APOB_HUMAN
ID APOB_HUMAN Reviewed; 4563 AA.
AC P04114; O00502; P78479; P78480; P78481; Q13779; Q13785; Q13786; Q13787;
AC Q13788; Q4ZG63; Q53QC8; Q7Z600; Q9UMN0;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 245.
DE RecName: Full=Apolipoprotein B-100;
DE Short=Apo B-100;
DE Contains:
DE RecName: Full=Apolipoprotein B-48;
DE Short=Apo B-48;
DE Flags: Precursor;
GN Name=APOB;
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], AND VARIANTS ASN-273; GLU-1218; CYS-1422; RP
RP VAL-2092; VAL-2313; THR-2365; GLN-2680; HIS-3319; LYS-3427; GLU-3432;
RP THR-3732; LEU-3949; PHE-3964; LYS-4181 AND ASN-4338.
RX PubMed=3763409; DOI=10.1093/nar/14.18.7501;
RA Knott T.C., Wallis S.C., Powell L.M., Pease R.J., Lusis A.J., Blackhart B.,
RA McCarthy B.J., Mahley R.W., Levy-Wilson B., Scott J.;
RT "Complete cDNA and derived protein sequence of human apolipoprotein B-
RT 100.";
RL Nucleic Acids Res. 14:7501-7503(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-1422; VAL-2313;
RP HIS-3319; LYS-3427; GLU-3432 AND ASN-4338.
RX PubMed=3652907; DOI=10.1089/dna.1987.6.363;
RA Ludwig E.H., Blackhart B.D., Pierotti V.R., Caiati L., Fortier C.,
RA Knott T., Scott J., Mahley R.W., Levy-Wilson B., McCarthy B.J.;
RT "DNA sequence of the human apolipoprotein B gene.";
RL DNA 6:363-372(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ILE-98; VAL-618; CYS-1422;
RP VAL-2313; HIS-3319; LYS-3427; GLU-3432 AND ASN-4338.
RX PubMed=3759943; DOI=10.1016/s0021-9258(18)69248-8;
RA Chen S.-H., Yang C.-Y., Chen P.-F., Setzer D., Tanimura M., Li W.-H.,
RA Gotto A.M. Jr., Chan L.;
RT "The complete cDNA and amino acid sequence of human apolipoprotein B-100.";
RL J. Biol. Chem. 261:12918-12921(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS CYS-1422; ASN-2037; VAL-2313;
RP HIS-3319; LYS-3427; GLU-3432; LEU-3949; LYS-4181 AND ASN-4338.
RX PubMed=3464946; DOI=10.1073/pnas.83.21.8142;
RA Law S.W., Grant S.M., Higuchi K., Hospattankar A.V., Lackner K.J., Lee N.,
RA Brewer H.B. Jr.;
RT "Human liver apolipoprotein B-100 cDNA: complete nucleic acid and derived
RT amino acid sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:8142-8146(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40, AND
RP VARIANTS VAL-618; CYS-1422; VAL-2313; HIS-3319; LYS-3427; GLU-3432;
RP THR-3732; LEU-3949; PHE-3964; LYS-4181 AND ASN-4338.
RX PubMed=3030729; DOI=10.1002/j.1460-2075.1986.tb04675.x;
RA Cladaras C., Hadzopoulou-Cladaras M., Nolte R.T., Atkinson D., Zannis V.I.;
RT "The complete sequence and structural analysis of human apolipoprotein B-
RT 100: relationship between apoB-100 and apoB-48 forms.";
RL EMBO J. 5:3495-3507(1986).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-1422; VAL-2313 AND
RP ASN-4338.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1670, AND VARIANTS ILE-98; CYS-1422 AND
RP ASP-1670.
RX PubMed=3461454; DOI=10.1073/pnas.83.15.5678;
RA Protter A.A., Hardman D.A., Sato K.Y., Schilling J.W., Yamanaka M.,
RA Hort Y.J., Hjerrild K.A., Chen G.C., Kane J.P.;
RT "Analysis of cDNA clones encoding the entire B-26 region of human
RT apolipoprotein B.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:5678-5682(1986).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-291.
RX PubMed=3513177; DOI=10.1073/pnas.83.5.1467;
RA Protter A.A., Hardman D.A., Schilling J.W., Miller J., Appleby V.,
RA Chen G.C., Kirsher S.W., McEnroe G., Kane J.P.;
RT "Isolation of a cDNA clone encoding the amino-terminal region of human
RT apolipoprotein B.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:1467-1471(1986).
RN [10]
RP PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, AND VARIANT ILE-98.
RX PubMed=2115173; DOI=10.1073/pnas.87.14.5523;
RA Yang C.Y., Kim T.W., Weng S.A., Lee B.R., Yang M.L., Gotto A.M. Jr.;
RT "Isolation and characterization of sulfhydryl and disulfide peptides of
RT human apolipoprotein B-100.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:5523-5527(1990).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 485-1044.
RC TISSUE=Liver;
RX PubMed=3001697; DOI=10.1073/pnas.82.24.8340;
RA Law S.W., Lackner K.J., Hospattankar A.V., Anchors J.M., Sakaguchi A.Y.,
RA Naylor S.L., Brewer H.B. Jr.;
RT "Human apolipoprotein B-100: cloning, analysis of liver mRNA, and
RT assignment of the gene to chromosome 2.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:8340-8344(1985).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 709-906.
RX PubMed=3860836; DOI=10.1073/pnas.82.15.4983;
RA Deeb S.S., Motulsky A.G., Albers J.J.;
RT "A partial cDNA clone for human apolipoprotein B.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:4983-4986(1985).
RN [13]
RP PROTEIN SEQUENCE OF 873-896 AND 3113-3137.
RX PubMed=6373369; DOI=10.1016/0014-5793(84)81378-2;
RA LeBoeuf R.C., Miller C., Shively J.E., Schumaker V.N., Balla M.A.,
RA Lusis A.J.;
RT "Human apolipoprotein B: partial amino acid sequence.";
RL FEBS Lett. 170:105-108(1984).
RN [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1042-1232.
RX PubMed=2567736; DOI=10.1016/s0021-9258(18)60477-6;
RA Huang L.S., Ripps M.E., Korman S.H., Deckelbaum R.J., Breslow J.L.;
RT "Hypobetalipoproteinemia due to an apolipoprotein B gene exon 21 deletion
RT derived by Alu-Alu recombination.";
RL J. Biol. Chem. 264:11394-11400(1989).
RN [15]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1282-4503, AND VARIANTS CYS-1422; VAL-2313;
RP HIS-3319; LYS-3427; GLU-3432; THR-3732 AND ASN-4338.
RX PubMed=2883086; DOI=10.1016/0378-1119(86)90383-5;
RA Carlsson P., Darnfors C., Olofsson S.O., Bjursell G.;
RT "Analysis of the human apolipoprotein B gene; complete structure of the B-
RT 74 region.";
RL Gene 49:29-51(1986).
RN [16]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1671-2398, AND VARIANT VAL-2313.
RX PubMed=3676265; DOI=10.1021/bi00391a040;
RA Hardman D.A., Protter A.A., Chen G.C., Schilling J.W., Sato K.Y., Lau K.,
RA Yamanaka M., Mikita T., Miller J., Crisp T., McEnroe G., Scarborough R.M.,
RA Kane J.P.;
RT "Structural comparison of human apolipoproteins B-48 and B-100.";
RL Biochemistry 26:5478-5486(1987).
RN [17]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1937-2018 AND 3811-4334.
RX PubMed=3841204; DOI=10.1093/nar/13.24.8813;
RA Carlsson P., Olofsson S.O., Bondjers G., Darnfors C., Wiklund O.,
RA Bjursell G.;
RT "Molecular cloning of human apolipoprotein B cDNA.";
RL Nucleic Acids Res. 13:8813-8826(1985).
RN [18]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2115-2179.
RC TISSUE=Small intestine;
RX PubMed=3621347; DOI=10.1016/0092-8674(87)90510-1;
RA Powell L.M., Wallis S.C., Pease R.J., Edwards Y.H., Knott T.J., Scott J.;
RT "A novel form of tissue-specific RNA processing produces apolipoprotein-B48
RT in intestine.";
RL Cell 50:831-840(1987).
RN [19]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2127-2179.
RX PubMed=2450346; DOI=10.1073/pnas.85.6.1772;
RA Higuchi K., Hospattankar A.V., Law S.W., Meglin N., Cortright J.,
RA Brewer H.B. Jr.;
RT "Human apolipoprotein B (apoB) mRNA: identification of two distinct apoB
RT mRNAs, an mRNA with the apoB-100 sequence and an apoB mRNA containing a
RT premature in-frame translational stop codon, in both liver and intestine.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:1772-1776(1988).
RN [20]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2129-2235.
RX PubMed=3426612; DOI=10.1016/0006-291x(87)90537-7;
RA Hardman D.A., Protter A.A., Schilling J.W., Kane J.P.;
RT "Carboxyl terminal analysis of human B-48 protein confirms the novel
RT mechanism proposed for chain termination.";
RL Biochem. Biophys. Res. Commun. 149:1214-1219(1987).
RN [21]
RP PROTEIN SEQUENCE OF 2169-2179.
RX PubMed=2445342; DOI=10.1016/0006-291x(87)91107-7;
RA Hospattankar A.V., Higuchi K., Law S.W., Meglin N., Brewer H.B. Jr.;
RT "Identification of a novel in-frame translational stop codon in human
RT intestine apoB mRNA.";
RL Biochem. Biophys. Res. Commun. 148:279-285(1987).
RN [22]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3056-3159.
RX PubMed=3903660; DOI=10.1093/nar/13.19.6937;
RA Mehrabian M., Schumaker V.N., Fareed G.C., West R., Johnson D.F.,
RA Kirchgessner T.G., Lin H.-C., Wang X., Ma Y., Mendiaz E., Lusis A.J.;
RT "Human apolipoprotein B: identification of cDNA clones and characterization
RT of mRNA.";
RL Nucleic Acids Res. 13:6937-6953(1985).
RN [23]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3109-4563, AND VARIANTS HIS-3319; LYS-3427;
RP GLU-3432; THR-3732; LEU-3949; PHE-3964; LYS-4181 AND ASN-4338.
RX PubMed=2994225; DOI=10.1126/science.2994225;
RA Knott T.J., Rall S.C. Jr., Innerarity T.L., Jacobson S.F., Urdea M.S.,
RA Levy-Wilson B., Powell L.M., Pease R.J., Eddy R., Nakai H., Byers M.,
RA Priestley L.M., Robertson E., Rall L.B., Betsholtz C., Shows T.B.,
RA Mahley R.W., Scott J.;
RT "Human apolipoprotein B: structure of carboxyl-terminal domains, sites of
RT gene expression, and chromosomal localization.";
RL Science 230:37-43(1985).
RN [24]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3728-4563, AND VARIANT ASN-4338.
RX PubMed=2932736; DOI=10.1073/pnas.82.21.7265;
RA Wei C.F., Chen S.H., Yang C.Y., Marcel Y.L., Milne R.W., Li W.H.,
RA Sparrow J.T., Gotto A.M. Jr., Chan L.;
RT "Molecular cloning and expression of partial cDNAs and deduced amino acid
RT sequence of a carboxyl-terminal fragment of human apolipoprotein B-100.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:7265-7269(1985).
RN [25]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3846-4298, AND VARIANTS LEU-3949; PHE-3964
RP AND LYS-4181.
RC TISSUE=Liver;
RX PubMed=3841481; DOI=10.1016/0021-9150(85)90073-5;
RA Shoulders C.C., Myant N.B., Sidoli A., Rodriguez J.C., Cortese C.,
RA Baralle F.E., Cortese R.;
RT "Molecular cloning of human LDL apolipoprotein B cDNA. Evidence for more
RT than one gene per haploid genome.";
RL Atherosclerosis 58:277-289(1985).
RN [26]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4217-4563.
RX PubMed=3024665; DOI=10.1515/bchm3.1986.367.2.1077;
RA Pfitzner R., Wagener R., Stoffel W.;
RT "Isolation, expression and characterization of a human apolipoprotein B
RT 100-specific cDNA clone.";
RL Biol. Chem. Hoppe-Seyler 367:1077-1083(1986).
RN [27]
RP PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION OF APO-B48.
RX PubMed=3659919; DOI=10.1126/science.3659919;
RA Chen S.-H., Habib G., Yang C.-H., Gu Z.-W., Lee B.R., Weng S.-H.,
RA Silberman S.R., Cai S.-J., Deslypere J.P., Rosseneu M., Gotto A.M. Jr.,
RA Li W.-H., Chan L.;
RT "Apolipoprotein B-48 is the product of a messenger RNA with an organ-
RT specific in-frame stop codon.";
RL Science 238:363-366(1987).
RN [28]
RP DOMAINS.
RX PubMed=3773997; DOI=10.1038/323734a0;
RA Knott T.C., Pease R.J., Powell L.M., Wallis S.C., Rall S.C. Jr.,
RA Innerarity T.L., Blackhart B., Taylor W.R., Marcel Y., Milne R.,
RA Johnson D., Fuller M., Lusis A.J., McCarthy B.J., Mahley R.W.,
RA Levy-Wilson B., Scott J.;
RT "Complete protein sequence and identification of structural domains of
RT human apolipoprotein B.";
RL Nature 323:734-738(1986).
RN [29]
RP DOMAINS.
RX PubMed=3095664; DOI=10.1038/323738a0;
RA Yang C.-Y., Chen S.-H., Gianturco S.H., Bradley W.A., Sparrow J.T.,
RA Tanimura M., Li W.-H., Sparrow D.A., Deloof H., Rosseneu M., Lee F.-S.,
RA Gu Z.-W., Gotto A.M. Jr., Chan L.;
RT "Sequence, structure, receptor-binding domains and internal repeats of
RT human apolipoprotein B-100.";
RL Nature 323:738-742(1986).
RN [30]
RP CALCIUM-BINDING.
RX PubMed=3087360; DOI=10.1016/0006-291x(86)91237-4;
RA Dashti N., Lee D.M., Mok T.;
RT "Apolipoprotein B is a calcium binding protein.";
RL Biochem. Biophys. Res. Commun. 137:493-499(1986).
RN [31]
RP PALMITOYLATION AT CYS-1112.
RX PubMed=10679026; DOI=10.1091/mbc.11.2.721;
RA Zhao Y., McCabe J.B., Vance J., Berthiaume L.G.;
RT "Palmitoylation of apolipoprotein B is required for proper intracellular
RT sorting and transport of cholesteroyl esters and triglycerides.";
RL Mol. Biol. Cell 11:721-734(2000).
RN [32]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-3358.
RC TISSUE=Plasma;
RX PubMed=14760718; DOI=10.1002/pmic.200300556;
RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
RT "Screening for N-glycosylated proteins by liquid chromatography mass
RT spectrometry.";
RL Proteomics 4:454-465(2004).
RN [33]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1523; ASN-2982; ASN-3465 AND
RP ASN-3895.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [34]
RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
RA Leong W.F., Chow V.T.;
RT "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal
RT differential cellular gene expression in response to enterovirus 71
RT infection.";
RL Cell. Microbiol. 8:565-580(2006).
RN [35]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185; ASN-1523; ASN-2239;
RP ASN-2779; ASN-2982; ASN-3101; ASN-3224; ASN-3411; ASN-3465 AND ASN-3895.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [36]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2004, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [37]
RP INVOLVEMENT IN LDLCQ4, AND VARIANT ILE-98.
RX PubMed=20686565; DOI=10.1038/nature09270;
RA Teslovich T.M., Musunuru K., Smith A.V., Edmondson A.C., Stylianou I.M.,
RA Koseki M., Pirruccello J.P., Ripatti S., Chasman D.I., Willer C.J.,
RA Johansen C.T., Fouchier S.W., Isaacs A., Peloso G.M., Barbalic M.,
RA Ricketts S.L., Bis J.C., Aulchenko Y.S., Thorleifsson G., Feitosa M.F.,
RA Chambers J., Orho-Melander M., Melander O., Johnson T., Li X., Guo X.,
RA Li M., Shin Cho Y., Jin Go M., Jin Kim Y., Lee J.Y., Park T., Kim K.,
RA Sim X., Twee-Hee Ong R., Croteau-Chonka D.C., Lange L.A., Smith J.D.,
RA Song K., Hua Zhao J., Yuan X., Luan J., Lamina C., Ziegler A., Zhang W.,
RA Zee R.Y., Wright A.F., Witteman J.C., Wilson J.F., Willemsen G.,
RA Wichmann H.E., Whitfield J.B., Waterworth D.M., Wareham N.J., Waeber G.,
RA Vollenweider P., Voight B.F., Vitart V., Uitterlinden A.G., Uda M.,
RA Tuomilehto J., Thompson J.R., Tanaka T., Surakka I., Stringham H.M.,
RA Spector T.D., Soranzo N., Smit J.H., Sinisalo J., Silander K.,
RA Sijbrands E.J., Scuteri A., Scott J., Schlessinger D., Sanna S.,
RA Salomaa V., Saharinen J., Sabatti C., Ruokonen A., Rudan I., Rose L.M.,
RA Roberts R., Rieder M., Psaty B.M., Pramstaller P.P., Pichler I., Perola M.,
RA Penninx B.W., Pedersen N.L., Pattaro C., Parker A.N., Pare G., Oostra B.A.,
RA O'Donnell C.J., Nieminen M.S., Nickerson D.A., Montgomery G.W.,
RA Meitinger T., McPherson R., McCarthy M.I., McArdle W., Masson D.,
RA Martin N.G., Marroni F., Mangino M., Magnusson P.K., Lucas G., Luben R.,
RA Loos R.J., Lokki M.L., Lettre G., Langenberg C., Launer L.J., Lakatta E.G.,
RA Laaksonen R., Kyvik K.O., Kronenberg F., Konig I.R., Khaw K.T., Kaprio J.,
RA Kaplan L.M., Johansson A., Jarvelin M.R., Janssens A.C., Ingelsson E.,
RA Igl W., Kees Hovingh G., Hottenga J.J., Hofman A., Hicks A.A.,
RA Hengstenberg C., Heid I.M., Hayward C., Havulinna A.S., Hastie N.D.,
RA Harris T.B., Haritunians T., Hall A.S., Gyllensten U., Guiducci C.,
RA Groop L.C., Gonzalez E., Gieger C., Freimer N.B., Ferrucci L., Erdmann J.,
RA Elliott P., Ejebe K.G., Doring A., Dominiczak A.F., Demissie S.,
RA Deloukas P., de Geus E.J., de Faire U., Crawford G., Collins F.S.,
RA Chen Y.D., Caulfield M.J., Campbell H., Burtt N.P., Bonnycastle L.L.,
RA Boomsma D.I., Boekholdt S.M., Bergman R.N., Barroso I., Bandinelli S.,
RA Ballantyne C.M., Assimes T.L., Quertermous T., Altshuler D., Seielstad M.,
RA Wong T.Y., Tai E.S., Feranil A.B., Kuzawa C.W., Adair L.S.,
RA Taylor H.A. Jr., Borecki I.B., Gabriel S.B., Wilson J.G., Holm H.,
RA Thorsteinsdottir U., Gudnason V., Krauss R.M., Mohlke K.L., Ordovas J.M.,
RA Munroe P.B., Kooner J.S., Tall A.R., Hegele R.A., Kastelein J.J.,
RA Schadt E.E., Rotter J.I., Boerwinkle E., Strachan D.P., Mooser V.,
RA Stefansson K., Reilly M.P., Samani N.J., Schunkert H., Cupples L.A.,
RA Sandhu M.S., Ridker P.M., Rader D.J., van Duijn C.M., Peltonen L.,
RA Abecasis G.R., Boehnke M., Kathiresan S.;
RT "Biological, clinical and population relevance of 95 loci for blood
RT lipids.";
RL Nature 466:707-713(2010).
RN [38]
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 [39]
RP INVOLVEMENT IN FHBL1.
RX PubMed=21981844; DOI=10.1016/j.jacl.2011.06.014;
RA Gangloff A., Bergeron J., Couture P., Martins R., Hegele R.A., Gagne C.;
RT "A novel mutation of apolipoprotein B in a French Canadian family with
RT homozygous hypobetalipoproteinemia.";
RL J. Clin. Lipidol. 5:414-417(2011).
RN [40]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PCSK9.
RX PubMed=22580899; DOI=10.1161/atvbaha.112.250043;
RA Sun H., Samarghandi A., Zhang N., Yao Z., Xiong M., Teng B.B.;
RT "Proprotein convertase subtilisin/kexin type 9 interacts with
RT apolipoprotein B and prevents its intracellular degradation, irrespective
RT of the low-density lipoprotein receptor.";
RL Arterioscler. Thromb. Vasc. Biol. 32:1585-1595(2012).
RN [41]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3279; SER-4048 AND THR-4052,
RP AND 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 [42]
RP PHOSPHORYLATION AT SER-4048.
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 INTERACTION WITH MTTP, AND SUBCELLULAR LOCATION.
RX PubMed=26224785; DOI=10.1161/circgenetics.115.001106;
RA Walsh M.T., Iqbal J., Josekutty J., Soh J., Di Leo E., Oezaydin E.,
RA Guenduez M., Tarugi P., Hussain M.M.;
RT "A novel abetalipoproteinemia missense mutation highlights the importance
RT of N-Terminal beta-barrel in microsomal triglyceride transfer protein
RT function.";
RL Circ. Cardiovasc. Genet. 8:677-687(2015).
RN [44]
RP INTERACTION WITH AUP1, AND SUBCELLULAR LOCATION.
RX PubMed=28183703; DOI=10.1161/atvbaha.117.309000;
RA Zhang J., Zamani M., Thiele C., Taher J., Amir Alipour M., Yao Z.,
RA Adeli K.;
RT "AUP1 (Ancient Ubiquitous Protein 1) Is a Key Determinant of Hepatic Very-
RT Low-Density Lipoprotein Assembly and Secretion.";
RL Arterioscler. Thromb. Vasc. Biol. 37:633-642(2017).
RN [45]
RP VARIANT ASN-4338.
RX PubMed=1979313; DOI=10.1007/bf00205183;
RA Navajas M., Laurent A.-M., Moreel J.-F., Ragab A., Cambou J.-P., Cunny G.,
RA Cambien F., Roizes G.;
RT "Detection by denaturing gradient gel electrophoresis of a new polymorphism
RT in the apolipoprotein B gene.";
RL Hum. Genet. 86:91-93(1990).
RN [46]
RP VARIANT FHCL2 GLN-3527.
RX PubMed=2563166; DOI=10.1073/pnas.86.2.587;
RA Soria L.F., Ludwig E.H., Clarke H.R.G., Vega G.L., Grundy S.M.,
RA McCarthy B.J.;
RT "Association between a specific apolipoprotein B mutation and familial
RT defective apolipoprotein B-100.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:587-591(1989).
RN [47]
RP VARIANT LEU-2739.
RX PubMed=2216805; DOI=10.1093/nar/18.19.5922-a;
RA Huang L.-S., Gavish D., Breslow J.L.;
RT "Sequence polymorphism in the human apoB gene at position 8344.";
RL Nucleic Acids Res. 18:5922-5922(1990).
RN [48]
RP VARIANT FHCL2 CYS-3558.
RX PubMed=7883971; DOI=10.1172/jci117772;
RA Pullinger C.R., Hennessy L.K., Chatterton J.E., Liu W., Love J.A.,
RA Mendel C.M., Frost P.H., Malloy M.J., Schumaker V.N., Kane J.P.;
RT "Familial ligand-defective apolipoprotein B. Identification of a new
RT mutation that decreases LDL receptor binding affinity.";
RL J. Clin. Invest. 95:1225-1234(1995).
RN [49]
RP VARIANTS LEU-1437; SER-1914; LYS-2566; THR-3121; ALA-3945; MET-4128 AND
RP THR-4481.
RX PubMed=8889592;
RX DOI=10.1002/(sici)1098-1004(1996)8:3<282::aid-humu16>3.0.co;2-z;
RA Poirier O., Ricard S., Behague I., Souriau C., Evans A.E., Arveiler D.,
RA Marques-Vidal P., Luc G., Roizes G., Cambien F.;
RT "Detection of new variants in the apolipoprotein B (Apo B) gene by PCR-
RT SSCP.";
RL Hum. Mutat. 8:282-285(1996).
RN [50]
RP VARIANTS FHCL2 GLN-3527 AND CYS-3558.
RX PubMed=9259199;
RX DOI=10.1002/(sici)1098-1004(1997)10:2<160::aid-humu8>3.0.co;2-o;
RA Rabes J.P., Varret M., Saint-Jore B., Erlich D., Jondeau G., Krempf M.,
RA Giraudet P., Junien C., Boileau C.;
RT "Familial ligand-defective apolipoprotein B-100: simultaneous detection of
RT the Arg3500-->Gln and Arg3531-->Cys mutations in a French population.";
RL Hum. Mutat. 10:160-163(1997).
RN [51]
RP VARIANTS SER-1914; ARG-1923; LEU-2739; HIS-3319; LYS-3427; GLU-3432 AND
RP ILE-3921.
RX PubMed=9490296; DOI=10.1007/s004390050651;
RA Leren T.P., Bakken K.S., Hoel V., Hjermann I., Berg K.;
RT "Screening for mutations of the apolipoprotein B gene causing
RT hypocholesterolemia.";
RL Hum. Genet. 102:44-49(1998).
RN [52]
RP VARIANT FHBL1 TRP-490, VARIANT ILE-98, CHARACTERIZATION OF VARIANT TRP-490,
RP AND MUTAGENESIS OF ASP-483 AND ARG-490.
RX PubMed=12551903; DOI=10.1074/jbc.m300235200;
RA Burnett J.R., Shan J., Miskie B.A., Whitfield A.J., Yuan J., Tran K.,
RA McKnight C.J., Hegele R.A., Yao Z.;
RT "A novel nontruncating APOB gene mutation, R463W, causes familial
RT hypobetalipoproteinemia.";
RL J. Biol. Chem. 278:13442-13452(2003).
RN [53]
RP VARIANT HIS-1128.
RX PubMed=14732481; DOI=10.1016/j.bbadis.2003.11.002;
RA Lancellotti S., Di Leo E., Penacchioni J.Y., Balli F., Viola L.,
RA Bertolini S., Calandra S., Tarugi P.;
RT "Hypobetalipoproteinemia with an apparently recessive inheritance due to a
RT 'de novo' mutation of apolipoprotein B.";
RL Biochim. Biophys. Acta 1688:61-67(2004).
RN [54]
RP VARIANT [LARGE SCALE ANALYSIS] CYS-2564.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [55]
RP VARIANT FHCL2 GLN-3527.
RX PubMed=21382890; DOI=10.1161/circulationaha.110.979450;
RA van der Graaf A., Avis H.J., Kusters D.M., Vissers M.N., Hutten B.A.,
RA Defesche J.C., Huijgen R., Fouchier S.W., Wijburg F.A., Kastelein J.J.,
RA Wiegman A.;
RT "Molecular basis of autosomal dominant hypercholesterolemia: assessment in
RT a large cohort of hypercholesterolemic children.";
RL Circulation 123:1167-1173(2011).
RN [56]
RP VARIANTS GLU-1218; ASP-1670; ASN-2037; CYS-2564 AND LYS-2566, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=22028381; DOI=10.1093/jmcb/mjr024;
RA Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H., Lin X.,
RA Zeng R., Wu J.R.;
RT "Quantitative detection of single amino acid polymorphisms by targeted
RT proteomics.";
RL J. Mol. Cell Biol. 3:309-315(2011).
RN [57]
RP VARIANTS 12-LEU--LEU-14 DEL; ILE-98; VAL-618; ILE-730; THR-1613; ARG-1923;
RP LYS-2566; LEU-2739; GLN-3638; LEU-3835; LYS-4181; THR-4270; VAL-4314;
RP ASN-4338; THR-4481 AND VAL-4482.
RX PubMed=22095935; DOI=10.1002/humu.21660;
RA Huijgen R., Sjouke B., Vis K., de Randamie J.S., Defesche J.C.,
RA Kastelein J.J., Hovingh G.K., Fouchier S.W.;
RT "Genetic variation in APOB, PCSK9, and ANGPTL3 in carriers of pathogenic
RT autosomal dominant hypercholesterolemic mutations with unexpected low LDL-
RT Cl Levels.";
RL Hum. Mutat. 33:448-455(2012).
RN [58]
RP VARIANT FHBL1 LEU-952, VARIANT THR-251, CHARACTERIZATION OF VARIANT FHBL1
RP LEU-952, CHARACTERIZATION OF VARIANT THR-251, AND INTERACTION WITH MTTP.
RX PubMed=27206948; DOI=10.1016/j.jacl.2016.01.006;
RA Miller S.A., Hooper A.J., Mantiri G.A., Marais D., Tanyanyiwa D.M.,
RA McKnight J., Burnett J.R.;
RT "Novel APOB missense variants, A224T and V925L, in a black South African
RT woman with marked hypocholesterolemia.";
RL J. Clin. Lipidol. 10:604-609(2016).
CC -!- FUNCTION: Apolipoprotein B is a major protein constituent of
CC chylomicrons (apo B-48), LDL (apo B-100) and VLDL (apo B-100). Apo B-
CC 100 functions as a recognition signal for the cellular binding and
CC internalization of LDL particles by the apoB/E receptor.
CC -!- SUBUNIT: Interacts with PCSK9 (PubMed:22580899). Interacts with MTTP
CC (PubMed:26224785, PubMed:27206948). Interacts with AUP1
CC (PubMed:28183703). {ECO:0000269|PubMed:22580899,
CC ECO:0000269|PubMed:26224785, ECO:0000269|PubMed:27206948,
CC ECO:0000269|PubMed:28183703}.
CC -!- INTERACTION:
CC P04114; P01130: LDLR; NbExp=4; IntAct=EBI-3926040, EBI-988319;
CC P04114; P55157: MTTP; NbExp=4; IntAct=EBI-3926040, EBI-11614052;
CC P04114; PRO_0000037946 [P29991]; Xeno; NbExp=3; IntAct=EBI-3926040, EBI-8826488;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22580899}. Secreted
CC {ECO:0000269|PubMed:22580899, ECO:0000269|PubMed:26224785}. Lipid
CC droplet {ECO:0000269|PubMed:28183703}.
CC -!- INDUCTION: Up-regulated in response to enterovirus 71 (EV71) infection
CC (at protein level). {ECO:0000269|PubMed:16548883}.
CC -!- PTM: Palmitoylated; structural requirement for proper assembly of the
CC hydrophobic core of the lipoprotein particle.
CC {ECO:0000269|PubMed:10679026}.
CC -!- RNA EDITING: Modified_positions=2180; Note=The stop codon (UAA) at
CC position 2180 is created by RNA editing. Apo B-48, derived from the
CC fully edited RNA, is produced only in the intestine and is found in
CC chylomicrons. Apo B-48 is a shortened form of apo B-100 which lacks the
CC LDL-receptor region. The unedited version (apo B-100) is produced by
CC the liver and is found in the VLDL and LDL.;
CC -!- POLYMORPHISM: Genetic variations in APOB define the low density
CC lipoprotein cholesterol level quantitative trait locus 4 (LDLCQ4)
CC [MIM:615558].
CC -!- DISEASE: Hypobetalipoproteinemia, familial, 1 (FHBL1) [MIM:615558]: A
CC disorder of lipid metabolism characterized by less than 5th percentile
CC age- and sex-specific levels of low density lipoproteins, and dietary
CC fat malabsorption. Clinical presentation may vary from no symptoms to
CC severe gastrointestinal and neurological dysfunction similar to
CC abetalipoproteinemia. {ECO:0000269|PubMed:12551903,
CC ECO:0000269|PubMed:21981844, ECO:0000269|PubMed:27206948}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry. Most cases of FHBL1 result from nonsense mutations in the APOB
CC gene that lead to a premature stop codon, which generate prematurely
CC truncated apo B protein products (PubMed:21981844).
CC {ECO:0000269|PubMed:21981844}.
CC -!- DISEASE: Hypercholesterolemia, familial, 2 (FHCL2) [MIM:144010]: A form
CC of hypercholesterolemia, a disorder of lipoprotein metabolism
CC characterized by elevated serum low-density lipoprotein (LDL)
CC cholesterol levels, which result in excess deposition of cholesterol in
CC tissues and leads to xanthelasma, xanthomas, accelerated
CC atherosclerosis and increased risk of premature coronary heart disease.
CC FHCL2 inheritance is autosomal dominant. {ECO:0000269|PubMed:21382890,
CC ECO:0000269|PubMed:2563166, ECO:0000269|PubMed:7883971,
CC ECO:0000269|PubMed:9259199}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Note=Defects in APOB associated with defects in other genes
CC (polygenic) can contribute to hypocholesterolemia.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA51752.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Apolipoprotein B entry;
CC URL="https://en.wikipedia.org/wiki/Apolipoprotein_B";
CC ---------------------------------------------------------------------------
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DR EMBL; X04506; CAA28191.1; -; mRNA.
DR EMBL; M19828; AAB00481.1; -; Genomic_DNA.
DR EMBL; M19808; AAB00481.1; JOINED; Genomic_DNA.
DR EMBL; M19809; AAB00481.1; JOINED; Genomic_DNA.
DR EMBL; M19810; AAB00481.1; JOINED; Genomic_DNA.
DR EMBL; M19811; AAB00481.1; JOINED; Genomic_DNA.
DR EMBL; M19812; AAB00481.1; JOINED; Genomic_DNA.
DR EMBL; M19813; AAB00481.1; JOINED; Genomic_DNA.
DR EMBL; M19815; AAB00481.1; JOINED; Genomic_DNA.
DR EMBL; M19816; AAB00481.1; JOINED; Genomic_DNA.
DR EMBL; M19818; AAB00481.1; JOINED; Genomic_DNA.
DR EMBL; M19820; AAB00481.1; JOINED; Genomic_DNA.
DR EMBL; M19821; AAB00481.1; JOINED; Genomic_DNA.
DR EMBL; M19823; AAB00481.1; JOINED; Genomic_DNA.
DR EMBL; M19824; AAB00481.1; JOINED; Genomic_DNA.
DR EMBL; M19825; AAB00481.1; JOINED; Genomic_DNA.
DR EMBL; M19827; AAB00481.1; JOINED; Genomic_DNA.
DR EMBL; J02610; AAA35549.1; -; mRNA.
DR EMBL; M14162; AAB04636.1; -; mRNA.
DR EMBL; M15053; AAB60718.1; -; Genomic_DNA.
DR EMBL; X04714; CAA28420.1; -; mRNA.
DR EMBL; AY324608; AAP72970.1; -; Genomic_DNA.
DR EMBL; AC010872; AAX88848.1; -; Genomic_DNA.
DR EMBL; AC115619; AAX93246.1; -; Genomic_DNA.
DR EMBL; M14081; AAA51752.1; ALT_FRAME; mRNA.
DR EMBL; M12681; AAA51753.1; -; mRNA.
DR EMBL; M12480; AAA51751.1; -; mRNA.
DR EMBL; K03175; AAA51759.1; -; mRNA.
DR EMBL; M15421; AAA51758.1; -; mRNA.
DR EMBL; M17367; AAA51741.1; -; mRNA.
DR EMBL; M31030; AAA51756.1; -; mRNA.
DR EMBL; X03325; CAA27044.1; -; mRNA.
DR EMBL; X03326; CAA27045.1; -; mRNA.
DR EMBL; M17779; AAA51755.1; -; mRNA.
DR EMBL; M19734; AAA35544.1; -; mRNA.
DR EMBL; M18471; AAA35541.1; -; mRNA.
DR EMBL; X03045; CAA26850.1; -; mRNA.
DR EMBL; M10374; AAA51750.1; -; mRNA.
DR EMBL; M12413; AAA51742.1; -; mRNA.
DR EMBL; M36676; AAA35548.1; -; mRNA.
DR CCDS; CCDS1703.1; -.
DR PIR; A27850; LPHUB.
DR RefSeq; NP_000375.2; NM_000384.2.
DR SMR; P04114; -.
DR BioGRID; 106835; 208.
DR DIP; DIP-44767N; -.
DR IntAct; P04114; 65.
DR MINT; P04114; -.
DR STRING; 9606.ENSP00000233242; -.
DR BindingDB; P04114; -.
DR ChEMBL; CHEMBL4549; -.
DR DrugBank; DB11886; Infigratinib.
DR DrugBank; DB00877; Sirolimus.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR CarbonylDB; P04114; -.
DR GlyConnect; 57; 67 N-Linked glycans (13 sites).
DR GlyGen; P04114; 28 sites, 82 N-linked glycans (16 sites), 1 O-linked glycan (7 sites).
DR iPTMnet; P04114; -.
DR PhosphoSitePlus; P04114; -.
DR SwissPalm; P04114; -.
DR BioMuta; APOB; -.
DR DMDM; 300669605; -.
DR CPTAC; CPTAC-1299; -.
DR CPTAC; CPTAC-1300; -.
DR CPTAC; CPTAC-2205; -.
DR CPTAC; CPTAC-652; -.
DR CPTAC; CPTAC-653; -.
DR CPTAC; non-CPTAC-1080; -.
DR CPTAC; non-CPTAC-1081; -.
DR CPTAC; non-CPTAC-1082; -.
DR EPD; P04114; -.
DR jPOST; P04114; -.
DR MassIVE; P04114; -.
DR MaxQB; P04114; -.
DR PaxDb; P04114; -.
DR PeptideAtlas; P04114; -.
DR PRIDE; P04114; -.
DR ProteomicsDB; 51654; -.
DR ABCD; P04114; 1 sequenced antibody.
DR Antibodypedia; 4232; 1071 antibodies from 41 providers.
DR CPTC; P04114; 3 antibodies.
DR DNASU; 338; -.
DR Ensembl; ENST00000233242.5; ENSP00000233242.1; ENSG00000084674.15.
DR GeneID; 338; -.
DR KEGG; hsa:338; -.
DR UCSC; uc002red.3; human.
DR CTD; 338; -.
DR DisGeNET; 338; -.
DR GeneCards; APOB; -.
DR GeneReviews; APOB; -.
DR HGNC; HGNC:603; APOB.
DR HPA; ENSG00000084674; Group enriched (intestine, liver).
DR MalaCards; APOB; -.
DR MIM; 107730; gene.
DR MIM; 144010; phenotype.
DR MIM; 615558; phenotype.
DR neXtProt; NX_P04114; -.
DR Orphanet; 391665; Homozygous familial hypercholesterolemia.
DR Orphanet; 426; NON RARE IN EUROPE: Familial hypobetalipoproteinemia.
DR Orphanet; 406; NON RARE IN EUROPE: Heterozygous familial hypercholesterolemia.
DR PharmGKB; PA50; -.
DR VEuPathDB; HostDB:ENSG00000084674; -.
DR eggNOG; KOG4338; Eukaryota.
DR InParanoid; P04114; -.
DR OrthoDB; 5350at2759; -.
DR PhylomeDB; P04114; -.
DR TreeFam; TF331316; -.
DR PathwayCommons; P04114; -.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-3000471; Scavenging by Class B Receptors.
DR Reactome; R-HSA-3000480; Scavenging by Class A Receptors.
DR Reactome; R-HSA-3000484; Scavenging by Class F Receptors.
DR Reactome; R-HSA-3000497; Scavenging by Class H Receptors.
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-432142; Platelet sensitization by LDL.
DR Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-8866423; VLDL assembly.
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR Reactome; R-HSA-8963888; Chylomicron assembly.
DR Reactome; R-HSA-8963901; Chylomicron remodeling.
DR Reactome; R-HSA-8964026; Chylomicron clearance.
DR Reactome; R-HSA-8964038; LDL clearance.
DR Reactome; R-HSA-8964041; LDL remodeling.
DR Reactome; R-HSA-8964046; VLDL clearance.
DR Reactome; R-HSA-9707616; Heme signaling.
DR Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR SignaLink; P04114; -.
DR SIGNOR; P04114; -.
DR BioGRID-ORCS; 338; 12 hits in 1071 CRISPR screens.
DR ChiTaRS; APOB; human.
DR GeneWiki; Apolipoprotein_B; -.
DR GenomeRNAi; 338; -.
DR Pharos; P04114; Tchem.
DR PRO; PR:P04114; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P04114; protein.
DR Bgee; ENSG00000084674; Expressed in jejunal mucosa and 86 other tissues.
DR ExpressionAtlas; P04114; baseline and differential.
DR Genevisible; P04114; HS.
DR GO; GO:0042627; C:chylomicron; IDA:BHF-UCL.
DR GO; GO:0034360; C:chylomicron remnant; TAS:BHF-UCL.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005769; C:early endosome; TAS:Reactome.
DR GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0031904; C:endosome lumen; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; ISS:BHF-UCL.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0034363; C:intermediate-density lipoprotein particle; IDA:BHF-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0034362; C:low-density lipoprotein particle; IDA:BHF-UCL.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0034359; C:mature chylomicron; IDA:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; TAS:Reactome.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:BHF-UCL.
DR GO; GO:0031983; C:vesicle lumen; IEA:Ensembl.
DR GO; GO:0120020; F:cholesterol transfer activity; IMP:BHF-UCL.
DR GO; GO:0008201; F:heparin binding; IDA:BHF-UCL.
DR GO; GO:0035473; F:lipase binding; IPI:BHF-UCL.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IMP:BHF-UCL.
DR GO; GO:0005543; F:phospholipid binding; IDA:BHF-UCL.
DR GO; GO:0048844; P:artery morphogenesis; IEA:Ensembl.
DR GO; GO:0071379; P:cellular response to prostaglandin stimulus; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0033344; P:cholesterol efflux; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
DR GO; GO:0008203; P:cholesterol metabolic process; IMP:BHF-UCL.
DR GO; GO:0030301; P:cholesterol transport; IMP:BHF-UCL.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0009566; P:fertilization; IEA:Ensembl.
DR GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:Ensembl.
DR GO; GO:0042159; P:lipoprotein catabolic process; IEA:Ensembl.
DR GO; GO:0042953; P:lipoprotein transport; IBA:GO_Central.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; IMP:BHF-UCL.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; IMP:BHF-UCL.
DR GO; GO:0007399; P:nervous system development; IEA:Ensembl.
DR GO; GO:0010886; P:positive regulation of cholesterol storage; IDA:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0010884; P:positive regulation of lipid storage; IDA:BHF-UCL.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IDA:BHF-UCL.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0045540; P:regulation of cholesterol biosynthetic process; IEA:Ensembl.
DR GO; GO:0009743; P:response to carbohydrate; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0010269; P:response to selenium ion; IEA:Ensembl.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0019433; P:triglyceride catabolic process; IEA:Ensembl.
DR GO; GO:0006642; P:triglyceride mobilization; IBA:GO_Central.
DR GO; GO:0034379; P:very-low-density lipoprotein particle assembly; IC:BHF-UCL.
DR Gene3D; 1.25.10.20; -; 1.
DR Gene3D; 2.20.50.20; -; 1.
DR Gene3D; 2.30.230.10; -; 1.
DR InterPro; IPR022176; ApoB100_C.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015819; Lipid_transp_b-sht_shell.
DR InterPro; IPR009454; Lipid_transpt_open_b-sht.
DR InterPro; IPR011030; Lipovitellin_superhlx_dom.
DR InterPro; IPR015816; Vitellinogen_b-sht_N.
DR InterPro; IPR015255; Vitellinogen_open_b-sht.
DR InterPro; IPR015817; Vitellinogen_open_b-sht_sub1.
DR InterPro; IPR001747; Vitellogenin_N.
DR Pfam; PF12491; ApoB100_C; 1.
DR Pfam; PF06448; DUF1081; 1.
DR Pfam; PF09172; DUF1943; 1.
DR Pfam; PF01347; Vitellogenin_N; 1.
DR SMART; SM01169; DUF1943; 1.
DR SMART; SM00638; LPD_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF48431; SSF48431; 1.
DR SUPFAM; SSF56968; SSF56968; 2.
DR PROSITE; PS51211; VITELLOGENIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Atherosclerosis; Cholesterol metabolism; Chylomicron;
KW Cytoplasm; Direct protein sequencing; Disease variant; Disulfide bond;
KW Glycoprotein; Heparin-binding; LDL; Lipid droplet; Lipid metabolism;
KW Lipid transport; Lipoprotein; Palmitate; Phosphoprotein;
KW Reference proteome; RNA editing; Secreted; Signal; Steroid metabolism;
KW Sterol metabolism; Transport; VLDL.
FT SIGNAL 1..27
FT CHAIN 28..4563
FT /note="Apolipoprotein B-100"
FT /id="PRO_0000020750"
FT CHAIN 28..2179
FT /note="Apolipoprotein B-48"
FT /id="PRO_0000020751"
FT DOMAIN 46..672
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT REGION 32..126
FT /note="Heparin-binding"
FT REGION 232..306
FT /note="Heparin-binding"
FT REGION 902..959
FT /note="Heparin-binding"
FT REGION 2043..2178
FT /note="Heparin-binding"
FT REGION 3161..3236
FT /note="Heparin-binding"
FT REGION 3174..3184
FT /note="Basic (possible receptor binding region)"
FT REGION 3373..3393
FT /note="LDL receptor binding"
FT REGION 3383..3516
FT /note="Heparin-binding"
FT REGION 3386..3394
FT /note="Basic (possible receptor binding region)"
FT MOD_RES 2004
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 3279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 4048
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 4052
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT LIPID 1112
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:10679026"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 983
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 2239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 2560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2779
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 2982
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 3101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 3224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 3336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:14760718"
FT CARBOHYD 3411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 3465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 3895
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 4237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 39..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557,
FT ECO:0000269|PubMed:2115173"
FT DISULFID 78..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557,
FT ECO:0000269|PubMed:2115173"
FT DISULFID 186..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557,
FT ECO:0000269|PubMed:2115173"
FT DISULFID 245..261
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557,
FT ECO:0000269|PubMed:2115173"
FT DISULFID 385..390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557,
FT ECO:0000269|PubMed:2115173"
FT DISULFID 478..513
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557,
FT ECO:0000269|PubMed:2115173"
FT DISULFID 966..976
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557,
FT ECO:0000269|PubMed:2115173"
FT DISULFID 3194..3324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557,
FT ECO:0000269|PubMed:2115173"
FT VARIANT 12..14
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:22095935"
FT /id="VAR_067277"
FT VARIANT 98
FT /note="T -> I (influences plasma concentrations of low
FT density lipoprotein cholesterol; dbSNP:rs1367117)"
FT /evidence="ECO:0000269|PubMed:12551903,
FT ECO:0000269|PubMed:20686565, ECO:0000269|PubMed:2115173,
FT ECO:0000269|PubMed:22095935, ECO:0000269|PubMed:3461454,
FT ECO:0000269|PubMed:3759943"
FT /id="VAR_016184"
FT VARIANT 103
FT /note="Y -> H (in dbSNP:rs9282603)"
FT /id="VAR_022036"
FT VARIANT 145
FT /note="P -> S (in dbSNP:rs6752026)"
FT /id="VAR_022037"
FT VARIANT 194
FT /note="T -> M (in dbSNP:rs13306198)"
FT /id="VAR_056737"
FT VARIANT 251
FT /note="A -> T (does not affect plasma lipid levels;
FT dbSNP:rs61741625)"
FT /evidence="ECO:0000269|PubMed:27206948"
FT /id="VAR_076538"
FT VARIANT 273
FT /note="K -> N"
FT /evidence="ECO:0000269|PubMed:3763409"
FT /id="VAR_019827"
FT VARIANT 408
FT /note="I -> T (in dbSNP:rs12714225)"
FT /id="VAR_029341"
FT VARIANT 490
FT /note="R -> W (in FHBL1; reduced protein secretion;
FT dbSNP:rs771541567)"
FT /evidence="ECO:0000269|PubMed:12551903"
FT /id="VAR_022610"
FT VARIANT 554
FT /note="P -> L (in dbSNP:rs12714214)"
FT /id="VAR_020135"
FT VARIANT 618
FT /note="A -> V (in dbSNP:rs679899)"
FT /evidence="ECO:0000269|PubMed:22095935,
FT ECO:0000269|PubMed:3030729, ECO:0000269|PubMed:3759943"
FT /id="VAR_019828"
FT VARIANT 730
FT /note="V -> I (in dbSNP:rs12691202)"
FT /evidence="ECO:0000269|PubMed:22095935"
FT /id="VAR_020136"
FT VARIANT 733
FT /note="V -> I (in dbSNP:rs1800476)"
FT /id="VAR_016185"
FT VARIANT 741
FT /note="T -> N (in dbSNP:rs12714192)"
FT /id="VAR_020137"
FT VARIANT 877
FT /note="P -> L (in dbSNP:rs12714097)"
FT /id="VAR_029342"
FT VARIANT 952
FT /note="V -> L (in FHBL1; unknown pathological significance;
FT does not affect interaction with MTTP)"
FT /evidence="ECO:0000269|PubMed:27206948"
FT /id="VAR_076539"
FT VARIANT 955
FT /note="P -> S (in dbSNP:rs13306206)"
FT /id="VAR_056738"
FT VARIANT 1086
FT /note="G -> S (in dbSNP:rs12720801)"
FT /id="VAR_029343"
FT VARIANT 1113
FT /note="D -> H (in dbSNP:rs12713844)"
FT /id="VAR_029344"
FT VARIANT 1128
FT /note="R -> H (in dbSNP:rs12713843)"
FT /evidence="ECO:0000269|PubMed:14732481"
FT /id="VAR_022611"
FT VARIANT 1218
FT /note="Q -> E (in dbSNP:rs1041956)"
FT /evidence="ECO:0000269|PubMed:22028381,
FT ECO:0000269|PubMed:3763409"
FT /id="VAR_019829"
FT VARIANT 1388
FT /note="R -> H (in dbSNP:rs13306187)"
FT /id="VAR_029345"
FT VARIANT 1422
FT /note="Y -> C (in dbSNP:rs568413)"
FT /evidence="ECO:0000269|PubMed:2883086,
FT ECO:0000269|PubMed:3030729, ECO:0000269|PubMed:3461454,
FT ECO:0000269|PubMed:3464946, ECO:0000269|PubMed:3652907,
FT ECO:0000269|PubMed:3759943, ECO:0000269|PubMed:3763409,
FT ECO:0000269|Ref.6"
FT /id="VAR_061558"
FT VARIANT 1437
FT /note="F -> L (in dbSNP:rs1801697)"
FT /evidence="ECO:0000269|PubMed:8889592"
FT /id="VAR_005016"
FT VARIANT 1613
FT /note="S -> T (in dbSNP:rs61742247)"
FT /evidence="ECO:0000269|PubMed:22095935"
FT /id="VAR_067278"
FT VARIANT 1670
FT /note="E -> D (in dbSNP:rs773681906)"
FT /evidence="ECO:0000269|PubMed:22028381,
FT ECO:0000269|PubMed:3461454"
FT /id="VAR_068911"
FT VARIANT 1914
FT /note="N -> S (in dbSNP:rs1801699)"
FT /evidence="ECO:0000269|PubMed:8889592,
FT ECO:0000269|PubMed:9490296"
FT /id="VAR_005017"
FT VARIANT 1923
FT /note="H -> R (in dbSNP:rs533617)"
FT /evidence="ECO:0000269|PubMed:22095935,
FT ECO:0000269|PubMed:9490296"
FT /id="VAR_005018"
FT VARIANT 2037
FT /note="I -> N"
FT /evidence="ECO:0000269|PubMed:22028381,
FT ECO:0000269|PubMed:3464946"
FT /id="VAR_068912"
FT VARIANT 2092
FT /note="L -> V (in dbSNP:rs1041960)"
FT /evidence="ECO:0000269|PubMed:3763409"
FT /id="VAR_019830"
FT VARIANT 2299
FT /note="D -> H (in dbSNP:rs12713681)"
FT /id="VAR_029346"
FT VARIANT 2313
FT /note="I -> V (in dbSNP:rs584542)"
FT /evidence="ECO:0000269|PubMed:2883086,
FT ECO:0000269|PubMed:3030729, ECO:0000269|PubMed:3464946,
FT ECO:0000269|PubMed:3652907, ECO:0000269|PubMed:3676265,
FT ECO:0000269|PubMed:3759943, ECO:0000269|PubMed:3763409,
FT ECO:0000269|Ref.6"
FT /id="VAR_059582"
FT VARIANT 2365
FT /note="A -> T (in dbSNP:rs1041971)"
FT /evidence="ECO:0000269|PubMed:3763409"
FT /id="VAR_019831"
FT VARIANT 2456
FT /note="A -> D (in dbSNP:rs12713675)"
FT /id="VAR_020138"
FT VARIANT 2564
FT /note="F -> C (in a colorectal cancer sample; somatic
FT mutation; confirmed at protein level)"
FT /evidence="ECO:0000269|PubMed:16959974,
FT ECO:0000269|PubMed:22028381"
FT /id="VAR_035795"
FT VARIANT 2566
FT /note="E -> K (in dbSNP:rs1801696)"
FT /evidence="ECO:0000269|PubMed:22028381,
FT ECO:0000269|PubMed:22095935, ECO:0000269|PubMed:8889592"
FT /id="VAR_005019"
FT VARIANT 2680
FT /note="L -> Q (in dbSNP:rs1042013)"
FT /evidence="ECO:0000269|PubMed:3763409"
FT /id="VAR_019832"
FT VARIANT 2739
FT /note="P -> L (in dbSNP:rs676210)"
FT /evidence="ECO:0000269|PubMed:22095935,
FT ECO:0000269|PubMed:2216805, ECO:0000269|PubMed:9490296"
FT /id="VAR_005020"
FT VARIANT 2785
FT /note="N -> H (in dbSNP:rs2163204)"
FT /id="VAR_022038"
FT VARIANT 3121
FT /note="A -> T (in dbSNP:rs1801694)"
FT /evidence="ECO:0000269|PubMed:8889592"
FT /id="VAR_005021"
FT VARIANT 3182
FT /note="H -> N (in dbSNP:rs12720848)"
FT /id="VAR_029347"
FT VARIANT 3279
FT /note="S -> G (in dbSNP:rs12720854)"
FT /id="VAR_029348"
FT VARIANT 3294
FT /note="S -> P (in dbSNP:rs12720855)"
FT /id="VAR_020139"
FT VARIANT 3319
FT /note="D -> H (in dbSNP:rs1042021)"
FT /evidence="ECO:0000269|PubMed:2883086,
FT ECO:0000269|PubMed:2994225, ECO:0000269|PubMed:3030729,
FT ECO:0000269|PubMed:3464946, ECO:0000269|PubMed:3652907,
FT ECO:0000269|PubMed:3759943, ECO:0000269|PubMed:3763409,
FT ECO:0000269|PubMed:9490296"
FT /id="VAR_005022"
FT VARIANT 3427
FT /note="T -> K (in dbSNP:rs1042022)"
FT /evidence="ECO:0000269|PubMed:2883086,
FT ECO:0000269|PubMed:2994225, ECO:0000269|PubMed:3030729,
FT ECO:0000269|PubMed:3464946, ECO:0000269|PubMed:3652907,
FT ECO:0000269|PubMed:3759943, ECO:0000269|PubMed:3763409,
FT ECO:0000269|PubMed:9490296"
FT /id="VAR_005023"
FT VARIANT 3432
FT /note="Q -> E (in dbSNP:rs1042023)"
FT /evidence="ECO:0000269|PubMed:2883086,
FT ECO:0000269|PubMed:2994225, ECO:0000269|PubMed:3030729,
FT ECO:0000269|PubMed:3464946, ECO:0000269|PubMed:3652907,
FT ECO:0000269|PubMed:3759943, ECO:0000269|PubMed:3763409,
FT ECO:0000269|PubMed:9490296"
FT /id="VAR_005024"
FT VARIANT 3527
FT /note="R -> Q (in FHCL2; dbSNP:rs5742904)"
FT /evidence="ECO:0000269|PubMed:21382890,
FT ECO:0000269|PubMed:2563166, ECO:0000269|PubMed:9259199"
FT /id="VAR_005025"
FT VARIANT 3558
FT /note="R -> C (in FHCL2; dbSNP:rs12713559)"
FT /evidence="ECO:0000269|PubMed:7883971,
FT ECO:0000269|PubMed:9259199"
FT /id="VAR_005026"
FT VARIANT 3638
FT /note="R -> Q (in dbSNP:rs1801701)"
FT /evidence="ECO:0000269|PubMed:22095935"
FT /id="VAR_016186"
FT VARIANT 3732
FT /note="I -> T (in dbSNP:rs1042025)"
FT /evidence="ECO:0000269|PubMed:2883086,
FT ECO:0000269|PubMed:2994225, ECO:0000269|PubMed:3030729,
FT ECO:0000269|PubMed:3763409"
FT /id="VAR_019833"
FT VARIANT 3801
FT /note="S -> T (in dbSNP:rs12713540)"
FT /id="VAR_029349"
FT VARIANT 3835
FT /note="I -> L (in dbSNP:rs776119459)"
FT /evidence="ECO:0000269|PubMed:22095935"
FT /id="VAR_067279"
FT VARIANT 3921
FT /note="V -> I (in dbSNP:rs72654409)"
FT /evidence="ECO:0000269|PubMed:9490296"
FT /id="VAR_005027"
FT VARIANT 3945
FT /note="T -> A (in dbSNP:rs1801698)"
FT /evidence="ECO:0000269|PubMed:8889592"
FT /id="VAR_005028"
FT VARIANT 3949
FT /note="F -> L (in dbSNP:rs1042027)"
FT /evidence="ECO:0000269|PubMed:2994225,
FT ECO:0000269|PubMed:3030729, ECO:0000269|PubMed:3464946,
FT ECO:0000269|PubMed:3763409, ECO:0000269|PubMed:3841481"
FT /id="VAR_019834"
FT VARIANT 3964
FT /note="Y -> F (in dbSNP:rs1126468)"
FT /evidence="ECO:0000269|PubMed:2994225,
FT ECO:0000269|PubMed:3030729, ECO:0000269|PubMed:3763409,
FT ECO:0000269|PubMed:3841481"
FT /id="VAR_019835"
FT VARIANT 4128
FT /note="V -> M (in dbSNP:rs1801703)"
FT /evidence="ECO:0000269|PubMed:8889592"
FT /id="VAR_005029"
FT VARIANT 4181
FT /note="E -> K (in dbSNP:rs1042031)"
FT /evidence="ECO:0000269|PubMed:22095935,
FT ECO:0000269|PubMed:2994225, ECO:0000269|PubMed:3030729,
FT ECO:0000269|PubMed:3464946, ECO:0000269|PubMed:3763409,
FT ECO:0000269|PubMed:3841481"
FT /id="VAR_016187"
FT VARIANT 4270
FT /note="R -> T (in dbSNP:rs1801702)"
FT /evidence="ECO:0000269|PubMed:22095935"
FT /id="VAR_016188"
FT VARIANT 4314
FT /note="I -> V (in dbSNP:rs72654423)"
FT /evidence="ECO:0000269|PubMed:22095935"
FT /id="VAR_067280"
FT VARIANT 4338
FT /note="S -> N (in dbSNP:rs1042034)"
FT /evidence="ECO:0000269|PubMed:1979313,
FT ECO:0000269|PubMed:22095935, ECO:0000269|PubMed:2883086,
FT ECO:0000269|PubMed:2932736, ECO:0000269|PubMed:2994225,
FT ECO:0000269|PubMed:3030729, ECO:0000269|PubMed:3464946,
FT ECO:0000269|PubMed:3652907, ECO:0000269|PubMed:3759943,
FT ECO:0000269|PubMed:3763409, ECO:0000269|Ref.6"
FT /id="VAR_005030"
FT VARIANT 4394
FT /note="V -> A (in dbSNP:rs12720843)"
FT /id="VAR_029350"
FT VARIANT 4481
FT /note="A -> T (in dbSNP:rs1801695)"
FT /evidence="ECO:0000269|PubMed:22095935,
FT ECO:0000269|PubMed:8889592"
FT /id="VAR_005031"
FT VARIANT 4482
FT /note="I -> V (in dbSNP:rs142702699)"
FT /evidence="ECO:0000269|PubMed:22095935"
FT /id="VAR_067281"
FT VARIANT 4484
FT /note="T -> M (in dbSNP:rs12713450)"
FT /id="VAR_020140"
FT MUTAGEN 483
FT /note="D->N: Impairs protein secretion."
FT /evidence="ECO:0000269|PubMed:12551903"
FT MUTAGEN 483
FT /note="D->Q: Does not affect protein secretion."
FT /evidence="ECO:0000269|PubMed:12551903"
FT MUTAGEN 490
FT /note="R->A: Impairs protein secretion."
FT /evidence="ECO:0000269|PubMed:12551903"
FT MUTAGEN 490
FT /note="R->K: Does not affect protein secretion."
FT /evidence="ECO:0000269|PubMed:12551903"
FT CONFLICT 11..13
FT /note="Missing (in Ref. 5; AAB60718/CAA28420)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="L -> V (in Ref. 3; AAA35549)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="L -> I (in Ref. 3; AAA35549)"
FT /evidence="ECO:0000305"
FT CONFLICT 704
FT /note="L -> P (in Ref. 4; AAB04636)"
FT /evidence="ECO:0000305"
FT CONFLICT 792..809
FT /note="LQLLGKLLLMGARTLQGI -> SSSWKAASHGCPHSAGD (in Ref. 12;
FT AAA51759)"
FT /evidence="ECO:0000305"
FT CONFLICT 793
FT /note="Q -> R (in Ref. 4; AAB04636)"
FT /evidence="ECO:0000305"
FT CONFLICT 893
FT /note="D -> K (in Ref. 13; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 919
FT /note="A -> P (in Ref. 3; AAA35549)"
FT /evidence="ECO:0000305"
FT CONFLICT 1109
FT /note="H -> D (in Ref. 5; CAA28420)"
FT /evidence="ECO:0000305"
FT CONFLICT 1180
FT /note="T -> R (in Ref. 8; AAA51752)"
FT /evidence="ECO:0000305"
FT CONFLICT 1271
FT /note="F -> S (in Ref. 4; AAB04636)"
FT /evidence="ECO:0000305"
FT CONFLICT 1418
FT /note="F -> S (in Ref. 5; CAA28420)"
FT /evidence="ECO:0000305"
FT CONFLICT 1445
FT /note="N -> I (in Ref. 8; AAA51752)"
FT /evidence="ECO:0000305"
FT CONFLICT 1535
FT /note="G -> E (in Ref. 8; AAA51752)"
FT /evidence="ECO:0000305"
FT CONFLICT 1867
FT /note="R -> G (in Ref. 4; AAB04636)"
FT /evidence="ECO:0000305"
FT CONFLICT 2098
FT /note="N -> K (in Ref. 5; CAA28420)"
FT /evidence="ECO:0000305"
FT CONFLICT 2218
FT /note="I -> T (in Ref. 4; AAB04636)"
FT /evidence="ECO:0000305"
FT CONFLICT 2221
FT /note="N -> I (in Ref. 5; CAA28420)"
FT /evidence="ECO:0000305"
FT CONFLICT 2324..2326
FT /note="LIG -> PYW (in Ref. 16; AAA51741)"
FT /evidence="ECO:0000305"
FT CONFLICT 2353
FT /note="Q -> H (in Ref. 16; AAA51741)"
FT /evidence="ECO:0000305"
FT CONFLICT 2540
FT /note="G -> S (in Ref. 5; CAA28420)"
FT /evidence="ECO:0000305"
FT CONFLICT 2718..2737
FT /note="Missing (in Ref. 15; AAA51758)"
FT /evidence="ECO:0000305"
FT CONFLICT 2933
FT /note="C -> S (in Ref. 4; AAB04636)"
FT /evidence="ECO:0000305"
FT CONFLICT 3114
FT /note="H -> L (in Ref. 13; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 3131
FT /note="T -> R (in Ref. 13; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 3134
FT /note="E -> P (in Ref. 13; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 3137
FT /note="L -> R (in Ref. 13; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 3239
FT /note="H -> Q (in Ref. 5; CAA28420)"
FT /evidence="ECO:0000305"
FT CONFLICT 3286
FT /note="L -> I (in Ref. 4; AAB04636)"
FT /evidence="ECO:0000305"
FT CONFLICT 3291
FT /note="R -> L (in Ref. 15; AAA51758)"
FT /evidence="ECO:0000305"
FT CONFLICT 3337
FT /note="I -> N (in Ref. 15; AAA51758)"
FT /evidence="ECO:0000305"
FT CONFLICT 3431
FT /note="A -> P (in Ref. 4; AAB04636)"
FT /evidence="ECO:0000305"
FT CONFLICT 3728
FT /note="D -> N (in Ref. 24; AAA51742)"
FT /evidence="ECO:0000305"
FT CONFLICT 3782
FT /note="N -> T (in Ref. 4; AAB04636)"
FT /evidence="ECO:0000305"
FT CONFLICT 3824
FT /note="Q -> R (in Ref. 5; CAA28420 and 23; AAA51750)"
FT /evidence="ECO:0000305"
FT CONFLICT 3876
FT /note="V -> A (in Ref. 3; AAA35549 and 24; AAA51742)"
FT /evidence="ECO:0000305"
FT CONFLICT 3911
FT /note="T -> Y (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 3983
FT /note="F -> S (in Ref. 24; AAA51742)"
FT /evidence="ECO:0000305"
FT CONFLICT 4002
FT /note="A -> P (in Ref. 24; AAA51742)"
FT /evidence="ECO:0000305"
FT CONFLICT 4110..4111
FT /note="NN -> DH (in Ref. 3; AAA35549 and 24; AAA51742)"
FT /evidence="ECO:0000305"
FT CONFLICT 4122
FT /note="Q -> E (in Ref. 3; AAA35549 and 24; AAA51742)"
FT /evidence="ECO:0000305"
FT CONFLICT 4128
FT /note="V -> E (in Ref. 3; AAA35549 and 24; AAA51742)"
FT /evidence="ECO:0000305"
FT CONFLICT 4133
FT /note="A -> G (in Ref. 3; AAA35549 and 24; AAA51742)"
FT /evidence="ECO:0000305"
FT CONFLICT 4188
FT /note="H -> K (in Ref. 4; AAB04636)"
FT /evidence="ECO:0000305"
FT CONFLICT 4217..4218
FT /note="CT -> FP (in Ref. 26; AAA35548)"
FT /evidence="ECO:0000305"
FT CONFLICT 4221
FT /note="I -> M (in Ref. 4; AAB04636)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4563 AA; 515605 MW; 6800F94BF6ADF698 CRC64;
MDPPRPALLA LLALPALLLL LLAGARAEEE MLENVSLVCP KDATRFKHLR KYTYNYEAES
SSGVPGTADS RSATRINCKV ELEVPQLCSF ILKTSQCTLK EVYGFNPEGK ALLKKTKNSE
EFAAAMSRYE LKLAIPEGKQ VFLYPEKDEP TYILNIKRGI ISALLVPPET EEAKQVLFLD
TVYGNCSTHF TVKTRKGNVA TEISTERDLG QCDRFKPIRT GISPLALIKG MTRPLSTLIS
SSQSCQYTLD AKRKHVAEAI CKEQHLFLPF SYKNKYGMVA QVTQTLKLED TPKINSRFFG
EGTKKMGLAF ESTKSTSPPK QAEAVLKTLQ ELKKLTISEQ NIQRANLFNK LVTELRGLSD
EAVTSLLPQL IEVSSPITLQ ALVQCGQPQC STHILQWLKR VHANPLLIDV VTYLVALIPE
PSAQQLREIF NMARDQRSRA TLYALSHAVN NYHKTNPTGT QELLDIANYL MEQIQDDCTG
DEDYTYLILR VIGNMGQTME QLTPELKSSI LKCVQSTKPS LMIQKAAIQA LRKMEPKDKD
QEVLLQTFLD DASPGDKRLA AYLMLMRSPS QADINKIVQI LPWEQNEQVK NFVASHIANI
LNSEELDIQD LKKLVKEALK ESQLPTVMDF RKFSRNYQLY KSVSLPSLDP ASAKIEGNLI
FDPNNYLPKE SMLKTTLTAF GFASADLIEI GLEGKGFEPT LEALFGKQGF FPDSVNKALY
WVNGQVPDGV SKVLVDHFGY TKDDKHEQDM VNGIMLSVEK LIKDLKSKEV PEARAYLRIL
GEELGFASLH DLQLLGKLLL MGARTLQGIP QMIGEVIRKG SKNDFFLHYI FMENAFELPT
GAGLQLQISS SGVIAPGAKA GVKLEVANMQ AELVAKPSVS VEFVTNMGII IPDFARSGVQ
MNTNFFHESG LEAHVALKAG KLKFIIPSPK RPVKLLSGGN TLHLVSTTKT EVIPPLIENR
QSWSVCKQVF PGLNYCTSGA YSNASSTDSA SYYPLTGDTR LELELRPTGE IEQYSVSATY
ELQREDRALV DTLKFVTQAE GAKQTEATMT FKYNRQSMTL SSEVQIPDFD VDLGTILRVN
DESTEGKTSY RLTLDIQNKK ITEVALMGHL SCDTKEERKI KGVISIPRLQ AEARSEILAH
WSPAKLLLQM DSSATAYGST VSKRVAWHYD EEKIEFEWNT GTNVDTKKMT SNFPVDLSDY
PKSLHMYANR LLDHRVPQTD MTFRHVGSKL IVAMSSWLQK ASGSLPYTQT LQDHLNSLKE
FNLQNMGLPD FHIPENLFLK SDGRVKYTLN KNSLKIEIPL PFGGKSSRDL KMLETVRTPA
LHFKSVGFHL PSREFQVPTF TIPKLYQLQV PLLGVLDLST NVYSNLYNWS ASYSGGNTST
DHFSLRARYH MKADSVVDLL SYNVQGSGET TYDHKNTFTL SYDGSLRHKF LDSNIKFSHV
EKLGNNPVSK GLLIFDASSS WGPQMSASVH LDSKKKQHLF VKEVKIDGQF RVSSFYAKGT
YGLSCQRDPN TGRLNGESNL RFNSSYLQGT NQITGRYEDG TLSLTSTSDL QSGIIKNTAS
LKYENYELTL KSDTNGKYKN FATSNKMDMT FSKQNALLRS EYQADYESLR FFSLLSGSLN
SHGLELNADI LGTDKINSGA HKATLRIGQD GISTSATTNL KCSLLVLENE LNAELGLSGA
SMKLTTNGRF REHNAKFSLD GKAALTELSL GSAYQAMILG VDSKNIFNFK VSQEGLKLSN
DMMGSYAEMK FDHTNSLNIA GLSLDFSSKL DNIYSSDKFY KQTVNLQLQP YSLVTTLNSD
LKYNALDLTN NGKLRLEPLK LHVAGNLKGA YQNNEIKHIY AISSAALSAS YKADTVAKVQ
GVEFSHRLNT DIAGLASAID MSTNYNSDSL HFSNVFRSVM APFTMTIDAH TNGNGKLALW
GEHTGQLYSK FLLKAEPLAF TFSHDYKGST SHHLVSRKSI SAALEHKVSA LLTPAEQTGT
WKLKTQFNNN EYSQDLDAYN TKDKIGVELT GRTLADLTLL DSPIKVPLLL SEPINIIDAL
EMRDAVEKPQ EFTIVAFVKY DKNQDVHSIN LPFFETLQEY FERNRQTIIV VLENVQRNLK
HINIDQFVRK YRAALGKLPQ QANDYLNSFN WERQVSHAKE KLTALTKKYR ITENDIQIAL
DDAKINFNEK LSQLQTYMIQ FDQYIKDSYD LHDLKIAIAN IIDEIIEKLK SLDEHYHIRV
NLVKTIHDLH LFIENIDFNK SGSSTASWIQ NVDTKYQIRI QIQEKLQQLK RHIQNIDIQH
LAGKLKQHIE AIDVRVLLDQ LGTTISFERI NDILEHVKHF VINLIGDFEV AEKINAFRAK
VHELIERYEV DQQIQVLMDK LVELAHQYKL KETIQKLSNV LQQVKIKDYF EKLVGFIDDA
VKKLNELSFK TFIEDVNKFL DMLIKKLKSF DYHQFVDETN DKIREVTQRL NGEIQALELP
QKAEALKLFL EETKATVAVY LESLQDTKIT LIINWLQEAL SSASLAHMKA KFRETLEDTR
DRMYQMDIQQ ELQRYLSLVG QVYSTLVTYI SDWWTLAAKN LTDFAEQYSI QDWAKRMKAL
VEQGFTVPEI KTILGTMPAF EVSLQALQKA TFQTPDFIVP LTDLRIPSVQ INFKDLKNIK
IPSRFSTPEF TILNTFHIPS FTIDFVEMKV KIIRTIDQML NSELQWPVPD IYLRDLKVED
IPLARITLPD FRLPEIAIPE FIIPTLNLND FQVPDLHIPE FQLPHISHTI EVPTFGKLYS
ILKIQSPLFT LDANADIGNG TTSANEAGIA ASITAKGESK LEVLNFDFQA NAQLSNPKIN
PLALKESVKF SSKYLRTEHG SEMLFFGNAI EGKSNTVASL HTEKNTLELS NGVIVKINNQ
LTLDSNTKYF HKLNIPKLDF SSQADLRNEI KTLLKAGHIA WTSSGKGSWK WACPRFSDEG
THESQISFTI EGPLTSFGLS NKINSKHLRV NQNLVYESGS LNFSKLEIQS QVDSQHVGHS
VLTAKGMALF GEGKAEFTGR HDAHLNGKVI GTLKNSLFFS AQPFEITAST NNEGNLKVRF
PLRLTGKIDF LNNYALFLSP SAQQASWQVS ARFNQYKYNQ NFSAGNNENI MEAHVGINGE
ANLDFLNIPL TIPEMRLPYT IITTPPLKDF SLWEKTGLKE FLKTTKQSFD LSVKAQYKKN
KHRHSITNPL AVLCEFISQS IKSFDRHFEK NRNNALDFVT KSYNETKIKF DKYKAEKSHD
ELPRTFQIPG YTVPVVNVEV SPFTIEMSAF GYVFPKAVSM PSFSILGSDV RVPSYTLILP
SLELPVLHVP RNLKLSLPDF KELCTISHIF IPAMGNITYD FSFKSSVITL NTNAELFNQS
DIVAHLLSSS SSVIDALQYK LEGTTRLTRK RGLKLATALS LSNKFVEGSH NSTVSLTTKN
MEVSVATTTK AQIPILRMNF KQELNGNTKS KPTVSSSMEF KYDFNSSMLY STAKGAVDHK
LSLESLTSYF SIESSTKGDV KGSVLSREYS GTIASEANTY LNSKSTRSSV KLQGTSKIDD
IWNLEVKENF AGEATLQRIY SLWEHSTKNH LQLEGLFFTN GEHTSKATLE LSPWQMSALV
QVHASQPSSF HDFPDLGQEV ALNANTKNQK IRWKNEVRIH SGSFQSQVEL SNDQEKAHLD
IAGSLEGHLR FLKNIILPVY DKSLWDFLKL DVTTSIGRRQ HLRVSTAFVY TKNPNGYSFS
IPVKVLADKF IIPGLKLNDL NSVLVMPTFH VPFTDLQVPS CKLDFREIQI YKKLRTSSFA
LNLPTLPEVK FPEVDVLTKY SQPEDSLIPF FEITVPESQL TVSQFTLPKS VSDGIAALDL
NAVANKIADF ELPTIIVPEQ TIEIPSIKFS VPAGIVIPSF QALTARFEVD SPVYNATWSA
SLKNKADYVE TVLDSTCSST VQFLEYELNV LGTHKIEDGT LASKTKGTFA HRDFSAEYEE
DGKYEGLQEW EGKAHLNIKS PAFTDLHLRY QKDKKGISTS AASPAVGTVG MDMDEDDDFS
KWNFYYSPQS SPDKKLTIFK TELRVRESDE ETQIKVNWEE EAASGLLTSL KDNVPKATGV
LYDYVNKYHW EHTGLTLREV SSKLRRNLQN NAEWVYQGAI RQIDDIDVRF QKAASGTTGT
YQEWKDKAQN LYQELLTQEG QASFQGLKDN VFDGLVRVTQ EFHMKVKHLI DSLIDFLNFP
RFQFPGKPGI YTREELCTMF IREVGTVLSQ VYSKVHNGSE ILFSYFQDLV ITLPFELRKH
KLIDVISMYR ELLKDLSKEA QEVFKAIQSL KTTEVLRNLQ DLLQFIFQLI EDNIKQLKEM
KFTYLINYIQ DEINTIFSDY IPYVFKLLKE NLCLNLHKFN EFIQNELQEA SQELQQIHQY
IMALREEYFD PSIVGWTVKY YELEEKIVSL IKNLLVALKD FHSEYIVSAS NFTSQLSSQV
EQFLHRNIQE YLSILTDPDG KGKEKIAELS ATAQEIIKSQ AIATKKIISD YHQQFRYKLQ
DFSDQLSDYY EKFIAESKRL IDLSIQNYHT FLIYITELLK KLQSTTVMNP YMKLAPGELT
IIL
