ALBU_HUMAN
ID ALBU_HUMAN Reviewed; 609 AA.
AC P02768; E7ESS9; O95574; P04277; Q13140; Q645G4; Q68DN5; Q6UXK4; Q86YG0;
AC Q8IUK7; Q9P157; Q9P1I7; Q9UHS3; Q9UJZ0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 03-AUG-2022, entry version 279.
DE RecName: Full=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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LYS-420.
RX PubMed=6171778; DOI=10.1093/nar/9.22.6103;
RA Lawn R.M., Adelman J., Bock S.C., Franke A.E., Houck C.M., Najarian R.C.,
RA Seeburg P.H., Wion K.L.;
RT "The sequence of human serum albumin cDNA and its expression in E. coli.";
RL Nucleic Acids Res. 9:6103-6114(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-121.
RX 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 albumin
RT mRNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:71-75(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3009475; DOI=10.1016/s0021-9258(19)62680-3;
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 nucleotide
RT 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 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 PubMed=11483580; DOI=10.1101/gr.175501;
RA Yu Y., Zhang C., Zhou G., Wu S., Qu X., Wei H., Xing G., Dong C., Zhai Y.,
RA Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C., He F.;
RT "Gene expression profiling in human fetal liver and identification of
RT tissue- and developmental-stage-specific genes through compiled expression
RT 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 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., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [16]
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 [17]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-167.
RX 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., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [18]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RX PubMed=2419329; DOI=10.1016/s0021-9258(17)35775-7;
RA Urano Y., Watanabe K., Sakai M., Tamaoki T.;
RT "The human albumin gene. Characterization of the 5' and 3' flanking regions
RT and the polymorphic gene transcripts.";
RL J. Biol. Chem. 261:3244-3251(1986).
RN [19]
RP PROTEIN SEQUENCE OF 25-609.
RX 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 [20]
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 [21]
RP PROTEIN SEQUENCE OF 25-44 AND 480-499.
RC TISSUE=Heart;
RX 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 1994.";
RL Electrophoresis 15:1459-1465(1994).
RN [22]
RP PROTEIN SEQUENCE OF 25-34.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [23]
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 IDENTIFICATION BY 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 [24]
RP PROTEIN SEQUENCE OF 166-174.
RX 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, neurotensin
RT and angiotensin.";
RL Biochem. Biophys. Res. Commun. 136:983-988(1986).
RN [25]
RP PROTEIN SEQUENCE OF 166-174.
RX PubMed=2437111; DOI=10.1016/s0021-9258(18)45523-8;
RA Carraway R.E., Mitra S.P., Cochrane D.E.;
RT "Structure of a biologically active neurotensin-related peptide obtained
RT from pepsin-treated albumin(s).";
RL J. Biol. Chem. 262:5968-5973(1987).
RN [26]
RP PROTEIN SEQUENCE OF 222-229, AND ASPIRIN-ACETYLATION AT LYS-223.
RX 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 acetylsalicylic
RT acid.";
RL FEBS Lett. 66:173-175(1976).
RN [27]
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; LYS-437;
RP LYS-468; LYS-560; LYS-549; LYS-569 AND LYS-597, LACK OF GLYCATION AT
RP LYS-28; LYS-44; LYS-65; LYS-88; LYS-97; LYS-117; LYS-130; LYS-160; LYS-183;
RP LYS-198; LYS-205; LYS-214; LYS-219; LYS-229; LYS-236; LYS-264; LYS-286;
RP LYS-298; LYS-310; LYS-383; LYS-396; LYS-413; LYS-426; LYS-438; LYS-456;
RP LYS-460; LYS-490; LYS-499; LYS-524; LYS-543; LYS-548; LYS-562; LYS-565;
RP LYS-581; LYS-584; LYS-588 AND LYS-598, AND IDENTIFICATION BY MASS
RP 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 [28]
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 [29]
RP BILIRUBIN-BINDING SITE.
RX PubMed=656055; DOI=10.1042/bj1710453;
RA Jacobsen C.;
RT "Lysine residue 240 of human serum albumin is involved in high-affinity
RT binding of bilirubin.";
RL Biochem. J. 171:453-459(1978).
RN [30]
RP GLYCATION AT LYS-223 AND LYS-549.
RX PubMed=6853480; DOI=10.1016/s0021-9258(18)32384-6;
RA Garlick R.L., Mazer J.S.;
RT "The principal site of nonenzymatic glycosylation of human serum albumin in
RT vivo.";
RL J. Biol. Chem. 258:6142-6146(1983).
RN [31]
RP FUNCTION.
RX PubMed=6234017; DOI=10.1021/bi00305a003;
RA Konopka K., Neilands J.B.;
RT "Effect of serum albumin on siderophore-mediated utilization of transferrin
RT iron.";
RL Biochemistry 23:2122-2127(1984).
RN [32]
RP GLYCATION AT LYS-549.
RX PubMed=6706980; DOI=10.1016/s0021-9258(17)43168-1;
RA Shaklai N., Garlick R.L., Bunn H.F.;
RT "Nonenzymatic glycosylation of human serum albumin alters its conformation
RT and function.";
RL J. Biol. Chem. 259:3812-3817(1984).
RN [33]
RP GLYCATION AT LYS-36; LYS-223; LYS-257; LYS-305; LYS-341; LYS-375; LYS-463;
RP LYS-549 AND LYS-558.
RX PubMed=3759977; DOI=10.1016/s0021-9258(18)67052-8;
RA Iberg N., Fluckiger R.;
RT "Nonenzymatic glycosylation of albumin in vivo. Identification of multiple
RT glycosylated sites.";
RL J. Biol. Chem. 261:13542-13545(1986).
RN [34]
RP INVOLVEMENT IN ANALBA.
RX PubMed=8134387; DOI=10.1073/pnas.91.6.2275;
RA Watkins S., Madison J., Galliano M., Minchiotti L., Putnam F.W.;
RT "A nucleotide insertion and frameshift cause analbuminemia in an Italian
RT family.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:2275-2279(1994).
RN [35]
RP INTERACTION WITH ALPHA-1-MICROGLOBULIN.
RX PubMed=9183005; DOI=10.1111/j.1432-1033.1997.00676.x;
RA Berggaard T., Thelin N., Falkenberg C., Enghild J.J., Akerstroem B.;
RT "Prothrombin, albumin and immunoglobulin A form covalent complexes with
RT alpha1-microglobulin in human plasma.";
RL Eur. J. Biochem. 245:676-683(1997).
RN [36]
RP FUNCTION.
RX PubMed=19021548; DOI=10.1042/bst0361317;
RA Lu J., Stewart A.J., Sadler P.J., Pinheiro T.J., Blindauer C.A.;
RT "Albumin as a zinc carrier: properties of its high-affinity zinc-binding
RT site.";
RL Biochem. Soc. Trans. 36:1317-1321(2008).
RN [37]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [38]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443; THR-444 AND THR-446, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [39]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [40]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-89 AND SER-513, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [41]
RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-558, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [42]
RP PHOSPHORYLATION AT SER-29; SER-82; SER-89 AND THR-107.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [43]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [44]
RP INTERACTION WITH FCGRT.
RX PubMed=28330995; DOI=10.1073/pnas.1618291114;
RA Pyzik M., Rath T., Kuo T.T., Win S., Baker K., Hubbard J.J., Grenha R.,
RA Gandhi A., Kraemer T.D., Mezo A.R., Taylor Z.S., McDonnell K., Nienaber V.,
RA Andersen J.T., Mizoguchi A., Blumberg L., Purohit S., Jones S.D.,
RA Christianson G., Lencer W.I., Sandlie I., Kaplowitz N., Roopenian D.C.,
RA Blumberg R.S.;
RT "Hepatic FcRn regulates albumin homeostasis and susceptibility to liver
RT injury.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E2862-E2871(2017).
RN [45]
RP X-RAY CRYSTALLOGRAPHY (6.0 ANGSTROMS).
RX PubMed=2727704; DOI=10.1126/science.2727704;
RA Carter D.C., He X.-M., Munson S.H., Twigg P.D., Gernert K.M., Broom M.B.,
RA Miller T.Y.;
RT "Three-dimensional structure of human serum albumin.";
RL Science 244:1195-1198(1989).
RN [46]
RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS).
RX 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 [47]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND FUNCTION.
RX 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 [48]
RP ERRATUM OF PUBMED:1630489.
RA He X.-M., Carter D.C.;
RL Nature 364:362-362(1993).
RN [49]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX 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 reveals
RT an asymmetric distribution of binding sites.";
RL Nat. Struct. Biol. 5:827-835(1998).
RN [50]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX 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 [51]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-609.
RX 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 serum
RT albumin. High resolution crystal structures.";
RL J. Biol. Chem. 275:38731-38738(2000).
RN [52]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX 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 monounsaturated
RT and polyunsaturated fatty acids.";
RL J. Mol. Biol. 314:955-960(2001).
RN [53] {ECO:0007744|PDB:5IJF}
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 25-609 IN COMPLEX WITH ZINC,
RP DISULFIDE BOND, AND MUTAGENESIS OF HIS-91.
RX PubMed=28567254; DOI=10.1039/c6sc02267g;
RA Handing K.B., Shabalin I.G., Kassaar O., Khazaipoul S., Blindauer C.A.,
RA Stewart A.J., Chruszcz M., Minor W.;
RT "Circulatory zinc transport is controlled by distinct interdomain sites on
RT mammalian albumins.";
RL Chem. Sci. 7:6635-6648(2016).
RN [54]
RP VARIANT CANTERBURY ASN-337.
RX 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 domain
RT of serum albumin.";
RL Biochim. Biophys. Acta 912:191-197(1987).
RN [55]
RP VARIANTS NASKAPI/MERSIN GLU-396 AND MEXICO GLY-574.
RX 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 and in
RT sequences inferred from molecular cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:4413-4417(1987).
RN [56]
RP VARIANTS NAGASAKI-3 GLN-27 YANOMAMA-2 GLU-396; NAGASAKI-2 ASN-399 AND MAKU
RP GLU-565.
RX PubMed=3479777; DOI=10.1073/pnas.84.22.8001;
RA Takshashi N., Takahashi Y., Isobe T., Putnam F.W., Fujita M., Satoh C.,
RA Neel J.V.;
RT "Amino acid substitutions in inherited albumin variants from Amerindian and
RT Japanese populations.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:8001-8005(1987).
RN [57]
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 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 different
RT populations.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:434-438(1989).
RN [58]
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 PubMed=2762316; DOI=10.1073/pnas.86.16.6092;
RA Arai K., Madison J., Huss K., Ishioka N., Satoh C., Fujita M., Neel J.V.,
RA Sakurabayashi I., Putnam F.W.;
RT "Point substitutions in Japanese alloalbumins.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:6092-6096(1989).
RN [59]
RP VARIANTS HONOLULU-1 PRO-24; HONOLULU-2 GLN-24; NAGOYA LYS-143; NEW GUINEA
RP ASN-337; MANAUS-1/LAMBADI LYS-525; FUKUOKA-1 ASN-587; OSAKA-1 LYS-589 AND
RP OSAKA-2 LYS-594.
RX 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 [60]
RP CHARACTERIZATION OF VARIANT REDHILL.
RX 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 human
RT serum albumin whose precursor has an aberrant signal peptidase cleavage
RT site.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:26-30(1990).
RN [61]
RP VARIANTS VARESE HIS-23; TORINO LYS-84 AND VIBO VALENTIA LYS-106.
RX 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 Italy.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:8721-8725(1990).
RN [62]
RP CHARACTERIZATION OF VARIANT VENEZIA.
RX PubMed=2068071; DOI=10.1073/pnas.88.14.5959;
RA Watkins S., Madison J., Davis E., Sakamoto Y., Galliano M., Minchiotti L.,
RA Putnam F.W.;
RT "A donor splice mutation and a single-base deletion produce two carboxyl-
RT terminal variants of human serum albumin.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:5959-5963(1991).
RN [63]
RP VARIANTS KOMAGOME-3 HIS-23; IOWA CITY-2 VAL-25; KOMAGOME-2 ARG-152; IOWA
RP CITY-1 VAL-389 AND KOMAGOME-1 GLU-396.
RX 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 [64]
RP VARIANT CASEBROOK ASN-518.
RX 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 [65]
RP VARIANTS SONDRIO LYS-357 AND PARIS-2 ASN-587.
RX PubMed=1347703; DOI=10.1016/0167-4838(92)90207-t;
RA Minchiotti L., Galliano M., Stoppini M., Ferri G., Crespeau H., Rochu D.,
RA Porta F.;
RT "Two alloalbumins with identical electrophoretic mobility are produced by
RT differently charged amino acid substitutions.";
RL Biochim. Biophys. Acta 1119:232-238(1992).
RN [66]
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 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 distribution of
RT nine albumin variants.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8225-8229(1992).
RN [67]
RP VARIANT HERBORN GLU-264.
RX PubMed=8513793; 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 [68]
RP VARIANT HAWKES BAY PHE-201.
RX 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 sulphydryl
RT group at position 177.";
RL Biochim. Biophys. Acta 1182:46-50(1993).
RN [69]
RP VARIANT ORTONOVO LYS-529.
RX 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: albumin
RT Ortonovo (Glu-505-->Lys).";
RL Biochim. Biophys. Acta 1225:27-32(1993).
RN [70]
RP VARIANTS LARINO TYR-27; TRADATE-2 GLN-249 AND CASERTA ASN-300.
RX PubMed=8022807; DOI=10.1073/pnas.91.14.6476;
RA Madison J., Galliano M., Watkins S., Minchiotti L., Porta F., Rossi A.,
RA 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 [71]
RP VARIANT FDAH HIS-242.
RX PubMed=8048949; DOI=10.1006/bbrc.1994.1998;
RA Sunthornthepvarakul T., Angkeow P., Weiss R.E., Hayashi Y., Retetoff S.;
RT "An identical missense mutation in the albumin gene results in familial
RT dysalbuminemic hyperthyroxinemia in 8 unrelated families.";
RL Biochem. Biophys. Res. Commun. 202:781-787(1994).
RN [72]
RP VARIANT FDAH HIS-242, AND PROTEIN SEQUENCE OF 25-51.
RX PubMed=7852505; DOI=10.1210/jcem.80.2.7852505;
RA Rushbrook J.I., Becker E., Schussler G.C., Divino C.M.;
RT "Identification of a human serum albumin species associated with familial
RT dysalbuminemic hyperthyroxinemia.";
RL J. Clin. Endocrinol. Metab. 80:461-467(1995).
RN [73]
RP VARIANT FDAH HIS-242.
RX PubMed=9329347; DOI=10.1210/jcem.82.10.4276;
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 distinct
RT phenotype of familial dysalbuminemic hyperthyroxinemia in a Japanese
RT kindred.";
RL J. Clin. Endocrinol. Metab. 82:3246-3250(1997).
RN [74]
RP VARIANT FDAH PRO-90.
RX PubMed=9589637; DOI=10.1210/jcem.83.5.4815;
RA Sunthornthepvarakul T., Likitmaskul S., Ngowngarmratana S., Angsusingha K.,
RA 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 [75]
RP VARIANT TYR-73, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Urine;
RX PubMed=11680902;
RX DOI=10.1002/1615-9861(200101)1:1<93::aid-prot93>3.0.co;2-3;
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., Luethy R.,
RA Patterson S.D.;
RT "Towards defining the urinary proteome using liquid chromatography-tandem
RT mass spectrometry I. Profiling an unfractionated tryptic digest.";
RL Proteomics 1:93-107(2001).
RN [76]
RP CHARACTERIZATION OF VARIANT KENITRA.
RX PubMed=11168369; DOI=10.1046/j.1432-1033.2001.01899.x;
RA Minchiotti L., Campagnoli M., Rossi A., Cosulich M.E., Monti M., Pucci P.,
RA Kragh-Hansen U., Granel B., Disdier P., Weiller P.J., Galliano M.;
RT "A nucleotide insertion and frameshift cause albumin Kenitra, an extended
RT and O-glycosylated mutant of human serum albumin with two additional
RT disulfide bridges.";
RL Eur. J. Biochem. 268:344-352(2001).
CC -!- FUNCTION: Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones,
CC bilirubin and drugs (Probable). Its main function is the regulation of
CC the colloidal osmotic pressure of blood (Probable). Major zinc
CC transporter in plasma, typically binds about 80% of all plasma zinc
CC (PubMed:19021548). Major calcium and magnesium transporter in plasma,
CC binds approximately 45% of circulating calcium and magnesium in plasma
CC (By similarity). Potentially has more than two calcium-binding sites
CC and might additionally bind calcium in a non-specific manner (By
CC similarity). The shared binding site between zinc and calcium at
CC residue Asp-273 suggests a crosstalk between zinc and calcium transport
CC in the blood (By similarity). The rank order of affinity is zinc >
CC calcium > magnesium (By similarity). Binds to the bacterial siderophore
CC enterobactin and inhibits enterobactin-mediated iron uptake of E.coli
CC from ferric transferrin, and may thereby limit the utilization of iron
CC and growth of enteric bacteria such as E.coli (PubMed:6234017). Does
CC not prevent iron uptake by the bacterial siderophore aerobactin
CC (PubMed:6234017). {ECO:0000250|UniProtKB:P02769,
CC ECO:0000269|PubMed:19021548, ECO:0000269|PubMed:6234017,
CC ECO:0000305|PubMed:1630489}.
CC -!- SUBUNIT: Interacts with FCGRT; this interaction regulates ALB
CC homeostasis (PubMed:28330995). Interacts with TASOR (By similarity). In
CC plasma, occurs in a covalently-linked complex with chromophore-bound
CC alpha-1-microglobulin with molar ratio 1:2 and 1:1; this interaction
CC does not prevent fatty acid binding to ALB.
CC {ECO:0000250|UniProtKB:P07724, ECO:0000269|PubMed:28330995,
CC ECO:0000269|PubMed:9183005}.
CC -!- INTERACTION:
CC P02768; P02768: ALB; NbExp=8; IntAct=EBI-714423, EBI-714423;
CC P02768; P02786: TFRC; NbExp=2; IntAct=EBI-714423, EBI-355727;
CC P02768-3; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-25830928, EBI-743960;
CC P02768-3; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-25830928, EBI-25830200;
CC P02768-3; Q07869: PPARA; NbExp=3; IntAct=EBI-25830928, EBI-78615;
CC P02768-3; Q09028: RBBP4; NbExp=3; IntAct=EBI-25830928, EBI-620823;
CC P02768-3; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-25830928, EBI-11525489;
CC P02768-3; O76024: WFS1; NbExp=3; IntAct=EBI-25830928, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P02768-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P02768-2; Sequence=VSP_021275;
CC Name=3;
CC IsoId=P02768-3; Sequence=VSP_057389;
CC -!- TISSUE SPECIFICITY: Plasma.
CC -!- PTM: Kenitra variant is partially O-glycosylated at Thr-620. It has two
CC new disulfide bonds Cys-600 to Cys-602 and Cys-601 to Cys-606.
CC -!- PTM: Glycated in diabetic patients.
CC -!- PTM: Phosphorylated by FAM20C in the extracellular medium.
CC {ECO:0000269|PubMed:26091039}.
CC -!- PTM: Acetylated on Lys-223 by acetylsalicylic acid.
CC -!- POLYMORPHISM: 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. The sequence shown is that of variant
CC albumin A.
CC -!- DISEASE: Hyperthyroxinemia, familial dysalbuminemic (FDAH)
CC [MIM:615999]: A disorder characterized by abnormally elevated levels of
CC total serum thyroxine (T4) in euthyroid patients. It is due to abnormal
CC serum albumin that binds T4 with enhanced affinity.
CC {ECO:0000269|PubMed:7852505, ECO:0000269|PubMed:8048949,
CC ECO:0000269|PubMed:9329347, ECO:0000269|PubMed:9589637}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Analbuminemia (ANALBA) [MIM:616000]: A rare autosomal
CC recessive disorder manifested by the presence of a very low amount of
CC circulating serum albumin. Affected individuals manifest mild edema,
CC hypotension, fatigue, and, occasionally, lower body lipodystrophy
CC (mainly in adult females). The most common biochemical finding is
CC hyperlipidemia, with a significant increase in the total and LDL
CC cholesterol concentrations, but normal concentrations of HDL
CC cholesterol and triglycerides. {ECO:0000269|PubMed:8134387}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the ALB/AFP/VDB family. {ECO:0000255|PROSITE-
CC ProRule:PRU00769}.
CC -!- CAUTION: A peptide arising from positions 166 to 174 was originally
CC (PubMed:3087352 and PubMed:2437111) termed neurotensin-related peptide
CC (NRP) or kinetensin and was thought to regulate fat digestion, lipid
CC absorption, and blood flow. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF22034.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF69644.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAG35503.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Albumin Website;
CC URL="https://albumin.org";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Serum albumin entry;
CC URL="https://en.wikipedia.org/wiki/Serum_albumin";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/alb/";
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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; -; mRNA.
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; AC108157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471057; EAX05676.1; -; Genomic_DNA.
DR EMBL; BC014308; AAH14308.1; -; mRNA.
DR EMBL; BC034023; AAH34023.1; -; mRNA.
DR EMBL; BC035969; AAH35969.1; -; 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; AH002596; AAA51688.1; -; Genomic_DNA.
DR CCDS; CCDS3555.1; -. [P02768-1]
DR PIR; A93743; ABHUS.
DR RefSeq; NP_000468.1; NM_000477.6. [P02768-1]
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; 2N0X; NMR; -; A=432-447.
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; 2XSI; X-ray; 2.70 A; A=25-609.
DR PDB; 2XVQ; X-ray; 2.90 A; A/B=25-609.
DR PDB; 2XVU; X-ray; 2.60 A; A/B=25-609.
DR PDB; 2XVV; X-ray; 2.40 A; A=25-609.
DR PDB; 2XVW; X-ray; 2.65 A; A=25-609.
DR PDB; 2XW0; X-ray; 2.40 A; A/B=25-609.
DR PDB; 2XW1; X-ray; 2.50 A; A/B=25-609.
DR PDB; 2YDF; X-ray; 2.75 A; A/B=25-609.
DR PDB; 3A73; X-ray; 2.19 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 PDB; 3JQZ; X-ray; 3.30 A; A/B=25-609.
DR PDB; 3JRY; X-ray; 2.30 A; A/B=25-609.
DR PDB; 3LU6; X-ray; 2.70 A; A/B=25-609.
DR PDB; 3LU7; X-ray; 2.80 A; A/B=25-609.
DR PDB; 3LU8; X-ray; 2.60 A; A/B=25-609.
DR PDB; 3SQJ; X-ray; 2.05 A; A/B=27-608.
DR PDB; 3TDL; X-ray; 2.60 A; A=25-609.
DR PDB; 3UIV; X-ray; 2.20 A; A/H=25-609.
DR PDB; 4BKE; X-ray; 2.35 A; A=1-609.
DR PDB; 4E99; X-ray; 2.30 A; A=25-609.
DR PDB; 4EMX; X-ray; 2.30 A; A/B=25-609.
DR PDB; 4G03; X-ray; 2.22 A; A/B=25-609.
DR PDB; 4G04; X-ray; 2.30 A; A/B=25-609.
DR PDB; 4HGK; X-ray; 3.04 A; A/B=25-609.
DR PDB; 4HGM; X-ray; 2.34 A; B=25-609.
DR PDB; 4IW1; X-ray; 2.56 A; A=25-609.
DR PDB; 4IW2; X-ray; 2.41 A; A=25-609.
DR PDB; 4K2C; X-ray; 3.23 A; A/B=25-609.
DR PDB; 4K71; X-ray; 2.40 A; A/D=25-609.
DR PDB; 4L8U; X-ray; 2.01 A; A=25-609.
DR PDB; 4L9K; X-ray; 2.40 A; A/B=25-609.
DR PDB; 4L9Q; X-ray; 2.70 A; A/B=25-609.
DR PDB; 4LA0; X-ray; 2.40 A; A/B=25-609.
DR PDB; 4LB2; X-ray; 2.80 A; A/B=25-609.
DR PDB; 4LB9; X-ray; 2.70 A; A=25-609.
DR PDB; 4N0F; X-ray; 3.02 A; D/G/J/M=25-609.
DR PDB; 4N0U; X-ray; 3.80 A; D=27-609.
DR PDB; 4S1Y; X-ray; 3.16 A; A=25-609.
DR PDB; 4Z69; X-ray; 2.19 A; A/I=25-609.
DR PDB; 5FUO; X-ray; 3.60 A; A=25-609.
DR PDB; 5GIX; X-ray; 2.80 A; A/B=27-607.
DR PDB; 5GIY; X-ray; 2.54 A; A=27-607.
DR PDB; 5ID7; X-ray; 2.26 A; A/B=25-609.
DR PDB; 5IFO; X-ray; 3.20 A; A=25-609.
DR PDB; 5IJF; X-ray; 2.65 A; A=25-609.
DR PDB; 5UJB; X-ray; 2.70 A; A/B=1-609.
DR PDB; 5VNW; X-ray; 2.60 A; A/B=25-609.
DR PDB; 5X52; X-ray; 3.00 A; A/B=25-609.
DR PDB; 5YB1; X-ray; 2.62 A; A/B=27-607.
DR PDB; 5YOQ; X-ray; 2.65 A; A/B=25-609.
DR PDB; 5Z0B; X-ray; 2.17 A; A/B/C=25-609.
DR PDB; 6A7P; X-ray; 2.28 A; A/B=25-609.
DR PDB; 6EZQ; X-ray; 2.39 A; A=25-609.
DR PDB; 6HSC; X-ray; 1.90 A; A/B=1-609.
DR PDB; 6JE7; X-ray; 3.90 A; A=26-608.
DR PDB; 6L4K; X-ray; 2.09 A; A/I=27-607.
DR PDB; 6M4R; X-ray; 2.49 A; A/B=25-609.
DR PDB; 6M58; X-ray; 2.95 A; A/B=25-609.
DR PDB; 6M5D; X-ray; 2.60 A; A=28-606.
DR PDB; 6M5E; X-ray; 2.80 A; A/B/C=25-609.
DR PDB; 6QIO; X-ray; 1.95 A; A=25-609.
DR PDB; 6QIP; X-ray; 2.45 A; A=25-609.
DR PDB; 6R7S; X-ray; 2.21 A; A=25-609.
DR PDB; 6WUW; X-ray; 2.20 A; A/B=25-609.
DR PDB; 6XV0; X-ray; 3.00 A; A=25-609.
DR PDB; 6YG9; X-ray; 1.89 A; A=25-609.
DR PDB; 6ZL1; X-ray; 3.27 A; A/B=1-609.
DR PDB; 7A9C; X-ray; 2.75 A; AAA=25-609.
DR PDB; 7AAE; X-ray; 2.27 A; AAA=26-609.
DR PDB; 7AAI; X-ray; 2.10 A; AAA=26-609.
DR PDB; 7D6J; X-ray; 3.29 A; A/B=25-609.
DR PDB; 7DJN; X-ray; 2.04 A; A/B=25-609.
DR PDB; 7DL4; X-ray; 2.40 A; A=25-609.
DR PDB; 7EEK; X-ray; 2.50 A; A/B=26-608.
DR PDB; 7JWN; X-ray; 2.60 A; A=26-609.
DR PDB; 7QFE; X-ray; 2.20 A; A=25-609.
DR PDB; 7VR9; X-ray; 2.30 A; A/B=25-609.
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; 2N0X; -.
DR PDBsum; 2VDB; -.
DR PDBsum; 2VUE; -.
DR PDBsum; 2VUF; -.
DR PDBsum; 2XSI; -.
DR PDBsum; 2XVQ; -.
DR PDBsum; 2XVU; -.
DR PDBsum; 2XVV; -.
DR PDBsum; 2XVW; -.
DR PDBsum; 2XW0; -.
DR PDBsum; 2XW1; -.
DR PDBsum; 2YDF; -.
DR PDBsum; 3A73; -.
DR PDBsum; 3B9L; -.
DR PDBsum; 3B9M; -.
DR PDBsum; 3CX9; -.
DR PDBsum; 3JQZ; -.
DR PDBsum; 3JRY; -.
DR PDBsum; 3LU6; -.
DR PDBsum; 3LU7; -.
DR PDBsum; 3LU8; -.
DR PDBsum; 3SQJ; -.
DR PDBsum; 3TDL; -.
DR PDBsum; 3UIV; -.
DR PDBsum; 4BKE; -.
DR PDBsum; 4E99; -.
DR PDBsum; 4EMX; -.
DR PDBsum; 4G03; -.
DR PDBsum; 4G04; -.
DR PDBsum; 4HGK; -.
DR PDBsum; 4HGM; -.
DR PDBsum; 4IW1; -.
DR PDBsum; 4IW2; -.
DR PDBsum; 4K2C; -.
DR PDBsum; 4K71; -.
DR PDBsum; 4L8U; -.
DR PDBsum; 4L9K; -.
DR PDBsum; 4L9Q; -.
DR PDBsum; 4LA0; -.
DR PDBsum; 4LB2; -.
DR PDBsum; 4LB9; -.
DR PDBsum; 4N0F; -.
DR PDBsum; 4N0U; -.
DR PDBsum; 4S1Y; -.
DR PDBsum; 4Z69; -.
DR PDBsum; 5FUO; -.
DR PDBsum; 5GIX; -.
DR PDBsum; 5GIY; -.
DR PDBsum; 5ID7; -.
DR PDBsum; 5IFO; -.
DR PDBsum; 5IJF; -.
DR PDBsum; 5UJB; -.
DR PDBsum; 5VNW; -.
DR PDBsum; 5X52; -.
DR PDBsum; 5YB1; -.
DR PDBsum; 5YOQ; -.
DR PDBsum; 5Z0B; -.
DR PDBsum; 6A7P; -.
DR PDBsum; 6EZQ; -.
DR PDBsum; 6HSC; -.
DR PDBsum; 6JE7; -.
DR PDBsum; 6L4K; -.
DR PDBsum; 6M4R; -.
DR PDBsum; 6M58; -.
DR PDBsum; 6M5D; -.
DR PDBsum; 6M5E; -.
DR PDBsum; 6QIO; -.
DR PDBsum; 6QIP; -.
DR PDBsum; 6R7S; -.
DR PDBsum; 6WUW; -.
DR PDBsum; 6XV0; -.
DR PDBsum; 6YG9; -.
DR PDBsum; 6ZL1; -.
DR PDBsum; 7A9C; -.
DR PDBsum; 7AAE; -.
DR PDBsum; 7AAI; -.
DR PDBsum; 7D6J; -.
DR PDBsum; 7DJN; -.
DR PDBsum; 7DL4; -.
DR PDBsum; 7EEK; -.
DR PDBsum; 7JWN; -.
DR PDBsum; 7QFE; -.
DR PDBsum; 7VR9; -.
DR AlphaFoldDB; P02768; -.
DR BMRB; P02768; -.
DR PCDDB; P02768; -.
DR SASBDB; P02768; -.
DR SMR; P02768; -.
DR BioGRID; 106715; 340.
DR DIP; DIP-29902N; -.
DR IntAct; P02768; 204.
DR MINT; P02768; -.
DR STRING; 9606.ENSP00000295897; -.
DR BindingDB; P02768; -.
DR ChEMBL; CHEMBL3253; -.
DR DrugBank; DB08496; (R)-warfarin.
DR DrugBank; DB07517; 3-CARBOXY-4-METHYL-5-PROPYL-2-FURANPROPIONIC.
DR DrugBank; DB12001; Abemaciclib.
DR DrugBank; DB05812; Abiraterone.
DR DrugBank; DB11703; Acalabrutinib.
DR DrugBank; DB01418; Acenocoumarol.
DR DrugBank; DB01614; Acepromazine.
DR DrugBank; DB00316; Acetaminophen.
DR DrugBank; DB00414; Acetohexamide.
DR DrugBank; DB09347; Acetrizoic acid.
DR DrugBank; DB06151; Acetylcysteine.
DR DrugBank; DB00459; Acitretin.
DR DrugBank; DB00787; Acyclovir.
DR DrugBank; DB00640; Adenosine.
DR DrugBank; DB00802; Alfentanil.
DR DrugBank; DB00346; Alfuzosin.
DR DrugBank; DB00404; Alprazolam.
DR DrugBank; DB01370; Aluminium.
DR DrugBank; DB14517; Aluminium phosphate.
DR DrugBank; DB14518; Aluminum acetate.
DR DrugBank; DB01118; Amiodarone.
DR DrugBank; DB00321; Amitriptyline.
DR DrugBank; DB01060; Amoxicillin.
DR DrugBank; DB00415; Ampicillin.
DR DrugBank; DB00276; Amsacrine.
DR DrugBank; DB06728; Aniline.
DR DrugBank; DB00714; Apomorphine.
DR DrugBank; DB04557; Arachidonic Acid.
DR DrugBank; DB09229; Aranidipine.
DR DrugBank; DB11217; Arbutin.
DR DrugBank; DB00278; Argatroban.
DR DrugBank; DB01238; Aripiprazole.
DR DrugBank; DB14185; Aripiprazole lauroxil.
DR DrugBank; DB09204; Arotinolol.
DR DrugBank; DB01169; Arsenic trioxide.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB09274; Artesunate.
DR DrugBank; DB00126; Ascorbic acid.
DR DrugBank; DB06216; Asenapine.
DR DrugBank; DB01072; Atazanavir.
DR DrugBank; DB00335; Atenolol.
DR DrugBank; DB00289; Atomoxetine.
DR DrugBank; DB01076; Atorvastatin.
DR DrugBank; DB00995; Auranofin.
DR DrugBank; DB06237; Avanafil.
DR DrugBank; DB07402; Azapropazone.
DR DrugBank; DB00993; Azathioprine.
DR DrugBank; DB08822; Azilsartan medoxomil.
DR DrugBank; DB16703; Belumosudil.
DR DrugBank; DB00245; Benzatropine.
DR DrugBank; DB01086; Benzocaine.
DR DrugBank; DB01053; Benzylpenicillin.
DR DrugBank; DB00443; Betamethasone.
DR DrugBank; DB14669; Betamethasone phosphate.
DR DrugBank; DB13909; Bismuth subgallate.
DR DrugBank; DB01294; Bismuth subsalicylate.
DR DrugBank; DB09223; Blonanserin.
DR DrugBank; DB00083; Botulinum toxin type A.
DR DrugBank; DB01222; Budesonide.
DR DrugBank; DB15248; Bulevirtide.
DR DrugBank; DB00490; Buspirone.
DR DrugBank; DB00237; Butabarbital.
DR DrugBank; DB11148; Butamben.
DR DrugBank; DB11751; Cabotegravir.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR DrugBank; DB04690; Camptothecin.
DR DrugBank; DB03600; Capric acid.
DR DrugBank; DB01197; Captopril.
DR DrugBank; DB01136; Carvedilol.
DR DrugBank; DB00456; Cefalotin.
DR DrugBank; DB01327; Cefazolin.
DR DrugBank; DB14879; Cefiderocol.
DR DrugBank; DB00274; Cefmetazole.
DR DrugBank; DB01328; Cefonicid.
DR DrugBank; DB01329; Cefoperazone.
DR DrugBank; DB00493; Cefotaxime.
DR DrugBank; DB01330; Cefotetan.
DR DrugBank; DB00430; Cefpiramide.
DR DrugBank; DB00438; Ceftazidime.
DR DrugBank; DB01212; Ceftriaxone.
DR DrugBank; DB06119; Cenobamate.
DR DrugBank; DB00567; Cephalexin.
DR DrugBank; DB07565; Chloramphenicol succinate.
DR DrugBank; DB00878; Chlorhexidine.
DR DrugBank; DB00608; Chloroquine.
DR DrugBank; DB00477; Chlorpromazine.
DR DrugBank; DB09093; Chlortetracycline.
DR DrugBank; DB00310; Chlorthalidone.
DR DrugBank; DB00501; Cimetidine.
DR DrugBank; DB00537; Ciprofloxacin.
DR DrugBank; DB00515; Cisplatin.
DR DrugBank; DB01013; Clobetasol propionate.
DR DrugBank; DB00845; Clofazimine.
DR DrugBank; DB01242; Clomipramine.
DR DrugBank; DB01068; Clonazepam.
DR DrugBank; DB00575; Clonidine.
DR DrugBank; DB01147; Cloxacillin.
DR DrugBank; DB15534; Colchiceine.
DR DrugBank; DB01394; Colchicine.
DR DrugBank; DB00286; Conjugated estrogens.
DR DrugBank; DB12483; Copanlisib.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB01380; Cortisone acetate.
DR DrugBank; DB11134; Cupric oxide.
DR DrugBank; DB06778; Cupric sulfate.
DR DrugBank; DB00924; Cyclobenzaprine.
DR DrugBank; DB00434; Cyproheptadine.
DR DrugBank; DB00847; Cysteamine.
DR DrugBank; DB01914; D-glucose.
DR DrugBank; DB06695; Dabigatran etexilate.
DR DrugBank; DB11963; Dacomitinib.
DR DrugBank; DB04816; Dantron.
DR DrugBank; DB00080; Daptomycin.
DR DrugBank; DB12941; Darolutamide.
DR DrugBank; DB01264; Darunavir.
DR DrugBank; DB11943; Delafloxacin.
DR DrugBank; DB11637; Delamanid.
DR DrugBank; DB01189; Desflurane.
DR DrugBank; DB00304; Desogestrel.
DR DrugBank; DB01234; Dexamethasone.
DR DrugBank; DB14649; Dexamethasone acetate.
DR DrugBank; DB09213; Dexibuprofen.
DR DrugBank; DB00829; Diazepam.
DR DrugBank; DB11397; Dichlorvos.
DR DrugBank; DB00586; Diclofenac.
DR DrugBank; DB00266; Dicoumarol.
DR DrugBank; DB00900; Didanosine.
DR DrugBank; DB00861; Diflunisal.
DR DrugBank; DB01396; Digitoxin.
DR DrugBank; DB00343; Diltiazem.
DR DrugBank; DB08995; Diosmin.
DR DrugBank; DB01142; Doxepin.
DR DrugBank; DB00997; Doxorubicin.
DR DrugBank; DB04855; Dronedarone.
DR DrugBank; DB00476; Duloxetine.
DR DrugBank; DB01126; Dutasteride.
DR DrugBank; DB01057; Echothiophate.
DR DrugBank; DB13421; Edoxudine.
DR DrugBank; DB00625; Efavirenz.
DR DrugBank; DB15444; Elexacaftor.
DR DrugBank; DB00879; Emtricitabine.
DR DrugBank; DB00584; Enalapril.
DR DrugBank; DB00228; Enflurane.
DR DrugBank; DB08899; Enzalutamide.
DR DrugBank; DB01364; Ephedrine.
DR DrugBank; DB00530; Erlotinib.
DR DrugBank; DB11827; Ertugliflozin.
DR DrugBank; DB12235; Estetrol.
DR DrugBank; DB00783; Estradiol.
DR DrugBank; DB13952; Estradiol acetate.
DR DrugBank; DB13953; Estradiol benzoate.
DR DrugBank; DB13954; Estradiol cypionate.
DR DrugBank; DB13955; Estradiol dienanthate.
DR DrugBank; DB13956; Estradiol valerate.
DR DrugBank; DB00655; Estrone.
DR DrugBank; DB04574; Estrone sulfate.
DR DrugBank; DB00903; Etacrynic acid.
DR DrugBank; DB00977; Ethinylestradiol.
DR DrugBank; DB00749; Etodolac.
DR DrugBank; DB00294; Etonogestrel.
DR DrugBank; DB01276; Exenatide.
DR DrugBank; DB12466; Favipiravir.
DR DrugBank; DB04854; Febuxostat.
DR DrugBank; DB01039; Fenofibrate.
DR DrugBank; DB00573; Fenoprofen.
DR DrugBank; DB00813; Fentanyl.
DR DrugBank; DB00950; Fexofenadine.
DR DrugBank; DB16165; Finerenone.
DR DrugBank; DB01195; Flecainide.
DR DrugBank; DB00687; Fludrocortisone.
DR DrugBank; DB15690; Fluoroestradiol F-18.
DR DrugBank; DB00544; Fluorouracil.
DR DrugBank; DB00472; Fluoxetine.
DR DrugBank; DB00712; Flurbiprofen.
DR DrugBank; DB00983; Formoterol.
DR DrugBank; DB01320; Fosphenytoin.
DR DrugBank; DB06716; Fospropofol.
DR DrugBank; DB11796; Fostemsavir.
DR DrugBank; DB00695; Furosemide.
DR DrugBank; DB00743; Gadobenic acid.
DR DrugBank; DB06705; Gadofosveset trisodium.
DR DrugBank; DB01044; Gatifloxacin.
DR DrugBank; DB00317; Gefitinib.
DR DrugBank; DB01241; Gemfibrozil.
DR DrugBank; DB12141; Gilteritinib.
DR DrugBank; DB11978; Glasdegib.
DR DrugBank; DB01120; Gliclazide.
DR DrugBank; DB01067; Glipizide.
DR DrugBank; DB01016; Glyburide.
DR DrugBank; DB00986; Glycopyrronium.
DR DrugBank; DB13751; Glycyrrhizic acid.
DR DrugBank; DB04539; Glyphosate.
DR DrugBank; DB12836; Grapiprant.
DR DrugBank; DB11575; Grazoprevir.
DR DrugBank; DB11359; Guaiacol.
DR DrugBank; DB01159; Halothane.
DR DrugBank; DB14999; Human interferon beta.
DR DrugBank; DB00070; Hyaluronidase (ovine).
DR DrugBank; DB01275; Hydralazine.
DR DrugBank; DB00999; Hydrochlorothiazide.
DR DrugBank; DB00774; Hydroflumethiazide.
DR DrugBank; DB00327; Hydromorphone.
DR DrugBank; DB09526; Hydroquinone.
DR DrugBank; DB01611; Hydroxychloroquine.
DR DrugBank; DB00557; Hydroxyzine.
DR DrugBank; DB13014; Hypericin.
DR DrugBank; DB12471; Ibrexafungerp.
DR DrugBank; DB09053; Ibrutinib.
DR DrugBank; DB01050; Ibuprofen.
DR DrugBank; DB00159; Icosapent.
DR DrugBank; DB00619; Imatinib.
DR DrugBank; DB09262; Imidafenacin.
DR DrugBank; DB00458; Imipramine.
DR DrugBank; DB00808; Indapamide.
DR DrugBank; DB00328; Indomethacin.
DR DrugBank; DB07992; Indoxyl sulfate.
DR DrugBank; DB09564; Insulin degludec.
DR DrugBank; DB01307; Insulin detemir.
DR DrugBank; DB05382; Iodine.
DR DrugBank; DB04711; Iodipamide.
DR DrugBank; DB09333; Iopodic acid.
DR DrugBank; DB00332; Ipratropium.
DR DrugBank; DB01029; Irbesartan.
DR DrugBank; DB00762; Irinotecan.
DR DrugBank; DB00753; Isoflurane.
DR DrugBank; DB00677; Isoflurophate.
DR DrugBank; DB00951; Isoniazid.
DR DrugBank; DB01064; Isoprenaline.
DR DrugBank; DB00982; Isotretinoin.
DR DrugBank; DB11757; Istradefylline.
DR DrugBank; DB08820; Ivacaftor.
DR DrugBank; DB01587; Ketazolam.
DR DrugBank; DB01026; Ketoconazole.
DR DrugBank; DB01009; Ketoprofen.
DR DrugBank; DB00598; Labetalol.
DR DrugBank; DB09236; Lacidipine.
DR DrugBank; DB00709; Lamivudine.
DR DrugBank; DB00555; Lamotrigine.
DR DrugBank; DB03017; Lauric acid.
DR DrugBank; DB01006; Letrozole.
DR DrugBank; DB09237; Levamlodipine.
DR DrugBank; DB06282; Levocetirizine.
DR DrugBank; DB01235; Levodopa.
DR DrugBank; DB01137; Levofloxacin.
DR DrugBank; DB00451; Levothyroxine.
DR DrugBank; DB00601; Linezolid.
DR DrugBank; DB00279; Liothyronine.
DR DrugBank; DB01583; Liotrix.
DR DrugBank; DB06655; Liraglutide.
DR DrugBank; DB01601; Lopinavir.
DR DrugBank; DB09195; Lorpiprazole.
DR DrugBank; DB00678; Losartan.
DR DrugBank; DB00227; Lovastatin.
DR DrugBank; DB09280; Lumacaftor.
DR DrugBank; DB15935; Lumasiran.
DR DrugBank; DB12674; Lurbinectedin.
DR DrugBank; DB00137; Lutein.
DR DrugBank; DB08932; Macitentan.
DR DrugBank; DB14513; Magnesium.
DR DrugBank; DB01397; Magnesium salicylate.
DR DrugBank; DB06796; Mangafodipir.
DR DrugBank; DB06234; Maribavir.
DR DrugBank; DB00737; Meclizine.
DR DrugBank; DB09124; Medrogestone.
DR DrugBank; DB00603; Medroxyprogesterone acetate.
DR DrugBank; DB00784; Mefenamic acid.
DR DrugBank; DB00814; Meloxicam.
DR DrugBank; DB00454; Meperidine.
DR DrugBank; DB09383; Meprednisone.
DR DrugBank; DB00931; Metacycline.
DR DrugBank; DB00333; Methadone.
DR DrugBank; DB00563; Methotrexate.
DR DrugBank; DB00968; Methyldopa.
DR DrugBank; DB09241; Methylene blue.
DR DrugBank; DB00959; Methylprednisolone.
DR DrugBank; DB06710; Methyltestosterone.
DR DrugBank; DB00264; Metoprolol.
DR DrugBank; DB01110; Miconazole.
DR DrugBank; DB08893; Mirabegron.
DR DrugBank; DB00295; Morphine.
DR DrugBank; DB08231; Myristic acid.
DR DrugBank; DB00461; Nabumetone.
DR DrugBank; DB00607; Nafcillin.
DR DrugBank; DB01183; Naloxone.
DR DrugBank; DB00788; Naproxen.
DR DrugBank; DB00731; Nateglinide.
DR DrugBank; DB04861; Nebivolol.
DR DrugBank; DB00220; Nelfinavir.
DR DrugBank; DB11828; Neratinib.
DR DrugBank; DB00238; Nevirapine.
DR DrugBank; DB01115; Nifedipine.
DR DrugBank; DB11820; Nifurtimox.
DR DrugBank; DB09079; Nintedanib.
DR DrugBank; DB06713; Norelgestromin.
DR DrugBank; DB00717; Norethisterone.
DR DrugBank; DB00957; Norgestimate.
DR DrugBank; DB00540; Nortriptyline.
DR DrugBank; DB00104; Octreotide.
DR DrugBank; DB00334; Olanzapine.
DR DrugBank; DB04224; Oleic Acid.
DR DrugBank; DB00768; Olopatadine.
DR DrugBank; DB12455; Omadacycline.
DR DrugBank; DB11130; Opium.
DR DrugBank; DB04911; Oritavancin.
DR DrugBank; DB01083; Orlistat.
DR DrugBank; DB00842; Oxazepam.
DR DrugBank; DB00776; Oxcarbazepine.
DR DrugBank; DB01062; Oxybutynin.
DR DrugBank; DB00497; Oxycodone.
DR DrugBank; DB06412; Oxymetholone.
DR DrugBank; DB03585; Oxyphenbutazone.
DR DrugBank; DB00595; Oxytetracycline.
DR DrugBank; DB09073; Palbociclib.
DR DrugBank; DB03796; Palmitic Acid.
DR DrugBank; DB13967; Patent Blue.
DR DrugBank; DB14582; Patisiran.
DR DrugBank; DB12978; Pexidartinib.
DR DrugBank; DB03255; Phenol.
DR DrugBank; DB00946; Phenprocoumon.
DR DrugBank; DB00252; Phenytoin.
DR DrugBank; DB01132; Pioglitazone.
DR DrugBank; DB01621; Pipotiazine.
DR DrugBank; DB04951; Pirfenidone.
DR DrugBank; DB00554; Piroxicam.
DR DrugBank; DB08860; Pitavastatin.
DR DrugBank; DB11642; Pitolisant.
DR DrugBank; DB01324; Polythiazide.
DR DrugBank; DB09087; Potassium alum.
DR DrugBank; DB09418; Potassium perchlorate.
DR DrugBank; DB06209; Prasugrel.
DR DrugBank; DB00860; Prednisolone.
DR DrugBank; DB15566; Prednisolone acetate.
DR DrugBank; DB14631; Prednisolone phosphate.
DR DrugBank; DB00635; Prednisone.
DR DrugBank; DB01032; Probenecid.
DR DrugBank; DB01069; Promethazine.
DR DrugBank; DB09348; Propiolactone.
DR DrugBank; DB00818; Propofol.
DR DrugBank; DB00571; Propranolol.
DR DrugBank; DB06480; Prucalopride.
DR DrugBank; DB00852; Pseudoephedrine.
DR DrugBank; DB00165; Pyridoxine.
DR DrugBank; DB04216; Quercetin.
DR DrugBank; DB00881; Quinapril.
DR DrugBank; DB00908; Quinidine.
DR DrugBank; DB08735; R,S-Warfarin alcohol.
DR DrugBank; DB00481; Raloxifene.
DR DrugBank; DB11853; Relugolix.
DR DrugBank; DB12404; Remimazolam.
DR DrugBank; DB00912; Repaglinide.
DR DrugBank; DB02709; Resveratrol.
DR DrugBank; DB11855; Revefenacin.
DR DrugBank; DB01045; Rifampicin.
DR DrugBank; DB11753; Rifamycin.
DR DrugBank; DB08864; Rilpivirine.
DR DrugBank; DB08931; Riociguat.
DR DrugBank; DB14840; Ripretinib.
DR DrugBank; DB15305; Risdiplam.
DR DrugBank; DB00734; Risperidone.
DR DrugBank; DB00503; Ritonavir.
DR DrugBank; DB11182; Rose bengal.
DR DrugBank; DB00412; Rosiglitazone.
DR DrugBank; DB01098; Rosuvastatin.
DR DrugBank; DB06201; Rufinamide.
DR DrugBank; DB08877; Ruxolitinib.
DR DrugBank; DB08736; S,R-Warfarin alcohol.
DR DrugBank; DB00936; Salicylic acid.
DR DrugBank; DB00938; Salmeterol.
DR DrugBank; DB01232; Saquinavir.
DR DrugBank; DB11689; Selumetinib.
DR DrugBank; DB13928; Semaglutide.
DR DrugBank; DB01104; Sertraline.
DR DrugBank; DB01236; Sevoflurane.
DR DrugBank; DB12965; Silver.
DR DrugBank; DB06290; Simeprevir.
DR DrugBank; DB00877; Sirolimus.
DR DrugBank; DB00815; Sodium lauryl sulfate.
DR DrugBank; DB15093; Somapacitan.
DR DrugBank; DB00421; Spironolactone.
DR DrugBank; DB00649; Stavudine.
DR DrugBank; DB03193; Stearic acid.
DR DrugBank; DB01581; Sulfamerazine.
DR DrugBank; DB01582; Sulfamethazine.
DR DrugBank; DB00576; Sulfamethizole.
DR DrugBank; DB01015; Sulfamethoxazole.
DR DrugBank; DB00605; Sulindac.
DR DrugBank; DB00391; Sulpiride.
DR DrugBank; DB00870; Suprofen.
DR DrugBank; DB00864; Tacrolimus.
DR DrugBank; DB00675; Tamoxifen.
DR DrugBank; DB05134; Tanespimycin.
DR DrugBank; DB09139; Technetium Tc-99m oxidronate.
DR DrugBank; DB05521; Telaprevir.
DR DrugBank; DB00853; Temozolomide.
DR DrugBank; DB14126; Tenofovir.
DR DrugBank; DB09299; Tenofovir alafenamide.
DR DrugBank; DB15133; Tepotinib.
DR DrugBank; DB00857; Terbinafine.
DR DrugBank; DB00624; Testosterone.
DR DrugBank; DB13943; Testosterone cypionate.
DR DrugBank; DB13944; Testosterone enanthate.
DR DrugBank; DB01420; Testosterone propionate.
DR DrugBank; DB13946; Testosterone undecanoate.
DR DrugBank; DB00759; Tetracycline.
DR DrugBank; DB00152; Thiamine.
DR DrugBank; DB11590; Thimerosal.
DR DrugBank; DB01622; Thioproperazine.
DR DrugBank; DB01623; Thiothixene.
DR DrugBank; DB09100; Thyroid, porcine.
DR DrugBank; DB08816; Ticagrelor.
DR DrugBank; DB01133; Tiludronic acid.
DR DrugBank; DB11800; Tivozanib.
DR DrugBank; DB01056; Tocainide.
DR DrugBank; DB08895; Tofacitinib.
DR DrugBank; DB01124; Tolbutamide.
DR DrugBank; DB00500; Tolmetin.
DR DrugBank; DB00273; Topiramate.
DR DrugBank; DB01685; Topiroxostat.
DR DrugBank; DB00214; Torasemide.
DR DrugBank; DB00755; Tretinoin.
DR DrugBank; DB00620; Triamcinolone.
DR DrugBank; DB00432; Trifluridine.
DR DrugBank; DB08814; Triflusal.
DR DrugBank; DB11677; Triheptanoin.
DR DrugBank; DB00376; Trihexyphenidyl.
DR DrugBank; DB09069; Trimetazidine.
DR DrugBank; DB08867; Ulipristal.
DR DrugBank; DB00313; Valproic acid.
DR DrugBank; DB00512; Vancomycin.
DR DrugBank; DB05294; Vandetanib.
DR DrugBank; DB08881; Vemurafenib.
DR DrugBank; DB00661; Verapamil.
DR DrugBank; DB15456; Vericiguat.
DR DrugBank; DB11641; Vinflunine.
DR DrugBank; DB08828; Vismodegib.
DR DrugBank; DB00162; Vitamin A.
DR DrugBank; DB00682; Warfarin.
DR DrugBank; DB00943; Zalcitabine.
DR DrugBank; DB00495; Zidovudine.
DR DrugBank; DB00744; Zileuton.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR DrugBank; DB00246; Ziprasidone.
DR DrugBank; DB04828; Zomepirac.
DR DrugCentral; P02768; -.
DR Allergome; 763; Hom s HSA.
DR CarbonylDB; P02768; -.
DR GlyConnect; 559; 2 N-Linked glycans (2 sites), 3 O-Linked glycans (2 sites).
DR GlyGen; P02768; 10 sites, 2 N-linked glycans (1 site), 6 O-linked glycans (9 sites).
DR iPTMnet; P02768; -.
DR MetOSite; P02768; -.
DR PhosphoSitePlus; P02768; -.
DR SwissPalm; P02768; -.
DR BioMuta; ALB; -.
DR DMDM; 113576; -.
DR DOSAC-COBS-2DPAGE; P02768; -.
DR OGP; P02768; -.
DR REPRODUCTION-2DPAGE; IPI00384697; -.
DR REPRODUCTION-2DPAGE; IPI00745872; -.
DR REPRODUCTION-2DPAGE; P02768; -.
DR SWISS-2DPAGE; P02768; -.
DR UCD-2DPAGE; P02768; -.
DR CPTAC; non-CPTAC-1160; -.
DR jPOST; P02768; -.
DR MassIVE; P02768; -.
DR PaxDb; P02768; -.
DR PeptideAtlas; P02768; -.
DR PRIDE; P02768; -.
DR ProteomicsDB; 51587; -. [P02768-1]
DR ProteomicsDB; 51588; -. [P02768-2]
DR ProteomicsDB; 70582; -.
DR ABCD; P02768; 26 sequenced antibodies.
DR Antibodypedia; 3342; 3149 antibodies from 51 providers.
DR DNASU; 213; -.
DR Ensembl; ENST00000295897.9; ENSP00000295897.4; ENSG00000163631.17. [P02768-1]
DR Ensembl; ENST00000621085.4; ENSP00000483421.1; ENSG00000163631.17. [P02768-3]
DR GeneID; 213; -.
DR KEGG; hsa:213; -.
DR MANE-Select; ENST00000295897.9; ENSP00000295897.4; NM_000477.7; NP_000468.1.
DR UCSC; uc003hgs.5; human. [P02768-1]
DR UCSC; uc062xfr.1; human.
DR CTD; 213; -.
DR DisGeNET; 213; -.
DR GeneCards; ALB; -.
DR HGNC; HGNC:399; ALB.
DR HPA; ENSG00000163631; Tissue enriched (liver).
DR MalaCards; ALB; -.
DR MIM; 103600; gene.
DR MIM; 615999; phenotype.
DR MIM; 616000; phenotype.
DR neXtProt; NX_P02768; -.
DR OpenTargets; ENSG00000163631; -.
DR Orphanet; 86816; Congenital analbuminemia.
DR Orphanet; 276271; NON RARE IN EUROPE: Familial dysalbuminemic hyperthyroxinemia.
DR PharmGKB; PA24690; -.
DR VEuPathDB; HostDB:ENSG00000163631; -.
DR eggNOG; ENOG502R7EA; Eukaryota.
DR GeneTree; ENSGT00390000000113; -.
DR InParanoid; P02768; -.
DR OMA; RVGTKCC; -.
DR OrthoDB; 1377476at2759; -.
DR PhylomeDB; P02768; -.
DR TreeFam; TF335561; -.
DR PathwayCommons; P02768; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-159418; Recycling of bile acids and salts.
DR Reactome; R-HSA-189451; Heme biosynthesis.
DR Reactome; R-HSA-189483; Heme degradation.
DR Reactome; R-HSA-2168880; Scavenging of heme from plasma.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR Reactome; R-HSA-8964058; HDL remodeling.
DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR Reactome; R-HSA-9749641; Aspirin ADME.
DR SignaLink; P02768; -.
DR SIGNOR; P02768; -.
DR BioGRID-ORCS; 213; 7 hits in 1071 CRISPR screens.
DR ChiTaRS; ALB; human.
DR EvolutionaryTrace; P02768; -.
DR GeneWiki; Serum_albumin; -.
DR GenomeRNAi; 213; -.
DR Pharos; P02768; Tchem.
DR PRO; PR:P02768; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P02768; protein.
DR Bgee; ENSG00000163631; Expressed in liver and 112 other tissues.
DR ExpressionAtlas; P02768; baseline and differential.
DR Genevisible; P02768; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0016209; F:antioxidant activity; NAS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IPI:BHF-UCL.
DR GO; GO:0005507; F:copper ion binding; NAS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:1903981; F:enterobactin binding; IDA:UniProtKB.
DR GO; GO:0140272; F:exogenous protein binding; IDA:UniProtKB.
DR GO; GO:0005504; F:fatty acid binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0015643; F:toxic substance binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; IDA:UniProtKB.
DR GO; GO:0051659; P:maintenance of mitochondrion location; IDA:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0043069; P:negative regulation of programmed cell death; NAS:UniProtKB.
DR GO; GO:0001895; P:retina homeostasis; HEP:UniProtKB.
DR CDD; cd00015; ALBUMIN; 3.
DR InterPro; IPR000264; ALB/AFP/VDB.
DR InterPro; IPR020858; Serum_albumin-like.
DR InterPro; IPR021177; Serum_albumin/AFP/Afamin.
DR InterPro; IPR020857; Serum_albumin_CS.
DR InterPro; IPR014760; Serum_albumin_N.
DR PANTHER; PTHR11385; PTHR11385; 1.
DR Pfam; PF00273; Serum_albumin; 3.
DR PIRSF; PIRSF002520; Serum_albumin_subgroup; 1.
DR PRINTS; PR00802; SERUMALBUMIN.
DR SMART; SM00103; ALBUMIN; 3.
DR SUPFAM; SSF48552; SSF48552; 3.
DR PROSITE; PS00212; ALBUMIN_1; 3.
DR PROSITE; PS51438; ALBUMIN_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium;
KW Cleavage on pair of basic residues; Copper; Direct protein sequencing;
KW Disease variant; Disulfide bond; Glycation; Glycoprotein; Lipid-binding;
KW Metal-binding; Methylation; Phosphoprotein; Reference proteome; Repeat;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..18
FT PROPEP 19..24
FT /id="PRO_0000001067"
FT CHAIN 25..609
FT /note="Albumin"
FT /id="PRO_0000001068"
FT DOMAIN 19..210
FT /note="Albumin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 211..403
FT /note="Albumin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT DOMAIN 404..601
FT /note="Albumin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769"
FT BINDING 27
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250|UniProtKB:P02770"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 37
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:28567254,
FT ECO:0007744|PDB:5IJF"
FT BINDING 264
FT /ligand="bilirubin IXalpha"
FT /ligand_id="ChEBI:CHEBI:57977"
FT /evidence="ECO:0000269|PubMed:656055"
FT BINDING 268
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:28567254,
FT ECO:0007744|PDB:5IJF"
FT BINDING 273
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:28567254,
FT ECO:0007744|PDB:5IJF"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 279
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT BINDING 283
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02769"
FT SITE 28
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 44
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 65
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 88
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 97
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 117
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 130
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 160
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 183
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 198
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 205
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 214
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 219
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 223
FT /note="Aspirin-acetylated lysine"
FT SITE 229
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 236
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 264
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 286
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 298
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 310
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 383
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 396
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 413
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 426
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 438
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 456
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 460
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 490
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 499
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 524
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 543
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 548
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 562
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 565
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 581
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 584
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 588
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT SITE 598
FT /note="Not glycated"
FT /evidence="ECO:0000269|PubMed:15047055"
FT MOD_RES 29
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 82
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:24275569"
FT MOD_RES 89
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 107
FT /note="Phosphothreonine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 229
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 444
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 446
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 460
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 543
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT MOD_RES 558
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 588
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P07724"
FT CARBOHYD 36
FT /note="N-linked (Glc) (glycation) lysine"
FT /evidence="ECO:0000269|PubMed:3759977"
FT CARBOHYD 75
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:15047055"
FT CARBOHYD 161
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:15047055"
FT CARBOHYD 186
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:15047055"
FT CARBOHYD 223
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:3759977,
FT ECO:0000269|PubMed:6853480"
FT CARBOHYD 249
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:15047055"
FT CARBOHYD 257
FT /note="N-linked (Glc) (glycation) lysine"
FT /evidence="ECO:0000269|PubMed:15047055,
FT ECO:0000269|PubMed:3759977"
FT CARBOHYD 300
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:15047055"
FT CARBOHYD 305
FT /note="N-linked (Glc) (glycation) lysine"
FT /evidence="ECO:0000269|PubMed:3759977"
FT CARBOHYD 337
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:15047055"
FT CARBOHYD 341
FT /note="N-linked (Glc) (glycation) lysine"
FT /evidence="ECO:0000269|PubMed:3759977"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine; in variant Redhill"
FT /id="CAR_000226"
FT CARBOHYD 347
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:15047055"
FT CARBOHYD 375
FT /note="N-linked (Glc) (glycation) lysine"
FT /evidence="ECO:0000269|PubMed:15047055,
FT ECO:0000269|PubMed:3759977"
FT CARBOHYD 402
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:15047055"
FT CARBOHYD 437
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:15047055"
FT CARBOHYD 463
FT /note="N-linked (Glc) (glycation) lysine"
FT /evidence="ECO:0000269|PubMed:3759977"
FT CARBOHYD 468
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:15047055"
FT CARBOHYD 518
FT /note="N-linked (GlcNAc...) asparagine; in variant
FT Casebrook"
FT /id="CAR_000069"
FT CARBOHYD 549
FT /note="N-linked (Glc) (glycation) lysine"
FT /evidence="ECO:0000269|PubMed:15047055,
FT ECO:0000269|PubMed:3759977, ECO:0000269|PubMed:6706980,
FT ECO:0000269|PubMed:6853480"
FT CARBOHYD 558
FT /note="N-linked (Glc) (glycation) lysine; alternate"
FT /evidence="ECO:0000269|PubMed:3759977"
FT CARBOHYD 560
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:15047055"
FT CARBOHYD 569
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:15047055"
FT CARBOHYD 597
FT /note="N-linked (Glc) (glycation) lysine; in vitro"
FT /evidence="ECO:0000269|PubMed:15047055"
FT DISULFID 77..86
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28,
FT ECO:0007744|PDB:5IJF"
FT DISULFID 99..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28,
FT ECO:0007744|PDB:5IJF"
FT DISULFID 114..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28,
FT ECO:0007744|PDB:5IJF"
FT DISULFID 148..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28,
FT ECO:0007744|PDB:5IJF"
FT DISULFID 192..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28,
FT ECO:0007744|PDB:5IJF"
FT DISULFID 224..270
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28,
FT ECO:0007744|PDB:5IJF"
FT DISULFID 269..277
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28,
FT ECO:0007744|PDB:5IJF"
FT DISULFID 289..303
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28,
FT ECO:0007744|PDB:5IJF"
FT DISULFID 302..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28,
FT ECO:0007744|PDB:5IJF"
FT DISULFID 340..385
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28,
FT ECO:0007744|PDB:5IJF"
FT DISULFID 384..393
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28,
FT ECO:0007744|PDB:5IJF"
FT DISULFID 416..462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28,
FT ECO:0007744|PDB:5IJF"
FT DISULFID 461..472
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28,
FT ECO:0007744|PDB:5IJF"
FT DISULFID 485..501
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28,
FT ECO:0007744|PDB:5IJF"
FT DISULFID 500..511
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28,
FT ECO:0007744|PDB:5IJF"
FT DISULFID 538..583
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28,
FT ECO:0007744|PDB:5IJF"
FT DISULFID 582..591
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00769,
FT ECO:0000269|PubMed:28567254, ECO:0000269|Ref.28,
FT ECO:0007744|PDB:5IJF"
FT VAR_SEQ 43..234
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.9"
FT /id="VSP_021275"
FT VAR_SEQ 164..376
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057389"
FT VARIANT 23
FT /note="R -> C (in Redhill/Malmo-I/Tradate; associated with
FT T-344 in Redhill; dbSNP:rs80008208)"
FT /evidence="ECO:0000269|PubMed:1518850"
FT /id="VAR_000499"
FT VARIANT 23
FT /note="R -> H (in Fukuoka-2/Lille/Taipei/Varese/Komagome-3;
FT dbSNP:rs72552709)"
FT /evidence="ECO:0000269|PubMed:1946412,
FT ECO:0000269|PubMed:2247440, ECO:0000269|PubMed:2911589"
FT /id="VAR_000500"
FT VARIANT 24
FT /note="R -> L (in Jaffna; dbSNP:rs74821926)"
FT /id="VAR_000501"
FT VARIANT 24
FT /note="R -> P (in Takefu/Honolulu-1; dbSNP:rs74821926)"
FT /evidence="ECO:0000269|PubMed:2404284"
FT /id="VAR_000502"
FT VARIANT 24
FT /note="R -> Q (in Christchurch/Honolulu-2;
FT dbSNP:rs74821926)"
FT /evidence="ECO:0000269|PubMed:2404284,
FT ECO:0000269|PubMed:2762316, ECO:0000269|PubMed:2911589"
FT /id="VAR_000503"
FT VARIANT 25
FT /note="D -> V (in Bleinheim/Iowa city-2; dbSNP:rs75353611)"
FT /evidence="ECO:0000269|PubMed:1946412"
FT /id="VAR_000504"
FT VARIANT 27
FT /note="H -> Q (in Nagasaki-3; dbSNP:rs76285851)"
FT /id="VAR_000505"
FT VARIANT 27
FT /note="H -> Y (in Larino; dbSNP:rs141733599)"
FT /evidence="ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:8022807"
FT /id="VAR_000506"
FT VARIANT 73
FT /note="F -> Y"
FT /evidence="ECO:0000269|PubMed:11680902"
FT /id="VAR_010657"
FT VARIANT 84
FT /note="E -> K (in Torino; dbSNP:rs77050410)"
FT /evidence="ECO:0000269|PubMed:2247440"
FT /id="VAR_000507"
FT VARIANT 87
FT /note="D -> N (in Malmo-95/Dalakarlia; dbSNP:rs78574148)"
FT /evidence="ECO:0000269|PubMed:1518850"
FT /id="VAR_000508"
FT VARIANT 90
FT /note="L -> P (in FDAH; dbSNP:rs77892378)"
FT /evidence="ECO:0000269|PubMed:9589637"
FT /id="VAR_013011"
FT VARIANT 106
FT /note="E -> K (in Vibo Valentia; dbSNP:rs80296402)"
FT /evidence="ECO:0000269|PubMed:2247440"
FT /id="VAR_000509"
FT VARIANT 121
FT /note="E -> G"
FT /evidence="ECO:0000269|PubMed:6275391"
FT /id="VAR_014290"
FT VARIANT 138
FT /note="R -> G (in Yanomama-2; dbSNP:rs77238412)"
FT /id="VAR_000510"
FT VARIANT 143
FT /note="E -> K (in Nagoya; dbSNP:rs75522063)"
FT /evidence="ECO:0000269|PubMed:2404284"
FT /id="VAR_000511"
FT VARIANT 146
FT /note="V -> E (in Tregasio; dbSNP:rs77752336)"
FT /id="VAR_013012"
FT VARIANT 152
FT /note="H -> R (in Komagome-2; dbSNP:rs80095457)"
FT /evidence="ECO:0000269|PubMed:1946412"
FT /id="VAR_000512"
FT VARIANT 201
FT /note="C -> F (in Hawkes bay; dbSNP:rs77656691)"
FT /evidence="ECO:0000269|PubMed:8347685"
FT /id="VAR_000513"
FT VARIANT 215
FT /note="A -> T (in dbSNP:rs3210154)"
FT /id="VAR_014291"
FT VARIANT 215
FT /note="A -> V (in dbSNP:rs3204504)"
FT /id="VAR_014292"
FT VARIANT 220
FT /note="Q -> L (in dbSNP:rs3210163)"
FT /id="VAR_014293"
FT VARIANT 242
FT /note="R -> H (in FDAH; dbSNP:rs75002628)"
FT /evidence="ECO:0000269|PubMed:7852505,
FT ECO:0000269|PubMed:8048949, ECO:0000269|PubMed:9329347"
FT /id="VAR_000514"
FT VARIANT 242
FT /note="R -> P (in FDAH; dbSNP:rs75002628)"
FT /id="VAR_013013"
FT VARIANT 249
FT /note="K -> Q (in Tradate-2; dbSNP:rs79804069)"
FT /evidence="ECO:0000269|PubMed:8022807"
FT /id="VAR_000515"
FT VARIANT 264
FT /note="K -> E (in Herborn; dbSNP:rs79377490)"
FT /evidence="ECO:0000269|PubMed:8513793"
FT /id="VAR_000516"
FT VARIANT 292
FT /note="Q -> R (in Malmo-10; dbSNP:rs80002911)"
FT /evidence="ECO:0000269|PubMed:1518850"
FT /id="VAR_000517"
FT VARIANT 293
FT /note="D -> G (in Nagasaki-1; dbSNP:rs79744198)"
FT /evidence="ECO:0000269|PubMed:2762316"
FT /id="VAR_000518"
FT VARIANT 300
FT /note="K -> N (in Caserta; dbSNP:rs74718349)"
FT /evidence="ECO:0000269|PubMed:8022807"
FT /id="VAR_000519"
FT VARIANT 337
FT /note="K -> N (in Canterbury/New Guinea/Tagliacozzo/Cuneo/
FT Cooperstown; dbSNP:rs72552710)"
FT /evidence="ECO:0000269|PubMed:2404284,
FT ECO:0000269|PubMed:2911589, ECO:0000269|PubMed:3828358"
FT /id="VAR_000520"
FT VARIANT 338
FT /note="D -> G (in Bergamo; dbSNP:rs76242087)"
FT /id="VAR_013014"
FT VARIANT 338
FT /note="D -> V (in Brest; dbSNP:rs76242087)"
FT /id="VAR_013015"
FT VARIANT 342
FT /note="N -> K (in Malmo-47; dbSNP:rs77544362)"
FT /evidence="ECO:0000269|PubMed:1518850"
FT /id="VAR_000521"
FT VARIANT 344
FT /note="A -> T (in Redhill; associated with C-23;
FT dbSNP:rs78953271)"
FT /id="VAR_000522"
FT VARIANT 345
FT /note="E -> K (in Roma; dbSNP:rs72552711)"
FT /id="VAR_000523"
FT VARIANT 357
FT /note="E -> K (in Sondrio; dbSNP:rs77354753)"
FT /evidence="ECO:0000269|PubMed:1347703"
FT /id="VAR_000524"
FT VARIANT 378
FT /note="E -> K (in Hiroshima-1; dbSNP:rs76593094)"
FT /evidence="ECO:0000269|PubMed:2762316, ECO:0000269|Ref.5"
FT /id="VAR_000525"
FT VARIANT 382
FT /note="E -> K (in Coari I/Porto Alegre; dbSNP:rs75791663)"
FT /id="VAR_000526"
FT VARIANT 383
FT /note="K -> N (in Trieste; dbSNP:rs75069738)"
FT /id="VAR_013016"
FT VARIANT 389
FT /note="D -> H (in Parklands; dbSNP:rs77187142)"
FT /id="VAR_000527"
FT VARIANT 389
FT /note="D -> V (in Iowa city-1; dbSNP:rs78538497)"
FT /evidence="ECO:0000269|PubMed:1946412"
FT /id="VAR_000528"
FT VARIANT 396
FT /note="K -> E (in Naskapi/Mersin/Komagome-1;
FT dbSNP:rs78166690)"
FT /evidence="ECO:0000269|PubMed:1946412,
FT ECO:0000269|PubMed:3474609, ECO:0000269|PubMed:3479777"
FT /id="VAR_000529"
FT VARIANT 399
FT /note="D -> N (in Nagasaki-2; dbSNP:rs77514449)"
FT /evidence="ECO:0000269|PubMed:3479777"
FT /id="VAR_000530"
FT VARIANT 400
FT /note="E -> K (in Tochigi; dbSNP:rs79047363)"
FT /evidence="ECO:0000269|PubMed:2762316"
FT /id="VAR_000531"
FT VARIANT 400
FT /note="E -> Q (in Malmo-5; dbSNP:rs79047363)"
FT /evidence="ECO:0000269|PubMed:1518850"
FT /id="VAR_000532"
FT VARIANT 406
FT /note="E -> K (in Hiroshima-2; dbSNP:rs76483862)"
FT /evidence="ECO:0000269|PubMed:2762316"
FT /id="VAR_000533"
FT VARIANT 420
FT /note="E -> K"
FT /evidence="ECO:0000269|PubMed:6171778"
FT /id="VAR_014294"
FT VARIANT 434
FT /note="R -> C (in Liprizzi; dbSNP:rs78575701)"
FT /id="VAR_013017"
FT VARIANT 490
FT /note="K -> E (in dbSNP:rs1063469)"
FT /id="VAR_014295"
FT VARIANT 503
FT /note="E -> K (in Dublin; dbSNP:rs80259813)"
FT /id="VAR_000534"
FT VARIANT 518
FT /note="D -> N (in Casebrook; dbSNP:rs75920790)"
FT /evidence="ECO:0000269|PubMed:1859851"
FT /id="VAR_000535"
FT VARIANT 525
FT /note="E -> K (in Manaus-1/Adana/Lambadi/Vancouver;
FT dbSNP:rs75523493)"
FT /evidence="ECO:0000269|PubMed:2404284"
FT /id="VAR_000536"
FT VARIANT 529
FT /note="E -> K (in Ortonovo; dbSNP:rs74826639)"
FT /evidence="ECO:0000269|PubMed:7902134"
FT /id="VAR_000537"
FT VARIANT 557
FT /note="V -> M (in Maddaloni; dbSNP:rs78284052)"
FT /id="VAR_013018"
FT VARIANT 560
FT /note="K -> E (in Castel di Sangro; dbSNP:rs77645174)"
FT /id="VAR_000538"
FT VARIANT 565
FT /note="K -> E (in Maku; dbSNP:rs80345158)"
FT /evidence="ECO:0000269|PubMed:3479777"
FT /id="VAR_000539"
FT VARIANT 574
FT /note="D -> A (in Malmo-61; dbSNP:rs79738788)"
FT /evidence="ECO:0000269|PubMed:1518850"
FT /id="VAR_000541"
FT VARIANT 574
FT /note="D -> G (in Mexico; dbSNP:rs79738788)"
FT /evidence="ECO:0000269|PubMed:3474609"
FT /id="VAR_000540"
FT VARIANT 584
FT /note="K -> E (in Church bay; dbSNP:rs76671808)"
FT /id="VAR_013019"
FT VARIANT 587
FT /note="D -> N (in Fukuoka-1/Paris-2; dbSNP:rs76587671)"
FT /evidence="ECO:0000269|PubMed:1347703,
FT ECO:0000269|PubMed:2404284"
FT /id="VAR_000542"
FT VARIANT 589
FT /note="E -> K (in Osaka-1; dbSNP:rs75709682)"
FT /evidence="ECO:0000269|PubMed:2404284"
FT /id="VAR_000543"
FT VARIANT 594
FT /note="E -> K (in Osaka-2/Phnom Phen/albumin B/Verona;
FT dbSNP:rs79228041)"
FT /evidence="ECO:0000269|PubMed:2404284,
FT ECO:0000269|PubMed:2762316, ECO:0000269|PubMed:2911589"
FT /id="VAR_000544"
FT VARIANT 596..609
FT /note="GKKLVAASQAALGL -> PTMRIRERK (in Venezia)"
FT /id="VAR_000547"
FT VARIANT 597
FT /note="K -> E (in Gent/Milano Fast; dbSNP:rs80106970)"
FT /id="VAR_000545"
FT VARIANT 598
FT /note="K -> N (in Vanves; dbSNP:rs75738598)"
FT /id="VAR_000546"
FT VARIANT 599..609
FT /note="LVAASQAALGL -> TCCCKSSCLRLITSHLKASQPTMRIRERK (in
FT Kenitra)"
FT /id="VAR_012981"
FT MUTAGEN 91
FT /note="H->A: Impairs metal binding."
FT /evidence="ECO:0000269|PubMed:28567254"
FT CONFLICT 55
FT /note="L -> P (in Ref. 11; CAH18185)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="R -> S (in Ref. 4; AAF01333)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="E -> Q (in Ref. 19; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="Y -> L (in Ref. 24; AA sequence and 25; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="Q -> E (in Ref. 19; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 327..332
FT /note="PSLAAD -> MFVLLC (in Ref. 10; AAF71067)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="V -> A (in Ref. 10; AAF71067)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="Q -> E (in Ref. 15; AAH14308)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="Q -> E (in Ref. 2; CAA23753)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="E -> G (in Ref. 4; AAF01333)"
FT /evidence="ECO:0000305"
FT CONFLICT 488..489
FT /note="HE -> EH (in Ref. 19; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="K -> R (in Ref. 11; CAH18185)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="E -> Q (in Ref. 19; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="T -> A (in Ref. 11; CAH18185)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="K -> R (in Ref. 11; CAH18185)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="Q -> R (in Ref. 5; AAN17825)"
FT /evidence="ECO:0000305"
FT HELIX 30..38
FT /evidence="ECO:0007829|PDB:6YG9"
FT HELIX 40..54
FT /evidence="ECO:0007829|PDB:6YG9"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:2BXH"
FT HELIX 60..79
FT /evidence="ECO:0007829|PDB:6YG9"
FT TURN 84..87
FT /evidence="ECO:0007829|PDB:6YG9"
FT HELIX 90..100
FT /evidence="ECO:0007829|PDB:6YG9"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:2BXH"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:6YG9"
FT HELIX 109..116
FT /evidence="ECO:0007829|PDB:6YG9"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:6A7P"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:6YG9"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:4N0F"
FT HELIX 144..153
FT /evidence="ECO:0007829|PDB:6YG9"
FT HELIX 155..169
FT /evidence="ECO:0007829|PDB:6YG9"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:5ID7"
FT HELIX 175..192
FT /evidence="ECO:0007829|PDB:6YG9"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:6YG9"
FT HELIX 198..246
FT /evidence="ECO:0007829|PDB:6YG9"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:6EZQ"
FT HELIX 252..271
FT /evidence="ECO:0007829|PDB:6YG9"
FT HELIX 274..289
FT /evidence="ECO:0007829|PDB:6YG9"
FT HELIX 290..294
FT /evidence="ECO:0007829|PDB:6YG9"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:5Z0B"
FT HELIX 300..304
FT /evidence="ECO:0007829|PDB:6YG9"
FT HELIX 307..315
FT /evidence="ECO:0007829|PDB:6YG9"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:6YG9"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:2BXP"
FT HELIX 339..344
FT /evidence="ECO:0007829|PDB:6YG9"
FT HELIX 347..361
FT /evidence="ECO:0007829|PDB:6YG9"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:4N0F"
FT HELIX 367..384
FT /evidence="ECO:0007829|PDB:6YG9"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:1N5U"
FT HELIX 390..394
FT /evidence="ECO:0007829|PDB:1N5U"
FT TURN 397..401
FT /evidence="ECO:0007829|PDB:6YG9"
FT HELIX 402..419
FT /evidence="ECO:0007829|PDB:6YG9"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:6YG9"
FT HELIX 423..438
FT /evidence="ECO:0007829|PDB:6YG9"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:6EZQ"
FT HELIX 444..461
FT /evidence="ECO:0007829|PDB:6YG9"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:2BXH"
FT TURN 466..468
FT /evidence="ECO:0007829|PDB:6YG9"
FT HELIX 469..490
FT /evidence="ECO:0007829|PDB:6YG9"
FT HELIX 495..502
FT /evidence="ECO:0007829|PDB:6YG9"
FT TURN 505..507
FT /evidence="ECO:0007829|PDB:6YG9"
FT HELIX 508..513
FT /evidence="ECO:0007829|PDB:6YG9"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:6R7S"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:6YG9"
FT HELIX 535..538
FT /evidence="ECO:0007829|PDB:6YG9"
FT HELIX 542..559
FT /evidence="ECO:0007829|PDB:6YG9"
FT STRAND 561..563
FT /evidence="ECO:0007829|PDB:1E7A"
FT HELIX 565..583
FT /evidence="ECO:0007829|PDB:1N5U"
FT STRAND 584..587
FT /evidence="ECO:0007829|PDB:1N5U"
FT HELIX 588..590
FT /evidence="ECO:0007829|PDB:2BXG"
FT TURN 591..593
FT /evidence="ECO:0007829|PDB:1N5U"
FT HELIX 596..602
FT /evidence="ECO:0007829|PDB:6YG9"
FT TURN 603..605
FT /evidence="ECO:0007829|PDB:6YG9"
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
