSG00000163631; Homo sapiens. DR GeneID; 213; -. DR KEGG; hsa:213; -. DR GeneCards; GC04P074509; -. DR H-InvDB; HIX0004278; -. DR HGNC; HGNC:399; ALB. DR HPA; CAB006262; -. DR MIM; 103600; gene+phenotype. DR MIM; 194470; phenotype. DR Orphanet; 86816; Congenital analbuminemia. DR PharmGKB; PA24690; -. DR HOVERGEN; P02768; -. DR Pathway_Interaction_DB; hnf3bpathway; FOXA2 and FOXA3 transcription factor networks. DR Reactome; REACT_602; Lipid and lipoprotein metabolism. DR Reactome; REACT_604; Hemostasis. DR DrugBank; DB01418; Acenocoumarol. DR DrugBank; DB00459; Acitretin. DR DrugBank; DB00802; Alfentanil. DR DrugBank; DB01370; Aluminium. DR DrugBank; DB00995; Auranofin. DR DrugBank; DB01402; Bismuth. DR DrugBank; DB01197; Captopril. DR DrugBank; DB00958; Carboplatin. DR DrugBank; DB00456; Cefalotin. DR DrugBank; DB01327; Cefazolin. DR DrugBank; DB01328; Cefonicid. DR DrugBank; DB01329; Cefoperazone. DR DrugBank; DB01114; Chlorpheniramine. DR DrugBank; DB00477; Chlorpromazine. DR DrugBank; DB00537; Ciprofloxacin. DR DrugBank; DB01068; Clonazepam. DR DrugBank; DB01147; Cloxacillin. DR DrugBank; DB00987; Cytarabine. DR DrugBank; DB01219; Dantrolene. DR DrugBank; DB00586; Diclofenac. DR DrugBank; DB00861; Diflunisal. DR DrugBank; DB01396; Digitoxin. DR DrugBank; DB00655; Estrone. DR DrugBank; DB00903; Ethacrynic acid. DR DrugBank; DB00749; Etodolac. DR DrugBank; DB00712; Flurbiprofen. DR DrugBank; DB00743; Gadobenate Dimeglumine. DR DrugBank; DB01044; Gatifloxacin. DR DrugBank; DB01120; Gliclazide. DR DrugBank; DB01159; Halothane. DR DrugBank; DB00062; Human Serum Albumin. DR DrugBank; DB00070; Hyaluronidase. DR DrugBank; DB01050; Ibuprofen. DR DrugBank; DB01307; Insulin-detemir. DR DrugBank; DB01308; Insulin-glargine. DR DrugBank; DB04711; Iodipamide. DR DrugBank; DB01009; Ketoprofen. DR DrugBank; DB00848; Levamisole. DR DrugBank; DB00451; Levothyroxine. DR DrugBank; DB00279; Liothyronine. DR DrugBank; DB00784; Mefenamic acid. DR DrugBank; DB00532; Mephenytoin. DR DrugBank; DB00563; Methotrexate. DR DrugBank; DB00540; Nortriptyline. DR DrugBank; DB00842; Oxazepam. DR DrugBank; DB01229; Paclitaxel. DR DrugBank; DB00946; Phenprocoumon. DR DrugBank; DB01032; Probenecid. DR DrugBank; DB00818; Propofol. DR DrugBank; DB00165; Pyridoxine. DR DrugBank; DB00936; Salicyclic acid. DR DrugBank; DB01232; Saquinavir. DR DrugBank; DB00096; Serum albumin. DR DrugBank; DB00064; Serum albumin iodonated. DR DrugBank; DB00815; Sodium lauryl sulfate. DR DrugBank; DB00364; Sucralfate. DR DrugBank; DB00576; Sulfamethizole. DR DrugBank; DB00605; Sulindac. DR DrugBank; DB00870; Suprofen. DR DrugBank; DB00624; Testosterone. DR DrugBank; DB00137; Xanthophyll. DR NextBio; 862; -. DR PMAP-CutDB; P02768; -. DR ArrayExpress; P02768; -. DR Bgee; P02768; -. DR GermOnline; ENSG00000163631; Homo sapiens. DR GO; GO:0005615; C:extracellular space; IEA:InterPro. DR GO; GO:0031093; C:platelet alpha granule lumen; EXP:Reactome. DR GO; GO:0043234; C:protein complex; IDA:UniProtKB. DR GO; GO:0016209; F:antioxidant activity; NAS:UniProtKB. DR GO; GO:0005507; F:copper ion binding; NAS:UniProtKB. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0008144; F:drug binding; IDA:UniProtKB. DR GO; GO:0005504; F:fatty acid binding; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB. DR GO; GO:0015643; F:toxin binding; IDA:UniProtKB. DR GO; GO:0009267; P:cellular response to starvation; IDA:UniProtKB. DR GO; GO:0019836; P:hemolysis by symbiont of host erythrocytes; IDA:UniProtKB. DR GO; GO:0051659; P:maintenance of mitochondrion location; IDA:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptosis; IDA:UniProtKB. DR GO; GO:0006810; P:transport; TAS:UniProtKB. DR InterPro; IPR001703; Alpha-fetoprotein. DR InterPro; IPR000264; Serum_albumin. DR InterPro; IPR014760; Serum_albumin_N. DR Pfam; PF00273; Serum_albumin; 3. DR PRINTS; PR00803; AFETOPROTEIN. DR PRINTS; PR00802; SERUMALBUMIN. DR ProDom; PD002486; Serum_albumin; 1. DR SMART; SM00103; ALBUMIN; 3. DR PROSITE; PS00212; ALBUMIN_1; 3. DR PROSITE; PS51438; ALBUMIN_2; 3. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; KW Cleavage on pair of basic residues; Copper; Direct protein sequencing; KW Disease mutation; Disulfide bond; Glycation; Glycoprotein; KW Lipid-binding; Metal-binding; Phosphoprotein; Polymorphism; Repeat; KW Secreted; Signal. FT SIGNAL 1 18 FT PROPEP 19 24 FT /FTId=PRO_0000001067. FT CHAIN 25 609 Serum albumin. FT /FTId=PRO_0000001068. FT DOMAIN 19 210 Albumin 1. FT DOMAIN 211 403 Albumin 2. FT DOMAIN 404 601 Albumin 3. FT METAL 27 27 Copper (By similarity). FT BINDING 264 264 Bilirubin (Potential). FT SITE 28 28 Not glycated. FT SITE 44 44 Not glycated. FT SITE 65 65 Not glycated. FT SITE 88 88 Not glycated. FT SITE 97 97 Not glycated. FT SITE 117 117 Not glycated. FT SITE 130 130 Not glycated. FT SITE 160 160 Not glycated. FT SITE 183 183 Not glycated. FT SITE 198 198 Not glycated. FT SITE 205 205 Not glycated. FT SITE 214 214 Not glycated. FT SITE 219 219 Not glycated. FT SITE 223 223 Aspirin-acetylated lysine. FT SITE 229 229 Not glycated. FT SITE 236 236 Not glycated. FT SITE 264 264 Not glycated. FT SITE 286 286 Not glycated. FT SITE 298 298 Not glycated. FT SITE 310 310 Not glycated. FT SITE 383 383 Not glycated. FT SITE 396 396 Not glycated. FT SITE 413 413 Not glycated. FT SITE 426 426 Not glycated. FT SITE 438 438 Not glycated. FT SITE 456 456 Not glycated. FT SITE 460 460 Not glycated. FT SITE 490 490 Not glycated. FT SITE 499 499 Not glycated. FT SITE 524 524 Not glycated. FT SITE 543 543 Not glycated. FT SITE 548 548 Not glycated. FT SITE 562 562 Not glycated. FT SITE 565 565 Not glycated. FT SITE 581 581 Not glycated. FT SITE 584 584 Not glycated. FT SITE 588 588 Not glycated. FT SITE 598 598 Not glycated. FT MOD_RES 82 82 Phosphoserine. FT MOD_RES 108 108 Phosphotyrosine. FT MOD_RES 164 164 Phosphotyrosine. FT CARBOHYD 36 36 N-linked (Glc) (glycation) (Probable). FT CARBOHYD 75 75 N-linked (Glc) (glycation); in vitro. FT CARBOHYD 161 161 N-linked (Glc) (glycation); in vitro. FT CARBOHYD 186 186 N-linked (Glc) (glycation); in vitro. FT CARBOHYD 223 223 N-linked (Glc) (glycation); in vitro. FT CARBOHYD 249 249 N-linked (Glc) (glycation); in vitro. FT CARBOHYD 257 257 N-linked (Glc) (glycation) (Probable). FT CARBOHYD 300 300 N-linked (Glc) (glycation); in vitro. FT CARBOHYD 305 305 N-linked (Glc) (glycation). FT CARBOHYD 337 337 N-linked (Glc) (glycation); in vitro. FT CARBOHYD 341 341 N-linked (Glc) (glycation) (Probable). FT CARBOHYD 342 342 N-linked (GlcNAc...); in variant Redhill. FT /FTId=CAR_000226. FT CARBOHYD 347 347 N-linked (Glc) (glycation); in vitro. FT CARBOHYD 375 375 N-linked (Glc) (glycation) (Probable). FT CARBOHYD 402 402 N-linked (Glc) (glycation); in vitro. FT CARBOHYD 437 437 N-linked (Glc) (glycation); in vitro. FT CARBOHYD 463 463 N-linked (Glc) (glycation). FT CARBOHYD 468 468 N-linked (Glc) (glycation); in vitro. FT CARBOHYD 518 518 N-linked (GlcNAc...); in variant FT Casebrook. FT /FTId=CAR_000069. FT CARBOHYD 549 549 N-linked (Glc) (glycation). FT CARBOHYD 558 558 N-linked (Glc) (glycation) (Probable). FT CARBOHYD 560 560 N-linked (Glc) (glycation); in vitro. FT CARBOHYD 569 569 N-linked (Glc) (glycation); in vitro. FT CARBOHYD 597 597 N-linked (Glc) (glycation); in vitro. FT DISULFID 77 86 FT DISULFID 99 115 FT DISULFID 114 125 FT DISULFID 148 193 FT DISULFID 192 201 FT DISULFID 224 270 FT DISULFID 269 277 FT DISULFID 289 303 FT DISULFID 302 313 FT DISULFID 340 385 FT DISULFID 384 393 FT DISULFID 416 462 FT DISULFID 461 472 FT DISULFID 485 501 FT DISULFID 500 511 FT DISULFID 538 583 FT DISULFID 582 591 FT VAR_SEQ 43 234 Missing (in isoform 2). FT /FTId=VSP_021275. FT VARIANT 23 23 R -> C (in Redhill/Malmo-I/Tradate; FT associated with T-344 in Redhill). FT /FTId=VAR_000499. FT VARIANT 23 23 R -> H (in Fukuoka-2/Lille/Taipei/Varese/ FT Komagome-3). FT /FTId=VAR_000500. FT VARIANT 24 24 R -> L (in Jaffna). FT /FTId=VAR_000501. FT VARIANT 24 24 R -> P (in Takefu/Honolulu-1). FT /FTId=VAR_000502. FT VARIANT 24 24 R -> Q (in Christchurch/Honolulu-2). FT /FTId=VAR_000503. FT VARIANT 25 25 D -> V (in Bleinheim/Iowa city-2). FT /FTId=VAR_000504. FT VARIANT 27 27 H -> Q (in Nagasaki-3). FT /FTId=VAR_000505. FT VARIANT 27 27 H -> Y (in Larino). FT /FTId=VAR_000506. FT VARIANT 73 73 F -> Y. FT /FTId=VAR_010657. FT VARIANT 84 84 E -> K (in Torino). FT /FTId=VAR_000507. FT VARIANT 87 87 D -> N (in Malmo-95/Dalakarlia). FT /FTId=VAR_000508. FT VARIANT 90 90 L -> P (in FDH). FT /FTId=VAR_013011. FT VARIANT 106 106 E -> K (in Vibo Valentia). FT /FTId=VAR_000509. FT VARIANT 121 121 E -> G. FT /FTId=VAR_014290. FT VARIANT 138 138 R -> G (in Yanomama-2). FT /FTId=VAR_000510. FT VARIANT 143 143 E -> K (in Nagoya). FT /FTId=VAR_000511. FT VARIANT 146 146 V -> E (in Tregasio). FT /FTId=VAR_013012. FT VARIANT 152 152 H -> R (in Komagome-2). FT /FTId=VAR_000512. FT VARIANT 201 201 C -> F (in Hawkes bay). FT /FTId=VAR_000513. FT VARIANT 215 215 A -> T (in dbSNP:rs3210154). FT /FTId=VAR_014291. FT VARIANT 215 215 A -> V (in dbSNP:rs3204504). FT /FTId=VAR_014292. FT VARIANT 220 220 Q -> L (in dbSNP:rs3210163). FT /FTId=VAR_014293. FT VARIANT 242 242 R -> H (in FDH). FT /FTId=VAR_000514. FT VARIANT 242 242 R -> P (in FDH). FT /FTId=VAR_013013. FT VARIANT 249 249 K -> Q (in Tradate-2). FT /FTId=VAR_000515. FT VARIANT 264 264 K -> E (in Herborn). FT /FTId=VAR_000516. FT VARIANT 292 292 Q -> R (in Malmo-10). FT /FTId=VAR_000517. FT VARIANT 293 293 D -> G (in Nagasaki-1). FT /FTId=VAR_000518. FT VARIANT 300 300 K -> N (in Caserta). FT /FTId=VAR_000519. FT VARIANT 337 337 K -> N (in Canterbury/New Guinea/ FT Tagliacozzo/Cuneo/Cooperstown). FT /FTId=VAR_000520. FT VARIANT 338 338 D -> G (in Bergamo). FT /FTId=VAR_013014. FT VARIANT 338 338 D -> V (in Brest). FT /FTId=VAR_013015. FT VARIANT 342 342 N -> K (in Malmo-47). FT /FTId=VAR_000521. FT VARIANT 344 344 A -> T (in Redhill; associated with C- FT 23). FT /FTId=VAR_000522. FT VARIANT 345 345 E -> K (in Roma). FT /FTId=VAR_000523. FT VARIANT 357 357 E -> K (in Sondrio). FT /FTId=VAR_000524. FT VARIANT 378 378 E -> K (in Hiroshima-1). FT /FTId=VAR_000525. FT VARIANT 382 382 E -> K (in Coari I/Porto Alegre). FT /FTId=VAR_000526. FT VARIANT 383 383 K -> N (in Trieste). FT /FTId=VAR_013016. FT VARIANT 389 389 D -> H (in Parklands). FT /FTId=VAR_000527. FT VARIANT 389 389 D -> V (in Iowa city-1). FT /FTId=VAR_000528. FT VARIANT 396 396 K -> E (in Naskapi/Mersin/Komagome-1). FT /FTId=VAR_000529. FT VARIANT 399 399 D -> N (in Nagasaki-2). FT /FTId=VAR_000530. FT VARIANT 400 400 E -> K (in Tochigi). FT /FTId=VAR_000531. FT VARIANT 400 400 E -> Q (in Malmo-5). FT /FTId=VAR_000532. FT VARIANT 406 406 E -> K (in Hiroshima-2). FT /FTId=VAR_000533. FT VARIANT 420 420 E -> K. FT /FTId=VAR_014294. FT VARIANT 434 434 R -> C (in Liprizzi). FT /FTId=VAR_013017. FT VARIANT 490 490 K -> E (in dbSNP:rs1063469). FT /FTId=VAR_014295. FT VARIANT 503 503 E -> K (in Dublin). FT /FTId=VAR_000534. FT VARIANT 518 518 D -> N (in Casebrook). FT /FTId=VAR_000535. FT VARIANT 525 525 E -> K (in Manaus-1/Adana/Lambadi/ FT Vancouver). FT /FTId=VAR_000536. FT VARIANT 529 529 E -> K (in Ortonovo). FT /FTId=VAR_000537. FT VARIANT 557 557 V -> M (in Maddaloni). FT /FTId=VAR_013018. FT VARIANT 560 560 K -> E (in Castel di Sangro). FT /FTId=VAR_000538. FT VARIANT 565 565 K -> E (in Maku). FT /FTId=VAR_000539. FT VARIANT 574 574 D -> A (in Malmo-61). FT /FTId=VAR_000541. FT VARIANT 574 574 D -> G (in Mexico). FT /FTId=VAR_000540. FT VARIANT 584 584 K -> E (in Church bay). FT /FTId=VAR_013019. FT VARIANT 587 587 D -> N (in Fukuoka-1/Paris-2). FT /FTId=VAR_000542. FT VARIANT 589 589 E -> K (in Osaka-1). FT /FTId=VAR_000543. FT VARIANT 594 594 E -> K (in Osaka-2/Phnom Phen/albumin B/ FT Verona). FT /FTId=VAR_000544. FT VARIANT 596 609 GKKLVAASQAALGL -> PTMRIRERK (in Venezia). FT /FTId=VAR_000547. FT VARIANT 597 597 K -> E (in Gent/Milano Fast). FT /FTId=VAR_000545. FT VARIANT 598 598 K -> N (in Vanves). FT /FTId=VAR_000546. FT VARIANT 599 609 LVAASQAALGL -> TCCCKSSCLRLITSHLKASQPTMRIR FT ERK (in Kenitra). FT /FTId=VAR_012981. FT CONFLICT 55 55 L -> P (in Ref. 11; CAH18185). FT CONFLICT 118 119 QE -> EQ (in Ref. 5). FT CONFLICT 122 122 R -> S (in Ref. 4; AAF01333). FT CONFLICT 155 155 E -> Q (in Ref. 18; AA sequence). FT CONFLICT 174 174 Y -> L (in Ref. 23 and 24). FT CONFLICT 194 194 Q -> E (in Ref. 18; AA sequence). FT CONFLICT 327 332 PSLAAD -> MFVLLC (in Ref. 10; AAF71067). FT CONFLICT 405 405 V -> A (in Ref. 10; AAF71067). FT CONFLICT 409 409 Q -> E (in Ref. 10; AAH14308). FT CONFLICT 441 441 Q -> E (in Ref. 2; CAA23753). FT CONFLICT 466 466 E -> G (in Ref. 4; AAF01333). FT CONFLICT 488 489 HE -> EH (in Ref. 18; AA sequence). FT CONFLICT 490 490 K -> R (in Ref. 11; CAH18185). FT CONFLICT 525 525 E -> Q (in Ref. 18; AA sequence). FT CONFLICT 551 551 T -> A (in Ref. 11; CAH18185). FT CONFLICT 560 560 K -> R (in Ref. 11; CAH18185). FT CONFLICT 604 604 Q -> R (in Ref. 5; AAN17825). FT HELIX 31 54 FT HELIX 60 79 FT STRAND 83 85 FT HELIX 90 102 FT HELIX 105 108 FT HELIX 111 115 FT TURN 119 123 FT HELIX 124 128 FT HELIX 144 153 FT HELIX 155 167 FT HELIX 175 192 FT STRAND 195 197 FT HELIX 198 230 FT HELIX 232 246 FT HELIX 252 271 FT HELIX 274 290 FT HELIX 292 295 FT HELIX 300 303 FT HELIX 307 314 FT HELIX 330 333 FT HELIX 339 345 FT HELIX 347 360 FT HELIX 367 385 FT HELIX 390 393 FT HELIX 394 397 FT HELIX 398 438 FT HELIX 444 461 FT HELIX 466 490 FT HELIX 495 503 FT HELIX 508 514 FT HELIX 528 530 FT HELIX 535 539 FT HELIX 542 559 FT STRAND 561 563 FT HELIX 567 584 FT HELIX 591 605 SQ SEQUENCE 609 AA; 69367 MW; F88FF61DD242E818 CRC64; MKWVTFISLL FLFSSAYSRG VFRRDAHKSE VAHRFKDLGE ENFKALVLIA FAQYLQQCPF EDHVKLVNEV TEFAKTCVAD ESAENCDKSL HTLFGDKLCT VATLRETYGE MADCCAKQEP ERNECFLQHK DDNPNLPRLV RPEVDVMCTA FHDNEETFLK KYLYEIARRH PYFYAPELLF FAKRYKAAFT ECCQAADKAA CLLPKLDELR DEGKASSAKQ RLKCASLQKF GERAFKAWAV ARLSQRFPKA EFAEVSKLVT DLTKVHTECC HGDLLECADD RADLAKYICE NQDSISSKLK ECCEKPLLEK SHCIAEVEND EMPADLPSLA ADFVESKDVC KNYAEAKDVF LGMFLYEYAR RHPDYSVVLL LRLAKTYETT LEKCCAAADP HECYAKVFDE FKPLVEEPQN LIKQNCELFE QLGEYKFQNA LLVRYTKKVP QVSTPTLVEV SRNLGKVGSK CCKHPEAKRM PCAEDYLSVV LNQLCVLHEK TPVSDRVTKC CTESLVNRRP CFSALEVDET YVPKEFNAET FTFHADICTL SEKERQIKKQ TALVELVKHK PKATKEQLKA VMDDFAAFVE KCCKADDKET CFAEEGKKLV AASQAALGL //