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Apolipoprotein B-100 (Apo B-100) [Cleaved into: Apolipoprotein B-48 (Apo B-48)]

 APOB_HUMAN              Reviewed;        4563 AA.
P04114; O00502; P78479; P78480; P78481; Q13779; Q13785; Q13786;
Q13787; Q13788; Q4ZG63; Q53QC8; Q7Z600; Q9UMN0;
01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
13-JUL-2010, sequence version 2.
25-OCT-2017, entry version 213.
RecName: Full=Apolipoprotein B-100;
Short=Apo B-100;
Contains:
RecName: Full=Apolipoprotein B-48;
Short=Apo B-48;
Flags: Precursor;
Name=APOB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ASN-273; GLU-1218; CYS-1422;
RP VAL-2092; VAL-2313; THR-2365; GLN-2680; HIS-3319; LYS-3427;
GLU-3432; THR-3732; LEU-3949; PHE-3964; LYS-4181 AND ASN-4338.
PubMed=3763409; DOI=10.1093/nar/14.18.7501;
Knott T.C., Wallis S.C., Powell L.M., Pease R.J., Lusis A.J.,
Blackhart B., McCarthy B.J., Mahley R.W., Levy-Wilson B., Scott J.;
"Complete cDNA and derived protein sequence of human apolipoprotein B-
100.";
Nucleic Acids Res. 14:7501-7503(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-1422; VAL-2313;
HIS-3319; LYS-3427; GLU-3432 AND ASN-4338.
PubMed=3652907; DOI=10.1089/dna.1987.6.363;
Ludwig E.H., Blackhart B.D., Pierotti V.R., Caiati L., Fortier C.,
Knott T., Scott J., Mahley R.W., Levy-Wilson B., McCarthy B.J.;
"DNA sequence of the human apolipoprotein B gene.";
DNA 6:363-372(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ILE-98; VAL-618; CYS-1422;
VAL-2313; HIS-3319; LYS-3427; GLU-3432 AND ASN-4338.
PubMed=3759943;
Chen S.-H., Yang C.-Y., Chen P.-F., Setzer D., Tanimura M., Li W.-H.,
Gotto A.M. Jr., Chan L.;
"The complete cDNA and amino acid sequence of human apolipoprotein B-
100.";
J. Biol. Chem. 261:12918-12921(1986).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS CYS-1422; ASN-2037; VAL-2313;
HIS-3319; LYS-3427; GLU-3432; LEU-3949; LYS-4181 AND ASN-4338.
PubMed=3464946; DOI=10.1073/pnas.83.21.8142;
Law S.W., Grant S.M., Higuchi K., Hospattankar A.V., Lackner K.J.,
Lee N., Brewer H.B. Jr.;
"Human liver apolipoprotein B-100 cDNA: complete nucleic acid and
derived amino acid sequence.";
Proc. Natl. Acad. Sci. U.S.A. 83:8142-8146(1986).
[5]
NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40,
AND VARIANTS VAL-618; CYS-1422; VAL-2313; HIS-3319; LYS-3427;
GLU-3432; THR-3732; LEU-3949; PHE-3964; LYS-4181 AND ASN-4338.
PubMed=3030729;
Cladaras C., Hadzopoulou-Cladaras M., Nolte R.T., Atkinson D.,
Zannis V.I.;
"The complete sequence and structural analysis of human apolipoprotein
B-100: relationship between apoB-100 and apoB-48 forms.";
EMBO J. 5:3495-3507(1986).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-1422; VAL-2313 AND
ASN-4338.
SeattleSNPs variation discovery resource;
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-1670, AND VARIANTS ILE-98; CYS-1422
AND ASP-1670.
PubMed=3461454; DOI=10.1073/pnas.83.15.5678;
Protter A.A., Hardman D.A., Sato K.Y., Schilling J.W., Yamanaka M.,
Hort Y.J., Hjerrild K.A., Chen G.C., Kane J.P.;
"Analysis of cDNA clones encoding the entire B-26 region of human
apolipoprotein B.";
Proc. Natl. Acad. Sci. U.S.A. 83:5678-5682(1986).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-291.
PubMed=3513177; DOI=10.1073/pnas.83.5.1467;
Protter A.A., Hardman D.A., Schilling J.W., Miller J., Appleby V.,
Chen G.C., Kirsher S.W., McEnroe G., Kane J.P.;
"Isolation of a cDNA clone encoding the amino-terminal region of human
apolipoprotein B.";
Proc. Natl. Acad. Sci. U.S.A. 83:1467-1471(1986).
[10]
PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, AND VARIANT ILE-98.
PubMed=2115173; DOI=10.1073/pnas.87.14.5523;
Yang C.Y., Kim T.W., Weng S.A., Lee B.R., Yang M.L., Gotto A.M. Jr.;
"Isolation and characterization of sulfhydryl and disulfide peptides
of human apolipoprotein B-100.";
Proc. Natl. Acad. Sci. U.S.A. 87:5523-5527(1990).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 485-1044.
TISSUE=Liver;
PubMed=3001697; DOI=10.1073/pnas.82.24.8340;
Law S.W., Lackner K.J., Hospattankar A.V., Anchors J.M.,
Sakaguchi A.Y., Naylor S.L., Brewer H.B. Jr.;
"Human apolipoprotein B-100: cloning, analysis of liver mRNA, and
assignment of the gene to chromosome 2.";
Proc. Natl. Acad. Sci. U.S.A. 82:8340-8344(1985).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 709-906.
PubMed=3860836; DOI=10.1073/pnas.82.15.4983;
Deeb S.S., Motulsky A.G., Albers J.J.;
"A partial cDNA clone for human apolipoprotein B.";
Proc. Natl. Acad. Sci. U.S.A. 82:4983-4986(1985).
[13]
PROTEIN SEQUENCE OF 873-896 AND 3113-3137.
PubMed=6373369; DOI=10.1016/0014-5793(84)81378-2;
LeBoeuf R.C., Miller C., Shively J.E., Schumaker V.N., Balla M.A.,
Lusis A.J.;
"Human apolipoprotein B: partial amino acid sequence.";
FEBS Lett. 170:105-108(1984).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1042-1232.
PubMed=2567736;
Huang L.S., Ripps M.E., Korman S.H., Deckelbaum R.J., Breslow J.L.;
"Hypobetalipoproteinemia due to an apolipoprotein B gene exon 21
deletion derived by Alu-Alu recombination.";
J. Biol. Chem. 264:11394-11400(1989).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 1282-4503, AND VARIANTS CYS-1422;
VAL-2313; HIS-3319; LYS-3427; GLU-3432; THR-3732 AND ASN-4338.
PubMed=2883086; DOI=10.1016/0378-1119(86)90383-5;
Carlsson P., Darnfors C., Olofsson S.O., Bjursell G.;
"Analysis of the human apolipoprotein B gene; complete structure of
the B-74 region.";
Gene 49:29-51(1986).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 1671-2398, AND VARIANT VAL-2313.
PubMed=3676265; DOI=10.1021/bi00391a040;
Hardman D.A., Protter A.A., Chen G.C., Schilling J.W., Sato K.Y.,
Lau K., Yamanaka M., Mikita T., Miller J., Crisp T., McEnroe G.,
Scarborough R.M., Kane J.P.;
"Structural comparison of human apolipoproteins B-48 and B-100.";
Biochemistry 26:5478-5486(1987).
[17]
NUCLEOTIDE SEQUENCE [MRNA] OF 1937-2018 AND 3811-4334.
PubMed=3841204; DOI=10.1093/nar/13.24.8813;
Carlsson P., Olofsson S.O., Bondjers G., Darnfors C., Wiklund O.,
Bjursell G.;
"Molecular cloning of human apolipoprotein B cDNA.";
Nucleic Acids Res. 13:8813-8826(1985).
[18]
NUCLEOTIDE SEQUENCE [MRNA] OF 2115-2179.
TISSUE=Small intestine;
PubMed=3621347; DOI=10.1016/0092-8674(87)90510-1;
Powell L.M., Wallis S.C., Pease R.J., Edwards Y.H., Knott T.J.,
Scott J.;
"A novel form of tissue-specific RNA processing produces
apolipoprotein-B48 in intestine.";
Cell 50:831-840(1987).
[19]
NUCLEOTIDE SEQUENCE [MRNA] OF 2127-2179.
PubMed=2450346; DOI=10.1073/pnas.85.6.1772;
Higuchi K., Hospattankar A.V., Law S.W., Meglin N., Cortright J.,
Brewer H.B. Jr.;
"Human apolipoprotein B (apoB) mRNA: identification of two distinct
apoB mRNAs, an mRNA with the apoB-100 sequence and an apoB mRNA
containing a premature in-frame translational stop codon, in both
liver and intestine.";
Proc. Natl. Acad. Sci. U.S.A. 85:1772-1776(1988).
[20]
NUCLEOTIDE SEQUENCE [MRNA] OF 2129-2235.
PubMed=3426612; DOI=10.1016/0006-291X(87)90537-7;
Hardman D.A., Protter A.A., Schilling J.W., Kane J.P.;
"Carboxyl terminal analysis of human B-48 protein confirms the novel
mechanism proposed for chain termination.";
Biochem. Biophys. Res. Commun. 149:1214-1219(1987).
[21]
PROTEIN SEQUENCE OF 2169-2179.
PubMed=2445342; DOI=10.1016/0006-291X(87)91107-7;
Hospattankar A.V., Higuchi K., Law S.W., Meglin N., Brewer H.B. Jr.;
"Identification of a novel in-frame translational stop codon in human
intestine apoB mRNA.";
Biochem. Biophys. Res. Commun. 148:279-285(1987).
[22]
NUCLEOTIDE SEQUENCE [MRNA] OF 3056-3159.
PubMed=3903660; DOI=10.1093/nar/13.19.6937;
Mehrabian M., Schumaker V.N., Fareed G.C., West R., Johnson D.F.,
Kirchgessner T.G., Lin H.-C., Wang X., Ma Y., Mendiaz E., Lusis A.J.;
"Human apolipoprotein B: identification of cDNA clones and
characterization of mRNA.";
Nucleic Acids Res. 13:6937-6953(1985).
[23]
NUCLEOTIDE SEQUENCE [MRNA] OF 3109-4563, AND VARIANTS HIS-3319;
LYS-3427; GLU-3432; THR-3732; LEU-3949; PHE-3964; LYS-4181 AND
ASN-4338.
PubMed=2994225; DOI=10.1126/science.2994225;
Knott T.J., Rall S.C. Jr., Innerarity T.L., Jacobson S.F., Urdea M.S.,
Levy-Wilson B., Powell L.M., Pease R.J., Eddy R., Nakai H., Byers M.,
Priestley L.M., Robertson E., Rall L.B., Betsholtz C., Shows T.B.,
Mahley R.W., Scott J.;
"Human apolipoprotein B: structure of carboxyl-terminal domains, sites
of gene expression, and chromosomal localization.";
Science 230:37-43(1985).
[24]
NUCLEOTIDE SEQUENCE [MRNA] OF 3728-4563, AND VARIANT ASN-4338.
PubMed=2932736; DOI=10.1073/pnas.82.21.7265;
Wei C.F., Chen S.H., Yang C.Y., Marcel Y.L., Milne R.W., Li W.H.,
Sparrow J.T., Gotto A.M. Jr., Chan L.;
"Molecular cloning and expression of partial cDNAs and deduced amino
acid sequence of a carboxyl-terminal fragment of human apolipoprotein
B-100.";
Proc. Natl. Acad. Sci. U.S.A. 82:7265-7269(1985).
[25]
NUCLEOTIDE SEQUENCE [MRNA] OF 3846-4298, AND VARIANTS LEU-3949;
PHE-3964 AND LYS-4181.
TISSUE=Liver;
PubMed=3841481; DOI=10.1016/0021-9150(85)90073-5;
Shoulders C.C., Myant N.B., Sidoli A., Rodriguez J.C., Cortese C.,
Baralle F.E., Cortese R.;
"Molecular cloning of human LDL apolipoprotein B cDNA. Evidence for
more than one gene per haploid genome.";
Atherosclerosis 58:277-289(1985).
[26]
NUCLEOTIDE SEQUENCE [MRNA] OF 4217-4563.
PubMed=3024665;
Pfitzner R., Wagener R., Stoffel W.;
"Isolation, expression and characterization of a human apolipoprotein
B 100-specific cDNA clone.";
Biol. Chem. Hoppe-Seyler 367:1077-1083(1986).
[27]
PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION OF APO-B48.
PubMed=3659919; DOI=10.1126/science.3659919;
Chen S.-H., Habib G., Yang C.-H., Gu Z.-W., Lee B.R., Weng S.-H.,
Silberman S.R., Cai S.-J., Deslypere J.P., Rosseneu M.,
Gotto A.M. Jr., Li W.-H., Chan L.;
"Apolipoprotein B-48 is the product of a messenger RNA with an organ-
specific in-frame stop codon.";
Science 238:363-366(1987).
[28]
DOMAINS.
PubMed=3773997; DOI=10.1038/323734a0;
Knott T.C., Pease R.J., Powell L.M., Wallis S.C., Rall S.C. Jr.,
Innerarity T.L., Blackhart B., Taylor W.R., Marcel Y., Milne R.,
Johnson D., Fuller M., Lusis A.J., McCarthy B.J., Mahley R.W.,
Levy-Wilson B., Scott J.;
"Complete protein sequence and identification of structural domains of
human apolipoprotein B.";
Nature 323:734-738(1986).
[29]
DOMAINS.
PubMed=3095664; DOI=10.1038/323738a0;
Yang C.-Y., Chen S.-H., Gianturco S.H., Bradley W.A., Sparrow J.T.,
Tanimura M., Li W.-H., Sparrow D.A., Deloof H., Rosseneu M.,
Lee F.-S., Gu Z.-W., Gotto A.M. Jr., Chan L.;
"Sequence, structure, receptor-binding domains and internal repeats of
human apolipoprotein B-100.";
Nature 323:738-742(1986).
[30]
CALCIUM-BINDING.
PubMed=3087360; DOI=10.1016/0006-291X(86)91237-4;
Dashti N., Lee D.M., Mok T.;
"Apolipoprotein B is a calcium binding protein.";
Biochem. Biophys. Res. Commun. 137:493-499(1986).
[31]
PALMITOYLATION AT CYS-1112.
PubMed=10679026; DOI=10.1091/mbc.11.2.721;
Zhao Y., McCabe J.B., Vance J., Berthiaume L.G.;
"Palmitoylation of apolipoprotein B is required for proper
intracellular sorting and transport of cholesteroyl esters and
triglycerides.";
Mol. Biol. Cell 11:721-734(2000).
[32]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-3358.
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass
spectrometry.";
Proteomics 4:454-465(2004).
[33]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1523; ASN-2982; ASN-3465
AND ASN-3895.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[34]
INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
Leong W.F., Chow V.T.;
"Transcriptomic and proteomic analyses of rhabdomyosarcoma cells
reveal differential cellular gene expression in response to
enterovirus 71 infection.";
Cell. Microbiol. 8:565-580(2006).
[35]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185; ASN-1523; ASN-2239;
ASN-2779; ASN-2982; ASN-3101; ASN-3224; ASN-3411; ASN-3465 AND
ASN-3895.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[36]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2004, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[37]
INVOLVEMENT IN LDLCQ4, AND VARIANT ILE-98.
PubMed=20686565; DOI=10.1038/nature09270;
Teslovich T.M., Musunuru K., Smith A.V., Edmondson A.C.,
Stylianou I.M., Koseki M., Pirruccello J.P., Ripatti S., Chasman D.I.,
Willer C.J., Johansen C.T., Fouchier S.W., Isaacs A., Peloso G.M.,
Barbalic M., Ricketts S.L., Bis J.C., Aulchenko Y.S., Thorleifsson G.,
Feitosa M.F., Chambers J., Orho-Melander M., Melander O., Johnson T.,
Li X., Guo X., Li M., Shin Cho Y., Jin Go M., Jin Kim Y., Lee J.Y.,
Park T., Kim K., Sim X., Twee-Hee Ong R., Croteau-Chonka D.C.,
Lange L.A., Smith J.D., Song K., Hua Zhao J., Yuan X., Luan J.,
Lamina C., Ziegler A., Zhang W., Zee R.Y., Wright A.F., Witteman J.C.,
Wilson J.F., Willemsen G., Wichmann H.E., Whitfield J.B.,
Waterworth D.M., Wareham N.J., Waeber G., Vollenweider P.,
Voight B.F., Vitart V., Uitterlinden A.G., Uda M., Tuomilehto J.,
Thompson J.R., Tanaka T., Surakka I., Stringham H.M., Spector T.D.,
Soranzo N., Smit J.H., Sinisalo J., Silander K., Sijbrands E.J.,
Scuteri A., Scott J., Schlessinger D., Sanna S., Salomaa V.,
Saharinen J., Sabatti C., Ruokonen A., Rudan I., Rose L.M.,
Roberts R., Rieder M., Psaty B.M., Pramstaller P.P., Pichler I.,
Perola M., Penninx B.W., Pedersen N.L., Pattaro C., Parker A.N.,
Pare G., Oostra B.A., O'Donnell C.J., Nieminen M.S., Nickerson D.A.,
Montgomery G.W., Meitinger T., McPherson R., McCarthy M.I.,
McArdle W., Masson D., Martin N.G., Marroni F., Mangino M.,
Magnusson P.K., Lucas G., Luben R., Loos R.J., Lokki M.L., Lettre G.,
Langenberg C., Launer L.J., Lakatta E.G., Laaksonen R., Kyvik K.O.,
Kronenberg F., Konig I.R., Khaw K.T., Kaprio J., Kaplan L.M.,
Johansson A., Jarvelin M.R., Janssens A.C., Ingelsson E., Igl W.,
Kees Hovingh G., Hottenga J.J., Hofman A., Hicks A.A.,
Hengstenberg C., Heid I.M., Hayward C., Havulinna A.S., Hastie N.D.,
Harris T.B., Haritunians T., Hall A.S., Gyllensten U., Guiducci C.,
Groop L.C., Gonzalez E., Gieger C., Freimer N.B., Ferrucci L.,
Erdmann J., Elliott P., Ejebe K.G., Doring A., Dominiczak A.F.,
Demissie S., Deloukas P., de Geus E.J., de Faire U., Crawford G.,
Collins F.S., Chen Y.D., Caulfield M.J., Campbell H., Burtt N.P.,
Bonnycastle L.L., Boomsma D.I., Boekholdt S.M., Bergman R.N.,
Barroso I., Bandinelli S., Ballantyne C.M., Assimes T.L.,
Quertermous T., Altshuler D., Seielstad M., Wong T.Y., Tai E.S.,
Feranil A.B., Kuzawa C.W., Adair L.S., Taylor H.A. Jr., Borecki I.B.,
Gabriel S.B., Wilson J.G., Holm H., Thorsteinsdottir U., Gudnason V.,
Krauss R.M., Mohlke K.L., Ordovas J.M., Munroe P.B., Kooner J.S.,
Tall A.R., Hegele R.A., Kastelein J.J., Schadt E.E., Rotter J.I.,
Boerwinkle E., Strachan D.P., Mooser V., Stefansson K., Reilly M.P.,
Samani N.J., Schunkert H., Cupples L.A., Sandhu M.S., Ridker P.M.,
Rader D.J., van Duijn C.M., Peltonen L., Abecasis G.R., Boehnke M.,
Kathiresan S.;
"Biological, clinical and population relevance of 95 loci for blood
lipids.";
Nature 466:707-713(2010).
[38]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[39]
INVOLVEMENT IN FHBL1.
PubMed=21981844; DOI=10.1016/j.jacl.2011.06.014;
Gangloff A., Bergeron J., Couture P., Martins R., Hegele R.A.,
Gagne C.;
"A novel mutation of apolipoprotein B in a French Canadian family with
homozygous hypobetalipoproteinemia.";
J. Clin. Lipidol. 5:414-417(2011).
[40]
SUBCELLULAR LOCATION, AND INTERACTION WITH PCSK9.
PubMed=22580899; DOI=10.1161/ATVBAHA.112.250043;
Sun H., Samarghandi A., Zhang N., Yao Z., Xiong M., Teng B.B.;
"Proprotein convertase subtilisin/kexin type 9 interacts with
apolipoprotein B and prevents its intracellular degradation,
irrespective of the low-density lipoprotein receptor.";
Arterioscler. Thromb. Vasc. Biol. 32:1585-1595(2012).
[41]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3279; SER-4048 AND
THR-4052, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[42]
PHOSPHORYLATION AT SER-4048.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[43]
INTERACTION WITH MTTP, AND SUBCELLULAR LOCATION.
PubMed=26224785; DOI=10.1161/CIRCGENETICS.115.001106;
Walsh M.T., Iqbal J., Josekutty J., Soh J., Di Leo E., Oezaydin E.,
Guenduez M., Tarugi P., Hussain M.M.;
"A novel abetalipoproteinemia missense mutation highlights the
importance of N-Terminal beta-barrel in microsomal triglyceride
transfer protein function.";
Circ. Cardiovasc. Genet. 8:677-687(2015).
[44]
VARIANT ASN-4338.
PubMed=1979313; DOI=10.1007/BF00205183;
Navajas M., Laurent A.-M., Moreel J.-F., Ragab A., Cambou J.-P.,
Cunny G., Cambien F., Roizes G.;
"Detection by denaturing gradient gel electrophoresis of a new
polymorphism in the apolipoprotein B gene.";
Hum. Genet. 86:91-93(1990).
[45]
VARIANT FDB GLN-3527.
PubMed=2563166; DOI=10.1073/pnas.86.2.587;
Soria L.F., Ludwig E.H., Clarke H.R.G., Vega G.L., Grundy S.M.,
McCarthy B.J.;
"Association between a specific apolipoprotein B mutation and familial
defective apolipoprotein B-100.";
Proc. Natl. Acad. Sci. U.S.A. 86:587-591(1989).
[46]
VARIANT LEU-2739.
PubMed=2216805; DOI=10.1093/nar/18.19.5922-a;
Huang L.-S., Gavish D., Breslow J.L.;
"Sequence polymorphism in the human apoB gene at position 8344.";
Nucleic Acids Res. 18:5922-5922(1990).
[47]
VARIANT FDB CYS-3558.
PubMed=7883971; DOI=10.1172/JCI117772;
Pullinger C.R., Hennessy L.K., Chatterton J.E., Liu W., Love J.A.,
Mendel C.M., Frost P.H., Malloy M.J., Schumaker V.N., Kane J.P.;
"Familial ligand-defective apolipoprotein B. Identification of a new
mutation that decreases LDL receptor binding affinity.";
J. Clin. Invest. 95:1225-1234(1995).
[48]
VARIANTS LEU-1437; SER-1914; LYS-2566; THR-3121; ALA-3945; MET-4128
AND THR-4481.
PubMed=8889592;
DOI=10.1002/(SICI)1098-1004(1996)8:3<282::AID-HUMU16>3.3.CO;2-Y;
Poirier O., Ricard S., Behague I., Souriau C., Evans A.E.,
Arveiler D., Marques-Vidal P., Luc G., Roizes G., Cambien F.;
"Detection of new variants in the apolipoprotein B (Apo B) gene by
PCR-SSCP.";
Hum. Mutat. 8:282-285(1996).
[49]
VARIANTS FDB GLN-3527 AND CYS-3558.
PubMed=9259199;
DOI=10.1002/(SICI)1098-1004(1997)10:2<160::AID-HUMU8>3.0.CO;2-O;
Rabes J.P., Varret M., Saint-Jore B., Erlich D., Jondeau G.,
Krempf M., Giraudet P., Junien C., Boileau C.;
"Familial ligand-defective apolipoprotein B-100: simultaneous
detection of the Arg3500-->Gln and Arg3531-->Cys mutations in a French
population.";
Hum. Mutat. 10:160-163(1997).
[50]
VARIANTS SER-1914; ARG-1923; LEU-2739; HIS-3319; LYS-3427; GLU-3432
AND ILE-3921.
PubMed=9490296; DOI=10.1007/s004390050651;
Leren T.P., Bakken K.S., Hoel V., Hjermann I., Berg K.;
"Screening for mutations of the apolipoprotein B gene causing
hypocholesterolemia.";
Hum. Genet. 102:44-49(1998).
[51]
VARIANT FHBL1 TRP-490, VARIANT ILE-98, CHARACTERIZATION OF VARIANT
TRP-490, AND MUTAGENESIS OF ASP-483 AND ARG-490.
PubMed=12551903; DOI=10.1074/jbc.M300235200;
Burnett J.R., Shan J., Miskie B.A., Whitfield A.J., Yuan J., Tran K.,
McKnight C.J., Hegele R.A., Yao Z.;
"A novel nontruncating APOB gene mutation, R463W, causes familial
hypobetalipoproteinemia.";
J. Biol. Chem. 278:13442-13452(2003).
[52]
VARIANT HIS-1128.
PubMed=14732481;
Lancellotti S., Di Leo E., Penacchioni J.Y., Balli F., Viola L.,
Bertolini S., Calandra S., Tarugi P.;
"Hypobetalipoproteinemia with an apparently recessive inheritance due
to a 'de novo' mutation of apolipoprotein B.";
Biochim. Biophys. Acta 1688:61-67(2004).
[53]
VARIANT [LARGE SCALE ANALYSIS] CYS-2564.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[54]
VARIANT FDB GLN-3527.
PubMed=21382890; DOI=10.1161/CIRCULATIONAHA.110.979450;
van der Graaf A., Avis H.J., Kusters D.M., Vissers M.N., Hutten B.A.,
Defesche J.C., Huijgen R., Fouchier S.W., Wijburg F.A.,
Kastelein J.J., Wiegman A.;
"Molecular basis of autosomal dominant hypercholesterolemia:
assessment in a large cohort of hypercholesterolemic children.";
Circulation 123:1167-1173(2011).
[55]
VARIANTS GLU-1218; ASP-1670; ASN-2037; CYS-2564 AND LYS-2566, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22028381; DOI=10.1093/jmcb/mjr024;
Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H.,
Lin X., Zeng R., Wu J.R.;
"Quantitative detection of single amino acid polymorphisms by targeted
proteomics.";
J. Mol. Cell Biol. 3:309-315(2011).
[56]
VARIANTS 12-LEU--LEU-14 DEL; ILE-98; VAL-618; ILE-730; THR-1613;
ARG-1923; LYS-2566; LEU-2739; GLN-3638; LEU-3835; LYS-4181; THR-4270;
VAL-4314; ASN-4338; THR-4481 AND VAL-4482.
PubMed=22095935; DOI=10.1002/humu.21660;
Huijgen R., Sjouke B., Vis K., de Randamie J.S., Defesche J.C.,
Kastelein J.J., Hovingh G.K., Fouchier S.W.;
"Genetic variation in APOB, PCSK9, and ANGPTL3 in carriers of
pathogenic autosomal dominant hypercholesterolemic mutations with
unexpected low LDL-Cl Levels.";
Hum. Mutat. 33:448-455(2012).
[57]
VARIANT FHBL1 LEU-952, VARIANT THR-251, CHARACTERIZATION OF VARIANT
FHBL1 LEU-952, CHARACTERIZATION OF VARIANT THR-251, AND INTERACTION
WITH MTTP.
PubMed=27206948; DOI=10.1016/j.jacl.2016.01.006;
Miller S.A., Hooper A.J., Mantiri G.A., Marais D., Tanyanyiwa D.M.,
McKnight J., Burnett J.R.;
"Novel APOB missense variants, A224T and V925L, in a black South
African woman with marked hypocholesterolemia.";
J. Clin. Lipidol. 10:604-609(2016).
-!- FUNCTION: Apolipoprotein B is a major protein constituent of
chylomicrons (apo B-48), LDL (apo B-100) and VLDL (apo B-100). Apo
B-100 functions as a recognition signal for the cellular binding
and internalization of LDL particles by the apoB/E receptor.
-!- SUBUNIT: Interacts with PCSK9 (PubMed:22580899). Interacts with
MTTP (PubMed:26224785, PubMed:27206948).
{ECO:0000269|PubMed:22580899, ECO:0000269|PubMed:26224785,
ECO:0000269|PubMed:27206948}.
-!- INTERACTION:
P29991:- (xeno); NbExp=3; IntAct=EBI-3926040, EBI-8826488;
P01130:LDLR; NbExp=4; IntAct=EBI-3926040, EBI-988319;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22580899}.
Secreted {ECO:0000269|PubMed:22580899,
ECO:0000269|PubMed:26224785}.
-!- INDUCTION: Up-regulated in response to enterovirus 71 (EV71)
infection (at protein level). {ECO:0000269|PubMed:16548883}.
-!- PTM: Palmitoylated; structural requirement for proper assembly of
the hydrophobic core of the lipoprotein particle.
{ECO:0000269|PubMed:10679026}.
-!- RNA EDITING: Modified_positions=2180; Note=The stop codon (UAA) at
position 2180 is created by RNA editing. Apo B-48, derived from
the fully edited RNA, is produced only in the intestine and is
found in chylomicrons. Apo B-48 is a shortened form of apo B-100
which lacks the LDL-receptor region. The unedited version (apo B-
100) is produced by the liver and is found in the VLDL and LDL.;
-!- POLYMORPHISM: Genetic variations in APOB define the low density
lipoprotein cholesterol level quantitative trait locus 4 (LDLCQ4)
[MIM:107730].
-!- DISEASE: Hypobetalipoproteinemia, familial, 1 (FHBL1)
[MIM:615558]: A disorder of lipid metabolism characterized by less
than 5th percentile age- and sex-specific levels of low density
lipoproteins, and dietary fat malabsorption. Clinical presentation
may vary from no symptoms to severe gastrointestinal and
neurological dysfunction similar to abetalipoproteinemia.
{ECO:0000269|PubMed:12551903, ECO:0000269|PubMed:21981844,
ECO:0000269|PubMed:27206948}. Note=The disease is caused by
mutations affecting the gene represented in this entry. Most cases
of FHBL1 result from nonsense mutations in the APOB gene that lead
to a premature stop codon, which generate prematurely truncated
apo B protein products (PubMed:21981844).
{ECO:0000269|PubMed:21981844}.
-!- DISEASE: Familial ligand-defective apolipoprotein B-100 (FDB)
[MIM:144010]: Dominantly inherited disorder of lipoprotein
metabolism leading to hypercholesterolemia and increased proneness
to coronary artery disease (CAD). The plasma cholesterol levels
are dramatically elevated due to impaired clearance of LDL
particles by defective APOB/E receptors.
{ECO:0000269|PubMed:21382890, ECO:0000269|PubMed:2563166,
ECO:0000269|PubMed:7883971, ECO:0000269|PubMed:9259199}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Note=Defects in APOB associated with defects in other
genes (polygenic) can contribute to hypocholesterolemia.
-!- SEQUENCE CAUTION:
Sequence=AAA51752.1; Type=Frameshift; Positions=942, 951, 1139, 1165, 1164, 1371, 1385; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=APOB";
-!- WEB RESOURCE: Name=Wikipedia; Note=Apolipoprotein B entry;
URL="https://en.wikipedia.org/wiki/Apolipoprotein_B";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X04506; CAA28191.1; -; mRNA.
EMBL; M19828; AAB00481.1; -; Genomic_DNA.
EMBL; M19808; AAB00481.1; JOINED; Genomic_DNA.
EMBL; M19809; AAB00481.1; JOINED; Genomic_DNA.
EMBL; M19810; AAB00481.1; JOINED; Genomic_DNA.
EMBL; M19811; AAB00481.1; JOINED; Genomic_DNA.
EMBL; M19812; AAB00481.1; JOINED; Genomic_DNA.
EMBL; M19813; AAB00481.1; JOINED; Genomic_DNA.
EMBL; M19815; AAB00481.1; JOINED; Genomic_DNA.
EMBL; M19816; AAB00481.1; JOINED; Genomic_DNA.
EMBL; M19818; AAB00481.1; JOINED; Genomic_DNA.
EMBL; M19820; AAB00481.1; JOINED; Genomic_DNA.
EMBL; M19821; AAB00481.1; JOINED; Genomic_DNA.
EMBL; M19823; AAB00481.1; JOINED; Genomic_DNA.
EMBL; M19824; AAB00481.1; JOINED; Genomic_DNA.
EMBL; M19825; AAB00481.1; JOINED; Genomic_DNA.
EMBL; M19827; AAB00481.1; JOINED; Genomic_DNA.
EMBL; J02610; AAA35549.1; -; mRNA.
EMBL; M14162; AAB04636.1; -; mRNA.
EMBL; M15053; AAB60718.1; -; Genomic_DNA.
EMBL; X04714; CAA28420.1; -; mRNA.
EMBL; AY324608; AAP72970.1; -; Genomic_DNA.
EMBL; AC010872; AAX88848.1; -; Genomic_DNA.
EMBL; AC115619; AAX93246.1; -; Genomic_DNA.
EMBL; M14081; AAA51752.1; ALT_FRAME; mRNA.
EMBL; M12681; AAA51753.1; -; mRNA.
EMBL; M12480; AAA51751.1; -; mRNA.
EMBL; K03175; AAA51759.1; -; mRNA.
EMBL; M15421; AAA51758.1; -; mRNA.
EMBL; M17367; AAA51741.1; -; mRNA.
EMBL; M31030; AAA51756.1; -; mRNA.
EMBL; X03325; CAA27044.1; -; mRNA.
EMBL; X03326; CAA27045.1; -; mRNA.
EMBL; M17779; AAA51755.1; -; mRNA.
EMBL; M19734; AAA35544.1; -; mRNA.
EMBL; M18471; AAA35541.1; -; mRNA.
EMBL; X03045; CAA26850.1; -; mRNA.
EMBL; M10374; AAA51750.1; -; mRNA.
EMBL; M12413; AAA51742.1; -; mRNA.
EMBL; M36676; AAA35548.1; -; mRNA.
CCDS; CCDS1703.1; -.
PIR; A27850; LPHUB.
RefSeq; NP_000375.2; NM_000384.2.
UniGene; Hs.120759; -.
ProteinModelPortal; P04114; -.
SMR; P04114; -.
BioGrid; 106835; 71.
DIP; DIP-44767N; -.
IntAct; P04114; 30.
MINT; MINT-1506918; -.
STRING; 9606.ENSP00000233242; -.
BindingDB; P04114; -.
ChEMBL; CHEMBL4549; -.
iPTMnet; P04114; -.
PhosphoSitePlus; P04114; -.
SwissPalm; P04114; -.
UniCarbKB; P04114; -.
BioMuta; APOB; -.
DMDM; 300669605; -.
EPD; P04114; -.
MaxQB; P04114; -.
PaxDb; P04114; -.
PeptideAtlas; P04114; -.
PRIDE; P04114; -.
Ensembl; ENST00000233242; ENSP00000233242; ENSG00000084674.
GeneID; 338; -.
KEGG; hsa:338; -.
UCSC; uc002red.3; human.
CTD; 338; -.
DisGeNET; 338; -.
EuPathDB; HostDB:ENSG00000084674.13; -.
GeneCards; APOB; -.
GeneReviews; APOB; -.
H-InvDB; HIX0024005; -.
HGNC; HGNC:603; APOB.
HPA; CAB016070; -.
HPA; HPA049793; -.
MalaCards; APOB; -.
MIM; 107730; gene+phenotype.
MIM; 144010; phenotype.
MIM; 615558; phenotype.
neXtProt; NX_P04114; -.
Orphanet; 426; Familial hypobetalipoproteinemia.
Orphanet; 406; Heterozygous familial hypercholesterolemia.
Orphanet; 391665; Homozygous familial hypercholesterolemia.
PharmGKB; PA50; -.
eggNOG; KOG4338; Eukaryota.
eggNOG; ENOG411104F; LUCA.
HOVERGEN; HBG050546; -.
InParanoid; P04114; -.
KO; K14462; -.
OrthoDB; EOG091G000G; -.
PhylomeDB; P04114; -.
TreeFam; TF331316; -.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-3000471; Scavenging by Class B Receptors.
Reactome; R-HSA-3000480; Scavenging by Class A Receptors.
Reactome; R-HSA-3000484; Scavenging by Class F Receptors.
Reactome; R-HSA-3000497; Scavenging by Class H Receptors.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-432142; Platelet sensitization by LDL.
Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand.
Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
Reactome; R-HSA-8866423; VLDL assembly.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
Reactome; R-HSA-8963888; Chylomicron assembly.
Reactome; R-HSA-8963901; Chylomicron remodeling.
Reactome; R-HSA-8964026; Chylomicron clearance.
Reactome; R-HSA-8964038; LDL clearance.
Reactome; R-HSA-8964041; LDL remodeling.
Reactome; R-HSA-8964046; VLDL clearance.
Reactome; R-HSA-975634; Retinoid metabolism and transport.
Reactome; R-MMU-8964038; LDL clearance.
Reactome; R-MMU-8964046; VLDL clearance.
SIGNOR; P04114; -.
ChiTaRS; APOB; human.
GeneWiki; Apolipoprotein_B; -.
GenomeRNAi; 338; -.
PRO; PR:P04114; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000084674; -.
ExpressionAtlas; P04114; baseline and differential.
Genevisible; P04114; HS.
GO; GO:0042627; C:chylomicron; IDA:BHF-UCL.
GO; GO:0034360; C:chylomicron remnant; TAS:BHF-UCL.
GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005769; C:early endosome; TAS:Reactome.
GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0031904; C:endosome lumen; TAS:Reactome.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; ISS:BHF-UCL.
GO; GO:0034363; C:intermediate-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0034362; C:low-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0034359; C:mature chylomicron; IDA:BHF-UCL.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005790; C:smooth endoplasmic reticulum; TAS:Reactome.
GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0017127; F:cholesterol transporter activity; IMP:BHF-UCL.
GO; GO:0008201; F:heparin binding; IDA:BHF-UCL.
GO; GO:0035473; F:lipase binding; IPI:BHF-UCL.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IMP:BHF-UCL.
GO; GO:0005543; F:phospholipid binding; IDA:BHF-UCL.
GO; GO:0048844; P:artery morphogenesis; IEA:Ensembl.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0071379; P:cellular response to prostaglandin stimulus; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0033344; P:cholesterol efflux; IEA:Ensembl.
GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
GO; GO:0008203; P:cholesterol metabolic process; IMP:BHF-UCL.
GO; GO:0030301; P:cholesterol transport; IMP:BHF-UCL.
GO; GO:0034378; P:chylomicron assembly; TAS:Reactome.
GO; GO:0034382; P:chylomicron remnant clearance; TAS:Reactome.
GO; GO:0034371; P:chylomicron remodeling; TAS:Reactome.
GO; GO:0009566; P:fertilization; IEA:Ensembl.
GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:Ensembl.
GO; GO:0042159; P:lipoprotein catabolic process; IEA:Ensembl.
GO; GO:0042953; P:lipoprotein transport; IEA:Ensembl.
GO; GO:0034383; P:low-density lipoprotein particle clearance; IMP:BHF-UCL.
GO; GO:0034374; P:low-density lipoprotein particle remodeling; IMP:BHF-UCL.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0007399; P:nervous system development; IEA:Ensembl.
GO; GO:0010886; P:positive regulation of cholesterol storage; IDA:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0010884; P:positive regulation of lipid storage; IDA:BHF-UCL.
GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IDA:BHF-UCL.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:0045540; P:regulation of cholesterol biosynthetic process; IEA:Ensembl.
GO; GO:0009743; P:response to carbohydrate; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0010269; P:response to selenium ion; IEA:Ensembl.
GO; GO:0009615; P:response to virus; IEP:UniProtKB.
GO; GO:0001523; P:retinoid metabolic process; TAS:Reactome.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0019433; P:triglyceride catabolic process; IEA:Ensembl.
GO; GO:0006642; P:triglyceride mobilization; IEA:Ensembl.
GO; GO:0034379; P:very-low-density lipoprotein particle assembly; TAS:Reactome.
GO; GO:0034447; P:very-low-density lipoprotein particle clearance; TAS:Reactome.
Gene3D; 1.25.10.20; -; 1.
Gene3D; 2.20.50.20; -; 1.
Gene3D; 2.30.230.10; -; 1.
InterPro; IPR022176; ApoB100_C.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR015819; Lipid_transp_b-sht_shell.
InterPro; IPR001747; Lipid_transpt_N.
InterPro; IPR009454; Lipid_transpt_open_b-sht.
InterPro; IPR011030; Lipovitellin_superhlx_dom.
InterPro; IPR015816; Vitellinogen_b-sht_N.
InterPro; IPR015255; Vitellinogen_open_b-sht.
InterPro; IPR015817; Vitellinogen_open_b-sht_sub1.
Pfam; PF12491; ApoB100_C; 1.
Pfam; PF06448; DUF1081; 1.
Pfam; PF09172; DUF1943; 1.
Pfam; PF01347; Vitellogenin_N; 1.
SMART; SM01169; DUF1943; 1.
SMART; SM00638; LPD_N; 1.
SUPFAM; SSF48371; SSF48371; 2.
SUPFAM; SSF48431; SSF48431; 1.
SUPFAM; SSF56968; SSF56968; 2.
PROSITE; PS51211; VITELLOGENIN; 1.
1: Evidence at protein level;
Acetylation; Atherosclerosis; Cholesterol metabolism; Chylomicron;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disease mutation; Disulfide bond; Glycoprotein; Heparin-binding; LDL;
Lipid metabolism; Lipid transport; Lipoprotein; Palmitate;
Phosphoprotein; Polymorphism; Reference proteome; RNA editing;
Secreted; Signal; Steroid metabolism; Sterol metabolism; Transport;
VLDL.
SIGNAL 1 27
CHAIN 28 4563 Apolipoprotein B-100.
/FTId=PRO_0000020750.
CHAIN 28 2179 Apolipoprotein B-48.
/FTId=PRO_0000020751.
DOMAIN 46 672 Vitellogenin. {ECO:0000255|PROSITE-
ProRule:PRU00557}.
REGION 32 126 Heparin-binding.
REGION 232 306 Heparin-binding.
REGION 902 959 Heparin-binding.
REGION 2043 2178 Heparin-binding.
REGION 3161 3236 Heparin-binding.
REGION 3174 3184 Basic (possible receptor binding region).
REGION 3373 3393 LDL receptor binding.
REGION 3383 3516 Heparin-binding.
REGION 3386 3394 Basic (possible receptor binding region).
MOD_RES 2004 2004 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 3279 3279 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 4048 4048 Phosphoserine; by FAM20C.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:26091039}.
MOD_RES 4052 4052 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
LIPID 1112 1112 S-palmitoyl cysteine.
{ECO:0000269|PubMed:10679026}.
CARBOHYD 34 34 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 185 185 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 983 983 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1368 1368 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1377 1377 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1523 1523 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
CARBOHYD 2239 2239 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 2560 2560 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2779 2779 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 2982 2982 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
CARBOHYD 3101 3101 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 3224 3224 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 3336 3336 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3358 3358 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14760718}.
CARBOHYD 3411 3411 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 3465 3465 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
CARBOHYD 3895 3895 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
CARBOHYD 4237 4237 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4431 4431 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 39 88 {ECO:0000255|PROSITE-ProRule:PRU00557,
ECO:0000269|PubMed:2115173}.
DISULFID 78 97 {ECO:0000255|PROSITE-ProRule:PRU00557,
ECO:0000269|PubMed:2115173}.
DISULFID 186 212 {ECO:0000255|PROSITE-ProRule:PRU00557,
ECO:0000269|PubMed:2115173}.
DISULFID 245 261 {ECO:0000255|PROSITE-ProRule:PRU00557,
ECO:0000269|PubMed:2115173}.
DISULFID 385 390 {ECO:0000255|PROSITE-ProRule:PRU00557,
ECO:0000269|PubMed:2115173}.
DISULFID 478 513 {ECO:0000255|PROSITE-ProRule:PRU00557,
ECO:0000269|PubMed:2115173}.
DISULFID 966 976 {ECO:0000255|PROSITE-ProRule:PRU00557,
ECO:0000269|PubMed:2115173}.
DISULFID 3194 3324 {ECO:0000255|PROSITE-ProRule:PRU00557,
ECO:0000269|PubMed:2115173}.
VARIANT 12 14 Missing. {ECO:0000269|PubMed:22095935}.
/FTId=VAR_067277.
VARIANT 98 98 T -> I (polymorphism that influences
plasma concentrations of low density
lipoprotein cholesterol;
dbSNP:rs1367117).
{ECO:0000269|PubMed:12551903,
ECO:0000269|PubMed:20686565,
ECO:0000269|PubMed:2115173,
ECO:0000269|PubMed:22095935,
ECO:0000269|PubMed:3461454,
ECO:0000269|PubMed:3759943}.
/FTId=VAR_016184.
VARIANT 103 103 Y -> H (in dbSNP:rs9282603).
/FTId=VAR_022036.
VARIANT 145 145 P -> S (in dbSNP:rs6752026).
/FTId=VAR_022037.
VARIANT 194 194 T -> M (in dbSNP:rs13306198).
/FTId=VAR_056737.
VARIANT 251 251 A -> T (polymorphism; does not affect
plasma lipid levels; dbSNP:rs61741625).
{ECO:0000269|PubMed:27206948}.
/FTId=VAR_076538.
VARIANT 273 273 K -> N. {ECO:0000269|PubMed:3763409}.
/FTId=VAR_019827.
VARIANT 408 408 I -> T (in dbSNP:rs12714225).
/FTId=VAR_029341.
VARIANT 490 490 R -> W (in FHBL1; reduced protein
secretion).
{ECO:0000269|PubMed:12551903}.
/FTId=VAR_022610.
VARIANT 554 554 P -> L (in dbSNP:rs12714214).
/FTId=VAR_020135.
VARIANT 618 618 A -> V (in dbSNP:rs679899).
{ECO:0000269|PubMed:22095935,
ECO:0000269|PubMed:3030729,
ECO:0000269|PubMed:3759943}.
/FTId=VAR_019828.
VARIANT 730 730 V -> I (in dbSNP:rs12691202).
{ECO:0000269|PubMed:22095935}.
/FTId=VAR_020136.
VARIANT 733 733 V -> I (in dbSNP:rs1800476).
/FTId=VAR_016185.
VARIANT 741 741 T -> N (in dbSNP:rs12714192).
/FTId=VAR_020137.
VARIANT 877 877 P -> L (in dbSNP:rs12714097).
/FTId=VAR_029342.
VARIANT 952 952 V -> L (in FHBL1; unknown pathological
significance; does not affect interaction
with MTTP).
{ECO:0000269|PubMed:27206948}.
/FTId=VAR_076539.
VARIANT 955 955 P -> S (in dbSNP:rs13306206).
/FTId=VAR_056738.
VARIANT 1086 1086 G -> S (in dbSNP:rs12720801).
/FTId=VAR_029343.
VARIANT 1113 1113 D -> H (in dbSNP:rs12713844).
/FTId=VAR_029344.
VARIANT 1128 1128 R -> H (in dbSNP:rs12713843).
{ECO:0000269|PubMed:14732481}.
/FTId=VAR_022611.
VARIANT 1218 1218 Q -> E (polymorphism; confirmed at
protein level; dbSNP:rs1041956).
{ECO:0000269|PubMed:22028381,
ECO:0000269|PubMed:3763409}.
/FTId=VAR_019829.
VARIANT 1388 1388 R -> H (in dbSNP:rs13306187).
/FTId=VAR_029345.
VARIANT 1422 1422 Y -> C (in dbSNP:rs568413).
{ECO:0000269|PubMed:2883086,
ECO:0000269|PubMed:3030729,
ECO:0000269|PubMed:3461454,
ECO:0000269|PubMed:3464946,
ECO:0000269|PubMed:3652907,
ECO:0000269|PubMed:3759943,
ECO:0000269|PubMed:3763409,
ECO:0000269|Ref.6}.
/FTId=VAR_061558.
VARIANT 1437 1437 F -> L (in dbSNP:rs1801697).
{ECO:0000269|PubMed:8889592}.
/FTId=VAR_005016.
VARIANT 1613 1613 S -> T. {ECO:0000269|PubMed:22095935}.
/FTId=VAR_067278.
VARIANT 1670 1670 E -> D (polymorphism; confirmed at
protein level).
{ECO:0000269|PubMed:22028381,
ECO:0000269|PubMed:3461454}.
/FTId=VAR_068911.
VARIANT 1914 1914 N -> S (in dbSNP:rs1801699).
{ECO:0000269|PubMed:8889592,
ECO:0000269|PubMed:9490296}.
/FTId=VAR_005017.
VARIANT 1923 1923 H -> R (in dbSNP:rs533617).
{ECO:0000269|PubMed:22095935,
ECO:0000269|PubMed:9490296}.
/FTId=VAR_005018.
VARIANT 2037 2037 I -> N (polymorphism; confirmed at
protein level).
{ECO:0000269|PubMed:22028381,
ECO:0000269|PubMed:3464946}.
/FTId=VAR_068912.
VARIANT 2092 2092 L -> V (in dbSNP:rs1041960).
{ECO:0000269|PubMed:3763409}.
/FTId=VAR_019830.
VARIANT 2299 2299 D -> H (in dbSNP:rs12713681).
/FTId=VAR_029346.
VARIANT 2313 2313 I -> V (in dbSNP:rs584542).
{ECO:0000269|PubMed:2883086,
ECO:0000269|PubMed:3030729,
ECO:0000269|PubMed:3464946,
ECO:0000269|PubMed:3652907,
ECO:0000269|PubMed:3676265,
ECO:0000269|PubMed:3759943,
ECO:0000269|PubMed:3763409,
ECO:0000269|Ref.6}.
/FTId=VAR_059582.
VARIANT 2365 2365 A -> T (in dbSNP:rs1041971).
{ECO:0000269|PubMed:3763409}.
/FTId=VAR_019831.
VARIANT 2456 2456 A -> D (in dbSNP:rs12713675).
/FTId=VAR_020138.
VARIANT 2564 2564 F -> C (in a colorectal cancer sample;
somatic mutation; confirmed at protein
level). {ECO:0000269|PubMed:16959974,
ECO:0000269|PubMed:22028381}.
/FTId=VAR_035795.
VARIANT 2566 2566 E -> K (polymorphism; confirmed at
protein level; dbSNP:rs1801696).
{ECO:0000269|PubMed:22028381,
ECO:0000269|PubMed:22095935,
ECO:0000269|PubMed:8889592}.
/FTId=VAR_005019.
VARIANT 2680 2680 L -> Q (in dbSNP:rs1042013).
{ECO:0000269|PubMed:3763409}.
/FTId=VAR_019832.
VARIANT 2739 2739 P -> L (in dbSNP:rs676210).
{ECO:0000269|PubMed:22095935,
ECO:0000269|PubMed:2216805,
ECO:0000269|PubMed:9490296}.
/FTId=VAR_005020.
VARIANT 2785 2785 N -> H (in dbSNP:rs2163204).
/FTId=VAR_022038.
VARIANT 3121 3121 A -> T (in dbSNP:rs1801694).
{ECO:0000269|PubMed:8889592}.
/FTId=VAR_005021.
VARIANT 3182 3182 H -> N (in dbSNP:rs12720848).
/FTId=VAR_029347.
VARIANT 3279 3279 S -> G (in dbSNP:rs12720854).
/FTId=VAR_029348.
VARIANT 3294 3294 S -> P (in dbSNP:rs12720855).
/FTId=VAR_020139.
VARIANT 3319 3319 D -> H. {ECO:0000269|PubMed:2883086,
ECO:0000269|PubMed:2994225,
ECO:0000269|PubMed:3030729,
ECO:0000269|PubMed:3464946,
ECO:0000269|PubMed:3652907,
ECO:0000269|PubMed:3759943,
ECO:0000269|PubMed:3763409,
ECO:0000269|PubMed:9490296}.
/FTId=VAR_005022.
VARIANT 3427 3427 T -> K. {ECO:0000269|PubMed:2883086,
ECO:0000269|PubMed:2994225,
ECO:0000269|PubMed:3030729,
ECO:0000269|PubMed:3464946,
ECO:0000269|PubMed:3652907,
ECO:0000269|PubMed:3759943,
ECO:0000269|PubMed:3763409,
ECO:0000269|PubMed:9490296}.
/FTId=VAR_005023.
VARIANT 3432 3432 Q -> E (in dbSNP:rs1042023).
{ECO:0000269|PubMed:2883086,
ECO:0000269|PubMed:2994225,
ECO:0000269|PubMed:3030729,
ECO:0000269|PubMed:3464946,
ECO:0000269|PubMed:3652907,
ECO:0000269|PubMed:3759943,
ECO:0000269|PubMed:3763409,
ECO:0000269|PubMed:9490296}.
/FTId=VAR_005024.
VARIANT 3527 3527 R -> Q (in FDB; dbSNP:rs5742904).
{ECO:0000269|PubMed:21382890,
ECO:0000269|PubMed:2563166,
ECO:0000269|PubMed:9259199}.
/FTId=VAR_005025.
VARIANT 3558 3558 R -> C (in FDB; dbSNP:rs12713559).
{ECO:0000269|PubMed:7883971,
ECO:0000269|PubMed:9259199}.
/FTId=VAR_005026.
VARIANT 3638 3638 R -> Q (in dbSNP:rs1801701).
{ECO:0000269|PubMed:22095935}.
/FTId=VAR_016186.
VARIANT 3732 3732 I -> T (in dbSNP:rs1042025).
{ECO:0000269|PubMed:2883086,
ECO:0000269|PubMed:2994225,
ECO:0000269|PubMed:3030729,
ECO:0000269|PubMed:3763409}.
/FTId=VAR_019833.
VARIANT 3801 3801 S -> T (in dbSNP:rs12713540).
/FTId=VAR_029349.
VARIANT 3835 3835 I -> L. {ECO:0000269|PubMed:22095935}.
/FTId=VAR_067279.
VARIANT 3921 3921 V -> I (in dbSNP:rs72654409).
{ECO:0000269|PubMed:9490296}.
/FTId=VAR_005027.
VARIANT 3945 3945 T -> A (in dbSNP:rs1801698).
{ECO:0000269|PubMed:8889592}.
/FTId=VAR_005028.
VARIANT 3949 3949 F -> L (in dbSNP:rs1042027).
{ECO:0000269|PubMed:2994225,
ECO:0000269|PubMed:3030729,
ECO:0000269|PubMed:3464946,
ECO:0000269|PubMed:3763409,
ECO:0000269|PubMed:3841481}.
/FTId=VAR_019834.
VARIANT 3964 3964 Y -> F (in dbSNP:rs1126468).
{ECO:0000269|PubMed:2994225,
ECO:0000269|PubMed:3030729,
ECO:0000269|PubMed:3763409,
ECO:0000269|PubMed:3841481}.
/FTId=VAR_019835.
VARIANT 4128 4128 V -> M (in dbSNP:rs1801703).
{ECO:0000269|PubMed:8889592}.
/FTId=VAR_005029.
VARIANT 4181 4181 E -> K (in dbSNP:rs1042031).
{ECO:0000269|PubMed:22095935,
ECO:0000269|PubMed:2994225,
ECO:0000269|PubMed:3030729,
ECO:0000269|PubMed:3464946,
ECO:0000269|PubMed:3763409,
ECO:0000269|PubMed:3841481}.
/FTId=VAR_016187.
VARIANT 4270 4270 R -> T (in dbSNP:rs1801702).
{ECO:0000269|PubMed:22095935}.
/FTId=VAR_016188.
VARIANT 4314 4314 I -> V (in dbSNP:rs72654423).
{ECO:0000269|PubMed:22095935}.
/FTId=VAR_067280.
VARIANT 4338 4338 S -> N (in dbSNP:rs1042034).
{ECO:0000269|PubMed:1979313,
ECO:0000269|PubMed:22095935,
ECO:0000269|PubMed:2883086,
ECO:0000269|PubMed:2932736,
ECO:0000269|PubMed:2994225,
ECO:0000269|PubMed:3030729,
ECO:0000269|PubMed:3464946,
ECO:0000269|PubMed:3652907,
ECO:0000269|PubMed:3759943,
ECO:0000269|PubMed:3763409,
ECO:0000269|Ref.6}.
/FTId=VAR_005030.
VARIANT 4394 4394 V -> A (in dbSNP:rs12720843).
/FTId=VAR_029350.
VARIANT 4481 4481 A -> T (in dbSNP:rs1801695).
{ECO:0000269|PubMed:22095935,
ECO:0000269|PubMed:8889592}.
/FTId=VAR_005031.
VARIANT 4482 4482 I -> V. {ECO:0000269|PubMed:22095935}.
/FTId=VAR_067281.
VARIANT 4484 4484 T -> M (in dbSNP:rs12713450).
/FTId=VAR_020140.
MUTAGEN 483 483 D->N: Impairs protein secretion.
{ECO:0000269|PubMed:12551903}.
MUTAGEN 483 483 D->Q: Does not affect protein secretion.
{ECO:0000269|PubMed:12551903}.
MUTAGEN 490 490 R->A: Impairs protein secretion.
{ECO:0000269|PubMed:12551903}.
MUTAGEN 490 490 R->K: Does not affect protein secretion.
{ECO:0000269|PubMed:12551903}.
CONFLICT 11 13 Missing (in Ref. 5; AAB60718/CAA28420).
{ECO:0000305}.
CONFLICT 329 329 L -> V (in Ref. 3; AAA35549).
{ECO:0000305}.
CONFLICT 645 645 L -> I (in Ref. 3; AAA35549).
{ECO:0000305}.
CONFLICT 704 704 L -> P (in Ref. 4; AAB04636).
{ECO:0000305}.
CONFLICT 792 809 LQLLGKLLLMGARTLQGI -> SSSWKAASHGCPHSAGD
(in Ref. 12; AAA51759). {ECO:0000305}.
CONFLICT 793 793 Q -> R (in Ref. 4; AAB04636).
{ECO:0000305}.
CONFLICT 893 893 D -> K (in Ref. 13; AA sequence).
{ECO:0000305}.
CONFLICT 919 919 A -> P (in Ref. 3; AAA35549).
{ECO:0000305}.
CONFLICT 1109 1109 H -> D (in Ref. 5; CAA28420).
{ECO:0000305}.
CONFLICT 1180 1180 T -> R (in Ref. 8; AAA51752).
{ECO:0000305}.
CONFLICT 1271 1271 F -> S (in Ref. 4; AAB04636).
{ECO:0000305}.
CONFLICT 1418 1418 F -> S (in Ref. 5; CAA28420).
{ECO:0000305}.
CONFLICT 1445 1445 N -> I (in Ref. 8; AAA51752).
{ECO:0000305}.
CONFLICT 1535 1535 G -> E (in Ref. 8; AAA51752).
{ECO:0000305}.
CONFLICT 1867 1867 R -> G (in Ref. 4; AAB04636).
{ECO:0000305}.
CONFLICT 2098 2098 N -> K (in Ref. 5; CAA28420).
{ECO:0000305}.
CONFLICT 2218 2218 I -> T (in Ref. 4; AAB04636).
{ECO:0000305}.
CONFLICT 2221 2221 N -> I (in Ref. 5; CAA28420).
{ECO:0000305}.
CONFLICT 2324 2326 LIG -> PYW (in Ref. 16; AAA51741).
{ECO:0000305}.
CONFLICT 2353 2353 Q -> H (in Ref. 16; AAA51741).
{ECO:0000305}.
CONFLICT 2540 2540 G -> S (in Ref. 5; CAA28420).
{ECO:0000305}.
CONFLICT 2718 2737 Missing (in Ref. 15; AAA51758).
{ECO:0000305}.
CONFLICT 2933 2933 C -> S (in Ref. 4; AAB04636).
{ECO:0000305}.
CONFLICT 3114 3114 H -> L (in Ref. 13; AA sequence).
{ECO:0000305}.
CONFLICT 3131 3131 T -> R (in Ref. 13; AA sequence).
{ECO:0000305}.
CONFLICT 3134 3134 E -> P (in Ref. 13; AA sequence).
{ECO:0000305}.
CONFLICT 3137 3137 L -> R (in Ref. 13; AA sequence).
{ECO:0000305}.
CONFLICT 3239 3239 H -> Q (in Ref. 5; CAA28420).
{ECO:0000305}.
CONFLICT 3286 3286 L -> I (in Ref. 4; AAB04636).
{ECO:0000305}.
CONFLICT 3291 3291 R -> L (in Ref. 15; AAA51758).
{ECO:0000305}.
CONFLICT 3337 3337 I -> N (in Ref. 15; AAA51758).
{ECO:0000305}.
CONFLICT 3431 3431 A -> P (in Ref. 4; AAB04636).
{ECO:0000305}.
CONFLICT 3728 3728 D -> N (in Ref. 24; AAA51742).
{ECO:0000305}.
CONFLICT 3782 3782 N -> T (in Ref. 4; AAB04636).
{ECO:0000305}.
CONFLICT 3824 3824 Q -> R (in Ref. 5; CAA28420 and 23;
AAA51750). {ECO:0000305}.
CONFLICT 3876 3876 V -> A (in Ref. 3; AAA35549 and 24;
AAA51742). {ECO:0000305}.
CONFLICT 3911 3911 T -> Y (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 3983 3983 F -> S (in Ref. 24; AAA51742).
{ECO:0000305}.
CONFLICT 4002 4002 A -> P (in Ref. 24; AAA51742).
{ECO:0000305}.
CONFLICT 4110 4111 NN -> DH (in Ref. 3; AAA35549 and 24;
AAA51742). {ECO:0000305}.
CONFLICT 4122 4122 Q -> E (in Ref. 3; AAA35549 and 24;
AAA51742). {ECO:0000305}.
CONFLICT 4128 4128 V -> E (in Ref. 3; AAA35549 and 24;
AAA51742). {ECO:0000305}.
CONFLICT 4133 4133 A -> G (in Ref. 3; AAA35549 and 24;
AAA51742). {ECO:0000305}.
CONFLICT 4188 4188 H -> K (in Ref. 4; AAB04636).
{ECO:0000305}.
CONFLICT 4217 4218 CT -> FP (in Ref. 26; AAA35548).
{ECO:0000305}.
CONFLICT 4221 4221 I -> M (in Ref. 4; AAB04636).
{ECO:0000305}.
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


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